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Volumn 14, Issue 3, 2013, Pages 287-324

Matrix metalloproteinases as potential targets in the venous dilation associated with varicose veins

Author keywords

Chronic venous insufficiency disease; Endothelium; Extracellular matrix; MMP; TIMP; Vascular smooth muscle

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL) CHROMONE; 2 [[(4 PHENOXYPHENYL) SULFONYL] METHYL] THIIRANE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL) IMIDAZOLE; BATIMASTAT; COUMARIN; DAFLON; DOXYCYCLINE; GELATINASE A; GELATINASE B; GINKGO BILOBA EXTRACT; GINKOR FORT; HEPTAMINOL; IBERIOTOXIN; ILOMASTAT; INCYCLINIDE; INTERSTITIAL COLLAGENASE; MACROPHAGE ELASTASE; MARIMASTAT; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 15; MATRIX METALLOPROTEINASE 16; MATRIX METALLOPROTEINASE 17; MATRIX METALLOPROTEINASE 19; MATRIX METALLOPROTEINASE 20; MATRIX METALLOPROTEINASE 26; MONOXERUTIN; OXERUTIN; PENTOXIFYLLINE; PLACEBO; PROSTAGLANDIN E1; TACROLIMUS; TROXERUTIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84876732671     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/1389450111314030003     Document Type: Article
Times cited : (86)

References (463)
  • 1
    • 44949120819 scopus 로고    scopus 로고
    • Mechanisms of varicose vein formation: Valve dysfunction and wall dilation
    • Raffetto JD, Khalil RA. Mechanisms of varicose vein formation: valve dysfunction and wall dilation. Phlebology 2008; 23(2): 85-98.
    • (2008) Phlebology , vol.23 , Issue.2 , pp. 85-98
    • Raffetto, J.D.1    Khalil, R.A.2
  • 3
    • 21844476414 scopus 로고    scopus 로고
    • Differential MMP-2 activity of ligament cells under mechanical stretch injury: An in vitro study on human ACL and MCL fibroblasts
    • Zhou D, Lee HS, Villarreal F, et al. Differential MMP-2 activity of ligament cells under mechanical stretch injury: an in vitro study on human ACL and MCL fibroblasts. J Orthop Res 2005; 23(4): 949-57.
    • (2005) J Orthop Res , vol.23 , Issue.4 , pp. 949-957
    • Zhou, D.1    Lee, H.S.2    Villarreal, F.3
  • 4
    • 23944486372 scopus 로고    scopus 로고
    • Effect of mechanical stretch on HIF-1{alpha} and MMP-2 expression in capillaries isolated from overloaded skeletal muscles: Laser capture microdissection study
    • Milkiewicz M, Haas TL. Effect of mechanical stretch on HIF-1{alpha} and MMP-2 expression in capillaries isolated from overloaded skeletal muscles: laser capture microdissection study. Am J Physiol Heart Circ Physiol 2005; 289(3): H1315-20.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289 , Issue.3
    • Milkiewicz, M.1    Haas, T.L.2
  • 5
    • 0034882846 scopus 로고    scopus 로고
    • New advances in the understanding of the pathophysiology of chronic venous insufficiency
    • Schmid-Schonbein GW, Takase S, Bergan JJ. New advances in the understanding of the pathophysiology of chronic venous insufficiency. Angiology 2001; 52 Suppl 1: S27-34.
    • (2001) Angiology , vol.52 , Issue.SUPPL. 1
    • Schmid-Schonbein, G.W.1    Takase, S.2    Bergan, J.J.3
  • 6
    • 0344837735 scopus 로고    scopus 로고
    • Uniaxial strain upregulates matrix-degrading enzymes produced by human vascular smooth muscle cells
    • Asanuma K, Magid R, Johnson C, Nerem RM, Galis ZS. Uniaxial strain upregulates matrix-degrading enzymes produced by human vascular smooth muscle cells. Am J Physiol Heart Circ Physiol 2003; 284(5): H1778-84.
    • (2003) Am J Physiol Heart Circ Physiol , vol.284 , Issue.5
    • Asanuma, K.1    Magid, R.2    Johnson, C.3    Nerem, R.M.4    Galis, Z.S.5
  • 7
    • 33846438987 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2-induced venous dilation via hyperpolarization and activation of K+ channels: Relevance to varicose vein formation
    • Raffetto JD, Ross RL, Khalil RA. Matrix metalloproteinase 2-induced venous dilation via hyperpolarization and activation of K+ channels: relevance to varicose vein formation. J Vasc Surg 2007; 45(2): 373-80.
    • (2007) J Vasc Surg , vol.45 , Issue.2 , pp. 373-380
    • Raffetto, J.D.1    Ross, R.L.2    Khalil, R.A.3
  • 8
    • 47249144255 scopus 로고    scopus 로고
    • Prolonged increases in vein wall tension increase matrix metalloproteinases and decrease constriction in rat vena cava: Potential implications in varicose veins
    • Raffetto JD, Qiao X, Koledova VV, Khalil RA. Prolonged increases in vein wall tension increase matrix metalloproteinases and decrease constriction in rat vena cava: Potential implications in varicose veins. J Vasc Surg 2008; 48(2): 447-56.
    • (2008) J Vasc Surg , vol.48 , Issue.2 , pp. 447-456
    • Raffetto, J.D.1    Qiao, X.2    Koledova, V.V.3    Khalil, R.A.4
  • 9
    • 77949486220 scopus 로고    scopus 로고
    • MMP-2 induced vein relaxation via inhibition of [Ca2+]e-dependent mechanisms of venous smooth muscle contraction. Role of RGD peptides
    • Raffetto JD, Barros YV, Wells AK, Khalil RA. MMP-2 induced vein relaxation via inhibition of [Ca2+]e-dependent mechanisms of venous smooth muscle contraction. Role of RGD peptides. J Surg Res 2010; 159(2): 755-64.
    • (2010) J Surg Res , vol.159 , Issue.2 , pp. 755-764
    • Raffetto, J.D.1    Barros, Y.V.2    Wells, A.K.3    Khalil, R.A.4
  • 11
    • 33845939566 scopus 로고    scopus 로고
    • Results of the national pilot screening program for venous disease by the American Venous Forum
    • McLafferty RB, Lohr JM, Caprini JA, et al. Results of the national pilot screening program for venous disease by the American Venous Forum. J Vasc Surg 2007; 45(1): 142-8.
    • (2007) J Vasc Surg , vol.45 , Issue.1 , pp. 142-148
    • McLafferty, R.B.1    Lohr, J.M.2    Caprini, J.A.3
  • 12
    • 19944392548 scopus 로고    scopus 로고
    • Revision of the CEAP classification for chronic venous disorders: Consensus statement
    • Eklof B, Rutherford RB, Bergan JJ, et al. Revision of the CEAP classification for chronic venous disorders: consensus statement. J Vasc Surg 2004; 40(6): 1248-52.
    • (2004) J Vasc Surg , vol.40 , Issue.6 , pp. 1248-1252
    • Eklof, B.1    Rutherford, R.B.2    Bergan, J.J.3
  • 13
    • 0028864146 scopus 로고
    • Risk factors for chronic venous insufficiency: A dual case-control study
    • Scott TE, LaMorte WW, Gorin DR, Menzoian JO. Risk factors for chronic venous insufficiency: a dual case-control study. J Vasc Surg 1995; 22(5): 622-8.
    • (1995) J Vasc Surg , vol.22 , Issue.5 , pp. 622-628
    • Scott, T.E.1    LaMorte, W.W.2    Gorin, D.R.3    Menzoian, J.O.4
  • 14
    • 0042667104 scopus 로고    scopus 로고
    • The influence of environmental factors in chronic venous insufficiency
    • Jawien A. The influence of environmental factors in chronic venous insufficiency. Angiology 2003; 54 Suppl 1: S19-31.
    • (2003) Angiology , vol.54 , Issue.SUPPL. 1
    • Jawien, A.1
  • 15
    • 0037929127 scopus 로고    scopus 로고
    • Epidemiology of venous insufficiency in an occupational population
    • Lacroix P, Aboyans V, Preux PM, Houles MB, Laskar M. Epidemiology of venous insufficiency in an occupational population. Int Angiol 2003; 22(2): 172-6.
    • (2003) Int Angiol , vol.22 , Issue.2 , pp. 172-176
    • Lacroix, P.1    Aboyans, V.2    Preux, P.M.3    Houles, M.B.4    Laskar, M.5
  • 16
  • 17
    • 0023938896 scopus 로고
    • Venous reflux: Quantification and correlation with the clinical severity of chronic venous disease
    • Christopoulos D, Nicolaides AN, Szendro G. Venous reflux: quantification and correlation with the clinical severity of chronic venous disease. Br J Surg 1988; 75(4): 352-6.
    • (1988) Br J Surg , vol.75 , Issue.4 , pp. 352-356
    • Christopoulos, D.1    Nicolaides, A.N.2    Szendro, G.3
  • 18
    • 22844447869 scopus 로고    scopus 로고
    • Serum iron and matrix metalloproteinase-9 variations in limbs affected by chronic venous disease and venous leg ulcers
    • discussion 9
    • Zamboni P, Scapoli G, Lanzara V, et al. Serum iron and matrix metalloproteinase-9 variations in limbs affected by chronic venous disease and venous leg ulcers. Dermatol Surg 2005; 31(6): 644-9; discussion 9.
    • (2005) Dermatol Surg , vol.31 , Issue.6 , pp. 644-649
    • Zamboni, P.1    Scapoli, G.2    Lanzara, V.3
  • 19
    • 33646155314 scopus 로고    scopus 로고
    • The overlapping of local iron overload and HFE mutation in venous leg ulcer pathogenesis
    • Zamboni P, Izzo M, Tognazzo S, et al. The overlapping of local iron overload and HFE mutation in venous leg ulcer pathogenesis. Free Radic Biol Med 2006; 40(10): 1869-73.
    • (2006) Free Radic Biol Med , vol.40 , Issue.10 , pp. 1869-1873
    • Zamboni, P.1    Izzo, M.2    Tognazzo, S.3
  • 20
    • 4744364274 scopus 로고    scopus 로고
    • Factor XIII contrasts the effects of metalloproteinases in human dermal fibroblast cultured cells
    • Zamboni P, De Mattei M, Ongaro A, et al. Factor XIII contrasts the effects of metalloproteinases in human dermal fibroblast cultured cells. Vasc Endovascular Surg 2004; 38(5): 431-8.
    • (2004) Vasc Endovascular Surg , vol.38 , Issue.5 , pp. 431-438
    • Zamboni, P.1    de Mattei, M.2    Ongaro, A.3
  • 21
    • 23744438772 scopus 로고    scopus 로고
    • Hemochromatosis C282Y gene mutation increases the risk of venous leg ulceration
    • Zamboni P, Tognazzo S, Izzo M, et al. Hemochromatosis C282Y gene mutation increases the risk of venous leg ulceration. J Vasc Surg 2005; 42(2): 309-14.
    • (2005) J Vasc Surg , vol.42 , Issue.2 , pp. 309-314
    • Zamboni, P.1    Tognazzo, S.2    Izzo, M.3
  • 22
    • 33748955977 scopus 로고    scopus 로고
    • Prognostic role of factor XIII gene variants in nonhealing venous leg ulcers
    • Tognazzo S, Gemmati D, Palazzo A, et al. Prognostic role of factor XIII gene variants in nonhealing venous leg ulcers. J Vasc Surg 2006; 44(4): 815-9.
    • (2006) J Vasc Surg , vol.44 , Issue.4 , pp. 815-819
    • Tognazzo, S.1    Gemmati, D.2    Palazzo, A.3
  • 23
    • 33747885218 scopus 로고    scopus 로고
    • Influence of gene polymorphisms in ulcer healing process after superficial venous surgery
    • Gemmati D, Tognazzo S, Catozzi L, et al. Influence of gene polymorphisms in ulcer healing process after superficial venous surgery. J Vasc Surg 2006; 44(3): 554-62.
    • (2006) J Vasc Surg , vol.44 , Issue.3 , pp. 554-562
    • Gemmati, D.1    Tognazzo, S.2    Catozzi, L.3
  • 25
    • 33847134294 scopus 로고    scopus 로고
    • Hemodynamic impairment, venous segmental disease, and clinical severity scoring in limbs with Klippel-Trenaunay syndrome
    • Delis KT, Gloviczki P, Wennberg PW, Rooke TW, Driscoll DJ. Hemodynamic impairment, venous segmental disease, and clinical severity scoring in limbs with Klippel-Trenaunay syndrome. J Vasc Surg 2007; 45(3): 561-7.
    • (2007) J Vasc Surg , vol.45 , Issue.3 , pp. 561-567
    • Delis, K.T.1    Gloviczki, P.2    Wennberg, P.W.3    Rooke, T.W.4    Driscoll, D.J.5
  • 26
    • 15044348467 scopus 로고    scopus 로고
    • Linkage to the FOXC2 region of chromosome 16 for varicose veins in otherwise healthy, unselected sibling pairs
    • Ng MY, Andrew T, Spector TD, Jeffery S. Linkage to the FOXC2 region of chromosome 16 for varicose veins in otherwise healthy, unselected sibling pairs. J Med Genet 2005; 42(3): 235-9.
    • (2005) J Med Genet , vol.42 , Issue.3 , pp. 235-239
    • Ng, M.Y.1    Andrew, T.2    Spector, T.D.3    Jeffery, S.4
  • 27
    • 18444378418 scopus 로고    scopus 로고
    • Analysis of the phenotypic abnormalities in lymphoedema-distichiasis syndrome in 74 patients with FOXC2 mutations or linkage to 16q24
    • Brice G, Mansour S, Bell R, et al. Analysis of the phenotypic abnormalities in lymphoedema-distichiasis syndrome in 74 patients with FOXC2 mutations or linkage to 16q24. J Med Genet 2002; 39(7): 478-83.
    • (2002) J Med Genet , vol.39 , Issue.7 , pp. 478-483
    • Brice, G.1    Mansour, S.2    Bell, R.3
  • 28
    • 84867062052 scopus 로고    scopus 로고
    • A genetic study of chronic venous insufficiency
    • Serra R, Buffone G, de Franciscis A, et al. A genetic study of chronic venous insufficiency. Ann Vasc Surg 2012; 26(5): 636-42.
    • (2012) Ann Vasc Surg , vol.26 , Issue.5 , pp. 636-642
    • Serra, R.1    Buffone, G.2    de Franciscis, A.3
  • 29
    • 33747067434 scopus 로고    scopus 로고
    • Varicose veins associated with CADASIL result from a novel mutation in the Notch3 gene
    • Saiki S, Sakai K, Saiki M, et al. Varicose veins associated with CADASIL result from a novel mutation in the Notch3 gene. Neurology 2006; 67(2): 337-9.
    • (2006) Neurology , vol.67 , Issue.2 , pp. 337-339
    • Saiki, S.1    Sakai, K.2    Saiki, M.3
  • 30
    • 20144388019 scopus 로고    scopus 로고
    • Gene expression profiles in varicose veins using complementary DNA microarray
    • Lee S, Lee W, Choe Y, et al. Gene expression profiles in varicose veins using complementary DNA microarray. Dermatol Surg 2005; 31(4): 391-5.
    • (2005) Dermatol Surg , vol.31 , Issue.4 , pp. 391-395
    • Lee, S.1    Lee, W.2    Choe, Y.3
  • 31
    • 25844466563 scopus 로고    scopus 로고
    • Hemihyperplasia with Ehlers-Danlos syndrome like skin changes
    • Dalal A, Phadke SR. Hemihyperplasia with Ehlers-Danlos syndrome like skin changes. Clin Dysmorphol 2005; 14(4): 207-8.
    • (2005) Clin Dysmorphol , vol.14 , Issue.4 , pp. 207-208
    • Dalal, A.1    Phadke, S.R.2
  • 33
    • 79955635216 scopus 로고    scopus 로고
    • Polymorphisms in MMP-9 and TIMP-2 in Chinese patients with varicose veins
    • Xu HM, Zhao Y, Zhang XM, Zhu T, Fu WG. Polymorphisms in MMP-9 and TIMP-2 in Chinese patients with varicose veins. J Surg Res 2011; 168(1): e143-8.
    • (2011) J Surg Res , vol.168 , Issue.1
    • Xu, H.M.1    Zhao, Y.2    Zhang, X.M.3    Zhu, T.4    Fu, W.G.5
  • 34
    • 0026692978 scopus 로고
    • Venous wall function in the pathogenesis of varicose veins
    • Clarke GH, Vasdekis SN, Hobbs JT, Nicolaides AN. Venous wall function in the pathogenesis of varicose veins. Surgery 1992; 111(4): 402-8.
    • (1992) Surgery , vol.111 , Issue.4 , pp. 402-408
    • Clarke, G.H.1    Vasdekis, S.N.2    Hobbs, J.T.3    Nicolaides, A.N.4
  • 35
    • 0014975693 scopus 로고
    • Lower limb venous dynamics in normal persons and children of patients with varicose veins
    • Reagan B, Folse R. Lower limb venous dynamics in normal persons and children of patients with varicose veins. Surg Gynecol Obstet 1971; 132(1): 15-8.
    • (1971) Surg Gynecol Obstet , vol.132 , Issue.1 , pp. 15-18
    • Reagan, B.1    Folse, R.2
  • 36
    • 0014021308 scopus 로고
    • Venous distensibility in patients with varicose veins
    • Zsoter T, Cronin RF. Venous distensibility in patients with varicose veins. Can Med Assoc J 1966; 94(25): 1293-7.
    • (1966) Can Med Assoc J , vol.94 , Issue.25 , pp. 1293-1297
    • Zsoter, T.1    Cronin, R.F.2
  • 37
    • 0035217825 scopus 로고    scopus 로고
    • Imbalance in the synthesis of collagen type I and collagen type III in smooth muscle cells derived from human varicose veins
    • Sansilvestri-Morel P, Rupin A, Badier-Commander C, et al. Imbalance in the synthesis of collagen type I and collagen type III in smooth muscle cells derived from human varicose veins. J Vasc Res 2001; 38(6): 560-8.
    • (2001) J Vasc Res , vol.38 , Issue.6 , pp. 560-568
    • Sansilvestri-Morel, P.1    Rupin, A.2    Badier-Commander, C.3
  • 38
    • 0022549620 scopus 로고
    • Human type III collagen gene expression is coordinately modulated with the type I collagen genes during fibroblast growth
    • Miskulin M, Dalgleish R, Kluve-Beckerman B, et al. Human type III collagen gene expression is coordinately modulated with the type I collagen genes during fibroblast growth. Biochemistry 1986; 25(6): 1408-13.
    • (1986) Biochemistry , vol.25 , Issue.6 , pp. 1408-1413
    • Miskulin, M.1    Dalgleish, R.2    Kluve-Beckerman, B.3
  • 41
    • 0001153981 scopus 로고    scopus 로고
    • What are the symptoms of varicose veins? Edinburgh vein study cross sectional population survey
    • Bradbury A, Evans C, Allan P, Lee A, Ruckley CV, Fowkes FG. What are the symptoms of varicose veins? Edinburgh vein study cross sectional population survey. BMJ 1999; 318(7180): 353-6.
    • (1999) BMJ , vol.318 , Issue.7180 , pp. 353-356
    • Bradbury, A.1    Evans, C.2    Allan, P.3    Lee, A.4    Ruckley, C.V.5    Fowkes, F.G.6
  • 42
    • 0032977870 scopus 로고    scopus 로고
    • Prevalence of varicose veins and chronic venous insufficiency in men and women in the general population: Edinburgh Vein Study
    • Evans CJ, Fowkes FG, Ruckley CV, Lee AJ. Prevalence of varicose veins and chronic venous insufficiency in men and women in the general population: Edinburgh Vein Study. J Epidemiol Community Health 1999; 53(3): 149-53.
    • (1999) J Epidemiol Community Health , vol.53 , Issue.3 , pp. 149-153
    • Evans, C.J.1    Fowkes, F.G.2    Ruckley, C.V.3    Lee, A.J.4
  • 43
    • 0036736435 scopus 로고    scopus 로고
    • Chronic venous insufficiency: Clinical and duplex correlations. The Edinburgh Vein Study of venous disorders in the general population
    • Ruckley CV, Evans CJ, Allan PL, Lee AJ, Fowkes FG. Chronic venous insufficiency: clinical and duplex correlations. The Edinburgh Vein Study of venous disorders in the general population. J Vasc Surg 2002; 36(3): 520-5.
    • (2002) J Vasc Surg , vol.36 , Issue.3 , pp. 520-525
    • Ruckley, C.V.1    Evans, C.J.2    Allan, P.L.3    Lee, A.J.4    Fowkes, F.G.5
  • 44
    • 77949891639 scopus 로고    scopus 로고
    • Estrogen receptor-mediated enhancement of venous relaxation in female rat: Implications in sex-related differences in varicose veins
    • Raffetto JD, Qiao X, Beauregard KG, Khalil RA. Estrogen receptor-mediated enhancement of venous relaxation in female rat: implications in sex-related differences in varicose veins. J Vasc Surg 2010; 51(4): 972-81.
    • (2010) J Vasc Surg , vol.51 , Issue.4 , pp. 972-981
    • Raffetto, J.D.1    Qiao, X.2    Beauregard, K.G.3    Khalil, R.A.4
  • 45
    • 0033709493 scopus 로고    scopus 로고
    • Endocrine and paracrine regulation of birth at term and preterm
    • Challis JRG, Matthews SG, Gibb W, Lye SJ. Endocrine and paracrine regulation of birth at term and preterm. Endocr Rev 2000; 21(5): 514-50.
    • (2000) Endocr Rev , vol.21 , Issue.5 , pp. 514-550
    • Challis, J.R.G.1    Matthews, S.G.2    Gibb, W.3    Lye, S.J.4
  • 46
    • 0035347146 scopus 로고    scopus 로고
    • Plasma volume expansion in early pregnancy
    • Bernstein IM, Ziegler W, Badger GJ. Plasma volume expansion in early pregnancy. Obstet Gynecol 2001; 97(5 Pt 1): 669-72.
    • (2001) Obstet Gynecol , vol.97 , Issue.5 PART 1 , pp. 669-672
    • Bernstein, I.M.1    Ziegler, W.2    Badger, G.J.3
  • 47
    • 7844247177 scopus 로고    scopus 로고
    • Temporal relationships between hormonal and hemodynamic changes in early human pregnancy
    • Chapman AB, Abraham WT, Zamudio S, et al. Temporal relationships between hormonal and hemodynamic changes in early human pregnancy. Kidney Int 1998; 54(6): 2056-63.
    • (1998) Kidney Int , vol.54 , Issue.6 , pp. 2056-2063
    • Chapman, A.B.1    Abraham, W.T.2    Zamudio, S.3
  • 48
    • 0034175879 scopus 로고    scopus 로고
    • Women, pregnancy, and varicose veins
    • Stansby G. Women, pregnancy, and varicose veins. Lancet 2000; 355(9210): 1117-8.
    • (2000) Lancet , vol.355 , Issue.9210 , pp. 1117-1118
    • Stansby, G.1
  • 49
    • 84965270787 scopus 로고
    • Varicose veins in women cotton workers. An epidemiological study in England and Egypt
    • Mekky S, Schilling RS, Walford J. Varicose veins in women cotton workers. An epidemiological study in England and Egypt. Br Med J 1969; 2(5657): 591-5.
    • (1969) Br Med J , vol.2 , Issue.5657 , pp. 591-595
    • Mekky, S.1    Schilling, R.S.2    Walford, J.3
  • 50
    • 0022545778 scopus 로고
    • Overweight and chronic illness--a retrospective cohort study, with a follow-up of 6-17 years, in men and women of initially 20-50 years of age
    • Seidell JC, Bakx KC, Deurenberg P, van den Hoogen HJ, Hautvast JG, Stijnen T. Overweight and chronic illness--a retrospective cohort study, with a follow-up of 6-17 years, in men and women of initially 20-50 years of age. J Chronic Dis 1986; 39(8): 585-93.
    • (1986) J Chronic Dis , vol.39 , Issue.8 , pp. 585-593
    • Seidell, J.C.1    Bakx, K.C.2    Deurenberg, P.3    van den Hoogen, H.J.4    Hautvast, J.G.5    Stijnen, T.6
  • 51
    • 0025818745 scopus 로고
    • Associations of body mass and fat distribution with sex hormone concentrations in postmenopausal women
    • Kaye SA, Folsom AR, Soler JT, Prineas RJ, Potter JD. Associations of body mass and fat distribution with sex hormone concentrations in postmenopausal women. Int J Epidemiol 1991; 20(1): 151-6.
    • (1991) Int J Epidemiol , vol.20 , Issue.1 , pp. 151-156
    • Kaye, S.A.1    Folsom, A.R.2    Soler, J.T.3    Prineas, R.J.4    Potter, J.D.5
  • 52
    • 0019386768 scopus 로고
    • The epidemiology of varicose veins. A survey in western Jerusalem
    • Abramson JH, Hopp C, Epstein LM. The epidemiology of varicose veins. A survey in western Jerusalem. J Epidemiol Community Health 1981; 35(3): 213-7.
    • (1981) J Epidemiol Community Health , vol.35 , Issue.3 , pp. 213-217
    • Abramson, J.H.1    Hopp, C.2    Epstein, L.M.3
  • 53
    • 84861816728 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease
    • Benjamin MM, Khalil RA. Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease. EXS 2012; 103: 209-79.
    • (2012) EXS , vol.103 , pp. 209-279
    • Benjamin, M.M.1    Khalil, R.A.2
  • 54
    • 0345935809 scopus 로고
    • Collagenolytic activity in amphibian tissues: A tissue culture assay
    • Gross J, Lapiere CM. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc Natl Acad Sci U S A 1962; 48: 1014-22.
    • (1962) Proc Natl Acad Sci U S A , vol.48 , pp. 1014-1022
    • Gross, J.1    Lapiere, C.M.2
  • 55
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 2003; 92(8): 827-39.
    • (2003) Circ Res , vol.92 , Issue.8 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 56
    • 0037155057 scopus 로고    scopus 로고
    • Matrix metalloproteinases in vascular remodeling and atherogenesis: The good, the bad, and the ugly
    • Galis ZS, Khatri JJ. Matrix metalloproteinases in vascular remodeling and atherogenesis: the good, the bad, and the ugly. Circ Res 2002; 90(3): 251-62.
    • (2002) Circ Res , vol.90 , Issue.3 , pp. 251-262
    • Galis, Z.S.1    Khatri, J.J.2
  • 57
    • 37349082926 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibitors in vascular remodeling and vascular disease
    • Raffetto JD, Khalil RA. Matrix metalloproteinases and their inhibitors in vascular remodeling and vascular disease. Biochem Pharmacol 2008; 75(2): 346-59.
    • (2008) Biochem Pharmacol , vol.75 , Issue.2 , pp. 346-359
    • Raffetto, J.D.1    Khalil, R.A.2
  • 58
    • 48549102413 scopus 로고    scopus 로고
    • Elucidating the function of non catalytic domains of collagenases and aggrecanases
    • Nagase H, Fushimi K. Elucidating the function of non catalytic domains of collagenases and aggrecanases. Connect Tissue Res 2008; 49(3): 169-74.
    • (2008) Connect Tissue Res , vol.49 , Issue.3 , pp. 169-174
    • Nagase, H.1    Fushimi, K.2
  • 59
    • 4143066015 scopus 로고    scopus 로고
    • Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis
    • Chung L, Dinakarpandian D, Yoshida N, et al. Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. EMBO J 2004; 23(15): 3020-30.
    • (2004) EMBO J , vol.23 , Issue.15 , pp. 3020-3030
    • Chung, L.1    Dinakarpandian, D.2    Yoshida, N.3
  • 60
    • 50049110249 scopus 로고    scopus 로고
    • Metabolism distribution and excretion of a matrix metalloproteinase-13 inhibitor, 4-[4-(4-fluorophenoxy)-benzenesulfonylamino]tetrahydropyran-4-carboxylic acid hydroxyamide (CP-544439), in rats and dogs: Assessment of the metabolic profile of CP-544439 in plasma and urine of humans
    • Dalvie D, Cosker T, Boyden T, Zhou S, Schroeder C, Potchoiba MJ. Metabolism distribution and excretion of a matrix metalloproteinase-13 inhibitor, 4-[4-(4-fluorophenoxy)-benzenesulfonylamino]tetrahydropyran-4-carboxylic acid hydroxyamide (CP-544439), in rats and dogs: assessment of the metabolic profile of CP-544439 in plasma and urine of humans. Drug Metab Dispos 2008; 36(9): 1869-83.
    • (2008) Drug Metab Dispos , vol.36 , Issue.9 , pp. 1869-1883
    • Dalvie, D.1    Cosker, T.2    Boyden, T.3    Zhou, S.4    Schroeder, C.5    Potchoiba, M.J.6
  • 62
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4-and 1/4-length fragments
    • Aimes RT, Quigley JP. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4-and 1/4-length fragments. J Biol Chem 1995; 270(11): 5872-6.
    • (1995) J Biol Chem , vol.270 , Issue.11 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 63
    • 0035903020 scopus 로고    scopus 로고
    • Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain
    • Patterson ML, Atkinson SJ, Knauper V, Murphy G. Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain. FEBS Lett 2001; 503(2-3): 158-62.
    • (2001) FEBS Lett , vol.503 , Issue.2-3 , pp. 158-162
    • Patterson, M.L.1    Atkinson, S.J.2    Knauper, V.3    Murphy, G.4
  • 64
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 2006; 69(3): 562-73.
    • (2006) Cardiovasc Res , vol.69 , Issue.3 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 65
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei D, Weiss SJ. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 1995; 375(6528): 244-7.
    • (1995) Nature , vol.375 , Issue.6528 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 66
    • 0034283015 scopus 로고    scopus 로고
    • Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity
    • Uria JA, Lopez-Otin C. Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity. Cancer Res 2000; 60(17): 4745-51.
    • (2000) Cancer Res , vol.60 , Issue.17 , pp. 4745-4751
    • Uria, J.A.1    Lopez-Otin, C.2
  • 67
    • 0034617262 scopus 로고    scopus 로고
    • Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor
    • Park HI, Ni J, Gerkema FE, Liu D, Belozerov VE, Sang QX. Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor. J Biol Chem 2000; 275(27): 20540-4.
    • (2000) J Biol Chem , vol.275 , Issue.27 , pp. 20540-20544
    • Park, H.I.1    Ni, J.2    Gerkema, F.E.3    Liu, D.4    Belozerov, V.E.5    Sang, Q.X.6
  • 68
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks WC, Wilson CL, Lopez-Boado YS. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol 2004; 4(8): 617-29.
    • (2004) Nat Rev Immunol , vol.4 , Issue.8 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 69
    • 1542285119 scopus 로고    scopus 로고
    • Beta-catenin regulates the gene of MMP-26, a novel metalloproteinase ex pressed both in carcinomas and normal epithelial cells
    • Marchenko ND, Marchenko GN, Weinreb RN, et al. Beta-catenin regulates the gene of MMP-26, a novel metalloproteinase ex pressed both in carcinomas and normal epithelial cells. Int J Biochem Cell Biol 2004; 36(5): 942-56.
    • (2004) Int J Biochem Cell Biol , vol.36 , Issue.5 , pp. 942-956
    • Marchenko, N.D.1    Marchenko, G.N.2    Weinreb, R.N.3
  • 70
    • 0035834666 scopus 로고    scopus 로고
    • Characterization of the role of the "MT-loop": An eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases
    • English WR, Holtz B, Vogt G, Knauper V, Murphy G. Characterization of the role of the "MT-loop": an eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases. J Biol Chem 2001; 276(45): 42018-26.
    • (2001) J Biol Chem , vol.276 , Issue.45 , pp. 42018-42026
    • English, W.R.1    Holtz, B.2    Vogt, G.3    Knauper, V.4    Murphy, G.5
  • 71
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem 1997; 272(4): 2446-51.
    • (1997) J Biol Chem , vol.272 , Issue.4 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 72
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme
    • Knauper V, Will H, Lopez-Otin C, et al. Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J Biol Chem 1996; 271(29): 17124-31.
    • (1996) J Biol Chem , vol.271 , Issue.29 , pp. 17124-17131
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3
  • 74
    • 0034748677 scopus 로고    scopus 로고
    • Human macrophage metalloelastase (MMP-12) expression is induced in chondrocytes during fetal development and malignant transformation
    • Kerkela E, Bohling T, Herva R, Uria JA, Saarialho-Kere U. Human macrophage metalloelastase (MMP-12) expression is induced in chondrocytes during fetal development and malignant transformation. Bone 2001; 29(5): 487-93.
    • (2001) Bone , vol.29 , Issue.5 , pp. 487-493
    • Kerkela, E.1    Bohling, T.2    Herva, R.3    Uria, J.A.4    Saarialho-Kere, U.5
  • 75
    • 0942268153 scopus 로고    scopus 로고
    • Matrix metalloproteinase-12 (MMP-12) in osteoclasts: New lesson on the involvement of MMPs in bone resorption
    • Hou P, Troen T, Ovejero MC, et al. Matrix metalloproteinase-12 (MMP-12) in osteoclasts: new lesson on the involvement of MMPs in bone resorption. Bone 2004; 34(1): 37-47.
    • (2004) Bone , vol.34 , Issue.1 , pp. 37-47
    • Hou, P.1    Troen, T.2    Ovejero, M.C.3
  • 76
    • 0034726067 scopus 로고    scopus 로고
    • Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)
    • Stracke JO, Fosang AJ, Last K, et al. Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP). FEBS Lett 2000; 478(1-2): 52-6.
    • (2000) FEBS Lett , vol.478 , Issue.1-2 , pp. 52-56
    • Stracke, J.O.1    Fosang, A.J.2    Last, K.3
  • 77
    • 0242574368 scopus 로고    scopus 로고
    • Matrix metalloproteinase-19 expression in normal and diseased skin: Dysregulation by epidermal proliferation
    • Sadowski T, Dietrich S, Muller M, et al. Matrix metalloproteinase-19 expression in normal and diseased skin: dysregulation by epidermal proliferation. J Invest Dermatol 2003; 121(5): 989-96.
    • (2003) J Invest Dermatol , vol.121 , Issue.5 , pp. 989-996
    • Sadowski, T.1    Dietrich, S.2    Muller, M.3
  • 78
    • 0345255740 scopus 로고    scopus 로고
    • Matrix metalloproteinase 19 regulates insulin-like growth factor-mediated proliferation, migration, and adhesion in human keratinocytes through proteolysis of insulin-like growth factor binding protein-3
    • Sadowski T, Dietrich S, Koschinsky F, Sedlacek R. Matrix metalloproteinase 19 regulates insulin-like growth factor-mediated proliferation, migration, and adhesion in human keratinocytes through proteolysis of insulin-like growth factor binding protein-3. Mol Biol Cell 2003; 14(11): 4569-80.
    • (2003) Mol Biol Cell , vol.14 , Issue.11 , pp. 4569-4580
    • Sadowski, T.1    Dietrich, S.2    Koschinsky, F.3    Sedlacek, R.4
  • 79
    • 18544385760 scopus 로고    scopus 로고
    • Matrix metalloproteinase 19 processes the laminin 5 gamma 2 chain and induces epithelial cell migration
    • Sadowski T, Dietrich S, Koschinsky F, et al. Matrix metalloproteinase 19 processes the laminin 5 gamma 2 chain and induces epithelial cell migration. Cell Mol Life Sci 2005; 62(7-8): 870-80.
    • (2005) Cell Mol Life Sci , vol.62 , Issue.7-8 , pp. 870-880
    • Sadowski, T.1    Dietrich, S.2    Koschinsky, F.3
  • 80
    • 2942629103 scopus 로고    scopus 로고
    • Diet-induced obesity and reduced skin cancer susceptibility in matrix metalloproteinase 19-deficient mice
    • Pendas AM, Folgueras AR, Llano E, et al. Diet-induced obesity and reduced skin cancer susceptibility in matrix metalloproteinase 19-deficient mice. Mol Cell Biol 2004; 24(12): 5304-13.
    • (2004) Mol Cell Biol , vol.24 , Issue.12 , pp. 5304-5313
    • Pendas, A.M.1    Folgueras, A.R.2    Llano, E.3
  • 81
    • 0033278065 scopus 로고    scopus 로고
    • Characterization of recombinant pig enamelysin activity and cleavage of recombinant pig and mouse amelogenins
    • Ryu OH, Fincham AG, Hu CC, et al. Characterization of recombinant pig enamelysin activity and cleavage of recombinant pig and mouse amelogenins. J Dent Res 1999; 78(3): 743-50.
    • (1999) J Dent Res , vol.78 , Issue.3 , pp. 743-750
    • Ryu, O.H.1    Fincham, A.G.2    Hu, C.C.3
  • 82
    • 0035133863 scopus 로고    scopus 로고
    • Reduced hydrolysis of amelogenin may result in X-linked amelogenesis imperfecta
    • Li W, Gibson CW, Abrams WR, Andrews DW, DenBesten PK. Reduced hydrolysis of amelogenin may result in X-linked amelogenesis imperfecta. Matrix Biol 2001; 19(8): 755-60.
    • (2001) Matrix Biol , vol.19 , Issue.8 , pp. 755-760
    • Li, W.1    Gibson, C.W.2    Abrams, W.R.3    Andrews, D.W.4    DenBesten, P.K.5
  • 84
    • 0346103788 scopus 로고    scopus 로고
    • Matrix metalloproteinase-21 is expressed epithelially during development and in cancer and is upregulated by transforming growth factor-beta1 in keratinocytes
    • Ahokas K, Lohi J, Illman SA, et al. Matrix metalloproteinase-21 is expressed epithelially during development and in cancer and is upregulated by transforming growth factor-beta1 in keratinocytes. Lab Invest 2003; 83(12): 1887-99.
    • (2003) Lab Invest , vol.83 , Issue.12 , pp. 1887-1899
    • Ahokas, K.1    Lohi, J.2    Illman, S.A.3
  • 85
    • 0032504177 scopus 로고    scopus 로고
    • Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain
    • Yang M, Kurkinen M. Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain. J Biol Chem 1998; 273(28): 17893-900.
    • (1998) J Biol Chem , vol.273 , Issue.28 , pp. 17893-17900
    • Yang, M.1    Kurkinen, M.2
  • 86
    • 0034721850 scopus 로고    scopus 로고
    • Cysteine array matrix metalloproteinase (CAMMP)/ MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation
    • Pei D, Kang T, Qi H. Cysteine array matrix metalloproteinase (CAMMP)/ MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation. J Biol Chem 2000; 275(43): 33988-97.
    • (2000) J Biol Chem , vol.275 , Issue.43 , pp. 33988-33997
    • Pei, D.1    Kang, T.2    Qi, H.3
  • 87
    • 0033582513 scopus 로고    scopus 로고
    • Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members
    • Velasco G, Pendas AM, Fueyo A, Knauper V, Murphy G, Lopez-Otin C. Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J Biol Chem 1999; 274(8): 4570-6.
    • (1999) J Biol Chem , vol.274 , Issue.8 , pp. 4570-4576
    • Velasco, G.1    Pendas, A.M.2    Fueyo, A.3    Knauper, V.4    Murphy, G.5    Lopez-Otin, C.6
  • 88
    • 34250312341 scopus 로고    scopus 로고
    • The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases
    • Cauwe B, Van den Steen PE, Opdenakker G. The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit Rev Biochem Mol Biol 2007; 42(3): 113-85.
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , Issue.3 , pp. 113-185
    • Cauwe, B.1    van den Steen, P.E.2    Opdenakker, G.3
  • 89
    • 0344443218 scopus 로고    scopus 로고
    • Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis
    • Bar-Or A, Nuttall RK, Duddy M, et al. Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis. Brain 2003; 126(Pt 12): 2738-49.
    • (2003) Brain , vol.126 , Issue.PART 12 , pp. 2738-2749
    • Bar-Or, A.1    Nuttall, R.K.2    Duddy, M.3
  • 90
    • 0035819913 scopus 로고    scopus 로고
    • MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors
    • Marchenko GN, Strongin AY. MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors. Gene 2001; 265(1-2): 87-93.
    • (2001) Gene , vol.265 , Issue.1-2 , pp. 87-93
    • Marchenko, G.N.1    Strongin, A.Y.2
  • 91
    • 0035971090 scopus 로고    scopus 로고
    • Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury
    • Lohi J, Wilson CL, Roby JD, Parks WC. Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury. J Biol Chem 2001; 276(13): 10134-44.
    • (2001) J Biol Chem , vol.276 , Issue.13 , pp. 10134-10144
    • Lohi, J.1    Wilson, C.L.2    Roby, J.D.3    Parks, W.C.4
  • 93
    • 9144230209 scopus 로고    scopus 로고
    • Expression profiling of metalloproteinases and their inhibitors in cartilage
    • Kevorkian L, Young DA, Darrah C, et al. Expression profiling of metalloproteinases and their inhibitors in cartilage. Arthritis Rheum 2004; 50(1): 131-41.
    • (2004) Arthritis Rheum , vol.50 , Issue.1 , pp. 131-141
    • Kevorkian, L.1    Young, D.A.2    Darrah, C.3
  • 94
    • 10444268099 scopus 로고    scopus 로고
    • Matrix metalloproteinase 28/epilysin expression in cartilage from patients with rheumatoid arthritis and osteoarthritis: Comment on the article by Kevorkian et al
    • author reply 5
    • Momohara S, Okamoto H, Komiya K, et al. Matrix metalloproteinase 28/epilysin expression in cartilage from patients with rheumatoid arthritis and osteoarthritis: comment on the article by Kevorkian et al. Arthritis Rheum 2004; 50(12): 4074-5; author reply 5.
    • (2004) Arthritis Rheum , vol.50 , Issue.12 , pp. 4074-4075
    • Momohara, S.1    Okamoto, H.2    Komiya, K.3
  • 95
    • 0036389631 scopus 로고    scopus 로고
    • Varicose veins possess greater quantities of MMP-1 than normal veins and demonstrate regional variation in MMP-1 and MMP-13
    • Gillespie DL, Patel A, Fileta B, et al. Varicose veins possess greater quantities of MMP-1 than normal veins and demonstrate regional variation in MMP-1 and MMP-13. J Surg Res 2002; 106(2): 233-8.
    • (2002) J Surg Res , vol.106 , Issue.2 , pp. 233-238
    • Gillespie, D.L.1    Patel, A.2    Fileta, B.3
  • 97
    • 0037771303 scopus 로고    scopus 로고
    • Morphologic characteristics of varicose veins: Possible role of metalloproteinases
    • Woodside KJ, Hu M, Burke A, et al. Morphologic characteristics of varicose veins: possible role of metalloproteinases. J Vasc Surg 2003; 38(1): 162-9.
    • (2003) J Vasc Surg , vol.38 , Issue.1 , pp. 162-169
    • Woodside, K.J.1    Hu, M.2    Burke, A.3
  • 98
    • 78649629120 scopus 로고    scopus 로고
    • Inhibitory effect of TIMP influences the morphology of varicose veins
    • Aravind B, Saunders B, Navin T, et al. Inhibitory effect of TIMP influences the morphology of varicose veins. Eur J Vasc Endovasc Surg 2010; 40(6): 754-65.
    • (2010) Eur J Vasc Endovasc Surg , vol.40 , Issue.6 , pp. 754-765
    • Aravind, B.1    Saunders, B.2    Navin, T.3
  • 99
    • 0038516370 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and urokinase-type plasminogen activator in varicose veins
    • Kosugi I, Urayama H, Kasashima F, Ohtake H, Watanabe Y. Matrix metalloproteinase-9 and urokinase-type plasminogen activator in varicose veins. Ann Vasc Surg 2003; 17(3): 234-8.
    • (2003) Ann Vasc Surg , vol.17 , Issue.3 , pp. 234-238
    • Kosugi, I.1    Urayama, H.2    Kasashima, F.3    Ohtake, H.4    Watanabe, Y.5
  • 100
    • 4744355701 scopus 로고    scopus 로고
    • Immunocytochemical characterisation of the inflammatory cell infiltrate of varicose veins
    • Sayer GL, Smith PD. Immunocytochemical characterisation of the inflammatory cell infiltrate of varicose veins. Eur J Vasc Endovasc Surg 2004; 28(5): 479-83.
    • (2004) Eur J Vasc Endovasc Surg , vol.28 , Issue.5 , pp. 479-483
    • Sayer, G.L.1    Smith, P.D.2
  • 101
    • 0033813165 scopus 로고    scopus 로고
    • Expression of adhesion molecules and cytokines on saphenous veins in chronic venous insufficiency
    • Takase S, Bergan JJ, Schmid-Schonbein G. Expression of adhesion molecules and cytokines on saphenous veins in chronic venous insufficiency. Ann Vasc Surg 2000; 14(5): 427-35.
    • (2000) Ann Vasc Surg , vol.14 , Issue.5 , pp. 427-435
    • Takase, S.1    Bergan, J.J.2    Schmid-Schonbein, G.3
  • 102
    • 33845339277 scopus 로고    scopus 로고
    • Outcome of ultrasoundguided sclerotherapy for varicose veins: Medium-term results assessed by ultrasound surveillance
    • Myers KA, Jolley D, Clough A, Kirwan J. Outcome of ultrasoundguided sclerotherapy for varicose veins: medium-term results assessed by ultrasound surveillance. Eur J Vasc Endovasc Surg 2007; 33(1): 116-21.
    • (2007) Eur J Vasc Endovasc Surg , vol.33 , Issue.1 , pp. 116-121
    • Myers, K.A.1    Jolley, D.2    Clough, A.3    Kirwan, J.4
  • 104
    • 84876715147 scopus 로고    scopus 로고
    • Assessment of the Infiltration of Inflammatory Cells in the Walls of Thrombotic Varicose Veins
    • Chu HB, Yan F, Zhao JH, Xu YB, Wang T, Guo WJ. Assessment of the Infiltration of Inflammatory Cells in the Walls of Thrombotic Varicose Veins. Angiology 2012.
    • (2012) Angiology
    • Chu, H.B.1    Yan, F.2    Zhao, J.H.3    Xu, Y.B.4    Wang, T.5    Guo, W.J.6
  • 105
    • 0031737360 scopus 로고    scopus 로고
    • Lipodermatosclerosis is characterized by elevated expression and activation of matrix metalloproteinases: Implications for venous ulcer formation
    • Herouy Y, May AE, Pornschlegel G, et al. Lipodermatosclerosis is characterized by elevated expression and activation of matrix metalloproteinases: implications for venous ulcer formation. J Invest Dermatol 1998; 111(5): 822-7.
    • (1998) J Invest Dermatol , vol.111 , Issue.5 , pp. 822-827
    • Herouy, Y.1    May, A.E.2    Pornschlegel, G.3
  • 106
    • 0032854998 scopus 로고    scopus 로고
    • The proliferative capacity of neonatal skin fibroblasts is reduced after exposure to venous ulcer wound fluid: A potential mechanism for senescence in venous ulcers
    • Mendez MV, Raffetto JD, Phillips T, Menzoian JO, Park HY. The proliferative capacity of neonatal skin fibroblasts is reduced after exposure to venous ulcer wound fluid: A potential mechanism for senescence in venous ulcers. J Vasc Surg 1999; 30(4): 734-43.
    • (1999) J Vasc Surg , vol.30 , Issue.4 , pp. 734-743
    • Mendez, M.V.1    Raffetto, J.D.2    Phillips, T.3    Menzoian, J.O.4    Park, H.Y.5
  • 107
    • 0035378382 scopus 로고    scopus 로고
    • Changes in cellular motility and cytoskeletal actin in fibroblasts from patients with chronic venous insufficiency and in neonatal fibroblasts in the presence of chronic wound fluid
    • Raffetto JD, Mendez MV, Marien BJ, et al. Changes in cellular motility and cytoskeletal actin in fibroblasts from patients with chronic venous insufficiency and in neonatal fibroblasts in the presence of chronic wound fluid. J Vasc Surg 2001; 33(6): 1233-41.
    • (2001) J Vasc Surg , vol.33 , Issue.6 , pp. 1233-1241
    • Raffetto, J.D.1    Mendez, M.V.2    Marien, B.J.3
  • 108
    • 0028786034 scopus 로고
    • Cytokine and protease levels in healing and non-healing chronic venous leg ulcers
    • Harris IR, Yee KC, Walters CE, et al. Cytokine and protease levels in healing and non-healing chronic venous leg ulcers. Exp Dermatol 1995; 4(6): 342-9.
    • (1995) Exp Dermatol , vol.4 , Issue.6 , pp. 342-349
    • Harris, I.R.1    Yee, K.C.2    Walters, C.E.3
  • 109
    • 0034108658 scopus 로고    scopus 로고
    • Level of fibronectin mRNA is markedly increased in human chronic wounds
    • Ongenae KC, Phillips TJ, Park HY. Level of fibronectin mRNA is markedly increased in human chronic wounds. Dermatol Surg 2000; 26(5): 447-51.
    • (2000) Dermatol Surg , vol.26 , Issue.5 , pp. 447-451
    • Ongenae, K.C.1    Phillips, T.J.2    Park, H.Y.3
  • 110
    • 0027202705 scopus 로고
    • Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9
    • Wysocki AB, Staiano-Coico L, Grinnell F. Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9. J Invest Dermatol 1993; 101(1): 64-8.
    • (1993) J Invest Dermatol , vol.101 , Issue.1 , pp. 64-68
    • Wysocki, A.B.1    Staiano-Coico, L.2    Grinnell, F.3
  • 111
    • 0029972104 scopus 로고    scopus 로고
    • Matrix metalloproteinases, gelatinase and collagenase, in chronic leg ulcers
    • Weckroth M, Vaheri A, Lauharanta J, Sorsa T, Konttinen YT. Matrix metalloproteinases, gelatinase and collagenase, in chronic leg ulcers. J Invest Dermatol 1996; 106(5): 1119-24.
    • (1996) J Invest Dermatol , vol.106 , Issue.5 , pp. 1119-1124
    • Weckroth, M.1    Vaheri, A.2    Lauharanta, J.3    Sorsa, T.4    Konttinen, Y.T.5
  • 112
    • 0030740249 scopus 로고    scopus 로고
    • Distinct populations of stromal cells express collagenase-3 (MMP-13) and collagenase-1 (MMP-1) in chronic ulcers but not in normally healing wounds
    • Vaalamo M, Mattila L, Johansson N, et al. Distinct populations of stromal cells express collagenase-3 (MMP-13) and collagenase-1 (MMP-1) in chronic ulcers but not in normally healing wounds. J Invest Dermatol 1997; 109(1): 96-101.
    • (1997) J Invest Dermatol , vol.109 , Issue.1 , pp. 96-101
    • Vaalamo, M.1    Mattila, L.2    Johansson, N.3
  • 113
    • 0035126373 scopus 로고    scopus 로고
    • Inflammation in stasis dermatitis upregulates MMP-1, MMP-2 and MMP-13 expression
    • Herouy Y, Mellios P, Bandemir E, et al. Inflammation in stasis dermatitis upregulates MMP-1, MMP-2 and MMP-13 expression. J Dermatol Sci 2001; 25(3): 198-205.
    • (2001) J Dermatol Sci , vol.25 , Issue.3 , pp. 198-205
    • Herouy, Y.1    Mellios, P.2    Bandemir, E.3
  • 114
    • 23044499048 scopus 로고    scopus 로고
    • Effect of chronic wound exudates and MMP-2/-9 inhibitor on angiogenesis in vitro
    • Ulrich D, Lichtenegger F, Unglaub F, Smeets R, Pallua N. Effect of chronic wound exudates and MMP-2/-9 inhibitor on angiogenesis in vitro. Plast Reconstr Surg 2005; 116(2): 539-45.
    • (2005) Plast Reconstr Surg , vol.116 , Issue.2 , pp. 539-545
    • Ulrich, D.1    Lichtenegger, F.2    Unglaub, F.3    Smeets, R.4    Pallua, N.5
  • 115
    • 0035511667 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases 1, 2, and 9 and tissue inhibitor of matrix metalloproteinase-1 in chronic venous insufficiency
    • Saito S, Trovato MJ, You R, et al. Role of matrix metalloproteinases 1, 2, and 9 and tissue inhibitor of matrix metalloproteinase-1 in chronic venous insufficiency. J Vasc Surg 2001; 34(5): 930-8.
    • (2001) J Vasc Surg , vol.34 , Issue.5 , pp. 930-938
    • Saito, S.1    Trovato, M.J.2    You, R.3
  • 116
    • 32044450322 scopus 로고    scopus 로고
    • Mitogenactivated protein kinase pathway regulates cell proliferation in venous ulcer fibroblasts
    • Raffetto JD, Vasquez R, Goodwin DG, Menzoian JO. Mitogenactivated protein kinase pathway regulates cell proliferation in venous ulcer fibroblasts. Vasc Endovascular Surg 2006; 40(1): 59-66.
    • (2006) Vasc Endovascular Surg , vol.40 , Issue.1 , pp. 59-66
    • Raffetto, J.D.1    Vasquez, R.2    Goodwin, D.G.3    Menzoian, J.O.4
  • 117
    • 12944249328 scopus 로고    scopus 로고
    • Chronic wound fluid suppresses proliferation of dermal fibroblasts through a Ras-mediated signaling pathway
    • Seah CC, Phillips TJ, Howard CE, et al. Chronic wound fluid suppresses proliferation of dermal fibroblasts through a Ras-mediated signaling pathway. J Invest Dermatol 2005; 124(2): 466-74.
    • (2005) J Invest Dermatol , vol.124 , Issue.2 , pp. 466-474
    • Seah, C.C.1    Phillips, T.J.2    Howard, C.E.3
  • 118
    • 0242406750 scopus 로고    scopus 로고
    • Matrix metalloproteinase-19 expression in dermal wounds and by fibroblasts in culture
    • Hieta N, Impola U, Lopez-Otin C, Saarialho-Kere U, Kahari VM. Matrix metalloproteinase-19 expression in dermal wounds and by fibroblasts in culture. J Invest Dermatol 2003; 121(5): 997-1004.
    • (2003) J Invest Dermatol , vol.121 , Issue.5 , pp. 997-1004
    • Hieta, N.1    Impola, U.2    Lopez-Otin, C.3    Saarialho-Kere, U.4    Kahari, V.M.5
  • 119
    • 0036885949 scopus 로고    scopus 로고
    • Elevated expression of extracellular matrix metalloproteinase inducer (CD147) and membrane-type matrix metalloproteinases in venous leg ulcers
    • Norgauer J, Hildenbrand T, Idzko M, et al. Elevated expression of extracellular matrix metalloproteinase inducer (CD147) and membrane-type matrix metalloproteinases in venous leg ulcers. Br J Dermatol 2002; 147(6): 1180-6.
    • (2002) Br J Dermatol , vol.147 , Issue.6 , pp. 1180-1186
    • Norgauer, J.1    Hildenbrand, T.2    Idzko, M.3
  • 120
    • 33144490286 scopus 로고    scopus 로고
    • The impact of differential expression of extracellular matrix metalloproteinase inducer, matrix metalloproteinase-2, tissue inhibitor of matrix metalloproteinase-2 and PDGF-AA on the chronicity of venous leg ulcers
    • Mwaura B, Mahendran B, Hynes N, et al. The impact of differential expression of extracellular matrix metalloproteinase inducer, matrix metalloproteinase-2, tissue inhibitor of matrix metalloproteinase-2 and PDGF-AA on the chronicity of venous leg ulcers. Eur J Vasc Endovasc Surg 2006; 31(3): 306-10.
    • (2006) Eur J Vasc Endovasc Surg , vol.31 , Issue.3 , pp. 306-310
    • Mwaura, B.1    Mahendran, B.2    Hynes, N.3
  • 121
    • 51349090066 scopus 로고    scopus 로고
    • Multiplexed analysis of matrix metalloproteinases in leg ulcer tissue of patients with chronic venous insufficiency before and after compression therapy
    • Beidler SK, Douillet CD, Berndt DF, Keagy BA, Rich PB, Marston WA. Multiplexed analysis of matrix metalloproteinases in leg ulcer tissue of patients with chronic venous insufficiency before and after compression therapy. Wound Repair Regen 2008; 16(5): 642-8.
    • (2008) Wound Repair Regen , vol.16 , Issue.5 , pp. 642-648
    • Beidler, S.K.1    Douillet, C.D.2    Berndt, D.F.3    Keagy, B.A.4    Rich, P.B.5    Marston, W.A.6
  • 122
    • 0032800451 scopus 로고    scopus 로고
    • Differential expression of tissue inhibitors of metalloproteinases (TIMP-1,-2,-3, and-4) in normal and aberrant wound healing
    • Vaalamo M, Leivo T, Saarialho-Kere U. Differential expression of tissue inhibitors of metalloproteinases (TIMP-1,-2,-3, and-4) in normal and aberrant wound healing. Hum Pathol 1999; 30(7): 795-802.
    • (1999) Hum Pathol , vol.30 , Issue.7 , pp. 795-802
    • Vaalamo, M.1    Leivo, T.2    Saarialho-Kere, U.3
  • 123
    • 0036672752 scopus 로고    scopus 로고
    • Nomenclature of the veins of the lower limbs: An international interdisciplinary consensus statement
    • Caggiati A, Bergan JJ, Gloviczki P, Jantet G, Wendell-Smith CP, Partsch H. Nomenclature of the veins of the lower limbs: an international interdisciplinary consensus statement. J Vasc Surg 2002; 36(2): 416-22.
    • (2002) J Vasc Surg , vol.36 , Issue.2 , pp. 416-422
    • Caggiati, A.1    Bergan, J.J.2    Gloviczki, P.3    Jantet, G.4    Wendell-Smith, C.P.5    Partsch, H.6
  • 124
    • 78651025601 scopus 로고
    • Venous pressure in the saphenous vein at the ankle in man during exercise and changes in posture
    • Pollack AA, Wood EH. Venous pressure in the saphenous vein at the ankle in man during exercise and changes in posture. J Appl Physiol 1949; 1(9): 649-62.
    • (1949) J Appl Physiol , vol.1 , Issue.9 , pp. 649-662
    • Pollack, A.A.1    Wood, E.H.2
  • 125
    • 33750029602 scopus 로고    scopus 로고
    • Conception of the venous hemodynamics in the lower extremity
    • Recek C. Conception of the venous hemodynamics in the lower extremity. Angiology 2006; 57(5): 556-63.
    • (2006) Angiology , vol.57 , Issue.5 , pp. 556-563
    • Recek, C.1
  • 126
    • 0037199422 scopus 로고    scopus 로고
    • Plasma matrix metalloproteinase-9 as a marker of blood stasis in varicose veins
    • Jacob MP, Cazaubon M, Scemama A, et al. Plasma matrix metalloproteinase-9 as a marker of blood stasis in varicose veins. Circulation 2002; 106(5): 535-8.
    • (2002) Circulation , vol.106 , Issue.5 , pp. 535-538
    • Jacob, M.P.1    Cazaubon, M.2    Scemama, A.3
  • 127
    • 79951851894 scopus 로고    scopus 로고
    • Prolonged mechanical stretch is associated with upregulation of hypoxia-inducible factors and reduced contraction in rat inferior vena cava
    • Lim CS, Qiao X, Reslan OM, et al. Prolonged mechanical stretch is associated with upregulation of hypoxia-inducible factors and reduced contraction in rat inferior vena cava. J Vasc Surg 2011; 53(3): 764-73.
    • (2011) J Vasc Surg , vol.53 , Issue.3 , pp. 764-773
    • Lim, C.S.1    Qiao, X.2    Reslan, O.M.3
  • 128
    • 25444496750 scopus 로고    scopus 로고
    • Venous hypertension and the inflammatory cascade: Major manifestations and trigger mechanisms
    • Pascarella L, Penn A, Schmid-Schonbein GW. Venous hypertension and the inflammatory cascade: major manifestations and trigger mechanisms. Angiology 2005; 56 Suppl 1: S3-10.
    • (2005) Angiology , vol.56 , Issue.SUPPL. 1 , pp. 3-10
    • Pascarella, L.1    Penn, A.2    Schmid-Schonbein, G.W.3
  • 130
    • 14844303781 scopus 로고    scopus 로고
    • An animal model of venous hypertension: The role of inflammation in venous valve failure
    • Pascarella L, Schmid-Schonbein GW, Bergan J. An animal model of venous hypertension: the role of inflammation in venous valve failure. J Vasc Surg 2005; 41(2): 303-11.
    • (2005) J Vasc Surg , vol.41 , Issue.2 , pp. 303-311
    • Pascarella, L.1    Schmid-Schonbein, G.W.2    Bergan, J.3
  • 131
    • 85047682984 scopus 로고    scopus 로고
    • Regulation of oxygen homeostasis by hypoxiainducible factor 1
    • Semenza GL. Regulation of oxygen homeostasis by hypoxiainducible factor 1. Physiology (Bethesda) 2009; 24: 97-106.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 97-106
    • Semenza, G.L.1
  • 132
    • 84860357030 scopus 로고    scopus 로고
    • Increased activation of the hypoxia-inducible factor pathway in varicose veins
    • Lim CS, Kiriakidis S, Paleolog EM, Davies AH. Increased activation of the hypoxia-inducible factor pathway in varicose veins. J Vasc Surg 2012; 55(5): 1427-39.
    • (2012) J Vasc Surg , vol.55 , Issue.5 , pp. 1427-1439
    • Lim, C.S.1    Kiriakidis, S.2    Paleolog, E.M.3    Davies, A.H.4
  • 134
    • 0013199207 scopus 로고    scopus 로고
    • Early expression of myocardial HIF-1alpha in response to mechanical stresses: Regulation by stretch-activated channels and the phosphatidylinositol 3-kinase signaling pathway
    • Kim CH, Cho YS, Chun YS, Park JW, Kim MS. Early expression of myocardial HIF-1alpha in response to mechanical stresses: regulation by stretch-activated channels and the phosphatidylinositol 3-kinase signaling pathway. Circ Res 2002; 90(2): E25-33.
    • (2002) Circ Res , vol.90 , Issue.2
    • Kim, C.H.1    Cho, Y.S.2    Chun, Y.S.3    Park, J.W.4    Kim, M.S.5
  • 135
    • 2942587279 scopus 로고    scopus 로고
    • Cyclic strain influences the expression of the vascular endothelial growth factor (VEGF) and the hypoxia inducible factor 1 alpha (HIF-1alpha) in tendon fibroblasts
    • Petersen W, Varoga D, Zantop T, Hassenpflug J, Mentlein R, Pufe T. Cyclic strain influences the expression of the vascular endothelial growth factor (VEGF) and the hypoxia inducible factor 1 alpha (HIF-1alpha) in tendon fibroblasts. J Orthop Res 2004; 22(4): 847-53.
    • (2004) J Orthop Res , vol.22 , Issue.4 , pp. 847-853
    • Petersen, W.1    Varoga, D.2    Zantop, T.3    Hassenpflug, J.4    Mentlein, R.5    Pufe, T.6
  • 136
    • 0141888524 scopus 로고    scopus 로고
    • Regulation of hypoxiainducible factor-1alpha by cyclical mechanical stretch in rat vascular smooth muscle cells
    • Chang H, Shyu KG, Wang BW, Kuan P. Regulation of hypoxiainducible factor-1alpha by cyclical mechanical stretch in rat vascular smooth muscle cells. Clin Sci (Lond) 2003; 105(4): 447-56.
    • (2003) Clin Sci (Lond) , vol.105 , Issue.4 , pp. 447-456
    • Chang, H.1    Shyu, K.G.2    Wang, B.W.3    Kuan, P.4
  • 137
    • 34548364176 scopus 로고    scopus 로고
    • HIF-1alpha and HIF-2alpha play a central role in stretchinduced but not shear-stress-induced angiogenesis in rat skeletal muscle
    • Milkiewicz M, Doyle JL, Fudalewski T, Ispanovic E, Aghasi M, Haas TL. HIF-1alpha and HIF-2alpha play a central role in stretchinduced but not shear-stress-induced angiogenesis in rat skeletal muscle. J Physiol 2007; 583(Pt 2): 753-66.
    • (2007) J Physiol , vol.583 , Issue.PART 2 , pp. 753-766
    • Milkiewicz, M.1    Doyle, J.L.2    Fudalewski, T.3    Ispanovic, E.4    Aghasi, M.5    Haas, T.L.6
  • 138
    • 33751169387 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 (HIF-1)
    • Ke Q, Costa M. Hypoxia-inducible factor-1 (HIF-1). Mol Pharmacol 2006; 70(5): 1469-80.
    • (2006) Mol Pharmacol , vol.70 , Issue.5 , pp. 1469-1480
    • Ke, Q.1    Costa, M.2
  • 139
    • 34247847903 scopus 로고    scopus 로고
    • Silencing hypoxiainducible factor-1alpha inhibits cell migration and invasion under hypoxic environment in malignant gliomas
    • Fujiwara S, Nakagawa K, Harada H, et al. Silencing hypoxiainducible factor-1alpha inhibits cell migration and invasion under hypoxic environment in malignant gliomas. Int J Oncol 2007; 30(4): 793-802.
    • (2007) Int J Oncol , vol.30 , Issue.4 , pp. 793-802
    • Fujiwara, S.1    Nakagawa, K.2    Harada, H.3
  • 140
    • 38349170116 scopus 로고    scopus 로고
    • Expression of hypoxia inducible factor-1 alpha, macrophage migration inhibition factor, matrix metalloproteinase-2 and-9, and their inhibitors in hemodialysis grafts and arteriovenous fistulas
    • Misra S, Fu AA, Rajan DK, et al. Expression of hypoxia inducible factor-1 alpha, macrophage migration inhibition factor, matrix metalloproteinase-2 and-9, and their inhibitors in hemodialysis grafts and arteriovenous fistulas. J Vasc Interv Radiol 2008; 19(2 Pt 1): 252-9.
    • (2008) J Vasc Interv Radiol , vol.19 , Issue.2 PART 1 , pp. 252-259
    • Misra, S.1    Fu, A.A.2    Rajan, D.K.3
  • 141
    • 33847357357 scopus 로고    scopus 로고
    • Molecular basis of the effects of mechanical stretch on vascular smooth muscle cells
    • Haga JH, Li YS, Chien S. Molecular basis of the effects of mechanical stretch on vascular smooth muscle cells. J Biomech 2007; 40(5): 947-60.
    • (2007) J Biomech , vol.40 , Issue.5 , pp. 947-960
    • Haga, J.H.1    Li, Y.S.2    Chien, S.3
  • 142
    • 66149088448 scopus 로고    scopus 로고
    • TRPV4 channels mediate cyclic strain-induced endothelial cell reorientation through integrinto-integrin signaling
    • Thodeti CK, Matthews B, Ravi A, et al. TRPV4 channels mediate cyclic strain-induced endothelial cell reorientation through integrinto-integrin signaling. Circ Res 2009; 104(9): 1123-30.
    • (2009) Circ Res , vol.104 , Issue.9 , pp. 1123-1130
    • Thodeti, C.K.1    Matthews, B.2    Ravi, A.3
  • 143
    • 0033612572 scopus 로고    scopus 로고
    • Integrinmediated activation of focal adhesion kinase is required for signaling to Jun NH2-terminal kinase and progression through the G1 phase of the cell cycle
    • Oktay M, Wary KK, Dans M, Birge RB, Giancotti FG. Integrinmediated activation of focal adhesion kinase is required for signaling to Jun NH2-terminal kinase and progression through the G1 phase of the cell cycle. J Cell Biol 1999; 145(7): 1461-9.
    • (1999) J Cell Biol , vol.145 , Issue.7 , pp. 1461-1469
    • Oktay, M.1    Wary, K.K.2    Dans, M.3    Birge, R.B.4    Giancotti, F.G.5
  • 144
    • 0033824335 scopus 로고    scopus 로고
    • Mechanical stress-initiated signal transductions in vascular smooth muscle cells
    • Li C, Xu Q. Mechanical stress-initiated signal transductions in vascular smooth muscle cells. Cell Signal 2000; 12(7): 435-45.
    • (2000) Cell Signal , vol.12 , Issue.7 , pp. 435-445
    • Li, C.1    Xu, Q.2
  • 145
    • 0030726328 scopus 로고    scopus 로고
    • Pulsatile stretch stimulates superoxide production and activates nuclear factorkappa B in human coronary smooth muscle
    • Hishikawa K, Oemar BS, Yang Z, Luscher TF. Pulsatile stretch stimulates superoxide production and activates nuclear factorkappa B in human coronary smooth muscle. Circ Res 1997; 81(5): 797-803.
    • (1997) Circ Res , vol.81 , Issue.5 , pp. 797-803
    • Hishikawa, K.1    Oemar, B.S.2    Yang, Z.3    Luscher, T.F.4
  • 146
    • 0041915623 scopus 로고    scopus 로고
    • High pressure induces superoxide production in isolated arteries via protein kinase C-dependent activation of NAD(P)H oxidase
    • Ungvari Z, Csiszar A, Huang A, Kaminski PM, Wolin MS, Koller A. High pressure induces superoxide production in isolated arteries via protein kinase C-dependent activation of NAD(P)H oxidase. Circulation 2003; 108(10): 1253-8.
    • (2003) Circulation , vol.108 , Issue.10 , pp. 1253-1258
    • Ungvari, Z.1    Csiszar, A.2    Huang, A.3    Kaminski, P.M.4    Wolin, M.S.5    Koller, A.6
  • 147
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • Bode W, Gomis-Ruth FX, Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett 1993; 331(1-2): 134-40.
    • (1993) FEBS Lett , vol.331 , Issue.1-2 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stockler, W.3
  • 148
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart HE, Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A 1990; 87(14): 5578-82.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.14 , pp. 5578-5582
    • van Wart, H.E.1    Birkedal-Hansen, H.2
  • 149
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • Browner MF, Smith WW, Castelhano AL. Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry 1995; 34(20): 6602-10.
    • (1995) Biochemistry , vol.34 , Issue.20 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 150
    • 0017395121 scopus 로고
    • Crystallographic study of the binding of dipeptide inhibitors to thermolysin: Implications for the mechanism of catalysis
    • Kester WR, Matthews BW. Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysis. Biochemistry 1977; 16(11): 2506-16.
    • (1977) Biochemistry , vol.16 , Issue.11 , pp. 2506-2516
    • Kester, W.R.1    Matthews, B.W.2
  • 151
    • 0346888553 scopus 로고    scopus 로고
    • Modeling of enzyme-substrate complexes for the metalloproteases MMP-3, ADAM-9 and ADAM-10
    • Manzetti S, McCulloch DR, Herington AC, van der Spoel D. Modeling of enzyme-substrate complexes for the metalloproteases MMP-3, ADAM-9 and ADAM-10. J Comput Aided Mol Des 2003; 17(9): 551-65.
    • (2003) J Comput Aided Mol Des , vol.17 , Issue.9 , pp. 551-565
    • Manzetti, S.1    McCulloch, D.R.2    Herington, A.C.3    van der Spoel, D.4
  • 152
    • 0035030734 scopus 로고    scopus 로고
    • The design, structure, and therapeutic application of matrix metalloproteinase inhibitors
    • Skiles JW, Gonnella NC, Jeng AY. The design, structure, and therapeutic application of matrix metalloproteinase inhibitors. Curr Med Chem 2001; 8(4): 425-74.
    • (2001) Curr Med Chem , vol.8 , Issue.4 , pp. 425-474
    • Skiles, J.W.1    Gonnella, N.C.2    Jeng, A.Y.3
  • 153
    • 0028128235 scopus 로고
    • Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself
    • Lovejoy B, Hassell AM, Luther MA, Weigl D, Jordan SR. Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself. Biochemistry 1994; 33(27): 8207-17.
    • (1994) Biochemistry , vol.33 , Issue.27 , pp. 8207-8217
    • Lovejoy, B.1    Hassell, A.M.2    Luther, M.A.3    Weigl, D.4    Jordan, S.R.5
  • 154
    • 13444273084 scopus 로고    scopus 로고
    • CD44 binding through the hemopexin-like domain is critical for its shedding by membranetype 1 matrix metalloproteinase
    • Suenaga N, Mori H, Itoh Y, Seiki M. CD44 binding through the hemopexin-like domain is critical for its shedding by membranetype 1 matrix metalloproteinase. Oncogene 2005; 24(5): 859-68.
    • (2005) Oncogene , vol.24 , Issue.5 , pp. 859-868
    • Suenaga, N.1    Mori, H.2    Itoh, Y.3    Seiki, M.4
  • 155
    • 0025026410 scopus 로고
    • Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin)
    • Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H. Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry 1990; 29(44): 10261-70.
    • (1990) Biochemistry , vol.29 , Issue.44 , pp. 10261-10270
    • Suzuki, K.1    Enghild, J.J.2    Morodomi, T.3    Salvesen, G.4    Nagase, H.5
  • 157
    • 0031985228 scopus 로고    scopus 로고
    • The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study
    • Butler GS, Butler MJ, Atkinson SJ, et al. The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study. J Biol Chem 1998; 273(2): 871-80.
    • (1998) J Biol Chem , vol.273 , Issue.2 , pp. 871-880
    • Butler, G.S.1    Butler, M.J.2    Atkinson, S.J.3
  • 158
    • 0034714202 scopus 로고    scopus 로고
    • TIMP-2 is required for efficient activation of proMMP-2 in vivo
    • Wang Z, Juttermann R, Soloway PD. TIMP-2 is required for efficient activation of proMMP-2 in vivo. J Biol Chem 2000; 275(34): 26411-5.
    • (2000) J Biol Chem , vol.275 , Issue.34 , pp. 26411-26415
    • Wang, Z.1    Juttermann, R.2    Soloway, P.D.3
  • 159
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh Y, Takamura A, Ito N, et al. Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J 2001; 20(17): 4782-93.
    • (2001) EMBO J , vol.20 , Issue.17 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3
  • 160
    • 34147135025 scopus 로고    scopus 로고
    • Substrate choice of membrane-type 1 matrix metalloproteinase is dictated by tissue inhibitor of metalloproteinase-2 levels
    • Kudo T, Takino T, Miyamori H, Thompson EW, Sato H. Substrate choice of membrane-type 1 matrix metalloproteinase is dictated by tissue inhibitor of metalloproteinase-2 levels. Cancer Sci 2007; 98(4): 563-8.
    • (2007) Cancer Sci , vol.98 , Issue.4 , pp. 563-568
    • Kudo, T.1    Takino, T.2    Miyamori, H.3    Thompson, E.W.4    Sato, H.5
  • 161
    • 0025522624 scopus 로고
    • Furin is a subtilisinlike proprotein processing enzyme in higher eukaryotes
    • van de Ven WJ, Voorberg J, Fontijn R, et al. Furin is a subtilisinlike proprotein processing enzyme in higher eukaryotes. Mol Biol Rep 1990; 14(4): 265-75.
    • (1990) Mol Biol Rep , vol.14 , Issue.4 , pp. 265-275
    • van de Ven, W.J.1    Voorberg, J.2    Fontijn, R.3
  • 162
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu X, Kassim SY, Parks WC, Heinecke JW. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J Biol Chem 2001; 276(44): 41279-87.
    • (2001) J Biol Chem , vol.276 , Issue.44 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 163
    • 1342346608 scopus 로고    scopus 로고
    • Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: Specific structural motifs control protein oxidation
    • Fu X, Kao JL, Bergt C, et al. Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: specific structural motifs control protein oxidation. J Biol Chem 2004; 279(8): 6209-12.
    • (2004) J Biol Chem , vol.279 , Issue.8 , pp. 6209-6212
    • Fu, X.1    Kao, J.L.2    Bergt, C.3
  • 164
    • 0031570730 scopus 로고    scopus 로고
    • Activation of human neutrophil procollagenase by nitrogen dioxide and peroxynitrite: A novel mechanism for procollagenase activation involving nitric oxide
    • Okamoto T, Akaike T, Nagano T, et al. Activation of human neutrophil procollagenase by nitrogen dioxide and peroxynitrite: a novel mechanism for procollagenase activation involving nitric oxide. Arch Biochem Biophys 1997; 342(2): 261-74.
    • (1997) Arch Biochem Biophys , vol.342 , Issue.2 , pp. 261-274
    • Okamoto, T.1    Akaike, T.2    Nagano, T.3
  • 165
    • 0037119624 scopus 로고    scopus 로고
    • S-nitrosylation of matrix metalloproteinases: Signaling pathway to neuronal cell death
    • Gu Z, Kaul M, Yan B, et al. S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death. Science 2002; 297(5584): 1186-90.
    • (2002) Science , vol.297 , Issue.5584 , pp. 1186-1190
    • Gu, Z.1    Kaul, M.2    Yan, B.3
  • 166
    • 45649083624 scopus 로고    scopus 로고
    • Intrauterine hypoxia upregulates proinflammatory cytokines and matrix metalloproteinases in fetal guinea pig hearts
    • Oh C, Dong Y, Liu H, Thompson LP. Intrauterine hypoxia upregulates proinflammatory cytokines and matrix metalloproteinases in fetal guinea pig hearts. Am J Obstet Gynecol 2008; 199(1): 78 e1-6.
    • (2008) Am J Obstet Gynecol , vol.199 , Issue.1
    • Oh, C.1    Dong, Y.2    Liu, H.3    Thompson, L.P.4
  • 167
    • 0026660964 scopus 로고
    • Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9
    • Ogata Y, Enghild JJ, Nagase H. Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J Biol Chem 1992; 267(6): 3581-4.
    • (1992) J Biol Chem , vol.267 , Issue.6 , pp. 3581-3584
    • Ogata, Y.1    Enghild, J.J.2    Nagase, H.3
  • 168
    • 31344469271 scopus 로고    scopus 로고
    • Atherosclerosis and proteinase activation
    • Dollery CM, Libby P. Atherosclerosis and proteinase activation. Cardiovasc Res 2006; 69(3): 625-35.
    • (2006) Cardiovasc Res , vol.69 , Issue.3 , pp. 625-635
    • Dollery, C.M.1    Libby, P.2
  • 169
    • 0034257889 scopus 로고    scopus 로고
    • The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo
    • Liu Z, Zhou X, Shapiro SD, et al. The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo. Cell 2000; 102(5): 647-55.
    • (2000) Cell , vol.102 , Issue.5 , pp. 647-655
    • Liu, Z.1    Zhou, X.2    Shapiro, S.D.3
  • 170
    • 0026705310 scopus 로고
    • Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases
    • Desrochers PE, Mookhtiar K, Van Wart HE, Hasty KA, Weiss SJ. Proteolytic inactivation of alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin by oxidatively activated human neutrophil metalloproteinases. J Biol Chem 1992; 267(7): 5005-12.
    • (1992) J Biol Chem , vol.267 , Issue.7 , pp. 5005-5012
    • Desrochers, P.E.1    Mookhtiar, K.2    van Wart, H.E.3    Hasty, K.A.4    Weiss, S.J.5
  • 171
    • 0027492897 scopus 로고
    • Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3 (stromelysin 1)
    • Chen LC, Noelken ME, Nagase H. Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3 (stromelysin 1). Biochemistry 1993; 32(39): 10289-95.
    • (1993) Biochemistry , vol.32 , Issue.39 , pp. 10289-10295
    • Chen, L.C.1    Noelken, M.E.2    Nagase, H.3
  • 173
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002; 2(3): 161-74.
    • (2002) Nat Rev Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 174
    • 0034297101 scopus 로고    scopus 로고
    • Matrix metalloproteinases in wound repair (review)
    • Ravanti L, Kahari VM. Matrix metalloproteinases in wound repair (review). Int J Mol Med 2000; 6(4): 391-407.
    • (2000) Int J Mol Med , vol.6 , Issue.4 , pp. 391-407
    • Ravanti, L.1    Kahari, V.M.2
  • 175
    • 0033569682 scopus 로고    scopus 로고
    • Defensins and host defense
    • Ganz T. Defensins and host defense. Science 1999; 286(5439): 420-1.
    • (1999) Science , vol.286 , Issue.5439 , pp. 420-421
    • Ganz, T.1
  • 176
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson CL, Ouellette AJ, Satchell DP, et al. Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 1999; 286(5437): 113-7.
    • (1999) Science , vol.286 , Issue.5437 , pp. 113-117
    • Wilson, C.L.1    Ouellette, A.J.2    Satchell, D.P.3
  • 177
    • 0036533267 scopus 로고    scopus 로고
    • Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin
    • Gearing AJ, Thorpe SJ, Miller K, et al. Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin. Immunol Lett 2002; 81(1): 41-8.
    • (2002) Immunol Lett , vol.81 , Issue.1 , pp. 41-48
    • Gearing, A.J.1    Thorpe, S.J.2    Miller, K.3
  • 178
    • 0032862491 scopus 로고    scopus 로고
    • Digestion of C1q collagen-like domain with MMPs-1,-2,-3, and-9 further defines the sequence involved in the stimulation of neutrophil superoxide production
    • Ruiz S, Henschen-Edman AH, Nagase H, Tenner AJ. Digestion of C1q collagen-like domain with MMPs-1,-2,-3, and-9 further defines the sequence involved in the stimulation of neutrophil superoxide production. J Leukoc Biol 1999; 66(3): 416-22.
    • (1999) J Leukoc Biol , vol.66 , Issue.3 , pp. 416-422
    • Ruiz, S.1    Henschen-Edman, A.H.2    Nagase, H.3    Tenner, A.J.4
  • 179
    • 0036498603 scopus 로고    scopus 로고
    • Cooperation of C1q receptors and integrins in C1q-mediated endothelial cell adhesion and spreading
    • Feng X, Tonnesen MG, Peerschke EI, Ghebrehiwet B. Cooperation of C1q receptors and integrins in C1q-mediated endothelial cell adhesion and spreading. J Immunol 2002; 168(5): 2441-8.
    • (2002) J Immunol , vol.168 , Issue.5 , pp. 2441-2448
    • Feng, X.1    Tonnesen, M.G.2    Peerschke, E.I.3    Ghebrehiwet, B.4
  • 180
    • 0037088631 scopus 로고    scopus 로고
    • The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR
    • Rozanov DV, Ghebrehiwet B, Postnova TI, Eichinger A, Deryugina EI, Strongin AY. The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR. J Biol Chem 2002; 277(11): 9318-25.
    • (2002) J Biol Chem , vol.277 , Issue.11 , pp. 9318-9325
    • Rozanov, D.V.1    Ghebrehiwet, B.2    Postnova, T.I.3    Eichinger, A.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 181
    • 33748189347 scopus 로고    scopus 로고
    • Cell-surface association between matrix metalloproteinases and integrins: Role of the complexes in leukocyte migration and cancer progression
    • Stefanidakis M, Koivunen E. Cell-surface association between matrix metalloproteinases and integrins: role of the complexes in leukocyte migration and cancer progression. Blood 2006; 108(5): 1441-50.
    • (2006) Blood , vol.108 , Issue.5 , pp. 1441-1450
    • Stefanidakis, M.1    Koivunen, E.2
  • 182
    • 71649085437 scopus 로고    scopus 로고
    • Matrix metalloproteinase and G protein coupled receptors: Coconspirators in the pathogenesis of autoimmune disease and cancer
    • Eck SM, Blackburn JS, Schmucker AC, Burrage PS, Brinckerhoff CE. Matrix metalloproteinase and G protein coupled receptors: coconspirators in the pathogenesis of autoimmune disease and cancer. J Autoimmun 2009; 33(3-4): 214-21.
    • (2009) J Autoimmun , vol.33 , Issue.3-4 , pp. 214-221
    • Eck, S.M.1    Blackburn, J.S.2    Schmucker, A.C.3    Burrage, P.S.4    Brinckerhoff, C.E.5
  • 183
    • 0028936798 scopus 로고
    • Proteinase expression in early mouse embryos is regulated by leukaemia inhibitory factor and epidermal growth factor
    • Harvey MB, Leco KJ, Arcellana-Panlilio MY, Zhang X, Edwards DR, Schultz GA. Proteinase expression in early mouse embryos is regulated by leukaemia inhibitory factor and epidermal growth factor. Development 1995; 121(4): 1005-14.
    • (1995) Development , vol.121 , Issue.4 , pp. 1005-1014
    • Harvey, M.B.1    Leco, K.J.2    Arcellana-Panlilio, M.Y.3    Zhang, X.4    Edwards, D.R.5    Schultz, G.A.6
  • 184
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Effectors of development and normal physiology
    • Vu TH, Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 2000; 14(17): 2123-33.
    • (2000) Genes Dev , vol.14 , Issue.17 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 185
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 2007; 8(3): 221-33.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.3 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 186
    • 0038575444 scopus 로고    scopus 로고
    • Functional structure and composition of the extracellular matrix
    • Bosman FT, Stamenkovic I. Functional structure and composition of the extracellular matrix. J Pathol 2003; 200(4): 423-8.
    • (2003) J Pathol , vol.200 , Issue.4 , pp. 423-428
    • Bosman, F.T.1    Stamenkovic, I.2
  • 187
    • 0026847984 scopus 로고
    • Regulation of cellular functions by extracellular matrix
    • Teti A. Regulation of cellular functions by extracellular matrix. J Am Soc Nephrol 1992; 2(10 Suppl): S83-7.
    • (1992) J Am Soc Nephrol , vol.2 , Issue.10 SUPPL.
    • Teti, A.1
  • 188
    • 0042347601 scopus 로고    scopus 로고
    • Extracellular matrix remodeling and matrix metalloproteinases in the vascular wall during aging and in pathological conditions
    • Jacob MP. Extracellular matrix remodeling and matrix metalloproteinases in the vascular wall during aging and in pathological conditions. Biomed Pharmacother 2003; 57(5-6): 195-202.
    • (2003) Biomed Pharmacother , vol.57 , Issue.5-6 , pp. 195-202
    • Jacob, M.P.1
  • 191
    • 0033048045 scopus 로고    scopus 로고
    • Crystal structures of MMP-1 and-13 reveal the structural basis for selectivity of collagenase inhibitors
    • Lovejoy B, Welch AR, Carr S, et al. Crystal structures of MMP-1 and-13 reveal the structural basis for selectivity of collagenase inhibitors. Nat Struct Biol 1999; 6(3): 217-21.
    • (1999) Nat Struct Biol , vol.6 , Issue.3 , pp. 217-221
    • Lovejoy, B.1    Welch, A.R.2    Carr, S.3
  • 192
    • 0032562786 scopus 로고    scopus 로고
    • High affinity binding of latent matrix metalloproteinase-9 to the alpha2(IV) chain of collagen IV
    • Olson MW, Toth M, Gervasi DC, Sado Y, Ninomiya Y, Fridman R. High affinity binding of latent matrix metalloproteinase-9 to the alpha2(IV) chain of collagen IV. J Biol Chem 1998; 273(17): 10672-81.
    • (1998) J Biol Chem , vol.273 , Issue.17 , pp. 10672-10681
    • Olson, M.W.1    Toth, M.2    Gervasi, D.C.3    Sado, Y.4    Ninomiya, Y.5    Fridman, R.6
  • 193
    • 0033135670 scopus 로고    scopus 로고
    • Production and inhibition of the gelatinolytic matrix metalloproteinases in a human model of vein graft stenosis
    • Porter KE, Thompson MM, Loftus IM, et al. Production and inhibition of the gelatinolytic matrix metalloproteinases in a human model of vein graft stenosis. Eur J Vasc Endovasc Surg 1999; 17(5): 404-12.
    • (1999) Eur J Vasc Endovasc Surg , vol.17 , Issue.5 , pp. 404-412
    • Porter, K.E.1    Thompson, M.M.2    Loftus, I.M.3
  • 195
    • 2442511808 scopus 로고    scopus 로고
    • Native matrix metalloproteinase characteristics may influence early stenosis of venous versus arterial coronary artery bypass grafting conduits
    • Anstadt MP, Franga DL, Portik-Dobos V, et al. Native matrix metalloproteinase characteristics may influence early stenosis of venous versus arterial coronary artery bypass grafting conduits. Chest 2004; 125(5): 1853-8.
    • (2004) Chest , vol.125 , Issue.5 , pp. 1853-1858
    • Anstadt, M.P.1    Franga, D.L.2    Portik-Dobos, V.3
  • 196
    • 0036177290 scopus 로고    scopus 로고
    • Histologic features of venous invasion, expression of vascular endothelial growth factor and matrix metalloproteinase-2 and matrix metalloproteinase-9, and the relation with liver metastasis in pancreatic cancer
    • Nagakawa Y, Aoki T, Kasuya K, Tsuchida A, Koyanagi Y. Histologic features of venous invasion, expression of vascular endothelial growth factor and matrix metalloproteinase-2 and matrix metalloproteinase-9, and the relation with liver metastasis in pancreatic cancer. Pancreas 2002; 24(2): 169-78.
    • (2002) Pancreas , vol.24 , Issue.2 , pp. 169-178
    • Nagakawa, Y.1    Aoki, T.2    Kasuya, K.3    Tsuchida, A.4    Koyanagi, Y.5
  • 197
    • 0037162375 scopus 로고    scopus 로고
    • Synthesis of collagen is dysregulated in cultured fibroblasts derived from skin of subjects with varicose veins as it is in venous smooth muscle cells
    • Sansilvestri-Morel P, Rupin A, Jaisson S, Fabiani JN, Verbeuren TJ, Vanhoutte PM. Synthesis of collagen is dysregulated in cultured fibroblasts derived from skin of subjects with varicose veins as it is in venous smooth muscle cells. Circulation 2002; 106(4): 479-83.
    • (2002) Circulation , vol.106 , Issue.4 , pp. 479-483
    • Sansilvestri-Morel, P.1    Rupin, A.2    Jaisson, S.3    Fabiani, J.N.4    Verbeuren, T.J.5    Vanhoutte, P.M.6
  • 198
  • 199
    • 0030060046 scopus 로고    scopus 로고
    • Biochemical assay of collagen and elastin in the normal and varicose vein wall
    • Venturi M, Bonavina L, Annoni F, et al. Biochemical assay of collagen and elastin in the normal and varicose vein wall. J Surg Res 1996; 60(1): 245-8.
    • (1996) J Surg Res , vol.60 , Issue.1 , pp. 245-248
    • Venturi, M.1    Bonavina, L.2    Annoni, F.3
  • 200
    • 0033257006 scopus 로고    scopus 로고
    • The determination of the collagen and elastin amount in the human varicose vein by the computer morphometric method
    • Haviarova Z, Weismann P, Stvrtinova V, Benuska J. The determination of the collagen and elastin amount in the human varicose vein by the computer morphometric method. Gen Physiol Biophys 1999; 18 Suppl 1: 30-3.
    • (1999) Gen Physiol Biophys , vol.18 , Issue.SUPPL. 1 , pp. 30-33
    • Haviarova, Z.1    Weismann, P.2    Stvrtinova, V.3    Benuska, J.4
  • 202
    • 0033818123 scopus 로고    scopus 로고
    • Changes in the extracellular matrix of the vein wall--the cause of primary varicosis?
    • Kirsch D, Dienes HP, Kuchle R, et al. Changes in the extracellular matrix of the vein wall--the cause of primary varicosis? Vasa 2000; 29(3): 173-7.
    • (2000) Vasa , vol.29 , Issue.3 , pp. 173-177
    • Kirsch, D.1    Dienes, H.P.2    Kuchle, R.3
  • 203
    • 33847007279 scopus 로고    scopus 로고
    • Comparison of extracellular matrix in skin and saphenous veins from patients with varicose veins: Does the skin reflect venous matrix changes?
    • Sansilvestri-Morel P, Fioretti F, Rupin A, et al. Comparison of extracellular matrix in skin and saphenous veins from patients with varicose veins: does the skin reflect venous matrix changes? Clin Sci (Lond) 2007; 112(4): 229-39.
    • (2007) Clin Sci (Lond) , vol.112 , Issue.4 , pp. 229-239
    • Sansilvestri-Morel, P.1    Fioretti, F.2    Rupin, A.3
  • 204
    • 0031726801 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 is increased in the saphenofemoral junction of patients with varices in the leg
    • Parra JR, Cambria RA, Hower CD, et al. Tissue inhibitor of metalloproteinase-1 is increased in the saphenofemoral junction of patients with varices in the leg. J Vasc Surg 1998; 28(4): 669-75.
    • (1998) J Vasc Surg , vol.28 , Issue.4 , pp. 669-675
    • Parra, J.R.1    Cambria, R.A.2    Hower, C.D.3
  • 205
    • 0033828464 scopus 로고    scopus 로고
    • Increased TIMP/MMP ratio in varicose veins: A possible explanation for extracellular matrix accumulation
    • Badier-Commander C, Verbeuren T, Lebard C, Michel JB, Jacob MP. Increased TIMP/MMP ratio in varicose veins: a possible explanation for extracellular matrix accumulation. J Pathol 2000; 192(1): 105-12.
    • (2000) J Pathol , vol.192 , Issue.1 , pp. 105-112
    • Badier-Commander, C.1    Verbeuren, T.2    Lebard, C.3    Michel, J.B.4    Jacob, M.P.5
  • 206
    • 0031896488 scopus 로고    scopus 로고
    • Abnormal deposition of extracellular matrix proteins by cultured smooth muscle cells from human varicose veins
    • Sansilvestri-Morel P, Nonotte I, Fournet-Bourguignon MP, et al. Abnormal deposition of extracellular matrix proteins by cultured smooth muscle cells from human varicose veins. J Vasc Res 1998; 35(2): 115-23.
    • (1998) J Vasc Res , vol.35 , Issue.2 , pp. 115-123
    • Sansilvestri-Morel, P.1    Nonotte, I.2    Fournet-Bourguignon, M.P.3
  • 207
    • 25444526347 scopus 로고    scopus 로고
    • Decreased production of collagen Type III in cultured smooth muscle cells from varicose vein patients is due to a degradation by MMPs: Possible implication of MMP-3
    • Sansilvestri-Morel P, Rupin A, Jullien ND, et al. Decreased production of collagen Type III in cultured smooth muscle cells from varicose vein patients is due to a degradation by MMPs: possible implication of MMP-3. J Vasc Res 2005; 42(5): 388-98.
    • (2005) J Vasc Res , vol.42 , Issue.5 , pp. 388-398
    • Sansilvestri-Morel, P.1    Rupin, A.2    Jullien, N.D.3
  • 208
    • 77956392303 scopus 로고    scopus 로고
    • Desmuslin gene knockdown causes altered expression of phenotype markers and differentiation of saphenous vein smooth muscle cells
    • Xiao Y, Huang Z, Yin H, Zhang H, Wang S. Desmuslin gene knockdown causes altered expression of phenotype markers and differentiation of saphenous vein smooth muscle cells. J Vasc Surg 2010; 52(3): 684-90.
    • (2010) J Vasc Surg , vol.52 , Issue.3 , pp. 684-690
    • Xiao, Y.1    Huang, Z.2    Yin, H.3    Zhang, H.4    Wang, S.5
  • 209
    • 70849132893 scopus 로고    scopus 로고
    • Maintenance of adrenergic vascular tone by MMP transactivation of the EGFR requires PI3K and mitochondrial ATP synthesis
    • Nagareddy PR, Chow FL, Hao L, et al. Maintenance of adrenergic vascular tone by MMP transactivation of the EGFR requires PI3K and mitochondrial ATP synthesis. Cardiovasc Res 2009; 84(3): 368-77.
    • (2009) Cardiovasc Res , vol.84 , Issue.3 , pp. 368-377
    • Nagareddy, P.R.1    Chow, F.L.2    Hao, L.3
  • 210
    • 8844258082 scopus 로고    scopus 로고
    • Matrix metalloproteinasespecific inhibition of Ca2+ entry mechanisms of vascular contraction
    • Chew DK, Conte MS, Khalil RA. Matrix metalloproteinasespecific inhibition of Ca2+ entry mechanisms of vascular contraction. J Vasc Surg 2004; 40(5): 1001-10.
    • (2004) J Vasc Surg , vol.40 , Issue.5 , pp. 1001-1010
    • Chew, D.K.1    Conte, M.S.2    Khalil, R.A.3
  • 211
    • 0033127460 scopus 로고    scopus 로고
    • Lipodermatosclerosis and the significance of proteolytic remodeling in the pathogenesis of venous ulceration (Review)
    • Herouy Y, Nockowski P, Schopf E, Norgauer J. Lipodermatosclerosis and the significance of proteolytic remodeling in the pathogenesis of venous ulceration (Review). Int J Mol Med 1999; 3(5): 511-5.
    • (1999) Int J Mol Med , vol.3 , Issue.5 , pp. 511-515
    • Herouy, Y.1    Nockowski, P.2    Schopf, E.3    Norgauer, J.4
  • 212
    • 0029999675 scopus 로고    scopus 로고
    • The venous wall and valvular function in chronic venous insufficiency
    • Thulesius O. The venous wall and valvular function in chronic venous insufficiency. Int Angiol 1996; 15(2): 114-8.
    • (1996) Int Angiol , vol.15 , Issue.2 , pp. 114-118
    • Thulesius, O.1
  • 213
    • 0037040825 scopus 로고    scopus 로고
    • alpha(4)beta(1) Integrin activation of L-type calcium channels in vascular smooth muscle causes arteriole vasoconstriction
    • Waitkus-Edwards KR, Martinez-Lemus LA, Wu X, et al. alpha(4)beta(1) Integrin activation of L-type calcium channels in vascular smooth muscle causes arteriole vasoconstriction. Circ Res 2002; 90(4): 473-80.
    • (2002) Circ Res , vol.90 , Issue.4 , pp. 473-480
    • Waitkus-Edwards, K.R.1    Martinez-Lemus, L.A.2    Wu, X.3
  • 215
    • 0032577955 scopus 로고    scopus 로고
    • Atypical protease-activated receptor mediates endothelium-dependent relaxation of human coronary arteries
    • Hamilton JR, Nguyen PB, Cocks TM. Atypical protease-activated receptor mediates endothelium-dependent relaxation of human coronary arteries. Circ Res 1998; 82(12): 1306-11.
    • (1998) Circ Res , vol.82 , Issue.12 , pp. 1306-1311
    • Hamilton, J.R.1    Nguyen, P.B.2    Cocks, T.M.3
  • 216
    • 73549087821 scopus 로고    scopus 로고
    • Interstitial flow induces MMP-1 expression and vascular SMC migration in collagen I gels via an ERK1/2-dependent and c-Jun-mediated mechanism
    • Shi ZD, Ji XY, Berardi DE, Qazi H, Tarbell JM. Interstitial flow induces MMP-1 expression and vascular SMC migration in collagen I gels via an ERK1/2-dependent and c-Jun-mediated mechanism. Am J Physiol Heart Circ Physiol 2010; 298(1): H127-35.
    • (2010) Am J Physiol Heart Circ Physiol , vol.298 , Issue.1
    • Shi, Z.D.1    Ji, X.Y.2    Berardi, D.E.3    Qazi, H.4    Tarbell, J.M.5
  • 217
    • 48549089462 scopus 로고    scopus 로고
    • Aortic smooth muscle cells migration and the role of metalloproteinases and hyaluronan
    • Vigetti D, Moretto P, Viola M, et al. Aortic smooth muscle cells migration and the role of metalloproteinases and hyaluronan. Connect Tissue Res 2008; 49(3): 189-92.
    • (2008) Connect Tissue Res , vol.49 , Issue.3 , pp. 189-192
    • Vigetti, D.1    Moretto, P.2    Viola, M.3
  • 218
    • 0842285678 scopus 로고    scopus 로고
    • Chemokine receptor-8 (CCR8) mediates human vascular smooth muscle cell chemotaxis and metalloproteinase-2 secretion
    • Haque NS, Fallon JT, Pan JJ, Taubman MB, Harpel PC. Chemokine receptor-8 (CCR8) mediates human vascular smooth muscle cell chemotaxis and metalloproteinase-2 secretion. Blood 2004; 103(4): 1296-304.
    • (2004) Blood , vol.103 , Issue.4 , pp. 1296-1304
    • Haque, N.S.1    Fallon, J.T.2    Pan, J.J.3    Taubman, M.B.4    Harpel, P.C.5
  • 219
    • 1542469612 scopus 로고    scopus 로고
    • Increased expression of elastolytic cysteine proteases, cathepsins S and K, in the neointima of balloon-injured rat carotid arteries
    • Cheng XW, Kuzuya M, Sasaki T, et al. Increased expression of elastolytic cysteine proteases, cathepsins S and K, in the neointima of balloon-injured rat carotid arteries. Am J Pathol 2004; 164(1): 243-51.
    • (2004) Am J Pathol , vol.164 , Issue.1 , pp. 243-251
    • Cheng, X.W.1    Kuzuya, M.2    Sasaki, T.3
  • 220
    • 0347192989 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and-9 differentially regulate smooth muscle cell migration and cell-mediated collagen organization
    • Johnson C, Galis ZS. Matrix metalloproteinase-2 and-9 differentially regulate smooth muscle cell migration and cell-mediated collagen organization. Arterioscler Thromb Vasc Biol 2004; 24(1): 54-60.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , Issue.1 , pp. 54-60
    • Johnson, C.1    Galis, Z.S.2
  • 221
    • 46449089508 scopus 로고    scopus 로고
    • Tanshinone IIA from Salvia miltiorrhiza BUNGE inhibits human aortic smooth muscle cell migration and MMP-9 activity through AKT signaling pathway
    • Jin UH, Suh SJ, Chang HW, et al. Tanshinone IIA from Salvia miltiorrhiza BUNGE inhibits human aortic smooth muscle cell migration and MMP-9 activity through AKT signaling pathway. J Cell Biochem 2008; 104(1): 15-26.
    • (2008) J Cell Biochem , vol.104 , Issue.1 , pp. 15-26
    • Jin, U.H.1    Suh, S.J.2    Chang, H.W.3
  • 222
    • 75349110026 scopus 로고    scopus 로고
    • Curcumin prevents human aortic smooth muscle cells migration by inhibiting of MMP-9 expression
    • Yu YM, Lin HC. Curcumin prevents human aortic smooth muscle cells migration by inhibiting of MMP-9 expression. Nutr Metab Cardiovasc Dis 2010; 20(2): 125-32.
    • (2010) Nutr Metab Cardiovasc Dis , vol.20 , Issue.2 , pp. 125-132
    • Yu, Y.M.1    Lin, H.C.2
  • 223
    • 0036843534 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 is necessary for the regulation of smooth muscle cell replication and migration after arterial injury
    • Cho A, Reidy MA. Matrix metalloproteinase-9 is necessary for the regulation of smooth muscle cell replication and migration after arterial injury. Circ Res 2002; 91(9): 845-51.
    • (2002) Circ Res , vol.91 , Issue.9 , pp. 845-851
    • Cho, A.1    Reidy, M.A.2
  • 224
    • 0036844555 scopus 로고    scopus 로고
    • Targeted disruption of the matrix metalloproteinase-9 gene impairs smooth muscle cell migration and geometrical arterial remodeling
    • Galis ZS, Johnson C, Godin D, et al. Targeted disruption of the matrix metalloproteinase-9 gene impairs smooth muscle cell migration and geometrical arterial remodeling. Circ Res 2002; 91(9): 852-9.
    • (2002) Circ Res , vol.91 , Issue.9 , pp. 852-859
    • Galis, Z.S.1    Johnson, C.2    Godin, D.3
  • 225
    • 0037869105 scopus 로고    scopus 로고
    • Relationship between type IV collagen degradation, metalloproteinase activity and smooth muscle cell migration and proliferation in cultured human saphenous vein
    • Aguilera CM, George SJ, Johnson JL, Newby AC. Relationship between type IV collagen degradation, metalloproteinase activity and smooth muscle cell migration and proliferation in cultured human saphenous vein. Cardiovasc Res 2003; 58(3): 679-88.
    • (2003) Cardiovasc Res , vol.58 , Issue.3 , pp. 679-688
    • Aguilera, C.M.1    George, S.J.2    Johnson, J.L.3    Newby, A.C.4
  • 226
    • 2342472716 scopus 로고    scopus 로고
    • Focal adhesion and actin dynamics: A place where kinases and proteases meet to promote invasion
    • Carragher NO, Frame MC. Focal adhesion and actin dynamics: a place where kinases and proteases meet to promote invasion. Trends Cell Biol 2004; 14(5): 241-9.
    • (2004) Trends Cell Biol , vol.14 , Issue.5 , pp. 241-249
    • Carragher, N.O.1    Frame, M.C.2
  • 227
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, beta-catenin, and cadherin pathways
    • Nelson WJ, Nusse R. Convergence of Wnt, beta-catenin, and cadherin pathways. Science 2004; 303(5663): 1483-7.
    • (2004) Science , vol.303 , Issue.5663 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 228
    • 0028930748 scopus 로고
    • Migration of bovine aortic smooth muscle cells after wounding injury. The role of hyaluronan and RHAMM
    • Savani RC, Wang C, Yang B, et al. Migration of bovine aortic smooth muscle cells after wounding injury. The role of hyaluronan and RHAMM. J Clin Invest 1995; 95(3): 1158-68.
    • (1995) J Clin Invest , vol.95 , Issue.3 , pp. 1158-1168
    • Savani, R.C.1    Wang, C.2    Yang, B.3
  • 229
    • 0038801626 scopus 로고    scopus 로고
    • Dismantling of cadherin-mediated cell-cell contacts modulates smooth muscle cell proliferation
    • Uglow EB, Slater S, Sala-Newby GB, et al. Dismantling of cadherin-mediated cell-cell contacts modulates smooth muscle cell proliferation. Circ Res 2003; 92(12): 1314-21.
    • (2003) Circ Res , vol.92 , Issue.12 , pp. 1314-1321
    • Uglow, E.B.1    Slater, S.2    Sala-Newby, G.B.3
  • 230
    • 13544255506 scopus 로고    scopus 로고
    • PAR1 is a matrix metalloprotease-1 receptor that promotes invasion and tumorigenesis of breast cancer cells
    • Boire A, Covic L, Agarwal A, Jacques S, Sherifi S, Kuliopulos A. PAR1 is a matrix metalloprotease-1 receptor that promotes invasion and tumorigenesis of breast cancer cells. Cell 2005; 120(3): 303-13.
    • (2005) Cell , vol.120 , Issue.3 , pp. 303-313
    • Boire, A.1    Covic, L.2    Agarwal, A.3    Jacques, S.4    Sherifi, S.5    Kuliopulos, A.6
  • 231
    • 33749827162 scopus 로고    scopus 로고
    • The histopathology of varicose vein disease
    • Somers P, Knaapen M. The histopathology of varicose vein disease. Angiology 2006; 57(5): 546-55.
    • (2006) Angiology , vol.57 , Issue.5 , pp. 546-555
    • Somers, P.1    Knaapen, M.2
  • 232
    • 0035736333 scopus 로고    scopus 로고
    • Smooth muscle changes in varicose veins: An ultrastructural study
    • Wali MA, Eid RA. Smooth muscle changes in varicose veins: an ultrastructural study. J Smooth Muscle Res 2001; 37(5-6): 123-35.
    • (2001) J Smooth Muscle Res , vol.37 , Issue.5-6 , pp. 123-135
    • Wali, M.A.1    Eid, R.A.2
  • 233
    • 0036626201 scopus 로고    scopus 로고
    • Intimal changes in varicose veins: An ultrastructural study
    • Wali MA, Eid RA. Intimal changes in varicose veins: an ultrastructural study. J Smooth Muscle Res 2002; 38(3): 63-74.
    • (2002) J Smooth Muscle Res , vol.38 , Issue.3 , pp. 63-74
    • Wali, M.A.1    Eid, R.A.2
  • 235
    • 0029838645 scopus 로고    scopus 로고
    • Overexpression of tissue inhibitor of matrix metalloproteinase-1 inhibits vascular smooth muscle cell functions in vitro and in vivo
    • Forough R, Koyama N, Hasenstab D, et al. Overexpression of tissue inhibitor of matrix metalloproteinase-1 inhibits vascular smooth muscle cell functions in vitro and in vivo. Circ Res 1996; 79(4): 812-20.
    • (1996) Circ Res , vol.79 , Issue.4 , pp. 812-820
    • Forough, R.1    Koyama, N.2    Hasenstab, D.3
  • 236
    • 0032521142 scopus 로고    scopus 로고
    • Divergent effects of tissue inhibitor of metalloproteinase-1,-2, or-3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP-3 promotes apoptosis
    • Baker AH, Zaltsman AB, George SJ, Newby AC. Divergent effects of tissue inhibitor of metalloproteinase-1,-2, or-3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP-3 promotes apoptosis. J Clin Invest 1998; 101(6): 1478-87.
    • (1998) J Clin Invest , vol.101 , Issue.6 , pp. 1478-1487
    • Baker, A.H.1    Zaltsman, A.B.2    George, S.J.3    Newby, A.C.4
  • 237
    • 0034711752 scopus 로고    scopus 로고
    • Inhibition of late vein graft neointima formation in human and porcine models by adenovirus-mediated overexpression of tissue inhibitor of metalloproteinase-3
    • George SJ, Lloyd CT, Angelini GD, Newby AC, Baker AH. Inhibition of late vein graft neointima formation in human and porcine models by adenovirus-mediated overexpression of tissue inhibitor of metalloproteinase-3. Circulation 2000; 101(3): 296-304.
    • (2000) Circulation , vol.101 , Issue.3 , pp. 296-304
    • George, S.J.1    Lloyd, C.T.2    Angelini, G.D.3    Newby, A.C.4    Baker, A.H.5
  • 238
    • 0029911386 scopus 로고    scopus 로고
    • The role of plasminogen, plasminogen activators, and matrix metalloproteinases in primate arterial smooth muscle cell migration
    • Kenagy RD, Vergel S, Mattsson E, Bendeck M, Reidy MA, Clowes AW. The role of plasminogen, plasminogen activators, and matrix metalloproteinases in primate arterial smooth muscle cell migration. Arterioscler Thromb Vasc Biol 1996; 16(11): 1373-82.
    • (1996) Arterioscler Thromb Vasc Biol , vol.16 , Issue.11 , pp. 1373-1382
    • Kenagy, R.D.1    Vergel, S.2    Mattsson, E.3    Bendeck, M.4    Reidy, M.A.5    Clowes, A.W.6
  • 239
    • 0141537147 scopus 로고    scopus 로고
    • A nonantibiotic chemically modified tetracycline (CMT-3) inhibits intimal thickening
    • Islam MM, Franco CD, Courtman DW, Bendeck MP. A nonantibiotic chemically modified tetracycline (CMT-3) inhibits intimal thickening. Am J Pathol 2003; 163(4): 1557-66.
    • (2003) Am J Pathol , vol.163 , Issue.4 , pp. 1557-1566
    • Islam, M.M.1    Franco, C.D.2    Courtman, D.W.3    Bendeck, M.P.4
  • 240
    • 77649152285 scopus 로고    scopus 로고
    • Buddleja officinalis suppresses high glucose-induced vascular smooth muscle cell proliferation: Role of mitogen-activated protein kinases, nuclear factor-kappaB and matrix metalloproteinases
    • Lee YJ, Kim JS, Kang DG, Lee HS. Buddleja officinalis suppresses high glucose-induced vascular smooth muscle cell proliferation: role of mitogen-activated protein kinases, nuclear factor-kappaB and matrix metalloproteinases. Exp Biol Med (Maywood) 2010; 235(2): 247-55.
    • (2010) Exp Biol Med (Maywood) , vol.235 , Issue.2 , pp. 247-255
    • Lee, Y.J.1    Kim, J.S.2    Kang, D.G.3    Lee, H.S.4
  • 241
    • 12844286997 scopus 로고    scopus 로고
    • Dual role of matrix metalloproteinases (matrixins) in intimal thickening and atherosclerotic plaque rupture
    • Newby AC. Dual role of matrix metalloproteinases (matrixins) in intimal thickening and atherosclerotic plaque rupture. Physiol Rev 2005; 85(1): 1-31.
    • (2005) Physiol Rev , vol.85 , Issue.1 , pp. 1-31
    • Newby, A.C.1
  • 242
    • 70350565362 scopus 로고    scopus 로고
    • In vitro differences between smooth muscle cells derived from varicose veins and normal veins
    • Xiao Y, Huang Z, Yin H, Lin Y, Wang S. In vitro differences between smooth muscle cells derived from varicose veins and normal veins. J Vasc Surg 2009; 50(5): 1149-54.
    • (2009) J Vasc Surg , vol.50 , Issue.5 , pp. 1149-1154
    • Xiao, Y.1    Huang, Z.2    Yin, H.3    Lin, Y.4    Wang, S.5
  • 243
    • 0038586462 scopus 로고    scopus 로고
    • Perlecan up-regulation of FRNK suppresses smooth muscle cell proliferation via inhibition of FAK signaling
    • Walker HA, Whitelock JM, Garl PJ, Nemenoff RA, Stenmark KR, Weiser-Evans MC. Perlecan up-regulation of FRNK suppresses smooth muscle cell proliferation via inhibition of FAK signaling. Mol Biol Cell 2003; 14(5): 1941-52.
    • (2003) Mol Biol Cell , vol.14 , Issue.5 , pp. 1941-1952
    • Walker, H.A.1    Whitelock, J.M.2    Garl, P.J.3    Nemenoff, R.A.4    Stenmark, K.R.5    Weiser-Evans, M.C.6
  • 244
    • 0034720452 scopus 로고    scopus 로고
    • Control of smooth muscle cell proliferation and phenotype by integrin signaling through focal adhesion kinase
    • Morla AO, Mogford JE. Control of smooth muscle cell proliferation and phenotype by integrin signaling through focal adhesion kinase. Biochem Biophys Res Commun 2000; 272(1): 298-302.
    • (2000) Biochem Biophys Res Commun , vol.272 , Issue.1 , pp. 298-302
    • Morla, A.O.1    Mogford, J.E.2
  • 245
    • 10044256495 scopus 로고    scopus 로고
    • Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries
    • Lucchesi PA, Sabri A, Belmadani S, Matrougui K. Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries. Circulation 2004; 110(23): 3587-93.
    • (2004) Circulation , vol.110 , Issue.23 , pp. 3587-3593
    • Lucchesi, P.A.1    Sabri, A.2    Belmadani, S.3    Matrougui, K.4
  • 246
    • 3042615183 scopus 로고    scopus 로고
    • Stem cell factor and c-kit are expressed by and may affect vascular SMCs through an autocrine pathway
    • Hollenbeck ST, Sakakibara K, Faries PL, Workhu B, Liu B, Kent KC. Stem cell factor and c-kit are expressed by and may affect vascular SMCs through an autocrine pathway. J Surg Res 2004; 120(2): 288-94.
    • (2004) J Surg Res , vol.120 , Issue.2 , pp. 288-294
    • Hollenbeck, S.T.1    Sakakibara, K.2    Faries, P.L.3    Workhu, B.4    Liu, B.5    Kent, K.C.6
  • 247
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFbeta activation
    • Annes JP, Munger JS, Rifkin DB. Making sense of latent TGFbeta activation. J Cell Sci 2003; 116(Pt 2): 217-24.
    • (2003) J Cell Sci , vol.116 , Issue.PART 2 , pp. 217-224
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 248
    • 0031467314 scopus 로고    scopus 로고
    • Matrix metalloproteinase-3 releases active heparin-binding EGFlike growth factor by cleavage at a specific juxtamembrane site
    • Suzuki M, Raab G, Moses MA, Fernandez CA, Klagsbrun M. Matrix metalloproteinase-3 releases active heparin-binding EGFlike growth factor by cleavage at a specific juxtamembrane site. J Biol Chem 1997; 272(50): 31730-7.
    • (1997) J Biol Chem , vol.272 , Issue.50 , pp. 31730-31737
    • Suzuki, M.1    Raab, G.2    Moses, M.A.3    Fernandez, C.A.4    Klagsbrun, M.5
  • 249
    • 0030958072 scopus 로고    scopus 로고
    • Degradation of decorin by matrix metalloproteinases: Identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release
    • Imai K, Hiramatsu A, Fukushima D, Pierschbacher MD, Okada Y. Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Biochem J 1997; 322 (Pt 3): 809-14.
    • (1997) Biochem J , vol.322 , Issue.PART 3 , pp. 809-814
    • Imai, K.1    Hiramatsu, A.2    Fukushima, D.3    Pierschbacher, M.D.4    Okada, Y.5
  • 250
    • 0040776938 scopus 로고    scopus 로고
    • Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3
    • Manes S, Mira E, Barbacid MM, et al. Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3. J Biol Chem 1997; 272(41): 25706-12.
    • (1997) J Biol Chem , vol.272 , Issue.41 , pp. 25706-25712
    • Manes, S.1    Mira, E.2    Barbacid, M.M.3
  • 251
    • 0035147313 scopus 로고    scopus 로고
    • Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1
    • Noe V, Fingleton B, Jacobs K, et al. Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J Cell Sci 2001; 114(Pt 1): 111-8.
    • (2001) J Cell Sci , vol.114 , Issue.PART 1 , pp. 111-118
    • Noe, V.1    Fingleton, B.2    Jacobs, K.3
  • 253
    • 0035874882 scopus 로고    scopus 로고
    • Prostate carcinomas developing in transgenic rats with SV40 T antigen expression under probasin promoter control are strictly androgen dependent
    • Asamoto M, Hokaiwado N, Cho YM, et al. Prostate carcinomas developing in transgenic rats with SV40 T antigen expression under probasin promoter control are strictly androgen dependent. Cancer Res 2001; 61(12): 4693-700.
    • (2001) Cancer Res , vol.61 , Issue.12 , pp. 4693-4700
    • Asamoto, M.1    Hokaiwado, N.2    Cho, Y.M.3
  • 254
    • 0036144901 scopus 로고    scopus 로고
    • Functional distinction between CXC chemokines, interleukin-8 (IL-8), and growth related oncogene (GRO)alpha in neutrophil infiltration
    • Fujiwara K, Matsukawa A, Ohkawara S, Takagi K, Yoshinaga M. Functional distinction between CXC chemokines, interleukin-8 (IL-8), and growth related oncogene (GRO)alpha in neutrophil infiltration. Lab Invest 2002; 82(1): 15-23.
    • (2002) Lab Invest , vol.82 , Issue.1 , pp. 15-23
    • Fujiwara, K.1    Matsukawa, A.2    Ohkawara, S.3    Takagi, K.4    Yoshinaga, M.5
  • 255
    • 0035941359 scopus 로고    scopus 로고
    • Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1
    • McQuibban GA, Butler GS, Gong JH, et al. Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1. J Biol Chem 2001; 276(47): 43503-8.
    • (2001) J Biol Chem , vol.276 , Issue.47 , pp. 43503-43508
    • McQuibban, G.A.1    Butler, G.S.2    Gong, J.H.3
  • 256
    • 0029959437 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1
    • Levi E, Fridman R, Miao HQ, Ma YS, Yayon A, Vlodavsky I. Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1. Proc Natl Acad Sci U S A 1996; 93(14): 7069-74.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.14 , pp. 7069-7074
    • Levi, E.1    Fridman, R.2    Miao, H.Q.3    Ma, Y.S.4    Yayon, A.5    Vlodavsky, I.6
  • 257
    • 0030064282 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase activity inhibits smooth muscle cell migration but not neointimal thickening after arterial injury
    • Bendeck MP, Irvin C, Reidy MA. Inhibition of matrix metalloproteinase activity inhibits smooth muscle cell migration but not neointimal thickening after arterial injury. Circ Res 1996; 78(1): 38-43.
    • (1996) Circ Res , vol.78 , Issue.1 , pp. 38-43
    • Bendeck, M.P.1    Irvin, C.2    Reidy, M.A.3
  • 258
    • 0030026574 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle cell migration and proliferation in vitro and in injured rat arteries by a synthetic matrix metalloproteinase inhibitor
    • Zempo N, Koyama N, Kenagy RD, Lea HJ, Clowes AW. Regulation of vascular smooth muscle cell migration and proliferation in vitro and in injured rat arteries by a synthetic matrix metalloproteinase inhibitor. Arterioscler Thromb Vasc Biol 1996; 16(1): 28-33.
    • (1996) Arterioscler Thromb Vasc Biol , vol.16 , Issue.1 , pp. 28-33
    • Zempo, N.1    Koyama, N.2    Kenagy, R.D.3    Lea, H.J.4    Clowes, A.W.5
  • 259
    • 0343006773 scopus 로고    scopus 로고
    • The synthetic metalloproteinase inhibitor batimastat suppresses injury-induced phosphorylation of MAP kinase ERK1/ERK2 and phenotypic modification of arterial smooth muscle cells in vitro
    • Lovdahl C, Thyberg J, Hultgardh-Nilsson A. The synthetic metalloproteinase inhibitor batimastat suppresses injury-induced phosphorylation of MAP kinase ERK1/ERK2 and phenotypic modification of arterial smooth muscle cells in vitro. J Vasc Res 2000; 37(5): 345-54.
    • (2000) J Vasc Res , vol.37 , Issue.5 , pp. 345-354
    • Lovdahl, C.1    Thyberg, J.2    Hultgardh-Nilsson, A.3
  • 260
    • 3042771798 scopus 로고    scopus 로고
    • R-cadherin:Beta-catenin complex and its association with vascular smooth muscle cell proliferation
    • Slater SC, Koutsouki E, Jackson CL, et al. R-cadherin:beta-catenin complex and its association with vascular smooth muscle cell proliferation. Arterioscler Thromb Vasc Biol 2004; 24(7): 1204-10.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , Issue.7 , pp. 1204-1210
    • Slater, S.C.1    Koutsouki, E.2    Jackson, C.L.3
  • 261
    • 0036118347 scopus 로고    scopus 로고
    • Doxycycline modulates smooth muscle cell growth, migration, and matrix remodeling after arterial injury
    • Bendeck MP, Conte M, Zhang M, Nili N, Strauss BH, Farwell SM. Doxycycline modulates smooth muscle cell growth, migration, and matrix remodeling after arterial injury. Am J Pathol 2002; 160(3): 1089-95.
    • (2002) Am J Pathol , vol.160 , Issue.3 , pp. 1089-1095
    • Bendeck, M.P.1    Conte, M.2    Zhang, M.3    Nili, N.4    Strauss, B.H.5    Farwell, S.M.6
  • 262
    • 0030996930 scopus 로고    scopus 로고
    • Cyclic straininduced monocyte chemotactic protein-1 gene expression in endothelial cells involves reactive oxygen species activation of activator protein 1
    • Wung BS, Cheng JJ, Hsieh HJ, Shyy YJ, Wang DL. Cyclic straininduced monocyte chemotactic protein-1 gene expression in endothelial cells involves reactive oxygen species activation of activator protein 1. Circ Res 1997; 81(1): 1-7.
    • (1997) Circ Res , vol.81 , Issue.1 , pp. 1-7
    • Wung, B.S.1    Cheng, J.J.2    Hsieh, H.J.3    Shyy, Y.J.4    Wang, D.L.5
  • 263
    • 37149018694 scopus 로고    scopus 로고
    • Corticotropinreleasing hormone activates connexin 43 via activator protein-1 transcription factor in human myometrial smooth muscle cells
    • Wu X, Shen H, Yu L, Peng M, Lai WS, Ding YL. Corticotropinreleasing hormone activates connexin 43 via activator protein-1 transcription factor in human myometrial smooth muscle cells. Am J Physiol Endocrinol Metab 2007; 293(6): E1789-94.
    • (2007) Am J Physiol Endocrinol Metab , vol.293 , Issue.6
    • Wu, X.1    Shen, H.2    Yu, L.3    Peng, M.4    Lai, W.S.5    Ding, Y.L.6
  • 264
    • 0037138520 scopus 로고    scopus 로고
    • Decoy oligodeoxynucleotide against activator protein-1 reduces neointimal proliferation after coronary angioplasty in hypercholesterolemic minipigs
    • Buchwald AB, Wagner AH, Webel C, Hecker M. Decoy oligodeoxynucleotide against activator protein-1 reduces neointimal proliferation after coronary angioplasty in hypercholesterolemic minipigs. J Am Coll Cardiol 2002; 39(4): 732-8.
    • (2002) J Am Coll Cardiol , vol.39 , Issue.4 , pp. 732-738
    • Buchwald, A.B.1    Wagner, A.H.2    Webel, C.3    Hecker, M.4
  • 265
    • 0033767577 scopus 로고    scopus 로고
    • Therapeutic applications of transcription factor decoy oligonucleotides
    • Mann MJ, Dzau VJ. Therapeutic applications of transcription factor decoy oligonucleotides. J Clin Invest 2000; 106(9): 1071-5.
    • (2000) J Clin Invest , vol.106 , Issue.9 , pp. 1071-1075
    • Mann, M.J.1    Dzau, V.J.2
  • 266
    • 54049106210 scopus 로고    scopus 로고
    • Stretch-induced activation of the transcription factor activator protein-1 controls monocyte chemoattractant protein-1 expression during arteriogenesis
    • Demicheva E, Hecker M, Korff T. Stretch-induced activation of the transcription factor activator protein-1 controls monocyte chemoattractant protein-1 expression during arteriogenesis. Circ Res 2008; 103(5): 477-84.
    • (2008) Circ Res , vol.103 , Issue.5 , pp. 477-484
    • Demicheva, E.1    Hecker, M.2    Korff, T.3
  • 267
    • 0037328007 scopus 로고    scopus 로고
    • A functional activating protein 1 (AP-1) site regulates matrix metalloproteinase 2 (MMP-2) transcription by cardiac cells through interactions with JunB-Fra1 and JunB-FosB heterodimers
    • Bergman MR, Cheng S, Honbo N, Piacentini L, Karliner JS, Lovett DH. A functional activating protein 1 (AP-1) site regulates matrix metalloproteinase 2 (MMP-2) transcription by cardiac cells through interactions with JunB-Fra1 and JunB-FosB heterodimers. Biochem J 2003; 369(Pt 3): 485-96.
    • (2003) Biochem J , vol.369 , Issue.PART 3 , pp. 485-496
    • Bergman, M.R.1    Cheng, S.2    Honbo, N.3    Piacentini, L.4    Karliner, J.S.5    Lovett, D.H.6
  • 268
    • 80053896621 scopus 로고    scopus 로고
    • Experimental hypertension triggers varicosis-like maladaptive venous remodeling through activator protein-1
    • Feldner A, Otto H, Rewerk S, Hecker M, Korff T. Experimental hypertension triggers varicosis-like maladaptive venous remodeling through activator protein-1. FASEB J 2011; 25(10): 3613-21.
    • (2011) FASEB J , vol.25 , Issue.10 , pp. 3613-3621
    • Feldner, A.1    Otto, H.2    Rewerk, S.3    Hecker, M.4    Korff, T.5
  • 269
    • 0036739920 scopus 로고    scopus 로고
    • Progression of atheroma: A struggle between death and procreation
    • Geng YJ, Libby P. Progression of atheroma: a struggle between death and procreation. Arterioscler Thromb Vasc Biol 2002; 22(9): 1370-80.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , Issue.9 , pp. 1370-1380
    • Geng, Y.J.1    Libby, P.2
  • 270
    • 6344226512 scopus 로고    scopus 로고
    • Role of apoptosis in atherosclerosis and its therapeutic implications
    • Stoneman VE, Bennett MR. Role of apoptosis in atherosclerosis and its therapeutic implications. Clin Sci (Lond) 2004; 107(4): 343-54.
    • (2004) Clin Sci (Lond) , vol.107 , Issue.4 , pp. 343-354
    • Stoneman, V.E.1    Bennett, M.R.2
  • 271
    • 0347951238 scopus 로고    scopus 로고
    • Agonist-induced activation of matrix metalloproteinase-7 promotes vasoconstriction through the epidermal growth factor-receptor pathway
    • Hao L, Du M, Lopez-Campistrous A, Fernandez-Patron C. Agonist-induced activation of matrix metalloproteinase-7 promotes vasoconstriction through the epidermal growth factor-receptor pathway. Circ Res 2004; 94(1): 68-76.
    • (2004) Circ Res , vol.94 , Issue.1 , pp. 68-76
    • Hao, L.1    Du, M.2    Lopez-Campistrous, A.3    Fernandez-Patron, C.4
  • 272
    • 33746951927 scopus 로고    scopus 로고
    • Acceleration of matrix metalloproteinase-1 production and activation of platelet-derived growth factor receptor beta in human coronary smooth muscle cells by oxidized LDL and 4-hydroxynonenal
    • Akiba S, Kumazawa S, Yamaguchi H, et al. Acceleration of matrix metalloproteinase-1 production and activation of platelet-derived growth factor receptor beta in human coronary smooth muscle cells by oxidized LDL and 4-hydroxynonenal. Biochim Biophys Acta 2006; 1763(8): 797-804.
    • (2006) Biochim Biophys Acta , vol.1763 , Issue.8 , pp. 797-804
    • Akiba, S.1    Kumazawa, S.2    Yamaguchi, H.3
  • 274
    • 0034194714 scopus 로고    scopus 로고
    • Matrix survival signaling: From fibronectin via focal adhesion kinase to c-Jun NH(2)-terminal kinase
    • Almeida EA, Ilic D, Han Q, et al. Matrix survival signaling: from fibronectin via focal adhesion kinase to c-Jun NH(2)-terminal kinase. J Cell Biol 2000; 149(3): 741-54.
    • (2000) J Cell Biol , vol.149 , Issue.3 , pp. 741-754
    • Almeida, E.A.1    Ilic, D.2    Han, Q.3
  • 275
    • 0032547796 scopus 로고    scopus 로고
    • Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis
    • Ilic D, Almeida EA, Schlaepfer DD, Dazin P, Aizawa S, Damsky CH. Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis. J Cell Biol 1998; 143(2): 547-60.
    • (1998) J Cell Biol , vol.143 , Issue.2 , pp. 547-560
    • Ilic, D.1    Almeida, E.A.2    Schlaepfer, D.D.3    Dazin, P.4    Aizawa, S.5    Damsky, C.H.6
  • 276
    • 12244295145 scopus 로고    scopus 로고
    • Activation of metalloproteinases and their association with integrins: An auxiliary apoptotic pathway in human endothelial cells
    • Levkau B, Kenagy RD, Karsan A, et al. Activation of metalloproteinases and their association with integrins: an auxiliary apoptotic pathway in human endothelial cells. Cell Death Differ 2002; 9(12): 1360-7.
    • (2002) Cell Death Differ , vol.9 , Issue.12 , pp. 1360-1367
    • Levkau, B.1    Kenagy, R.D.2    Karsan, A.3
  • 277
    • 0037900632 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Old dogs with new tricks
    • Somerville RP, Oblander SA, Apte SS. Matrix metalloproteinases: old dogs with new tricks. Genome Biol 2003; 4(6): 216.
    • (2003) Genome Biol , vol.4 , Issue.6 , pp. 216
    • Somerville, R.P.1    Oblander, S.A.2    Apte, S.S.3
  • 278
    • 17644414459 scopus 로고    scopus 로고
    • Multiple roles of matrix metalloproteinases during apoptosis
    • Mannello F, Luchetti F, Falcieri E, Papa S. Multiple roles of matrix metalloproteinases during apoptosis. Apoptosis 2005; 10(1): 19-24.
    • (2005) Apoptosis , vol.10 , Issue.1 , pp. 19-24
    • Mannello, F.1    Luchetti, F.2    Falcieri, E.3    Papa, S.4
  • 279
    • 0034731478 scopus 로고    scopus 로고
    • Localization of the death domain of tissue inhibitor of metalloproteinase-3 to the N terminus. Metalloproteinase inhibition is associated with proapoptotic activity
    • Bond M, Murphy G, Bennett MR, et al. Localization of the death domain of tissue inhibitor of metalloproteinase-3 to the N terminus. Metalloproteinase inhibition is associated with proapoptotic activity. J Biol Chem 2000; 275(52): 41358-63.
    • (2000) J Biol Chem , vol.275 , Issue.52 , pp. 41358-41363
    • Bond, M.1    Murphy, G.2    Bennett, M.R.3
  • 280
    • 3042745695 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro
    • Kwan JA, Schulze CJ, Wang W, et al. Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro. FASEB J 2004; 18(6): 690-2.
    • (2004) FASEB J , vol.18 , Issue.6 , pp. 690-692
    • Kwan, J.A.1    Schulze, C.J.2    Wang, W.3
  • 281
    • 4444360286 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-4 suppresses vascular smooth muscle cell migration and induces cell apoptosis
    • Guo YH, Gao W, Li Q, Li PF, Yao PY, Chen K. Tissue inhibitor of metalloproteinases-4 suppresses vascular smooth muscle cell migration and induces cell apoptosis. Life Sci 2004; 75(20): 2483-93.
    • (2004) Life Sci , vol.75 , Issue.20 , pp. 2483-2493
    • Guo, Y.H.1    Gao, W.2    Li, Q.3    Li, P.F.4    Yao, P.Y.5    Chen, K.6
  • 282
    • 33745023668 scopus 로고    scopus 로고
    • Endothelium-derived hyperpolarizing factor: Where are we now?
    • Feletou M, Vanhoutte PM. Endothelium-derived hyperpolarizing factor: where are we now? Arterioscler Thromb Vasc Biol 2006; 26(6): 1215-25.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , Issue.6 , pp. 1215-1225
    • Feletou, M.1    Vanhoutte, P.M.2
  • 283
    • 5544308057 scopus 로고    scopus 로고
    • Expression of endothelial nitric oxide synthase in the vascular wall during arteriogenesis
    • Cai WJ, Kocsis E, Luo X, Schaper W, Schaper J. Expression of endothelial nitric oxide synthase in the vascular wall during arteriogenesis. Mol Cell Biochem 2004; 264(1-2): 193-200.
    • (2004) Mol Cell Biochem , vol.264 , Issue.1-2 , pp. 193-200
    • Cai, W.J.1    Kocsis, E.2    Luo, X.3    Schaper, W.4    Schaper, J.5
  • 284
    • 4944266251 scopus 로고    scopus 로고
    • Endothelial potassium channels, endothelium-dependent hyperpolarization and the regulation of vascular tone in health and disease
    • Coleman HA, Tare M, Parkington HC. Endothelial potassium channels, endothelium-dependent hyperpolarization and the regulation of vascular tone in health and disease. Clin Exp Pharmacol Physiol 2004; 31(9): 641-9.
    • (2004) Clin Exp Pharmacol Physiol , vol.31 , Issue.9 , pp. 641-649
    • Coleman, H.A.1    Tare, M.2    Parkington, H.C.3
  • 285
    • 0035281807 scopus 로고    scopus 로고
    • K+ currents underlying the action of endothelium-derived hyperpolarizing factor in guinea-pig, rat and human blood vessels
    • Coleman HA, Tare M, Parkington HC. K+ currents underlying the action of endothelium-derived hyperpolarizing factor in guinea-pig, rat and human blood vessels. J Physiol 2001; 531(Pt 2): 359-73.
    • (2001) J Physiol , vol.531 , Issue.PART 2 , pp. 359-373
    • Coleman, H.A.1    Tare, M.2    Parkington, H.C.3
  • 286
    • 39149106425 scopus 로고    scopus 로고
    • Endothelial dependence of matrix metalloproteinase-mediated vascular hyporeactivity caused by lipopolysaccharide
    • Cena J, Lalu MM, Rosenfelt C, Schulz R. Endothelial dependence of matrix metalloproteinase-mediated vascular hyporeactivity caused by lipopolysaccharide. Eur J Pharmacol 2008; 582(1-3): 116-22.
    • (2008) Eur J Pharmacol , vol.582 , Issue.1-3 , pp. 116-122
    • Cena, J.1    Lalu, M.M.2    Rosenfelt, C.3    Schulz, R.4
  • 287
    • 13844297614 scopus 로고    scopus 로고
    • The endothelium-derived hyperpolarizing factor puzzle: A mechanism without a mediator?
    • Cohen RA. The endothelium-derived hyperpolarizing factor puzzle: a mechanism without a mediator? Circulation 2005; 111(6): 724-7.
    • (2005) Circulation , vol.111 , Issue.6 , pp. 724-727
    • Cohen, R.A.1
  • 288
    • 38549083858 scopus 로고    scopus 로고
    • Forkhead factor, FOXO3a, induces apoptosis of endothelial cells through activation of matrix metalloproteinases
    • Lee HY, You HJ, Won JY, et al. Forkhead factor, FOXO3a, induces apoptosis of endothelial cells through activation of matrix metalloproteinases. Arterioscler Thromb Vasc Biol 2008; 28(2): 302-8.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , Issue.2 , pp. 302-308
    • Lee, H.Y.1    You, H.J.2    Won, J.Y.3
  • 289
    • 73449101781 scopus 로고    scopus 로고
    • Evidence for the involvement of matrix metalloproteinases in the cardiovascular effects produced by nicotine
    • Jacob-Ferreira AL, Palei AC, Cau SB, et al. Evidence for the involvement of matrix metalloproteinases in the cardiovascular effects produced by nicotine. Eur J Pharmacol 2010; 627(1-3): 216-22.
    • (2010) Eur J Pharmacol , vol.627 , Issue.1-3 , pp. 216-222
    • Jacob-Ferreira, A.L.1    Palei, A.C.2    Cau, S.B.3
  • 290
    • 63349099519 scopus 로고    scopus 로고
    • Antioxidant treatment reduces matrix metalloproteinase-2-induced vascular changes in renovascular hypertension
    • Castro MM, Rizzi E, Rodrigues GJ, et al. Antioxidant treatment reduces matrix metalloproteinase-2-induced vascular changes in renovascular hypertension. Free Radic Biol Med 2009; 46(9): 1298-307.
    • (2009) Free Radic Biol Med , vol.46 , Issue.9 , pp. 1298-1307
    • Castro, M.M.1    Rizzi, E.2    Rodrigues, G.J.3
  • 291
    • 33747871452 scopus 로고    scopus 로고
    • Tumor-derived matrix metalloproteinase-1 targets endothelial proteinase-activated receptor 1 promoting endothelial cell activation
    • Goerge T, Barg A, Schnaeker EM, et al. Tumor-derived matrix metalloproteinase-1 targets endothelial proteinase-activated receptor 1 promoting endothelial cell activation. Cancer Res 2006; 66(15): 7766-74.
    • (2006) Cancer Res , vol.66 , Issue.15 , pp. 7766-7774
    • Goerge, T.1    Barg, A.2    Schnaeker, E.M.3
  • 292
    • 58849101696 scopus 로고    scopus 로고
    • Endothelial nitric oxide deficiency reduces MMP-13-mediated cleavage of ICAM-1 in vascular endothelium: A role in atherosclerosis
    • Tarin C, Gomez M, Calvo E, Lopez JA, Zaragoza C. Endothelial nitric oxide deficiency reduces MMP-13-mediated cleavage of ICAM-1 in vascular endothelium: a role in atherosclerosis. Arterioscler Thromb Vasc Biol 2009; 29(1): 27-32.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , Issue.1 , pp. 27-32
    • Tarin, C.1    Gomez, M.2    Calvo, E.3    Lopez, J.A.4    Zaragoza, C.5
  • 293
    • 24344450341 scopus 로고    scopus 로고
    • Histopathological changes and expression of adhesion molecules and laminin in varicose veins
    • Aunapuu M, Arend A. Histopathological changes and expression of adhesion molecules and laminin in varicose veins. Vasa 2005; 34(3): 170-5.
    • (2005) Vasa , vol.34 , Issue.3 , pp. 170-175
    • Aunapuu, M.1    Arend, A.2
  • 294
    • 77955468508 scopus 로고    scopus 로고
    • HIV-1 gp120-induced injury to the blood-brain barrier: Role of metalloproteinases 2 and 9 and relationship to oxidative stress
    • Louboutin JP, Agrawal L, Reyes BA, Van Bockstaele EJ, Strayer DS. HIV-1 gp120-induced injury to the blood-brain barrier: role of metalloproteinases 2 and 9 and relationship to oxidative stress. J Neuropathol Exp Neurol 2010; 69(8): 801-16.
    • (2010) J Neuropathol Exp Neurol , vol.69 , Issue.8 , pp. 801-816
    • Louboutin, J.P.1    Agrawal, L.2    Reyes, B.A.3    van Bockstaele, E.J.4    Strayer, D.S.5
  • 295
    • 77955982672 scopus 로고    scopus 로고
    • Regulation of the blood-brain barrier integrity by pericytes via matrix metalloproteinases mediated activation of vascular endothelial growth factor in vitro
    • Thanabalasundaram G, Pieper C, Lischper M, Galla HJ. Regulation of the blood-brain barrier integrity by pericytes via matrix metalloproteinases mediated activation of vascular endothelial growth factor in vitro. Brain Res 2010; 1347: 1-10.
    • (2010) Brain Res , vol.1347 , pp. 1-10
    • Thanabalasundaram, G.1    Pieper, C.2    Lischper, M.3    Galla, H.J.4
  • 296
    • 77950048543 scopus 로고    scopus 로고
    • Metalloproteinase mediated occludin cleavage in the cerebral microcapillary endothelium under pathological conditions
    • Lischper M, Beuck S, Thanabalasundaram G, Pieper C, Galla HJ. Metalloproteinase mediated occludin cleavage in the cerebral microcapillary endothelium under pathological conditions. Brain Res 2010; 1326: 114-27.
    • (2010) Brain Res , vol.1326 , pp. 114-127
    • Lischper, M.1    Beuck, S.2    Thanabalasundaram, G.3    Pieper, C.4    Galla, H.J.5
  • 297
    • 0018907307 scopus 로고
    • Value of graduated compression stockings in deep venous insufficiency
    • Horner J, Fernandes J, Fernandes E, Nicolaides AN. Value of graduated compression stockings in deep venous insufficiency. Br Med J 1980; 280(6217): 820-1.
    • (1980) Br Med J , vol.280 , Issue.6217 , pp. 820-821
    • Horner, J.1    Fernandes, J.2    Fernandes, E.3    Nicolaides, A.N.4
  • 298
    • 0028140327 scopus 로고
    • Graduated compression stockings in the prevention of postoperative venous thromboembolism. A meta-analysis
    • Wells PS, Lensing AW, Hirsh J. Graduated compression stockings in the prevention of postoperative venous thromboembolism. A meta-analysis. Arch Intern Med 1994; 154(1): 67-72.
    • (1994) Arch Intern Med , vol.154 , Issue.1 , pp. 67-72
    • Wells, P.S.1    Lensing, A.W.2    Hirsh, J.3
  • 299
    • 0033511901 scopus 로고    scopus 로고
    • Evaluation of therapeutic compression stockings in the treatment of chronic venous insufficiency
    • Motykie GD, Caprini JA, Arcelus JI, Reyna JJ, Overom E, Mokhtee D. Evaluation of therapeutic compression stockings in the treatment of chronic venous insufficiency. Dermatol Surg 1999; 25(2): 116-20.
    • (1999) Dermatol Surg , vol.25 , Issue.2 , pp. 116-120
    • Motykie, G.D.1    Caprini, J.A.2    Arcelus, J.I.3    Reyna, J.J.4    Overom, E.5    Mokhtee, D.6
  • 300
    • 4644288189 scopus 로고    scopus 로고
    • Prevention of venous thromboembolism: The Seventh ACCP Conference on Antithrombotic and Thrombolytic Therapy
    • Geerts WH, Pineo GF, Heit JA, et al. Prevention of venous thromboembolism: the Seventh ACCP Conference on Antithrombotic and Thrombolytic Therapy. Chest 2004; 126(3 Suppl): 338S-400S.
    • (2004) Chest , vol.126 , Issue.3 SUPPL.
    • Geerts, W.H.1    Pineo, G.F.2    Heit, J.A.3
  • 301
    • 84925223500 scopus 로고    scopus 로고
    • Elastic compression stockings for prevention of deep vein thrombosis
    • Amaragiri SV, Lees TA. Elastic compression stockings for prevention of deep vein thrombosis. Cochrane Database Syst Rev 2000; (3): CD001484.
    • (2000) Cochrane Database Syst Rev , Issue.3
    • Amaragiri, S.V.1    Lees, T.A.2
  • 302
    • 0026029590 scopus 로고
    • The influence of elastic compression stockings on deep venous hemodynamics
    • discussion 9-100
    • Mayberry JC, Moneta GL, DeFrang RD, Porter JM. The influence of elastic compression stockings on deep venous hemodynamics. J Vasc Surg 1991; 13(1): 91-9; discussion 9-100.
    • (1991) J Vasc Surg , vol.13 , Issue.1 , pp. 91-99
    • Mayberry, J.C.1    Moneta, G.L.2    DeFrang, R.D.3    Porter, J.M.4
  • 303
    • 0037323468 scopus 로고    scopus 로고
    • Effect of elastic compression stockings on venous hemodynamics during walking
    • Ibegbuna V, Delis KT, Nicolaides AN, Aina O. Effect of elastic compression stockings on venous hemodynamics during walking. J Vasc Surg 2003; 37(2): 420-5.
    • (2003) J Vasc Surg , vol.37 , Issue.2 , pp. 420-425
    • Ibegbuna, V.1    Delis, K.T.2    Nicolaides, A.N.3    Aina, O.4
  • 304
    • 25444496749 scopus 로고    scopus 로고
    • Chronic venous insufficiency and the therapeutic effects of Daflon 500 mg
    • Bergan JJ. Chronic venous insufficiency and the therapeutic effects of Daflon 500 mg. Angiology 2005; 56 Suppl 1: S21-4.
    • (2005) Angiology , vol.56 , Issue.SUPPL. 1
    • Bergan, J.J.1
  • 305
    • 0036625649 scopus 로고    scopus 로고
    • Pharmacological targets of drugs employed in chronic venous and lymphatic insufficiency
    • Boisseau MR. Pharmacological targets of drugs employed in chronic venous and lymphatic insufficiency. Int Angiol 2002; 21(2 Suppl 1): 33-9.
    • (2002) Int Angiol , vol.21 , Issue.2 SUPPL. 1 , pp. 33-39
    • Boisseau, M.R.1
  • 306
    • 34249329866 scopus 로고    scopus 로고
    • Endothelium protectant and contractile effects of the antivaricose principle escin in rat aorta
    • Carrasco OF, Vidrio H. Endothelium protectant and contractile effects of the antivaricose principle escin in rat aorta. Vascul Pharmacol 2007; 47(1): 68-73.
    • (2007) Vascul Pharmacol , vol.47 , Issue.1 , pp. 68-73
    • Carrasco, O.F.1    Vidrio, H.2
  • 307
    • 79961165994 scopus 로고    scopus 로고
    • Ca(2+)-dependent contraction by the saponoside escin in rat vena cava: Implications in venotonic treatment of varicose veins
    • Raffetto JD, Khalil RA. Ca(2+)-dependent contraction by the saponoside escin in rat vena cava: implications in venotonic treatment of varicose veins. J Vasc Surg 2011; 54(2): 489-96.
    • (2011) J Vasc Surg , vol.54 , Issue.2 , pp. 489-496
    • Raffetto, J.D.1    Khalil, R.A.2
  • 308
    • 0031300139 scopus 로고    scopus 로고
    • Evaluation of haemorheological and microcirculatory disturbances in chronic venous insufficiency: Activity of Daflon 500 mg
    • Le Devehat C, Khodabandehlou T, Vimeux M, Kempf C. Evaluation of haemorheological and microcirculatory disturbances in chronic venous insufficiency: activity of Daflon 500 mg. Int J Microcirc Clin Exp 1997; 17 Suppl 1: 27-33.
    • (1997) Int J Microcirc Clin Exp , vol.17 , Issue.SUPPL. 1 , pp. 27-33
    • Le Devehat, C.1    Khodabandehlou, T.2    Vimeux, M.3    Kempf, C.4
  • 309
    • 33645740058 scopus 로고    scopus 로고
    • Venoruton vs Daflon: Evaluation of effects on quality of life in chronic venous insufficiency
    • Cesarone MR, Belcaro G, Pellegrini L, et al. Venoruton vs Daflon: evaluation of effects on quality of life in chronic venous insufficiency. Angiology 2006; 57(2): 131-8.
    • (2006) Angiology , vol.57 , Issue.2 , pp. 131-138
    • Cesarone, M.R.1    Belcaro, G.2    Pellegrini, L.3
  • 310
    • 33645705224 scopus 로고    scopus 로고
    • Circulating endothelial cells in venous blood as a marker of endothelial damage in chronic venous insufficiency: Improvement with venoruton
    • Cesarone MR, Belcaro G, Pellegrini L, et al. Circulating endothelial cells in venous blood as a marker of endothelial damage in chronic venous insufficiency: improvement with venoruton. J Cardiovasc Pharmacol Ther 2006; 11(1): 93-8.
    • (2006) J Cardiovasc Pharmacol Ther , vol.11 , Issue.1 , pp. 93-98
    • Cesarone, M.R.1    Belcaro, G.2    Pellegrini, L.3
  • 311
    • 0032900891 scopus 로고    scopus 로고
    • Increase in circulating endothelial cells in patients with primary chronic venous insufficiency: Protective effect of Ginkor Fort in a randomized double-blind, placebo-controlled clinical trial
    • Janssens D, Michiels C, Guillaume G, Cuisinier B, Louagie Y, Remacle J. Increase in circulating endothelial cells in patients with primary chronic venous insufficiency: protective effect of Ginkor Fort in a randomized double-blind, placebo-controlled clinical trial. J Cardiovasc Pharmacol 1999; 33(1): 7-11.
    • (1999) J Cardiovasc Pharmacol , vol.33 , Issue.1 , pp. 7-11
    • Janssens, D.1    Michiels, C.2    Guillaume, G.3    Cuisinier, B.4    Louagie, Y.5    Remacle, J.6
  • 312
    • 0028243209 scopus 로고
    • Controlled studies of Daflon 500 mg in chronic venous insufficiency
    • Geroulakos G, Nicolaides AN. Controlled studies of Daflon 500 mg in chronic venous insufficiency. Angiology 1994; 45(6 Pt 2): 549-53.
    • (1994) Angiology , vol.45 , Issue.6 PART 2 , pp. 549-553
    • Geroulakos, G.1    Nicolaides, A.N.2
  • 313
    • 77954818134 scopus 로고    scopus 로고
    • The efficacy and safety of a coumarin-/troxerutin-combination (SB-LOT) in patients with chronic venous insufficiency: A double blind placebocontrolled randomised study
    • Vanscheidt W, Rabe E, Naser-Hijazi B, et al. The efficacy and safety of a coumarin-/troxerutin-combination (SB-LOT) in patients with chronic venous insufficiency: a double blind placebocontrolled randomised study. Vasa 2002; 31(3): 185-90.
    • (2002) Vasa , vol.31 , Issue.3 , pp. 185-190
    • Vanscheidt, W.1    Rabe, E.2    Naser-Hijazi, B.3
  • 314
    • 0038048009 scopus 로고    scopus 로고
    • Efficacy of a 6-month treatment with Daflon 500 mg in patients with venous leg ulcers associated with chronic venous insufficiency
    • Roztocil K, Stvrtinova V, Strejcek J. Efficacy of a 6-month treatment with Daflon 500 mg in patients with venous leg ulcers associated with chronic venous insufficiency. Int Angiol 2003; 22(1): 24-31.
    • (2003) Int Angiol , vol.22 , Issue.1 , pp. 24-31
    • Roztocil, K.1    Stvrtinova, V.2    Strejcek, J.3
  • 315
    • 0036941577 scopus 로고    scopus 로고
    • Efficacy, routine effectiveness, and safety of horsechestnut seed extract in the treatment of chronic venous insufficiency. A meta-analysis of randomized controlled trials and large observational studies
    • Siebert U, Brach M, Sroczynski G, Berla K. Efficacy, routine effectiveness, and safety of horsechestnut seed extract in the treatment of chronic venous insufficiency. A meta-analysis of randomized controlled trials and large observational studies. Int Angiol 2002; 21(4): 305-15.
    • (2002) Int Angiol , vol.21 , Issue.4 , pp. 305-315
    • Siebert, U.1    Brach, M.2    Sroczynski, G.3    Berla, K.4
  • 316
    • 84872195490 scopus 로고    scopus 로고
    • Horse chestnut seed extract for chronic venous insufficiency
    • Pittler MH, Ernst E. Horse chestnut seed extract for chronic venous insufficiency. Cochrane Database Syst Rev 2006; (1): CD003230.
    • (2006) Cochrane Database Syst Rev , Issue.1
    • Pittler, M.H.1    Ernst, E.2
  • 317
    • 0032820043 scopus 로고    scopus 로고
    • Systemic treatment of venous leg ulcers with high doses of pentoxifylline: Efficacy in a randomized, placebo-controlled trial
    • Falanga V, Fujitani RM, Diaz C, et al. Systemic treatment of venous leg ulcers with high doses of pentoxifylline: efficacy in a randomized, placebo-controlled trial. Wound Repair Regen 1999; 7(4): 208-13.
    • (1999) Wound Repair Regen , vol.7 , Issue.4 , pp. 208-213
    • Falanga, V.1    Fujitani, R.M.2    Diaz, C.3
  • 318
    • 0036173177 scopus 로고    scopus 로고
    • Treatment of venous ulcers with pentoxifylline: A 6-month randomized, double-blind, placebo controlled trial
    • Belcaro G, Cesarone MR, Nicolaides AN, De Sanctis MT, Incandela L, Geroulakos G. Treatment of venous ulcers with pentoxifylline: a 6-month randomized, double-blind, placebo controlled trial. Angiology 2002; 53 Suppl 1: S45-7.
    • (2002) Angiology , vol.53 , Issue.SUPPL. 1
    • Belcaro, G.1    Cesarone, M.R.2    Nicolaides, A.N.3    de Sanctis, M.T.4    Incandela, L.5    Geroulakos, G.6
  • 319
    • 2342553510 scopus 로고    scopus 로고
    • Improvement of cutaneous microcirculation and oxygen supply in patients with chronic venous insufficiency by orally administered extract of red vine leaves AS 195: A randomised, doubleblind, placebo-controlled, crossover study
    • Kalus U, Koscielny J, Grigorov A, Schaefer E, Peil H, Kiesewetter H. Improvement of cutaneous microcirculation and oxygen supply in patients with chronic venous insufficiency by orally administered extract of red vine leaves AS 195: a randomised, doubleblind, placebo-controlled, crossover study. Drugs R D 2004; 5(2): 63-71.
    • (2004) Drugs R D , vol.5 , Issue.2 , pp. 63-71
    • Kalus, U.1    Koscielny, J.2    Grigorov, A.3    Schaefer, E.4    Peil, H.5    Kiesewetter, H.6
  • 320
    • 23744499621 scopus 로고    scopus 로고
    • Efficacy of the treatment with prostaglandin E-1 in venous ulcers of the lower limbs
    • Milio G, Mina C, Cospite V, Almasio PL, Novo S. Efficacy of the treatment with prostaglandin E-1 in venous ulcers of the lower limbs. J Vasc Surg 2005; 42(2): 304-8.
    • (2005) J Vasc Surg , vol.42 , Issue.2 , pp. 304-308
    • Milio, G.1    Mina, C.2    Cospite, V.3    Almasio, P.L.4    Novo, S.5
  • 321
    • 2442706775 scopus 로고    scopus 로고
    • Efficacy of sclerotherapy in varicose veins--prospective, blinded, placebo-controlled study
    • discussion 8
    • Kahle B, Leng K. Efficacy of sclerotherapy in varicose veins--prospective, blinded, placebo-controlled study. Dermatol Surg 2004; 30(5): 723-8; discussion 8.
    • (2004) Dermatol Surg , vol.30 , Issue.5 , pp. 723-728
    • Kahle, B.1    Leng, K.2
  • 322
    • 2442666762 scopus 로고    scopus 로고
    • European Consensus Meeting on Foam Sclerotherapy, April, 4-6, 2003, Tegernsee, Germany
    • discussion 17
    • Breu FX, Guggenbichler S. European Consensus Meeting on Foam Sclerotherapy, April, 4-6, 2003, Tegernsee, Germany. Dermatol Surg 2004; 30(5): 709-17; discussion 17.
    • (2004) Dermatol Surg , vol.30 , Issue.5 , pp. 709-717
    • Breu, F.X.1    Guggenbichler, S.2
  • 323
    • 0036154853 scopus 로고    scopus 로고
    • Sclerosing foam in the treatment of varicose veins and telangiectases: History and analysis of safety and complications
    • Frullini A, Cavezzi A. Sclerosing foam in the treatment of varicose veins and telangiectases: history and analysis of safety and complications. Dermatol Surg 2002; 28(1): 11-5.
    • (2002) Dermatol Surg , vol.28 , Issue.1 , pp. 11-15
    • Frullini, A.1    Cavezzi, A.2
  • 324
    • 2042517547 scopus 로고    scopus 로고
    • The history of sclerosing foams
    • discussion
    • Wollmann JC. The history of sclerosing foams. Dermatol Surg 2004; 30(5): 694-703; discussion
    • (2004) Dermatol Surg , vol.30 , Issue.5 , pp. 694-703
    • Wollmann, J.C.1
  • 325
    • 0036546892 scopus 로고    scopus 로고
    • Endovenous treatment of the greater saphenous vein with a 940-nm diode laser: Thrombotic occlusion after endoluminal thermal damage by laser-generated steam bubbles
    • Proebstle TM, Lehr HA, Kargl A, et al. Endovenous treatment of the greater saphenous vein with a 940-nm diode laser: thrombotic occlusion after endoluminal thermal damage by laser-generated steam bubbles. J Vasc Surg 2002; 35(4): 729-36.
    • (2002) J Vasc Surg , vol.35 , Issue.4 , pp. 729-736
    • Proebstle, T.M.1    Lehr, H.A.2    Kargl, A.3
  • 326
    • 33745907791 scopus 로고    scopus 로고
    • The first 1000 cases of Italian Endovenous-laser Working Group (IEWG). Rationale, and long-term outcomes for the 1999-2003 period
    • Agus GB, Mancini S, Magi G. The first 1000 cases of Italian Endovenous-laser Working Group (IEWG). Rationale, and long-term outcomes for the 1999-2003 period. Int Angiol 2006; 25(2): 209-15.
    • (2006) Int Angiol , vol.25 , Issue.2 , pp. 209-215
    • Agus, G.B.1    Mancini, S.2    Magi, G.3
  • 327
    • 0042068171 scopus 로고    scopus 로고
    • Endovenous laser treatment of saphenous vein reflux: Long-term results
    • Min RJ, Khilnani N, Zimmet SE. Endovenous laser treatment of saphenous vein reflux: long-term results. J Vasc Interv Radiol 2003; 14(8): 991-6.
    • (2003) J Vasc Interv Radiol , vol.14 , Issue.8 , pp. 991-996
    • Min, R.J.1    Khilnani, N.2    Zimmet, S.E.3
  • 328
    • 15044341487 scopus 로고    scopus 로고
    • Four-year follow-up on endovascular radiofrequency obliteration of great saphenous reflux
    • Merchant RF, Pichot O, Myers KA. Four-year follow-up on endovascular radiofrequency obliteration of great saphenous reflux. Dermatol Surg 2005; 31(2): 129-34.
    • (2005) Dermatol Surg , vol.31 , Issue.2 , pp. 129-134
    • Merchant, R.F.1    Pichot, O.2    Myers, K.A.3
  • 329
    • 0027932654 scopus 로고
    • Stripping of the long saphenous vein in the treatment of primary varicose veins
    • Sarin S, Scurr JH, Coleridge Smith PD. Stripping of the long saphenous vein in the treatment of primary varicose veins. Br J Surg 1994; 81(10): 1455-8.
    • (1994) Br J Surg , vol.81 , Issue.10 , pp. 1455-1458
    • Sarin, S.1    Scurr, J.H.2    Coleridge Smith, P.D.3
  • 330
    • 9144249634 scopus 로고    scopus 로고
    • Prospective randomized controlled trial: Conventional versus powered phlebectomy
    • Aremu MA, Mahendran B, Butcher W, et al. Prospective randomized controlled trial: conventional versus powered phlebectomy. J Vasc Surg 2004; 39(1): 88-94.
    • (2004) J Vasc Surg , vol.39 , Issue.1 , pp. 88-94
    • Aremu, M.A.1    Mahendran, B.2    Butcher, W.3
  • 331
    • 2942525459 scopus 로고    scopus 로고
    • Comparison of surgery and compression with compression alone in chronic venous ulceration (ESCHAR study): Randomised controlled trial
    • Barwell JR, Davies CE, Deacon J, et al. Comparison of surgery and compression with compression alone in chronic venous ulceration (ESCHAR study): randomised controlled trial. Lancet 2004; 363(9424): 1854-9.
    • (2004) Lancet , vol.363 , Issue.9424 , pp. 1854-1859
    • Barwell, J.R.1    Davies, C.E.2    Deacon, J.3
  • 332
    • 14544300624 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: A review on pharmacophore mapping and (Q)SARs results
    • Kontogiorgis CA, Papaioannou P, Hadjipavlou-Litina DJ. Matrix metalloproteinase inhibitors: a review on pharmacophore mapping and (Q)SARs results. Curr Med Chem 2005; 12(3): 339-55.
    • (2005) Curr Med Chem , vol.12 , Issue.3 , pp. 339-355
    • Kontogiorgis, C.A.1    Papaioannou, P.2    Hadjipavlou-Litina, D.J.3
  • 333
    • 34447520043 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
    • Hu J, Van den Steen PE, Sang QX, Opdenakker G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nat Rev Drug Discov 2007; 6(6): 480-98.
    • (2007) Nat Rev Drug Discov , vol.6 , Issue.6 , pp. 480-498
    • Hu, J.1    van den Steen, P.E.2    Sang, Q.X.3    Opdenakker, G.4
  • 334
    • 0025944065 scopus 로고
    • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
    • Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJ. The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry 1991; 30(33): 8097-102.
    • (1991) Biochemistry , vol.30 , Issue.33 , pp. 8097-8102
    • Murphy, G.1    Houbrechts, A.2    Cockett, M.I.3    Williamson, R.A.4    O'Shea, M.5    Docherty, A.J.6
  • 335
    • 0025341267 scopus 로고
    • Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)
    • Williamson RA, Marston FA, Angal S, et al. Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP). Biochem J 1990; 268(2): 267-74.
    • (1990) Biochem J , vol.268 , Issue.2 , pp. 267-274
    • Williamson, R.A.1    Marston, F.A.2    Angal, S.3
  • 336
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker AH, Edwards DR, Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J Cell Sci 2002; 115(Pt 19): 3719-27.
    • (2002) J Cell Sci , vol.115 , Issue.PART 19 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 337
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3
    • Will H, Atkinson SJ, Butler GS, Smith B, Murphy G. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J Biol Chem 1996; 271(29): 17119-23.
    • (1996) J Biol Chem , vol.271 , Issue.29 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 338
    • 0034685834 scopus 로고    scopus 로고
    • The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3
    • Amour A, Knight CG, Webster A, et al. The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett 2000; 473(3): 275-9.
    • (2000) FEBS Lett , vol.473 , Issue.3 , pp. 275-279
    • Amour, A.1    Knight, C.G.2    Webster, A.3
  • 339
    • 38849148339 scopus 로고    scopus 로고
    • Catalytic properties of ADAM12 and its domain deletion mutants
    • Jacobsen J, Visse R, Sorensen HP, et al. Catalytic properties of ADAM12 and its domain deletion mutants. Biochemistry 2008; 47(2): 537-47.
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 537-547
    • Jacobsen, J.1    Visse, R.2    Sorensen, H.P.3
  • 340
    • 0035918309 scopus 로고    scopus 로고
    • TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5)
    • Kashiwagi M, Tortorella M, Nagase H, Brew K. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). J Biol Chem 2001; 276(16): 12501-4.
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 12501-12504
    • Kashiwagi, M.1    Tortorella, M.2    Nagase, H.3    Brew, K.4
  • 341
    • 0036295493 scopus 로고    scopus 로고
    • ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors
    • Rodriguez-Manzaneque JC, Westling J, Thai SN, et al. ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors. Biochem Biophys Res Commun 2002; 293(1): 501-8.
    • (2002) Biochem Biophys Res Commun , vol.293 , Issue.1 , pp. 501-508
    • Rodriguez-Manzaneque, J.C.1    Westling, J.2    Thai, S.N.3
  • 342
    • 0034833362 scopus 로고    scopus 로고
    • Spontaneous air space enlargement in the lungs of mice lacking tissue inhibitor of metalloproteinases-3 (TIMP-3)
    • Leco KJ, Waterhouse P, Sanchez OH, et al. Spontaneous air space enlargement in the lungs of mice lacking tissue inhibitor of metalloproteinases-3 (TIMP-3). J Clin Invest 2001; 108(6): 817-29.
    • (2001) J Clin Invest , vol.108 , Issue.6 , pp. 817-829
    • Leco, K.J.1    Waterhouse, P.2    Sanchez, O.H.3
  • 343
    • 0034823461 scopus 로고    scopus 로고
    • Accelerated apoptosis in the Timp-3-deficient mammary gland
    • Fata JE, Leco KJ, Voura EB, et al. Accelerated apoptosis in the Timp-3-deficient mammary gland. J Clin Invest 2001; 108(6): 831-41.
    • (2001) J Clin Invest , vol.108 , Issue.6 , pp. 831-841
    • Fata, J.E.1    Leco, K.J.2    Voura, E.B.3
  • 344
    • 84860868139 scopus 로고    scopus 로고
    • Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: Binding studies and crystal structure
    • Batra J, Robinson J, Soares AS, Fields AP, Radisky DC, Radisky ES. Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure. J Biol Chem 2012; 287(19): 15935-46.
    • (2012) J Biol Chem , vol.287 , Issue.19 , pp. 15935-15946
    • Batra, J.1    Robinson, J.2    Soares, A.S.3    Fields, A.P.4    Radisky, D.C.5    Radisky, E.S.6
  • 345
    • 0033538059 scopus 로고    scopus 로고
    • Residue 2 of TIMP-1 is a major determinant of affinity and specificity for matrix metalloproteinases but effects of substitutions do not correlate with those of the corresponding P1' residue of substrate
    • Meng Q, Malinovskii V, Huang W, et al. Residue 2 of TIMP-1 is a major determinant of affinity and specificity for matrix metalloproteinases but effects of substitutions do not correlate with those of the corresponding P1' residue of substrate. J Biol Chem 1999; 274(15): 10184-9.
    • (1999) J Biol Chem , vol.274 , Issue.15 , pp. 10184-10189
    • Meng, Q.1    Malinovskii, V.2    Huang, W.3
  • 346
    • 33847007324 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1
    • Iyer S, Wei S, Brew K, Acharya KR. Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1. J Biol Chem 2007; 282(1): 364-71.
    • (2007) J Biol Chem , vol.282 , Issue.1 , pp. 364-371
    • Iyer, S.1    Wei, S.2    Brew, K.3    Acharya, K.R.4
  • 347
    • 0031050409 scopus 로고    scopus 로고
    • The catalytic domain of activated collagenase I (MMP-1) is absolutely required for interaction with its specific inhibitor, tissue inhibitor of metalloproteinases-1 (TIMP-1)
    • Vallon R, Muller R, Moosmayer D, Gerlach E, Angel P. The catalytic domain of activated collagenase I (MMP-1) is absolutely required for interaction with its specific inhibitor, tissue inhibitor of metalloproteinases-1 (TIMP-1). Eur J Biochem 1997; 244(1): 81-8.
    • (1997) Eur J Biochem , vol.244 , Issue.1 , pp. 81-88
    • Vallon, R.1    Muller, R.2    Moosmayer, D.3    Gerlach, E.4    Angel, P.5
  • 348
    • 0025080835 scopus 로고
    • Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor
    • Strickland DK, Ashcom JD, Williams S, Burgess WH, Migliorini M, Argraves WS. Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor. J Biol Chem 1990; 265(29): 17401-4.
    • (1990) J Biol Chem , vol.265 , Issue.29 , pp. 17401-17404
    • Strickland, D.K.1    Ashcom, J.D.2    Williams, S.3    Burgess, W.H.4    Migliorini, M.5    Argraves, W.S.6
  • 349
    • 0038052349 scopus 로고    scopus 로고
    • Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase A
    • Higashi S, Miyazaki K. Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase A. Biochemistry 2003; 42(21): 6514-26.
    • (2003) Biochemistry , vol.42 , Issue.21 , pp. 6514-6526
    • Higashi, S.1    Miyazaki, K.2
  • 350
    • 0033955104 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor
    • Mott JD, Thomas CL, Rosenbach MT, Takahara K, Greenspan DS, Banda MJ. Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor. J Biol Chem 2000; 275(2): 1384-90.
    • (2000) J Biol Chem , vol.275 , Issue.2 , pp. 1384-1390
    • Mott, J.D.1    Thomas, C.L.2    Rosenbach, M.T.3    Takahara, K.4    Greenspan, D.S.5    Banda, M.J.6
  • 351
    • 0035023342 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor-2 is a novel inhibitor of matrix metalloproteinases with implications for atherosclerosis
    • Herman MP, Sukhova GK, Kisiel W, et al. Tissue factor pathway inhibitor-2 is a novel inhibitor of matrix metalloproteinases with implications for atherosclerosis. J Clin Invest 2001; 107(9): 1117-26.
    • (2001) J Clin Invest , vol.107 , Issue.9 , pp. 1117-1126
    • Herman, M.P.1    Sukhova, G.K.2    Kisiel, W.3
  • 352
    • 52949084668 scopus 로고    scopus 로고
    • Progress in matrix metalloproteinase research
    • Murphy G, Nagase H. Progress in matrix metalloproteinase research. Mol Aspects Med 2008; 29(5): 290-308.
    • (2008) Mol Aspects Med , vol.29 , Issue.5 , pp. 290-308
    • Murphy, G.1    Nagase, H.2
  • 353
    • 14044274265 scopus 로고    scopus 로고
    • Recent developments in the design of specific Matrix Metalloproteinase inhibitors aided by structural and computational studies
    • Rao BG. Recent developments in the design of specific Matrix Metalloproteinase inhibitors aided by structural and computational studies. Curr Pharm Des 2005; 11(3): 295-322.
    • (2005) Curr Pharm Des , vol.11 , Issue.3 , pp. 295-322
    • Rao, B.G.1
  • 354
    • 77149131528 scopus 로고    scopus 로고
    • To bind zinc or not to bind zinc: An examination of innovative approaches to improved metalloproteinase inhibition
    • Jacobsen JA, Major Jourden JL, Miller MT, Cohen SM. To bind zinc or not to bind zinc: an examination of innovative approaches to improved metalloproteinase inhibition. Biochim Biophys Acta 2010; 1803(1): 72-94.
    • (2010) Biochim Biophys Acta , vol.1803 , Issue.1 , pp. 72-94
    • Jacobsen, J.A.1    Major Jourden, J.L.2    Miller, M.T.3    Cohen, S.M.4
  • 355
    • 4444347179 scopus 로고    scopus 로고
    • Quest for selectivity in inhibition of matrix metalloproteinases
    • Brown S, Meroueh SO, Fridman R, Mobashery S. Quest for selectivity in inhibition of matrix metalloproteinases. Curr Top Med Chem 2004; 4(12): 1227-38.
    • (2004) Curr Top Med Chem , vol.4 , Issue.12 , pp. 1227-1238
    • Brown, S.1    Meroueh, S.O.2    Fridman, R.3    Mobashery, S.4
  • 357
    • 2542530041 scopus 로고    scopus 로고
    • Sultam hydroxamates as novel matrix metalloproteinase inhibitors
    • Cherney RJ, Mo R, Meyer DT, et al. Sultam hydroxamates as novel matrix metalloproteinase inhibitors. J Med Chem 2004; 47(12): 2981-3.
    • (2004) J Med Chem , vol.47 , Issue.12 , pp. 2981-2983
    • Cherney, R.J.1    Mo, R.2    Meyer, D.T.3
  • 358
    • 33745152754 scopus 로고    scopus 로고
    • Design and synthesis of novel metalloproteinase inhibitors
    • Nakatani S, Ikura M, Yamamoto S, et al. Design and synthesis of novel metalloproteinase inhibitors. Bioorg Med Chem 2006; 14(15): 5402-22.
    • (2006) Bioorg Med Chem , vol.14 , Issue.15 , pp. 5402-5422
    • Nakatani, S.1    Ikura, M.2    Yamamoto, S.3
  • 359
    • 20244383477 scopus 로고    scopus 로고
    • A new development of matrix metalloproteinase inhibitors: Twin hydroxamic acids as potent inhibitors of MMPs
    • Rossello A, Nuti E, Catalani MP, et al. A new development of matrix metalloproteinase inhibitors: twin hydroxamic acids as potent inhibitors of MMPs. Bioorg Med Chem Lett 2005; 15(9): 2311-4.
    • (2005) Bioorg Med Chem Lett , vol.15 , Issue.9 , pp. 2311-2314
    • Rossello, A.1    Nuti, E.2    Catalani, M.P.3
  • 362
    • 15244342010 scopus 로고    scopus 로고
    • Matrix metalloproteinases as therapeutic targets in cancer
    • Vihinen P, Ala-aho R, Kahari VM. Matrix metalloproteinases as therapeutic targets in cancer. Curr Cancer Drug Targets 2005; 5(3): 203-20.
    • (2005) Curr Cancer Drug Targets , vol.5 , Issue.3 , pp. 203-220
    • Vihinen, P.1    Ala-aho, R.2    Kahari, V.M.3
  • 363
    • 36849073658 scopus 로고    scopus 로고
    • MMPs as therapeutic targets--still a viable option?
    • Fingleton B. MMPs as therapeutic targets--still a viable option? Semin Cell Dev Biol 2008; 19(1): 61-8.
    • (2008) Semin Cell Dev Biol , vol.19 , Issue.1 , pp. 61-68
    • Fingleton, B.1
  • 364
    • 15244355692 scopus 로고    scopus 로고
    • Hydroxamatebased peptide inhibitors of matrix metalloprotease 2
    • Jani M, Tordai H, Trexler M, Banyai L, Patthy L. Hydroxamatebased peptide inhibitors of matrix metalloprotease 2. Biochimie 2005; 87(3-4): 385-92.
    • (2005) Biochimie , vol.87 , Issue.3-4 , pp. 385-392
    • Jani, M.1    Tordai, H.2    Trexler, M.3    Banyai, L.4    Patthy, L.5
  • 365
    • 0038146970 scopus 로고    scopus 로고
    • Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2)
    • Trexler M, Briknarova K, Gehrmann M, Llinas M, Patthy L. Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2). J Biol Chem 2003; 278(14): 12241-6.
    • (2003) J Biol Chem , vol.278 , Issue.14 , pp. 12241-12246
    • Trexler, M.1    Briknarova, K.2    Gehrmann, M.3    Llinas, M.4    Patthy, L.5
  • 366
    • 0034609778 scopus 로고    scopus 로고
    • Carbonic anhydrase and matrix metalloproteinase inhibitors: Sulfonylated amino acid hydroxamates with MMP inhibitory properties act as efficient inhibitors of CA isozymes I, II, and IV, and N-hydroxysulfonamides inhibit both these zinc enzymes
    • Scozzafava A, Supuran CT. Carbonic anhydrase and matrix metalloproteinase inhibitors: sulfonylated amino acid hydroxamates with MMP inhibitory properties act as efficient inhibitors of CA isozymes I, II, and IV, and N-hydroxysulfonamides inhibit both these zinc enzymes. J Med Chem 2000; 43(20): 3677-87.
    • (2000) J Med Chem , vol.43 , Issue.20 , pp. 3677-3687
    • Scozzafava, A.1    Supuran, C.T.2
  • 367
    • 12444254805 scopus 로고    scopus 로고
    • Acetylenic TACE inhibitors. Part 1. SAR of the acyclic sulfonamide hydroxamates
    • Levin JI, Chen JM, Cheung K, et al. Acetylenic TACE inhibitors. Part 1. SAR of the acyclic sulfonamide hydroxamates. Bioorg Med Chem Lett 2003; 13(16): 2799-803.
    • (2003) Bioorg Med Chem Lett , vol.13 , Issue.16 , pp. 2799-2803
    • Levin, J.I.1    Chen, J.M.2    Cheung, K.3
  • 368
    • 30344439523 scopus 로고    scopus 로고
    • Conversion of potent MMP inhibitors into selective TACE inhibitors
    • Cherney RJ, King BW, Gilmore JL, et al. Conversion of potent MMP inhibitors into selective TACE inhibitors. Bioorg Med Chem Lett 2006; 16(4): 1028-31.
    • (2006) Bioorg Med Chem Lett , vol.16 , Issue.4 , pp. 1028-1031
    • Cherney, R.J.1    King, B.W.2    Gilmore, J.L.3
  • 369
    • 32344433663 scopus 로고    scopus 로고
    • Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonates
    • Pochetti G, Gavuzzo E, Campestre C, et al. Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonates. J Med Chem 2006; 49(3): 923-31.
    • (2006) J Med Chem , vol.49 , Issue.3 , pp. 923-931
    • Pochetti, G.1    Gavuzzo, E.2    Campestre, C.3
  • 370
    • 0346887176 scopus 로고    scopus 로고
    • Tetrahydroisoquinoline based sulfonamide hydroxamates as potent matrix metalloproteinase inhibitors
    • Ma D, Wu W, Yang G, Li J, Ye Q. Tetrahydroisoquinoline based sulfonamide hydroxamates as potent matrix metalloproteinase inhibitors. Bioorg Med Chem Lett 2004; 14(1): 47-50.
    • (2004) Bioorg Med Chem Lett , vol.14 , Issue.1 , pp. 47-50
    • Ma, D.1    Wu, W.2    Yang, G.3    Li, J.4    Ye, Q.5
  • 371
    • 0033552866 scopus 로고    scopus 로고
    • Design and synthesis of phosphinamide-based hydroxamic acids as inhibitors of matrix metalloproteinases
    • Pikul S, McDow Dunham KL, Almstead NG, et al. Design and synthesis of phosphinamide-based hydroxamic acids as inhibitors of matrix metalloproteinases. J Med Chem 1999; 42(1): 87-94.
    • (1999) J Med Chem , vol.42 , Issue.1 , pp. 87-94
    • Pikul, S.1    McDow Dunham, K.L.2    Almstead, N.G.3
  • 372
    • 0034757396 scopus 로고    scopus 로고
    • Design and synthesis of carboxylate inhibitors for matrix metalloproteinases
    • Fujisawa T, Katakura S, Odake S, et al. Design and synthesis of carboxylate inhibitors for matrix metalloproteinases. Chem Pharm Bull (Tokyo) 2001; 49(10): 1272-9.
    • (2001) Chem Pharm Bull (Tokyo) , vol.49 , Issue.10 , pp. 1272-1279
    • Fujisawa, T.1    Katakura, S.2    Odake, S.3
  • 373
    • 0036836679 scopus 로고    scopus 로고
    • Tetrahydroisoquinoline-3-carboxylate based matrix-metalloproteinase inhibitors: Design, synthesis and structure-activity relationship
    • Matter H, Schudok M, Schwab W, et al. Tetrahydroisoquinoline-3-carboxylate based matrix-metalloproteinase inhibitors: design, synthesis and structure-activity relationship. Bioorg Med Chem 2002; 10(11): 3529-44.
    • (2002) Bioorg Med Chem , vol.10 , Issue.11 , pp. 3529-3544
    • Matter, H.1    Schudok, M.2    Schwab, W.3
  • 374
    • 33645832556 scopus 로고    scopus 로고
    • Comparison of the pharmacology of hydroxamate-and carboxylate-based matrix metalloproteinase inhibitors (MMPIs) for the treatment of osteoarthritis
    • Janusz MJ, Hookfin EB, Brown KK, et al. Comparison of the pharmacology of hydroxamate-and carboxylate-based matrix metalloproteinase inhibitors (MMPIs) for the treatment of osteoarthritis. Inflamm Res 2006; 55(2): 60-5.
    • (2006) Inflamm Res , vol.55 , Issue.2 , pp. 60-65
    • Janusz, M.J.1    Hookfin, E.B.2    Brown, K.K.3
  • 375
    • 0345352736 scopus 로고    scopus 로고
    • Protease inhibitors: Synthesis of bacterial collagenase and matrix metalloproteinase inhibitors incorporating arylsulfonylureido and 5-dibenzo-suberenyl/suberyl moieties
    • Ilies M, Banciu MD, Scozzafava A, Ilies MA, Caproiu MT, Supuran CT. Protease inhibitors: synthesis of bacterial collagenase and matrix metalloproteinase inhibitors incorporating arylsulfonylureido and 5-dibenzo-suberenyl/suberyl moieties. Bioorg Med Chem 2003; 11(10): 2227-39.
    • (2003) Bioorg Med Chem , vol.11 , Issue.10 , pp. 2227-2239
    • Ilies, M.1    Banciu, M.D.2    Scozzafava, A.3    Ilies, M.A.4    Caproiu, M.T.5    Supuran, C.T.6
  • 377
    • 0038038524 scopus 로고    scopus 로고
    • Structural basis for potent slow binding inhibition of human matrix metalloproteinase-2 (MMP-2)
    • Rosenblum G, Meroueh SO, Kleifeld O, et al. Structural basis for potent slow binding inhibition of human matrix metalloproteinase-2 (MMP-2). J Biol Chem 2003; 278(29): 27009-15.
    • (2003) J Biol Chem , vol.278 , Issue.29 , pp. 27009-27015
    • Rosenblum, G.1    Meroueh, S.O.2    Kleifeld, O.3
  • 378
    • 25844469594 scopus 로고    scopus 로고
    • Synthesis and SAR of highly selective MMP-13 inhibitors
    • Li J, Rush TS, 3rd, Li W, et al. Synthesis and SAR of highly selective MMP-13 inhibitors. Bioorg Med Chem Lett 2005; 15(22): 4961-6.
    • (2005) Bioorg Med Chem Lett , vol.15 , Issue.22 , pp. 4961-4966
    • Li, J.1    Rush 3rd, T.S.2    Li, W.3
  • 379
    • 0037447184 scopus 로고    scopus 로고
    • Macrophage metalloelastase mediates acute cigarette smoke-induced inflammation via tumor necrosis factor-alpha release
    • Churg A, Wang RD, Tai H, et al. Macrophage metalloelastase mediates acute cigarette smoke-induced inflammation via tumor necrosis factor-alpha release. Am J Respir Crit Care Med 2003; 167(8): 1083-9.
    • (2003) Am J Respir Crit Care Med , vol.167 , Issue.8 , pp. 1083-1089
    • Churg, A.1    Wang, R.D.2    Tai, H.3
  • 380
    • 0041842667 scopus 로고    scopus 로고
    • A potent, selective inhibitor of matrix metalloproteinase-3 for the topical treatment of chronic dermal ulcers
    • Fray MJ, Dickinson RP, Huggins JP, Occleston NL. A potent, selective inhibitor of matrix metalloproteinase-3 for the topical treatment of chronic dermal ulcers. J Med Chem 2003; 46(16): 3514-25.
    • (2003) J Med Chem , vol.46 , Issue.16 , pp. 3514-3525
    • Fray, M.J.1    Dickinson, R.P.2    Huggins, J.P.3    Occleston, N.L.4
  • 381
    • 0037687744 scopus 로고    scopus 로고
    • Improved gelatinase a selectivity by novel zinc binding groups containing galardin derivatives
    • Auge F, Hornebeck W, Decarme M, Laronze JY. Improved gelatinase a selectivity by novel zinc binding groups containing galardin derivatives. Bioorg Med Chem Lett 2003; 13(10): 1783-6.
    • (2003) Bioorg Med Chem Lett , vol.13 , Issue.10 , pp. 1783-1786
    • Auge, F.1    Hornebeck, W.2    Decarme, M.3    Laronze, J.Y.4
  • 382
    • 51849144056 scopus 로고    scopus 로고
    • Introduction of the 4-(4-bromophenyl)benzenesulfonyl group to hydrazide analogs of Ilomastat leads to potent gelatinase B (MMP-9) inhibitors with improved selectivity
    • Ledour G, Moroy G, Rouffet M, et al. Introduction of the 4-(4-bromophenyl)benzenesulfonyl group to hydrazide analogs of Ilomastat leads to potent gelatinase B (MMP-9) inhibitors with improved selectivity. Bioorg Med Chem 2008; 16(18): 8745-59.
    • (2008) Bioorg Med Chem , vol.16 , Issue.18 , pp. 8745-8759
    • Ledour, G.1    Moroy, G.2    Rouffet, M.3
  • 383
    • 29644432986 scopus 로고    scopus 로고
    • Inhibition of enzyme activity of and cell-mediated substrate cleavage by membrane type 1 matrix metalloproteinase by newly developed mercaptosulphide inhibitors
    • Hurst DR, Schwartz MA, Jin Y, et al. Inhibition of enzyme activity of and cell-mediated substrate cleavage by membrane type 1 matrix metalloproteinase by newly developed mercaptosulphide inhibitors. Biochem J 2005; 392(Pt 3): 527-36.
    • (2005) Biochem J , vol.392 , Issue.PART 3 , pp. 527-536
    • Hurst, D.R.1    Schwartz, M.A.2    Jin, Y.3
  • 384
    • 41349106390 scopus 로고    scopus 로고
    • Carbamoylphosphonate matrix metalloproteinase inhibitors 6: Cis-2-aminocyclohexylcarbamoylphosphonic acid, a novel orally active antimetastatic matrix metalloproteinase-2 selective inhibitor--synthesis and pharmacodynamic and pharmacokinetic analysis
    • Hoffman A, Qadri B, Frant J, et al. Carbamoylphosphonate matrix metalloproteinase inhibitors 6: cis-2-aminocyclohexylcarbamoylphosphonic acid, a novel orally active antimetastatic matrix metalloproteinase-2 selective inhibitor--synthesis and pharmacodynamic and pharmacokinetic analysis. J Med Chem 2008; 51(5): 1406-14.
    • (2008) J Med Chem , vol.51 , Issue.5 , pp. 1406-1414
    • Hoffman, A.1    Qadri, B.2    Frant, J.3
  • 385
    • 2442713986 scopus 로고    scopus 로고
    • Carbamoylphosphonates, a new class of in vivo active matrix metalloproteinase inhibitors. 1. Alkyl-and cycloalkylcarbamoylphosphonic acids
    • Breuer E, Salomon CJ, Katz Y, et al. Carbamoylphosphonates, a new class of in vivo active matrix metalloproteinase inhibitors. 1. Alkyl-and cycloalkylcarbamoylphosphonic acids. J Med Chem 2004; 47(11): 2826-32.
    • (2004) J Med Chem , vol.47 , Issue.11 , pp. 2826-2832
    • Breuer, E.1    Salomon, C.J.2    Katz, Y.3
  • 386
    • 33644944087 scopus 로고    scopus 로고
    • A new role for old ligands: Discerning chelators for zinc metalloproteinases
    • Jacobsen FE, Lewis JA, Cohen SM. A new role for old ligands: discerning chelators for zinc metalloproteinases. J Am Chem Soc 2006; 128(10): 3156-7.
    • (2006) J Am Chem Soc , vol.128 , Issue.10 , pp. 3156-3157
    • Jacobsen, F.E.1    Lewis, J.A.2    Cohen, S.M.3
  • 388
    • 33749233835 scopus 로고    scopus 로고
    • Potent, selective pyrimidinetrione-based inhibitors of MMP-13
    • Reiter LA, Freeman-Cook KD, Jones CS, et al. Potent, selective pyrimidinetrione-based inhibitors of MMP-13. Bioorg Med Chem Lett 2006; 16(22): 5822-6.
    • (2006) Bioorg Med Chem Lett , vol.16 , Issue.22 , pp. 5822-5826
    • Reiter, L.A.1    Freeman-Cook, K.D.2    Jones, C.S.3
  • 389
    • 17944374569 scopus 로고    scopus 로고
    • Pyrimidine-2,4,6-Triones: A new effective and selective class of matrix metalloproteinase inhibitors
    • Grams F, Brandstetter H, D'Alo S, et al. Pyrimidine-2,4,6-Triones: a new effective and selective class of matrix metalloproteinase inhibitors. Biol Chem 2001; 382(8): 1277-85.
    • (2001) Biol Chem , vol.382 , Issue.8 , pp. 1277-1285
    • Grams, F.1    Brandstetter, H.2    D'Alo, S.3
  • 390
    • 0035938352 scopus 로고    scopus 로고
    • Novel 5,5-disubstitutedpyrimidine-2,4,6-triones as selective MMP inhibitors
    • Foley LH, Palermo R, Dunten P, Wang P. Novel 5,5-disubstitutedpyrimidine-2,4,6-triones as selective MMP inhibitors. Bioorg Med Chem Lett 2001; 11(8): 969-72.
    • (2001) Bioorg Med Chem Lett , vol.11 , Issue.8 , pp. 969-972
    • Foley, L.H.1    Palermo, R.2    Dunten, P.3    Wang, P.4
  • 391
    • 20144387816 scopus 로고    scopus 로고
    • Structure-based design of potent and selective inhibitors of collagenase-3 (MMP-13)
    • Kim SH, Pudzianowski AT, Leavitt KJ, et al. Structure-based design of potent and selective inhibitors of collagenase-3 (MMP-13). Bioorg Med Chem Lett 2005; 15(4): 1101-6.
    • (2005) Bioorg Med Chem Lett , vol.15 , Issue.4 , pp. 1101-1106
    • Kim, S.H.1    Pudzianowski, A.T.2    Leavitt, K.J.3
  • 392
    • 20144369218 scopus 로고    scopus 로고
    • Potent pyrimidinetrione-based inhibitors of MMP-13 with enhanced selectivity over MMP-14
    • Blagg JA, Noe MC, Wolf-Gouveia LA, et al. Potent pyrimidinetrione-based inhibitors of MMP-13 with enhanced selectivity over MMP-14. Bioorg Med Chem Lett 2005; 15(7): 1807-10.
    • (2005) Bioorg Med Chem Lett , vol.15 , Issue.7 , pp. 1807-1810
    • Blagg, J.A.1    Noe, M.C.2    Wolf-Gouveia, L.A.3
  • 393
    • 35648973186 scopus 로고    scopus 로고
    • Potent, selective spiropyrrolidine pyrimidinetrione inhibitors of MMP-13
    • Freeman-Cook KD, Reiter LA, Noe MC, et al. Potent, selective spiropyrrolidine pyrimidinetrione inhibitors of MMP-13. Bioorg Med Chem Lett 2007; 17(23): 6529-34.
    • (2007) Bioorg Med Chem Lett , vol.17 , Issue.23 , pp. 6529-6534
    • Freeman-Cook, K.D.1    Reiter, L.A.2    Noe, M.C.3
  • 394
    • 85047700070 scopus 로고    scopus 로고
    • The new synthetic matrix metalloproteinase inhibitor (Roche 28-2653) reduces tumor growth and prolongs survival in a prostate cancer standard rat model
    • Lein M, Jung K, Ortel B, et al. The new synthetic matrix metalloproteinase inhibitor (Roche 28-2653) reduces tumor growth and prolongs survival in a prostate cancer standard rat model. Oncogene 2002; 21(13): 2089-96.
    • (2002) Oncogene , vol.21 , Issue.13 , pp. 2089-2096
    • Lein, M.1    Jung, K.2    Ortel, B.3
  • 395
    • 3042526364 scopus 로고    scopus 로고
    • Anti-invasive, antitumoral, and antiangiogenic efficacy of a pyrimidine-2,4,6-trione derivative, an orally active and selective matrix metalloproteinases inhibitor
    • Maquoi E, Sounni NE, Devy L, et al. Anti-invasive, antitumoral, and antiangiogenic efficacy of a pyrimidine-2,4,6-trione derivative, an orally active and selective matrix metalloproteinases inhibitor. Clin Cancer Res 2004; 10(12 Pt 1): 4038-47.
    • (2004) Clin Cancer Res , vol.10 , Issue.12 PART 1 , pp. 4038-4047
    • Maquoi, E.1    Sounni, N.E.2    Devy, L.3
  • 396
    • 8244221001 scopus 로고    scopus 로고
    • Ro 32-3555, an orally active collagenase inhibitor, prevents cartilage breakdown in vitro and in vivo
    • Lewis EJ, Bishop J, Bottomley KM, et al. Ro 32-3555, an orally active collagenase inhibitor, prevents cartilage breakdown in vitro and in vivo. Br J Pharmacol 1997; 121(3): 540-6.
    • (1997) Br J Pharmacol , vol.121 , Issue.3 , pp. 540-546
    • Lewis, E.J.1    Bishop, J.2    Bottomley, K.M.3
  • 397
    • 3142738143 scopus 로고    scopus 로고
    • New beginnings for matrix metalloproteinase inhibitors: Identification of high-affinity zincbinding groups
    • Puerta DT, Lewis JA, Cohen SM. New beginnings for matrix metalloproteinase inhibitors: identification of high-affinity zincbinding groups. J Am Chem Soc 2004; 126(27): 8388-9.
    • (2004) J Am Chem Soc , vol.126 , Issue.27 , pp. 8388-8389
    • Puerta, D.T.1    Lewis, J.A.2    Cohen, S.M.3
  • 398
    • 0038779334 scopus 로고    scopus 로고
    • Examination of novel zinc-binding groups for use in matrix metalloproteinase inhibitors
    • Puerta DT, Cohen SM. Examination of novel zinc-binding groups for use in matrix metalloproteinase inhibitors. Inorg Chem 2003; 42(11): 3423-30.
    • (2003) Inorg Chem , vol.42 , Issue.11 , pp. 3423-3430
    • Puerta, D.T.1    Cohen, S.M.2
  • 399
    • 34047168930 scopus 로고    scopus 로고
    • The design of inhibitors for medicinally relevant metalloproteins
    • Jacobsen FE, Lewis JA, Cohen SM. The design of inhibitors for medicinally relevant metalloproteins. ChemMedChem 2007; 2(2): 152-71.
    • (2007) ChemMedChem , vol.2 , Issue.2 , pp. 152-171
    • Jacobsen, F.E.1    Lewis, J.A.2    Cohen, S.M.3
  • 400
    • 32444434063 scopus 로고    scopus 로고
    • Heterocyclic zinc-binding groups for use in next-generation matrix metalloproteinase inhibitors: Potency, toxicity, and reactivity
    • Puerta DT, Griffin MO, Lewis JA, et al. Heterocyclic zinc-binding groups for use in next-generation matrix metalloproteinase inhibitors: potency, toxicity, and reactivity. J Biol Inorg Chem 2006; 11(2): 131-8.
    • (2006) J Biol Inorg Chem , vol.11 , Issue.2 , pp. 131-138
    • Puerta, D.T.1    Griffin, M.O.2    Lewis, J.A.3
  • 403
    • 34547192664 scopus 로고    scopus 로고
    • Efficient synthesis of 5-amido-3-hydroxy-4-pyrones as inhibitors of matrix metalloproteinases
    • Yan YL, Cohen SM. Efficient synthesis of 5-amido-3-hydroxy-4-pyrones as inhibitors of matrix metalloproteinases. Org Lett 2007; 9(13): 2517-20.
    • (2007) Org Lett , vol.9 , Issue.13 , pp. 2517-2520
    • Yan, Y.L.1    Cohen, S.M.2
  • 404
    • 39749124201 scopus 로고    scopus 로고
    • Quinazolinones and pyrido[3,4-d]pyrimidin-4-ones as orally active and specific matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis
    • Li JJ, Nahra J, Johnson AR, et al. Quinazolinones and pyrido[3,4-d]pyrimidin-4-ones as orally active and specific matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis. J Med Chem 2008; 51(4): 835-41.
    • (2008) J Med Chem , vol.51 , Issue.4 , pp. 835-841
    • Li, J.J.1    Nahra, J.2    Johnson, A.R.3
  • 405
    • 3843152629 scopus 로고    scopus 로고
    • Crystal structures of novel non-peptidic, non-zinc chelating inhibitors bound to MMP-12
    • Morales R, Perrier S, Florent JM, et al. Crystal structures of novel non-peptidic, non-zinc chelating inhibitors bound to MMP-12. J Mol Biol 2004; 341(4): 1063-76.
    • (2004) J Mol Biol , vol.341 , Issue.4 , pp. 1063-1076
    • Morales, R.1    Perrier, S.2    Florent, J.M.3
  • 406
    • 14144252682 scopus 로고    scopus 로고
    • Structural basis for the highly selective inhibition of MMP-13
    • Engel CK, Pirard B, Schimanski S, et al. Structural basis for the highly selective inhibition of MMP-13. Chem Biol 2005; 12(2): 181-9.
    • (2005) Chem Biol , vol.12 , Issue.2 , pp. 181-189
    • Engel, C.K.1    Pirard, B.2    Schimanski, S.3
  • 407
    • 22844434878 scopus 로고    scopus 로고
    • Structure-based design and synthesis of novel non-zinc chelating MMP-12 inhibitors
    • Dublanchet AC, Ducrot P, Andrianjara C, et al. Structure-based design and synthesis of novel non-zinc chelating MMP-12 inhibitors. Bioorg Med Chem Lett 2005; 15(16): 3787-90.
    • (2005) Bioorg Med Chem Lett , vol.15 , Issue.16 , pp. 3787-3790
    • Dublanchet, A.C.1    Ducrot, P.2    Andrianjara, C.3
  • 408
    • 37549010964 scopus 로고    scopus 로고
    • Characterization of an exosite binding inhibitor of matrix metalloproteinase 13
    • Gooljarsingh LT, Lakdawala A, Coppo F, et al. Characterization of an exosite binding inhibitor of matrix metalloproteinase 13. Protein Sci 2008; 17(1): 66-71.
    • (2008) Protein Sci , vol.17 , Issue.1 , pp. 66-71
    • Gooljarsingh, L.T.1    Lakdawala, A.2    Coppo, F.3
  • 409
    • 64349106309 scopus 로고    scopus 로고
    • Extra binding region induced by non-zinc chelating inhibitors into the S1' subsite of matrix metalloproteinase 8 (MMP-8)
    • Pochetti G, Montanari R, Gege C, Chevrier C, Taveras AG, Mazza F. Extra binding region induced by non-zinc chelating inhibitors into the S1' subsite of matrix metalloproteinase 8 (MMP-8). J Med Chem 2009; 52(4): 1040-9.
    • (2009) J Med Chem , vol.52 , Issue.4 , pp. 1040-1049
    • Pochetti, G.1    Montanari, R.2    Gege, C.3    Chevrier, C.4    Taveras, A.G.5    Mazza, F.6
  • 410
    • 34948864524 scopus 로고    scopus 로고
    • Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects
    • Johnson AR, Pavlovsky AG, Ortwine DF, et al. Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects. J Biol Chem 2007; 282(38): 27781-91.
    • (2007) J Biol Chem , vol.282 , Issue.38 , pp. 27781-27791
    • Johnson, A.R.1    Pavlovsky, A.G.2    Ortwine, D.F.3
  • 411
    • 0037192860 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases
    • Bernardo MM, Brown S, Li ZH, Fridman R, Mobashery S. Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases. J Biol Chem 2002; 277(13): 11201-7.
    • (2002) J Biol Chem , vol.277 , Issue.13 , pp. 11201-11207
    • Bernardo, M.M.1    Brown, S.2    Li, Z.H.3    Fridman, R.4    Mobashery, S.5
  • 412
    • 0023728105 scopus 로고
    • The behavior and significance of slowbinding enzyme inhibitors
    • Morrison JF, Walsh CT. The behavior and significance of slowbinding enzyme inhibitors. Adv Enzymol Relat Areas Mol Biol 1988; 61: 201-301.
    • (1988) Adv Enzymol Relat Areas Mol Biol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 413
    • 18144370787 scopus 로고    scopus 로고
    • Antimetastatic activity of a novel mechanism-based gelatinase inhibitor
    • Kruger A, Arlt MJ, Gerg M, et al. Antimetastatic activity of a novel mechanism-based gelatinase inhibitor. Cancer Res 2005; 65(9): 3523-6.
    • (2005) Cancer Res , vol.65 , Issue.9 , pp. 3523-3526
    • Kruger, A.1    Arlt, M.J.2    Gerg, M.3
  • 414
    • 33646352955 scopus 로고    scopus 로고
    • Inhibition of human prostate cancer growth, osteolysis and angiogenesis in a bone metastasis model by a novel mechanism-based selective gelatinase inhibitor
    • Bonfil RD, Sabbota A, Nabha S, et al. Inhibition of human prostate cancer growth, osteolysis and angiogenesis in a bone metastasis model by a novel mechanism-based selective gelatinase inhibitor. Int J Cancer 2006; 118(11): 2721-6.
    • (2006) Int J Cancer , vol.118 , Issue.11 , pp. 2721-2726
    • Bonfil, R.D.1    Sabbota, A.2    Nabha, S.3
  • 415
    • 34447324943 scopus 로고    scopus 로고
    • Prostate cancerassociated membrane type 1-matrix metalloproteinase: A pivotal role in bone response and intraosseous tumor growth
    • Bonfil RD, Dong Z, Trindade Filho JC, et al. Prostate cancerassociated membrane type 1-matrix metalloproteinase: a pivotal role in bone response and intraosseous tumor growth. Am J Pathol 2007; 170(6): 2100-11.
    • (2007) Am J Pathol , vol.170 , Issue.6 , pp. 2100-2111
    • Bonfil, R.D.1    Dong, Z.2    Trindade Filho, J.C.3
  • 416
    • 27844610322 scopus 로고    scopus 로고
    • Effective inhibition of experimental metastasis and prolongation of survival in mice by a potent factor Xa-specific synthetic serine protease inhibitor with weak anticoagulant activity
    • Banke IJ, Arlt MJ, Mueller MM, et al. Effective inhibition of experimental metastasis and prolongation of survival in mice by a potent factor Xa-specific synthetic serine protease inhibitor with weak anticoagulant activity. Thromb Haemost 2005; 94(5): 1084-93.
    • (2005) Thromb Haemost , vol.94 , Issue.5 , pp. 1084-1093
    • Banke, I.J.1    Arlt, M.J.2    Mueller, M.M.3
  • 417
    • 21844450866 scopus 로고    scopus 로고
    • A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia
    • Gu Z, Cui J, Brown S, et al. A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia. J Neurosci 2005; 25(27): 6401-8.
    • (2005) J Neurosci , vol.25 , Issue.27 , pp. 6401-6408
    • Gu, Z.1    Cui, J.2    Brown, S.3
  • 418
    • 35348950561 scopus 로고    scopus 로고
    • Metabolism of a highly selective gelatinase inhibitor generates active metabolite
    • Lee M, Villegas-Estrada A, Celenza G, et al. Metabolism of a highly selective gelatinase inhibitor generates active metabolite. Chem Biol Drug Des 2007; 70(5): 371-82.
    • (2007) Chem Biol Drug Des , vol.70 , Issue.5 , pp. 371-382
    • Lee, M.1    Villegas-Estrada, A.2    Celenza, G.3
  • 419
    • 38849184744 scopus 로고    scopus 로고
    • Metabolism of (4-phenoxyphenylsulfonyl) methylthiirane, a selective gelatinase inhibitor
    • Celenza G, Villegas-Estrada A, Lee M, et al. Metabolism of (4-phenoxyphenylsulfonyl) methylthiirane, a selective gelatinase inhibitor. Chem Biol Drug Des 2008; 71(3): 187-96.
    • (2008) Chem Biol Drug Des , vol.71 , Issue.3 , pp. 187-196
    • Celenza, G.1    Villegas-Estrada, A.2    Lee, M.3
  • 420
    • 58849102666 scopus 로고    scopus 로고
    • A potent gelatinase inhibitor with anti-tumor-invasive activity and its metabolic disposition
    • Lee M, Celenza G, Boggess B, et al. A potent gelatinase inhibitor with anti-tumor-invasive activity and its metabolic disposition. Chem Biol Drug Des 2009; 73(2): 189-202.
    • (2009) Chem Biol Drug Des , vol.73 , Issue.2 , pp. 189-202
    • Lee, M.1    Celenza, G.2    Boggess, B.3
  • 421
    • 34447269445 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: New challenges in the era of post broad-spectrum inhibitors
    • Nuti E, Tuccinardi T, Rossello A. Matrix metalloproteinase inhibitors: new challenges in the era of post broad-spectrum inhibitors. Curr Pharm Des 2007; 13(20): 2087-100.
    • (2007) Curr Pharm Des , vol.13 , Issue.20 , pp. 2087-2100
    • Nuti, E.1    Tuccinardi, T.2    Rossello, A.3
  • 422
    • 52949136266 scopus 로고    scopus 로고
    • Specific targeting of metzincin family members with small-molecule inhibitors: Progress toward a multifarious challenge
    • Georgiadis D, Yiotakis A. Specific targeting of metzincin family members with small-molecule inhibitors: progress toward a multifarious challenge. Bioorg Med Chem 2008; 16(19): 8781-94.
    • (2008) Bioorg Med Chem , vol.16 , Issue.19 , pp. 8781-8794
    • Georgiadis, D.1    Yiotakis, A.2
  • 423
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens LM, Fingleton B, Matrisian LM. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002; 295(5564): 2387-92.
    • (2002) Science , vol.295 , Issue.5564 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 424
    • 0037975559 scopus 로고    scopus 로고
    • Broad-spectrum matrix metalloproteinase inhibitor marimastat-induced musculoskeletal side effects in rats
    • Renkiewicz R, Qiu L, Lesch C, et al. Broad-spectrum matrix metalloproteinase inhibitor marimastat-induced musculoskeletal side effects in rats. Arthritis Rheum 2003; 48(6): 1742-9.
    • (2003) Arthritis Rheum , vol.48 , Issue.6 , pp. 1742-1749
    • Renkiewicz, R.1    Qiu, L.2    Lesch, C.3
  • 425
    • 34250630512 scopus 로고    scopus 로고
    • A phase II and pharmacological study of the matrix metalloproteinase inhibitor (MMPI) COL-3 in patients with advanced soft tissue sarcomas
    • Chu QS, Forouzesh B, Syed S, et al. A phase II and pharmacological study of the matrix metalloproteinase inhibitor (MMPI) COL-3 in patients with advanced soft tissue sarcomas. Invest New Drugs 2007; 25(4): 359-67.
    • (2007) Invest New Drugs , vol.25 , Issue.4 , pp. 359-367
    • Chu, Q.S.1    Forouzesh, B.2    Syed, S.3
  • 426
    • 32244447110 scopus 로고    scopus 로고
    • HMG-CoA reductase inhibitors reduce matrix metalloproteinase-9 activity in human varicose veins
    • Nomura S, Yoshimura K, Akiyama N, et al. HMG-CoA reductase inhibitors reduce matrix metalloproteinase-9 activity in human varicose veins. Eur Surg Res 2005; 37(6): 370-8.
    • (2005) Eur Surg Res , vol.37 , Issue.6 , pp. 370-378
    • Nomura, S.1    Yoshimura, K.2    Akiyama, N.3
  • 427
    • 84876699288 scopus 로고    scopus 로고
    • Glycosaminoglycan Sulodexide Inhibition of MMP-9 Gelatinase Secretion and Activity: Possible Pharmacological Role Against Collagen Degradation in Vascular Chronic Diseases
    • Mannello F, Medda V, Ligi D, Raffetto JD. Glycosaminoglycan Sulodexide Inhibition of MMP-9 Gelatinase Secretion and Activity: Possible Pharmacological Role Against Collagen Degradation in Vascular Chronic Diseases. Curr Vasc Pharmacol 2012.
    • (2012) Curr Vasc Pharmacol
    • Mannello, F.1    Medda, V.2    Ligi, D.3    Raffetto, J.D.4
  • 428
    • 79952928710 scopus 로고    scopus 로고
    • Matrix metalloproteinase activity and glycosaminoglycans in chronic venous disease: The linkage among cell biology, pathology and translational research
    • Mannello F, Raffetto JD. Matrix metalloproteinase activity and glycosaminoglycans in chronic venous disease: the linkage among cell biology, pathology and translational research. Am J Transl Res 2011; 3(2): 149-58.
    • (2011) Am J Transl Res , vol.3 , Issue.2 , pp. 149-158
    • Mannello, F.1    Raffetto, J.D.2
  • 429
    • 42249090193 scopus 로고    scopus 로고
    • The inhibition of matrix metalloproteinase activity in chronic wounds by a polyacrylate superabsorber
    • Eming S, Smola H, Hartmann B, et al. The inhibition of matrix metalloproteinase activity in chronic wounds by a polyacrylate superabsorber. Biomaterials 2008; 29(19): 2932-40.
    • (2008) Biomaterials , vol.29 , Issue.19 , pp. 2932-2940
    • Eming, S.1    Smola, H.2    Hartmann, B.3
  • 430
    • 0036777547 scopus 로고    scopus 로고
    • The healing properties of Promogran in venous leg ulcers
    • Vin F, Teot L, Meaume S. The healing properties of Promogran in venous leg ulcers. J Wound Care 2002; 11(9): 335-41.
    • (2002) J Wound Care , vol.11 , Issue.9 , pp. 335-341
    • Vin, F.1    Teot, L.2    Meaume, S.3
  • 431
    • 44349154896 scopus 로고    scopus 로고
    • Effect of oxidised regenerated cellulose/collagen matrix on proteases in wound exudate of patients with chronic venous ulceration
    • Smeets R, Ulrich D, Unglaub F, Woltje M, Pallua N. Effect of oxidised regenerated cellulose/collagen matrix on proteases in wound exudate of patients with chronic venous ulceration. Int Wound J 2008; 5(2): 195-203.
    • (2008) Int Wound J , vol.5 , Issue.2 , pp. 195-203
    • Smeets, R.1    Ulrich, D.2    Unglaub, F.3    Woltje, M.4    Pallua, N.5
  • 432
    • 44349104854 scopus 로고    scopus 로고
    • Evaluation of the nanooligosaccharide factor lipido-colloid matrix in the local management of venous leg ulcers: Results of a randomised, controlled trial
    • Schmutz JL, Meaume S, Fays S, et al. Evaluation of the nanooligosaccharide factor lipido-colloid matrix in the local management of venous leg ulcers: results of a randomised, controlled trial. Int Wound J 2008; 5(2): 172-82.
    • (2008) Int Wound J , vol.5 , Issue.2 , pp. 172-182
    • Schmutz, J.L.1    Meaume, S.2    Fays, S.3
  • 433
    • 27944504766 scopus 로고    scopus 로고
    • Combination therapy of doxycycline and topical tacrolimus for venous ulcers
    • Mackelfresh J, Soon S, Arbiser JL. Combination therapy of doxycycline and topical tacrolimus for venous ulcers. Arch Dermatol 2005; 141(11): 1476-7.
    • (2005) Arch Dermatol , vol.141 , Issue.11 , pp. 1476-1477
    • Mackelfresh, J.1    Soon, S.2    Arbiser, J.L.3
  • 434
    • 33845910687 scopus 로고    scopus 로고
    • A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fibronectin or zinc binding domains
    • Martens E, Leyssen A, Van Aelst I, et al. A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fibronectin or zinc binding domains. Biochim Biophys Acta 2007; 1770(2): 178-86.
    • (2007) Biochim Biophys Acta , vol.1770 , Issue.2 , pp. 178-186
    • Martens, E.1    Leyssen, A.2    van Aelst, I.3
  • 435
    • 0029584651 scopus 로고
    • Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity
    • Paemen L, Martens E, Masure S, Opdenakker G. Monoclonal antibodies specific for natural human neutrophil gelatinase B used for affinity purification, quantitation by two-site ELISA and inhibition of enzymatic activity. Eur J Biochem 1995; 234(3): 759-65.
    • (1995) Eur J Biochem , vol.234 , Issue.3 , pp. 759-765
    • Paemen, L.1    Martens, E.2    Masure, S.3    Opdenakker, G.4
  • 436
    • 1042275537 scopus 로고    scopus 로고
    • Inhibitors of gelatinase B/matrix metalloproteinase-9 activity comparison of a peptidomimetic and polyhistidine with single-chain derivatives of a neutralizing monoclonal antibody
    • Hu J, Van den Steen PE, Houde M, Ilenchuk TT, Opdenakker G. Inhibitors of gelatinase B/matrix metalloproteinase-9 activity comparison of a peptidomimetic and polyhistidine with single-chain derivatives of a neutralizing monoclonal antibody. Biochem Pharmacol 2004; 67(5): 1001-9.
    • (2004) Biochem Pharmacol , vol.67 , Issue.5 , pp. 1001-1009
    • Hu, J.1    van den Steen, P.E.2    Houde, M.3    Ilenchuk, T.T.4    Opdenakker, G.5
  • 437
    • 34250333704 scopus 로고    scopus 로고
    • MMP-9 short interfering RNA induced senescence resulting in inhibition of medulloblastoma growth via p16(INK4a) and mitogen-activated protein kinase pathway
    • Rao JS, Bhoopathi P, Chetty C, Gujrati M, Lakka SS. MMP-9 short interfering RNA induced senescence resulting in inhibition of medulloblastoma growth via p16(INK4a) and mitogen-activated protein kinase pathway. Cancer Res 2007; 67(10): 4956-64.
    • (2007) Cancer Res , vol.67 , Issue.10 , pp. 4956-4964
    • Rao, J.S.1    Bhoopathi, P.2    Chetty, C.3    Gujrati, M.4    Lakka, S.S.5
  • 438
    • 12944288132 scopus 로고    scopus 로고
    • siRNA mediated inhibition of MMP-1 reduces invasive potential of a human chondrosarcoma cell line
    • Jiang X, Dutton CM, Qi WN, Block JA, Garamszegi N, Scully SP. siRNA mediated inhibition of MMP-1 reduces invasive potential of a human chondrosarcoma cell line. J Cell Physiol 2005; 202(3): 723-30.
    • (2005) J Cell Physiol , vol.202 , Issue.3 , pp. 723-730
    • Jiang, X.1    Dutton, C.M.2    Qi, W.N.3    Block, J.A.4    Garamszegi, N.5    Scully, S.P.6
  • 439
    • 34247267118 scopus 로고    scopus 로고
    • MT1-MMP down-regulates the glucose 6-phosphate transporter expression in marrow stromal cells: A molecular link between pro-MMP-2 activation, chemotaxis, and cell survival
    • Currie JC, Fortier S, Sina A, Galipeau J, Cao J, Annabi B. MT1-MMP down-regulates the glucose 6-phosphate transporter expression in marrow stromal cells: a molecular link between pro-MMP-2 activation, chemotaxis, and cell survival. J Biol Chem 2007; 282(11): 8142-9.
    • (2007) J Biol Chem , vol.282 , Issue.11 , pp. 8142-8149
    • Currie, J.C.1    Fortier, S.2    Sina, A.3    Galipeau, J.4    Cao, J.5    Annabi, B.6
  • 440
    • 20444470108 scopus 로고    scopus 로고
    • Specific interference of urokinase-type plasminogen activator receptor and matrix metalloproteinase-9 gene expression induced by double-stranded RNA results in decreased invasion, tumor growth, and angiogenesis in gliomas
    • Lakka SS, Gondi CS, Dinh DH, et al. Specific interference of urokinase-type plasminogen activator receptor and matrix metalloproteinase-9 gene expression induced by double-stranded RNA results in decreased invasion, tumor growth, and angiogenesis in gliomas. J Biol Chem 2005; 280(23): 21882-92.
    • (2005) J Biol Chem , vol.280 , Issue.23 , pp. 21882-21892
    • Lakka, S.S.1    Gondi, C.S.2    Dinh, D.H.3
  • 441
    • 0034954524 scopus 로고    scopus 로고
    • In vivo molecular target assessment of matrix metalloproteinase inhibition
    • Bremer C, Tung CH, Weissleder R. In vivo molecular target assessment of matrix metalloproteinase inhibition. Nat Med 2001; 7(6): 743-8.
    • (2001) Nat Med , vol.7 , Issue.6 , pp. 743-748
    • Bremer, C.1    Tung, C.H.2    Weissleder, R.3
  • 442
    • 0037062686 scopus 로고    scopus 로고
    • In vivo imaging of proteolytic activity in atherosclerosis
    • Chen J, Tung CH, Mahmood U, et al. In vivo imaging of proteolytic activity in atherosclerosis. Circulation 2002; 105(23): 2766-71.
    • (2002) Circulation , vol.105 , Issue.23 , pp. 2766-2771
    • Chen, J.1    Tung, C.H.2    Mahmood, U.3
  • 443
    • 21044444039 scopus 로고    scopus 로고
    • Matrix metalloproteinase knockout studies and the potential use of matrix metalloproteinase inhibitors in the rheumatic diseases
    • Milner JM, Cawston TE. Matrix metalloproteinase knockout studies and the potential use of matrix metalloproteinase inhibitors in the rheumatic diseases. Curr Drug Targets Inflamm Allergy 2005; 4(3): 363-75.
    • (2005) Curr Drug Targets Inflamm Allergy , vol.4 , Issue.3 , pp. 363-375
    • Milner, J.M.1    Cawston, T.E.2
  • 444
    • 1642457200 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma-independent repression of collagenase gene expression by 2-cyano-3,12-dioxooleana-1,9-dien-28-oic acid and prostaglandin 15-deoxydelta(12,14) J2: A role for Smad signaling
    • Mix KS, Coon CI, Rosen ED, Suh N, Sporn MB, Brinckerhoff CE. Peroxisome proliferator-activated receptor-gamma-independent repression of collagenase gene expression by 2-cyano-3,12-dioxooleana-1,9-dien-28-oic acid and prostaglandin 15-deoxydelta(12,14) J2: a role for Smad signaling. Mol Pharmacol 2004; 65(2): 309-18.
    • (2004) Mol Pharmacol , vol.65 , Issue.2 , pp. 309-318
    • Mix, K.S.1    Coon, C.I.2    Rosen, E.D.3    Suh, N.4    Sporn, M.B.5    Brinckerhoff, C.E.6
  • 446
    • 0037319185 scopus 로고    scopus 로고
    • Cartilage degradation and invasion by rheumatoid synovial fibroblasts is inhibited by gene transfer of TIMP-1 and TIMP-3
    • van der Laan WH, Quax PH, Seemayer CA, et al. Cartilage degradation and invasion by rheumatoid synovial fibroblasts is inhibited by gene transfer of TIMP-1 and TIMP-3. Gene Ther 2003; 10(3): 234-42.
    • (2003) Gene Ther , vol.10 , Issue.3 , pp. 234-242
    • van der Laan, W.H.1    Quax, P.H.2    Seemayer, C.A.3
  • 447
    • 0017596472 scopus 로고
    • Effect of a benzopyrone preparation in venous diseases during pregnancy
    • Krajnovic P. [Effect of a benzopyrone preparation in venous diseases during pregnancy]. Med Monatsschr 1977; 31(2): 86-8.
    • (1977) Med Monatsschr , vol.31 , Issue.2 , pp. 86-88
    • Krajnovic, P.1
  • 448
    • 0032837028 scopus 로고    scopus 로고
    • Broad antitumor and antiangiogenic activities of AG3340, a potent and selective MMP inhibitor undergoing advanced oncology clinical trials
    • Shalinsky DR, Brekken J, Zou H, et al. Broad antitumor and antiangiogenic activities of AG3340, a potent and selective MMP inhibitor undergoing advanced oncology clinical trials. Ann N Y Acad Sci 1999; 878: 236-70.
    • (1999) Ann N Y Acad Sci , vol.878 , pp. 236-270
    • Shalinsky, D.R.1    Brekken, J.2    Zou, H.3
  • 449
    • 6344225957 scopus 로고    scopus 로고
    • The effect of prinomastat (AG3340), a potent inhibitor of matrix metalloproteinase, on a new animal model of epiretinal membrane
    • El-Bradey MH, Cheng L, Bartsch DU, Niessman M, El-Musharaf A, Freeman WR. The effect of prinomastat (AG3340), a potent inhibitor of matrix metalloproteinase, on a new animal model of epiretinal membrane. Retina 2004; 24(5): 783-9.
    • (2004) Retina , vol.24 , Issue.5 , pp. 783-789
    • El-Bradey, M.H.1    Cheng, L.2    Bartsch, D.U.3    Niessman, M.4    El-Musharaf, A.5    Freeman, W.R.6
  • 450
    • 0035996280 scopus 로고    scopus 로고
    • Efficacy of Prinomastat) (AG3340), a matrix metalloprotease inhibitor, in treatment of retinal neovascularization
    • Garcia C, Bartsch DU, Rivero ME, et al. Efficacy of Prinomastat) (AG3340), a matrix metalloprotease inhibitor, in treatment of retinal neovascularization. Curr Eye Res 2002; 24(1): 33-8.
    • (2002) Curr Eye Res , vol.24 , Issue.1 , pp. 33-38
    • Garcia, C.1    Bartsch, D.U.2    Rivero, M.E.3
  • 451
    • 0035986464 scopus 로고    scopus 로고
    • The effect of prinomastat (AG3340), a synthetic inhibitor of matrix metalloproteinases, on uveal melanoma rabbit model
    • Ozerdem U, Mach-Hofacre B, Varki N, et al. The effect of prinomastat (AG3340), a synthetic inhibitor of matrix metalloproteinases, on uveal melanoma rabbit model. Curr Eye Res 2002; 24(2): 86-91.
    • (2002) Curr Eye Res , vol.24 , Issue.2 , pp. 86-91
    • Ozerdem, U.1    Mach-Hofacre, B.2    Varki, N.3
  • 452
    • 0035198816 scopus 로고    scopus 로고
    • Ventilator-induced lung injury upregulates and activates gelatinases and EMMPRIN: Attenuation by the synthetic matrix metalloproteinase inhibitor, Prinomastat (AG3340)
    • Foda HD, Rollo EE, Drews M, et al. Ventilator-induced lung injury upregulates and activates gelatinases and EMMPRIN: attenuation by the synthetic matrix metalloproteinase inhibitor, Prinomastat (AG3340). Am J Respir Cell Mol Biol 2001; 25(6): 717-24.
    • (2001) Am J Respir Cell Mol Biol , vol.25 , Issue.6 , pp. 717-724
    • Foda, H.D.1    Rollo, E.E.2    Drews, M.3
  • 453
    • 0032905581 scopus 로고    scopus 로고
    • Marked inhibition of tumor growth in a malignant glioma tumor model by a novel synthetic matrix metalloproteinase inhibitor AG3340
    • Price A, Shi Q, Morris D, et al. Marked inhibition of tumor growth in a malignant glioma tumor model by a novel synthetic matrix metalloproteinase inhibitor AG3340. Clin Cancer Res 1999; 5(4): 845-54.
    • (1999) Clin Cancer Res , vol.5 , Issue.4 , pp. 845-854
    • Price, A.1    Shi, Q.2    Morris, D.3
  • 454
    • 0028382506 scopus 로고
    • Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor
    • Borkakoti N, Winkler FK, Williams DH, et al. Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor. Nat Struct Biol 1994; 1(2): 106-10.
    • (1994) Nat Struct Biol , vol.1 , Issue.2 , pp. 106-110
    • Borkakoti, N.1    Winkler, F.K.2    Williams, D.H.3
  • 455
    • 27644451659 scopus 로고    scopus 로고
    • Potent, selective, and orally bioavailable matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis
    • Hu Y, Xiang JS, DiGrandi MJ, et al. Potent, selective, and orally bioavailable matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis. Bioorg Med Chem 2005; 13(24): 6629-44.
    • (2005) Bioorg Med Chem , vol.13 , Issue.24 , pp. 6629-6644
    • Hu, Y.1    Xiang, J.S.2    DiGrandi, M.J.3
  • 456
    • 64549096788 scopus 로고    scopus 로고
    • A selective matrix metalloprotease 12 inhibitor for potential treatment of chronic obstructive pulmonary disease (COPD): Discovery of (S)-2-(8-(methoxycarbonylamino)dibenzo[b, d]furan-3-sulfonamido)-3-methylbu tanoic acid (MMP408)
    • Li W, Li J, Wu Y, et al. A selective matrix metalloprotease 12 inhibitor for potential treatment of chronic obstructive pulmonary disease (COPD): discovery of (S)-2-(8-(methoxycarbonylamino)dibenzo[b, d]furan-3-sulfonamido)-3-methylbu tanoic acid (MMP408). J Med Chem 2009; 52(7): 1799-802.
    • (2009) J Med Chem , vol.52 , Issue.7 , pp. 1799-1802
    • Li, W.1    Li, J.2    Wu, Y.3
  • 457
    • 0035907471 scopus 로고    scopus 로고
    • Biaryl ether retrohydroxamates as potent, long-lived, orally bioavailable MMP inhibitors
    • Michaelides MR, Dellaria JF, Gong J, et al. Biaryl ether retrohydroxamates as potent, long-lived, orally bioavailable MMP inhibitors. Bioorg Med Chem Lett 2001; 11(12): 1553-6.
    • (2001) Bioorg Med Chem Lett , vol.11 , Issue.12 , pp. 1553-1556
    • Michaelides, M.R.1    Dellaria, J.F.2    Gong, J.3
  • 458
    • 27744506564 scopus 로고    scopus 로고
    • N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: Mode of binding in a complex with MMP-8
    • Campestre C, Agamennone M, Tortorella P, et al. N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: mode of binding in a complex with MMP-8. Bioorg Med Chem Lett 2006; 16(1): 20-4.
    • (2006) Bioorg Med Chem Lett , vol.16 , Issue.1 , pp. 20-24
    • Campestre, C.1    Agamennone, M.2    Tortorella, P.3
  • 459
    • 28244445602 scopus 로고    scopus 로고
    • Resistance of collagenase-2 (matrix metalloproteinase-8)-deficient mice to TNF-induced lethal hepatitis
    • Van Lint P, Wielockx B, Puimege L, Noel A, Lopez-Otin C, Libert C. Resistance of collagenase-2 (matrix metalloproteinase-8)-deficient mice to TNF-induced lethal hepatitis. J Immunol 2005; 175(11): 7642-9.
    • (2005) J Immunol , vol.175 , Issue.11 , pp. 7642-7649
    • van Lint, P.1    Wielockx, B.2    Puimege, L.3    Noel, A.4    Lopez-Otin, C.5    Libert, C.6
  • 460
    • 33845283570 scopus 로고    scopus 로고
    • alpha-Biphenylsulfonylamino 2-methylpropyl phosphonates: Enantioselective synthesis and selective inhibition of MMPs
    • Biasone A, Tortorella P, Campestre C, et al. alpha-Biphenylsulfonylamino 2-methylpropyl phosphonates: enantioselective synthesis and selective inhibition of MMPs. Bioorg Med Chem 2007; 15(2): 791-9.
    • (2007) Bioorg Med Chem , vol.15 , Issue.2 , pp. 791-799
    • Biasone, A.1    Tortorella, P.2    Campestre, C.3
  • 461
    • 44049090904 scopus 로고    scopus 로고
    • Collagenase-2 deficiency or inhibition impairs experimental autoimmune encephalomyelitis in mice
    • Folgueras AR, Fueyo A, Garcia-Suarez O, et al. Collagenase-2 deficiency or inhibition impairs experimental autoimmune encephalomyelitis in mice. J Biol Chem 2008; 283(14): 9465-74.
    • (2008) J Biol Chem , vol.283 , Issue.14 , pp. 9465-9474
    • Folgueras, A.R.1    Fueyo, A.2    Garcia-Suarez, O.3
  • 462
    • 0346333073 scopus 로고    scopus 로고
    • Evaluation of P1'-diversified phosphinic peptides leads to the development of highly selective inhibitors of MMP-11
    • Matziari M, Beau F, Cuniasse P, Dive V, Yiotakis A. Evaluation of P1'-diversified phosphinic peptides leads to the development of highly selective inhibitors of MMP-11. J Med Chem 2004; 47(2): 325-36.
    • (2004) J Med Chem , vol.47 , Issue.2 , pp. 325-336
    • Matziari, M.1    Beau, F.2    Cuniasse, P.3    Dive, V.4    Yiotakis, A.5
  • 463
    • 51449111071 scopus 로고    scopus 로고
    • Cardiac uptake of minocycline and mechanisms for in vivo cardioprotection
    • Romero-Perez D, Fricovsky E, Yamasaki KG, et al. Cardiac uptake of minocycline and mechanisms for in vivo cardioprotection. J Am Coll Cardiol 2008; 52(13): 1086-94.
    • (2008) J Am Coll Cardiol , vol.52 , Issue.13 , pp. 1086-1094
    • Romero-Perez, D.1    Fricovsky, E.2    Yamasaki, K.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.