메뉴 건너뛰기




Volumn 10, Issue 1, 1999, Pages 5-16

Multiple functions of tissue inhibitors of metalloproteinases (TIMPs): New aspects in hematopoiesis

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROID POTENTIATING FACTOR; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 0032967881     PISSN: 09537104     EISSN: None     Source Type: Journal    
DOI: 10.1080/09537109976293     Document Type: Review
Times cited : (29)

References (94)
  • 2
    • 0025847582 scopus 로고
    • Matrix metalloproteins and their inhibitors in connective tissue remodeling
    • Woessner JF Jr. Matrix metalloproteins and their inhibitors in connective tissue remodeling. FASEB J 1991; 5: 2145-54.
    • (1991) FASEB J , vol.5 , pp. 2145-2154
    • Woessner J.F., Jr.1
  • 4
    • 0000736684 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • NM Hooper, ed. London: Talor and Francis
    • Nagase H. Matrix metalloproteinases. In NM Hooper, ed. Zinc Metalloproteinases in Health and Disease. London: Talor and Francis, 1996; 153-204.
    • (1996) Zinc Metalloproteinases in Health and Disease , pp. 153-204
    • Nagase, H.1
  • 5
    • 0000414262 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) in the development and disease of oral tissues
    • Hayakawa T. Matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) in the development and disease of oral tissues. Dent Japan 1998; 34: 167-77.
    • (1998) Dent Japan , vol.34 , pp. 167-177
    • Hayakawa, T.1
  • 6
    • 0027435065 scopus 로고
    • Tissue inhibitors of metalloproteinases (TIMP aka EPA): Structure, control of expression and biological functions
    • Denhart D, Feng B, Edwards DR, Cocuzzi ET, Malyanker UM. Tissue inhibitors of metalloproteinases (TIMP aka EPA): structure, control of expression and biological functions. Pharmac Ther 1993; 59: 329-41.
    • (1993) Pharmac Ther , vol.59 , pp. 329-341
    • Denhart, D.1    Feng, B.2    Edwards, D.R.3    Cocuzzi, E.T.4    Malyanker, U.M.5
  • 7
    • 0028339748 scopus 로고
    • Tissue inhibitors of metalloproteinases and their cell growth-promoting activity
    • Hayakawa T. Tissue inhibitors of metalloproteinases and their cell growth-promoting activity. Cell Struct Func 1994; 19: 109-14.
    • (1994) Cell Struct Func , vol.19 , pp. 109-114
    • Hayakawa, T.1
  • 8
    • 0029969277 scopus 로고    scopus 로고
    • The roles of tissue inhibitors of metalloproteinases in tissue remodeling and cell growth
    • 1996
    • Edwards DR, Beaudry PP, Laing TD, Kowal V, Leco KJ, Leco PA et al. The roles of tissue inhibitors of metalloproteinases in tissue remodeling and cell growth. 1996, Int J Obes 1996; 20(suppl. 3): 9-15.
    • (1996) Int J Obes , vol.20 , Issue.SUPPL. 3 , pp. 9-15
    • Edwards, D.R.1    Beaudry, P.P.2    Laing, T.D.3    Kowal, V.4    Leco, K.J.5    Leco, P.A.6
  • 9
    • 1842377505 scopus 로고    scopus 로고
    • Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
    • Gomis-Ruth FX, Maskos K, Betz M, Bergner A, Huber R, Suzuki K, et al. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 1997; 89: 77-81.
    • (1997) Nature , vol.89 , pp. 77-81
    • Gomis-Ruth, F.X.1    Maskos, K.2    Betz, M.3    Bergner, A.4    Huber, R.5    Suzuki, K.6
  • 10
    • 0025739240 scopus 로고
    • Regulation of the autoactivation of human 72-kDa progelatinase by tissue inhibitor of metalloproteinase-2
    • Howard EW, Bullen EC, Banda MJ. Regulation of the autoactivation of human 72-kDa progelatinase by tissue inhibitor of metalloproteinase-2. J Biol Chem 1991; 266: 13064-9.
    • (1991) J Biol Chem , vol.266 , pp. 13064-13069
    • Howard, E.W.1    Bullen, E.C.2    Banda, M.J.3
  • 11
    • 0025834914 scopus 로고
    • The purification of tissue inhibitor of metalloproteinase-2 from its 72 kDa progelatinase complex
    • Ward R, Hembry RM, Reynolds JJ, Murphy G. The purification of tissue inhibitor of metalloproteinase-2 from its 72 kDa progelatinase complex. Biochem J 1991; 278: 179-87.
    • (1991) Biochem J , vol.278 , pp. 179-187
    • Ward, R.1    Hembry, R.M.2    Reynolds, J.J.3    Murphy, G.4
  • 12
    • 0028279004 scopus 로고
    • Different domain interactions are involved in the binding of tissue inhibitor of metalloproteinases to stromelysin-1 and gelatinase A
    • Nguyen Q, Willenbrock F, Cockett MI, O'Shea M, Docherty AJP, Murphy G. Different domain interactions are involved in the binding of tissue inhibitor of metalloproteinases to stromelysin-1 and gelatinase A. Biochemistry 1994; 33: 2089-95.
    • (1994) Biochemistry , vol.33 , pp. 2089-2095
    • Nguyen, Q.1    Willenbrock, F.2    Cockett, M.I.3    O'Shea, M.4    Docherty, A.J.P.5    Murphy, G.6
  • 13
    • 0029019867 scopus 로고
    • The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family
    • Apte SS, Olsen BR, Murphy G. The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family. J Biol Chem 1995; 270: 14313-8.
    • (1995) J Biol Chem , vol.270 , pp. 14313-14318
    • Apte, S.S.1    Olsen, B.R.2    Murphy, G.3
  • 15
    • 0029891956 scopus 로고    scopus 로고
    • Processing of a precursor of 72-kilo Dalton type IV collagenase/gelatinase A by a recombinant membrane-type 1 matrix metalloproteinase
    • Kinoshita T, Sato H, Takino T, Itoh M, Akizawa T, Seiki M. Processing of a precursor of 72-kilo Dalton type IV collagenase/gelatinase A by a recombinant membrane-type 1 matrix metalloproteinase. Cancer Res 1996; 56: 2535-8.
    • (1996) Cancer Res , vol.56 , pp. 2535-2538
    • Kinoshita, T.1    Sato, H.2    Takino, T.3    Itoh, M.4    Akizawa, T.5    Seiki, M.6
  • 16
    • 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
    • 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. J Biol Chem 1996; 271: 17119-23.
    • (1996) J Biol Chem , vol.271 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 17
    • 0025809874 scopus 로고
    • Inhibition of autoproteolytic activation of interstitial procollagenase by recombinant metalloproteinase inhibitor M1/TIMP-2
    • DeClerck YA, Yean TD, Lu HS, Ting J, Langley KE. Inhibition of autoproteolytic activation of interstitial procollagenase by recombinant metalloproteinase inhibitor M1/TIMP-2. J Biol Chem 1991; 266: 3893-9.
    • (1991) J Biol Chem , vol.266 , pp. 3893-3899
    • DeClerck, Y.A.1    Yean, T.D.2    Lu, H.S.3    Ting, J.4    Langley, K.E.5
  • 18
    • 0030995022 scopus 로고    scopus 로고
    • Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelkatinase A
    • Bigg HF, Shi YE, Liu YE, Steffensen B, Overall CM. Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelkatinase A. J Biol Chem 1997; 272: 15496-500.
    • (1997) J Biol Chem , vol.272 , pp. 15496-15500
    • Bigg, H.F.1    Shi, Y.E.2    Liu, Y.E.3    Steffensen, B.4    Overall, C.M.5
  • 19
    • 0030323007 scopus 로고    scopus 로고
    • A review of tissue inhibitor of metalloproteinases-3 (TIMP-3) and experimental analysis of its effect on primary tumour growth
    • Anand-Apte B, Bao L, Smith R, Iwata K, Olsen BR, Zetter B et al. A review of tissue inhibitor of metalloproteinases-3 (TIMP-3) and experimental analysis of its effect on primary tumour growth. Biochem Cell Biol 1996; 74: 853-62.
    • (1996) Biochem Cell Biol , vol.74 , pp. 853-862
    • Anand-Apte, B.1    Bao, L.2    Smith, R.3    Iwata, K.4    Olsen, B.R.5    Zetter, B.6
  • 20
    • 0028097742 scopus 로고
    • Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44, and link protein
    • Yang B, Yang BL, Savani RC, Turley EA. Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44, and link protein. EMBO J 1994; 13: 286-96.
    • (1994) EMBO J , vol.13 , pp. 286-296
    • Yang, B.1    Yang, B.L.2    Savani, R.C.3    Turley, E.A.4
  • 21
    • 0027230170 scopus 로고
    • Regulation of development and differentiation by the extracellular matrix
    • Adams JC, Watt EM. Regulation of development and differentiation by the extracellular matrix. Development 1993; 117: 1183-98.
    • (1993) Development , vol.117 , pp. 1183-1198
    • Adams, J.C.1    Watt, E.M.2
  • 22
    • 0027322018 scopus 로고
    • Regulation of gene expression and cell function by the extracellular matrix
    • Jones PL, Schmidhauser C, Bissell MJ. Regulation of gene expression and cell function by the extracellular matrix. Crit Rev Euk Gene Exp 1993; 3: 37-154.
    • (1993) Crit Rev Euk Gene Exp , vol.3 , pp. 37-154
    • Jones, P.L.1    Schmidhauser, C.2    Bissell, M.J.3
  • 23
    • 0026768210 scopus 로고
    • Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial functions during involution
    • Talhouk RS, Bissell MJ, Werb Z. Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial functions during involution. J Cell Biol 1992; 118: 1271-82.
    • (1992) J Cell Biol , vol.118 , pp. 1271-1282
    • Talhouk, R.S.1    Bissell, M.J.2    Werb, Z.3
  • 24
    • 0025976838 scopus 로고
    • Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor
    • Yayon A, Klagsbrun M, Esko JD, Leder P, Ornitz DM. Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 1991; 64: 841-8.
    • (1991) Cell , vol.64 , pp. 841-848
    • Yayon, A.1    Klagsbrun, M.2    Esko, J.D.3    Leder, P.4    Ornitz, D.M.5
  • 25
    • 0027276765 scopus 로고
    • Betaglcan presents ligand to the TGF-β signaling receptor
    • Lopez-Casillas F, Payne HM, Andres JL, Massague J. Betaglcan presents ligand to the TGF-β signaling receptor. Cell 1993; 73: 1435-44.
    • (1993) Cell , vol.73 , pp. 1435-1444
    • Lopez-Casillas, F.1    Payne, H.M.2    Andres, J.L.3    Massague, J.4
  • 26
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-β by the proteoglycan decorin
    • Yamaguchi Y, Mann DM, Ruoslahti E. Negative regulation of transforming growth factor-β by the proteoglycan decorin. Nature 1990; 346: 281-4.
    • (1990) Nature , vol.346 , pp. 281-284
    • Yamaguchi, Y.1    Mann, D.M.2    Ruoslahti, E.3
  • 28
    • 0026012155 scopus 로고
    • Angiotensin II induces secretion of plasminogen activator inhibitor 1 and a tissue metalloproteinase-inhibitor related protein from rat brain astrocytes
    • Olson JA Jr, Shiverick KT, Ogilvie S, Buhi WC, Raizada MK. Angiotensin II induces secretion of plasminogen activator inhibitor 1 and a tissue metalloproteinase-inhibitor related protein from rat brain astrocytes. Proc Natl Acad Sci USA 1991; 88: 1928-32.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1928-1932
    • Olson J.A., Jr.1    Shiverick, K.T.2    Ogilvie, S.3    Buhi, W.C.4    Raizada, M.K.5
  • 29
    • 0025734094 scopus 로고
    • Interleukin-6 induces the synthesis of tissue inhibitor of metalloproteinases-1/erythroid potentiating activity (TIMP-1/EPA)
    • Lotz M, Guerne PA. Interleukin-6 induces the synthesis of tissue inhibitor of metalloproteinases-1/erythroid potentiating activity (TIMP-1/EPA). J Biol Chem 1991; 266: 2017-20.
    • (1991) J Biol Chem , vol.266 , pp. 2017-2020
    • Lotz, M.1    Guerne, P.A.2
  • 30
    • 0025740859 scopus 로고
    • Identification of a serum- and phorbol-ester responsive elements in the murine tissue inhibitor of metalloproteinase gene
    • Campbell CE, Flenniken AM, Skup D, Williams BR. Identification of a serum- and phorbol-ester responsive elements in the murine tissue inhibitor of metalloproteinase gene. J Biol Chem 1991; 266: 7199-206.
    • (1991) J Biol Chem , vol.266 , pp. 7199-7206
    • Campbell, C.E.1    Flenniken, A.M.2    Skup, D.3    Williams, B.R.4
  • 31
    • 0026496059 scopus 로고
    • Involvement of AP1 and PEA3 binding sites in the regulation of murine tissue inhibitor of metalloproteinases-1 (TIMP-1) transcription
    • Edwards DR, Rocheleau H, Sharma RR, Willis AJ, Cowie A, Hassell TA et al. Involvement of AP1 and PEA3 binding sites in the regulation of murine tissue inhibitor of metalloproteinases-1 (TIMP-1) transcription. Biochem Biophys Acta 1992; 171: 41-55.
    • (1992) Biochem Biophys Acta , vol.171 , pp. 41-55
    • Edwards, D.R.1    Rocheleau, H.2    Sharma, R.R.3    Willis, A.J.4    Cowie, A.5    Hassell, T.A.6
  • 32
    • 0028198497 scopus 로고
    • Characterization of the promoter of the gene encoding human tissue inhibitor of metalloproteinases-2 (TIMP-2)
    • Declerck YA, Yean TD, Lee Y, Tornich JM, Langley KE. Characterization of the promoter of the gene encoding human tissue inhibitor of metalloproteinases-2 (TIMP-2). Gene 1994; 139: 185-91.
    • (1994) Gene , vol.139 , pp. 185-191
    • Declerck, Y.A.1    Yean, T.D.2    Lee, Y.3    Tornich, J.M.4    Langley, K.E.5
  • 33
    • 0024553199 scopus 로고
    • Developmental expression of tissue inhibitor of metalloproteinases (TIMP) RNA
    • Nomura S, Hogan BLM, Wills AJ, Heath JK, Edwards DR. Developmental expression of tissue inhibitor of metalloproteinases (TIMP) RNA. Development 1989; 105: 575-83.
    • (1989) Development , vol.105 , pp. 575-583
    • Nomura, S.1    Hogan, B.L.M.2    Wills, A.J.3    Heath, J.K.4    Edwards, D.R.5
  • 34
    • 0027260519 scopus 로고
    • Temporal expression of tissue inhibitors of metalloproteinases in mouse reproductive tissues during gestation
    • Waterhouse P, Denhardt DT, Khokha R. Temporal expression of tissue inhibitors of metalloproteinases in mouse reproductive tissues during gestation. Mol Reprod Dev 1993; 35: 219-26.
    • (1993) Mol Reprod Dev , vol.35 , pp. 219-226
    • Waterhouse, P.1    Denhardt, D.T.2    Khokha, R.3
  • 35
    • 0027932836 scopus 로고
    • Gene encoding a novel murine TIMP, TIMP-3, is expressed in developing mouse epithelia, cartilage, and muscle and is located on chromosome 10
    • Apte SS, Hayashi K, Seldin MF, Mattei MG, Hayashi M, Olsen BR. Gene encoding a novel murine TIMP, TIMP-3, is expressed in developing mouse epithelia, cartilage, and muscle and is located on chromosome 10. Develop Dynam 1994; 200: 177-97.
    • (1994) Develop Dynam , vol.200 , pp. 177-197
    • Apte, S.S.1    Hayashi, K.2    Seldin, M.F.3    Mattei, M.G.4    Hayashi, M.5    Olsen, B.R.6
  • 36
    • 0022382006 scopus 로고
    • Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid potentiating activity
    • Docherty AJP, Lyons A, Smith BJ, Wright EM, Stephens PE, Harris TJ. Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid potentiating activity. Nature 1985; 318: 66-69.
    • (1985) Nature , vol.318 , pp. 66-69
    • Docherty, A.J.P.1    Lyons, A.2    Smith, B.J.3    Wright, E.M.4    Stephens, P.E.5    Harris, T.J.6
  • 37
    • 0022258814 scopus 로고
    • Molecular characterization and expression of the gene encoding human erythroid-potentiating activity
    • Gasson JC, Golde DW, Kaufman SE, Westbrook CA, Hewick RM, Kaufman RJ et al. Molecular characterization and expression of the gene encoding human erythroid-potentiating activity. Nature 1985; 315: 768-71.
    • (1985) Nature , vol.315 , pp. 768-771
    • Gasson, J.C.1    Golde, D.W.2    Kaufman, S.E.3    Westbrook, C.A.4    Hewick, R.M.5    Kaufman, R.J.6
  • 38
    • 0021229564 scopus 로고
    • Purification and characterization of human T-lymphocyte-derived erythroid-potentiating activity
    • Westbrook CA, Gasson JC, Gerber SE, Selsted ME, Golde DW. Purification and characterization of human T-lymphocyte-derived erythroid-potentiating activity. J Biol Chem 1984; 259: 992-6.
    • (1984) J Biol Chem , vol.259 , pp. 992-996
    • Westbrook, C.A.1    Gasson, J.C.2    Gerber, S.E.3    Selsted, M.E.4    Golde, D.W.5
  • 40
    • 0025297180 scopus 로고
    • Tissue inhibitor of metalloproteinases from human bone marrow stromal cell line KM102 has erythroid-potentiating activity, suggesting its possibly bifunctional role in the hematopoietic microenvironment
    • Hayakawa T, Yamashita K, Kishi J, Harigaya K. Tissue inhibitor of metalloproteinases from human bone marrow stromal cell line KM102 has erythroid-potentiating activity, suggesting its possibly bifunctional role in the hematopoietic microenvironment. FEBS Lett 1990; 268: 125-8.
    • (1990) FEBS Lett , vol.268 , pp. 125-128
    • Hayakawa, T.1    Yamashita, K.2    Kishi, J.3    Harigaya, K.4
  • 41
    • 0026601513 scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2) has erythroid potentiating activity
    • Stetler-Stevenson WG, Bersch N, Golde DW. Tissue inhibitor of metalloproteinase-2 (TIMP-2) has erythroid potentiating activity. FEBS Lett 1992; 296: 231-4.
    • (1992) FEBS Lett , vol.296 , pp. 231-234
    • Stetler-Stevenson, W.G.1    Bersch, N.2    Golde, D.W.3
  • 42
    • 0027851841 scopus 로고
    • Erythroid potentiating activity of tissue inhibitor of metalloproteinases on the differentiation of erythropoietin-responsive mouse erythroleukemia cell line, ELM-I-1-3, is closely related to its cell growth potentiating activity
    • Murate T, Yamashita K, Ohashi H, Kagami Y, Tushita K, Kinoshita T et al. Erythroid potentiating activity of tissue inhibitor of metalloproteinases on the differentiation of erythropoietin-responsive mouse erythroleukemia cell line, ELM-I-1-3, is closely related to its cell growth potentiating activity. Exp Hematol 1993; 21: 169-76.
    • (1993) Exp Hematol , vol.21 , pp. 169-176
    • Murate, T.1    Yamashita, K.2    Ohashi, H.3    Kagami, Y.4    Tushita, K.5    Kinoshita, T.6
  • 43
    • 0025988402 scopus 로고
    • Growth stimulation of human keratinocytes by tissue inhibitor of metalloproteinases
    • Bertaux B, Hornebeck W, Eisen AZ, Dubertret L. Growth stimulation of human keratinocytes by tissue inhibitor of metalloproteinases. J Invest Dermatol 1991; 97: 670-85.
    • (1991) J Invest Dermatol , vol.97 , pp. 670-685
    • Bertaux, B.1    Hornebeck, W.2    Eisen, A.Z.3    Dubertret, L.4
  • 44
    • 0026568011 scopus 로고
    • Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells
    • Hayakawa T, Yamashita K, Tanzawa K, Uchijima E, Iwata K. Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells. FEBS Lett 1992; 298: 29-32.
    • (1992) FEBS Lett , vol.298 , pp. 29-32
    • Hayakawa, T.1    Yamashita, K.2    Tanzawa, K.3    Uchijima, E.4    Iwata, K.5
  • 45
    • 0028132867 scopus 로고
    • Cell growth-promoting activity of tissue inhibitor of tissue inhibitor of metalloproteinases-2 (TIMP-2)
    • Hayakawa T, Yamashita K, Ohuchi E, Shinagawa A. Cell growth-promoting activity of tissue inhibitor of tissue inhibitor of metalloproteinases-2 (TIMP-2). J Cell Sci 1994; 107: 2373-9.
    • (1994) J Cell Sci , vol.107 , pp. 2373-2379
    • Hayakawa, T.1    Yamashita, K.2    Ohuchi, E.3    Shinagawa, A.4
  • 46
    • 0027301930 scopus 로고
    • TIMP-2, a growth-stimulating protein from SV-40 transformed human fibroblasts
    • Nemeth JA, Goolsby CL. TIMP-2, a growth-stimulating protein from SV-40 transformed human fibroblasts. Exp Cell Res 1993; 207: 376-82.
    • (1993) Exp Cell Res , vol.207 , pp. 376-382
    • Nemeth, J.A.1    Goolsby, C.L.2
  • 47
    • 0025822038 scopus 로고
    • The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor
    • Kolkenbrock H, Orgel D, Hecker-Kia A, Noack W, Ulbrich N. The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor. Eur J Biochem 1991; 198: 775-81.
    • (1991) Eur J Biochem , vol.198 , pp. 775-781
    • Kolkenbrock, H.1    Orgel, D.2    Hecker-Kia, A.3    Noack, W.4    Ulbrich, N.5
  • 49
    • 0030605008 scopus 로고    scopus 로고
    • Tyrosine phosphorylation is crucial for growth signaling by tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2)
    • Yamashita K, Suzuki M, Iwata H, Koike T, Hamaguchi M, Shinagawa A et al. Tyrosine phosphorylation is crucial for growth signaling by tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2). FEBS Lett 1996; 396: 103-7.
    • (1996) FEBS Lett , vol.396 , pp. 103-107
    • Yamashita, K.1    Suzuki, M.2    Iwata, H.3    Koike, T.4    Hamaguchi, M.5    Shinagawa, A.6
  • 50
    • 0013563259 scopus 로고    scopus 로고
    • Growth signaling through tyrosine and mitogen-activated protein kinases by TIMP-1 and TIMP-2
    • (SP Hawkes, DR Edwards, R Khokha) eds. Lausanne, Switzerland: Harwood Academic Publishing, in press
    • Yamashita K, Suzuki M, Iwata H, Koike T, Hamaguchi M, Shinagawa A et al. Growth signaling through tyrosine and mitogen-activated protein kinases by TIMP-1 and TIMP-2. In Inhibitors of Metallorpoteinases in Development and Diseases (SP Hawkes, DR Edwards, R Khokha) eds. Lausanne, Switzerland: Harwood Academic Publishing, in press, 1998.
    • (1998) Inhibitors of Metallorpoteinases in Development and Diseases
    • Yamashita, K.1    Suzuki, M.2    Iwata, H.3    Koike, T.4    Hamaguchi, M.5    Shinagawa, A.6
  • 51
    • 0026465338 scopus 로고
    • Role of the 21-kDa protein TIMP-3 in oncogenic transformation of cultured chicken embryo fibroblasts
    • Yang TT, Hawkes SP. Role of the 21-kDa protein TIMP-3 in oncogenic transformation of cultured chicken embryo fibroblasts. Proc Natl Acad Sci USA 1992; 89: 10676-80.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10676-10680
    • Yang, T.T.1    Hawkes, S.P.2
  • 52
    • 0024570443 scopus 로고
    • A sandwich enzyme immunoassay for collagenase inhibitor using monoclonal antibodies
    • Kodama S, Yamashita K, Kishi J, Iwata K, Hayakawa T. A sandwich enzyme immunoassay for collagenase inhibitor using monoclonal antibodies. Matrix 1989; 9: 1-6.
    • (1989) Matrix , vol.9 , pp. 1-6
    • Kodama, S.1    Yamashita, K.2    Kishi, J.3    Iwata, K.4    Hayakawa, T.5
  • 53
    • 0027363784 scopus 로고
    • A one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases-2 using monoclonal antibodies
    • Fujimoto N, Zhang J, Iwata K, Shinya T, Okada Y, Hayakawa T. A one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases-2 using monoclonal antibodies. Clin Chim Acta 1993; 220: 31-45.
    • (1993) Clin Chim Acta , vol.220 , pp. 31-45
    • Fujimoto, N.1    Zhang, J.2    Iwata, K.3    Shinya, T.4    Okada, Y.5    Hayakawa, T.6
  • 54
    • 0031750878 scopus 로고    scopus 로고
    • Cell cycle-associated accumulation of tissue inhibitor of metalloproteinases-1 (TIMP-1) in the nuclei of human gingival fibroblasts
    • in press
    • Zhao WQ, Li H, Yamashita K, Guo XK, Hoshino T, Yoshida S et al. Cell cycle-associated accumulation of tissue inhibitor of metalloproteinases-1 (TIMP-1) in the nuclei of human gingival fibroblasts. J Cell Sci in press 1998.
    • (1998) J Cell Sci
    • Zhao, W.Q.1    Li, H.2    Yamashita, K.3    Guo, X.K.4    Hoshino, T.5    Yoshida, S.6
  • 55
    • 0027383944 scopus 로고
    • Tissue inhibitor of metalloproteinases-2 inhibits bFGF-induced human microvascular endothelial cell proliferation
    • Murphy AN, Unsworth EJ, Stetler-Stevenson WG. Tissue inhibitor of metalloproteinases-2 inhibits bFGF-induced human microvascular endothelial cell proliferation. J Cell Physiol 1993; 157: 351-458.
    • (1993) J Cell Physiol , vol.157 , pp. 351-458
    • Murphy, A.N.1    Unsworth, E.J.2    Stetler-Stevenson, W.G.3
  • 56
    • 0027953576 scopus 로고
    • Researches test TIMP-2 as potential tumor terminator
    • Parkins T. Researches test TIMP-2 as potential tumor terminator. J Natl Canter Inst 1994; 86: 174-5.
    • (1994) J Natl Canter Inst , vol.86 , pp. 174-175
    • Parkins, T.1
  • 57
    • 0028258310 scopus 로고
    • Tissue inhibitor of metalloproteinases (TIMP-1) produced by granulosa and oviduct cells enhances in vitro development of bovine embryo
    • Satoh H, Kobayashi K, Yamashita S, Kikuchi M, Sendai Y, Hoshi H. Tissue inhibitor of metalloproteinases (TIMP-1) produced by granulosa and oviduct cells enhances in vitro development of bovine embryo. Biol Reprod 1994; 50: 835-44.
    • (1994) Biol Reprod , vol.50 , pp. 835-844
    • Satoh, H.1    Kobayashi, K.2    Yamashita, S.3    Kikuchi, M.4    Sendai, Y.5    Hoshi, H.6
  • 58
    • 0030936664 scopus 로고    scopus 로고
    • Effect of estrus-associated glycoprotein and tissue inhibitor of metalloproteinase-1 secreted by oviduct cells on in vitro bovine embryo development
    • Vansteenbrugge A, Van Langendonckt A, Massip A, Dessy F. Effect of estrus-associated glycoprotein and tissue inhibitor of metalloproteinase-1 secreted by oviduct cells on in vitro bovine embryo development. Mol Reproduct Develop 1997; 46: 527-34.
    • (1997) Mol Reproduct Develop , vol.46 , pp. 527-534
    • Vansteenbrugge, A.1    Van Langendonckt, A.2    Massip, A.3    Dessy, F.4
  • 60
    • 0030936152 scopus 로고    scopus 로고
    • Assessment of the role of tissue inhibitor of metalloproteinase-1 (TIMP-1) during the periovulatory period in female mice lacking a functional TIMP-1 gene
    • Nothnick WB, Soloway P, Curry TE Jr. Assessment of the role of tissue inhibitor of metalloproteinase-1 (TIMP-1) during the periovulatory period in female mice lacking a functional TIMP-1 gene. Biol Reproduct 1997; 56: 1181-8.
    • (1997) Biol Reproduct , vol.56 , pp. 1181-1188
    • Nothnick, W.B.1    Soloway, P.2    Curry T.E., Jr.3
  • 61
    • 0027177799 scopus 로고
    • Newly established murine pituitary folliculo-stellate-like cell line secretes potent pituitary glandular cell survival factors
    • Matsumoto H, Ishibashi Y, Ohtaki T, Hasegawa Y, Koyama C, Inoue K. Newly established murine pituitary folliculo-stellate-like cell line secretes potent pituitary glandular cell survival factors. Biochem Biophys Res Commun 1993; 194: 909-15.
    • (1993) Biochem Biophys Res Commun , vol.194 , pp. 909-915
    • Matsumoto, H.1    Ishibashi, Y.2    Ohtaki, T.3    Hasegawa, Y.4    Koyama, C.5    Inoue, K.6
  • 62
    • 0028793708 scopus 로고
    • Partial purification and amino acid sequence analysis of endometriosis protein-II (ENDO-II) reveals homology with TIMP-1
    • Sharpe-Timms KL, Penney LL, Zimmer RL, Wright JA, Zhang Y, Surewick K. Partial purification and amino acid sequence analysis of endometriosis protein-II (ENDO-II) reveals homology with TIMP-1. J Clin Endocrine Metab 1995; 80: 3784-7.
    • (1995) J Clin Endocrine Metab , vol.80 , pp. 3784-3787
    • Sharpe-Timms, K.L.1    Penney, L.L.2    Zimmer, R.L.3    Wright, J.A.4    Zhang, Y.5    Surewick, K.6
  • 63
    • 0028168842 scopus 로고
    • Tissue inhibitor of metalloproteinases (TIMP-1) stimulates the secretion of collagenase from human skin fibroblasts
    • Clark IM, Powell LK, Cawston TE. Tissue inhibitor of metalloproteinases (TIMP-1) stimulates the secretion of collagenase from human skin fibroblasts. Biochem Biopys Res Commun 1994; 203: 874-80.
    • (1994) Biochem Biopys Res Commun , vol.203 , pp. 874-880
    • Clark, I.M.1    Powell, L.K.2    Cawston, T.E.3
  • 64
    • 0022362769 scopus 로고
    • Human alveolar macrophages produce a fibroblast like collagenase and collagenase like inhibitor
    • Welgus HG, Campbell EJ, Bar-Shavit Z, Senior RM, Teitelbaum SL. Human alveolar macrophages produce a fibroblast like collagenase and collagenase like inhibitor. J Clin Invest 1985; 76: 219-24.
    • (1985) J Clin Invest , vol.76 , pp. 219-224
    • Welgus, H.G.1    Campbell, E.J.2    Bar-Shavit, Z.3    Senior, R.M.4    Teitelbaum, S.L.5
  • 65
    • 0025001756 scopus 로고
    • Immunoassays for the detection of human collagenase, stromelysin, tissue inhibitor of metalloproteinases (TIMP) and enzyme-inhibitor complexes
    • Cooksley S, Hipkiss JB, Tickle SP, Holmes-Levers E, Docherty AJ, Murphy G et al. Immunoassays for the detection of human collagenase, stromelysin, tissue inhibitor of metalloproteinases (TIMP) and enzyme-inhibitor complexes. Matrix 1990; 10: 285-91.
    • (1990) Matrix , vol.10 , pp. 285-291
    • Cooksley, S.1    Hipkiss, J.B.2    Tickle, S.P.3    Holmes-Levers, E.4    Docherty, A.J.5    Murphy, G.6
  • 66
    • 0025827840 scopus 로고
    • Polyclonal and monoclonal antibodies against human tissue inhibitor of metalloproteinases (TIMP) and the design of an enzyme-linked immunosorbent assay to measure TIMP
    • Clark IM, Powell LK, Wright JK, Cawston TE. Polyclonal and monoclonal antibodies against human tissue inhibitor of metalloproteinases (TIMP) and the design of an enzyme-linked immunosorbent assay to measure TIMP. Matrix 1991; 11: 76-85.
    • (1991) Matrix , vol.11 , pp. 76-85
    • Clark, I.M.1    Powell, L.K.2    Wright, J.K.3    Cawston, T.E.4
  • 67
    • 0027097568 scopus 로고
    • Dissociation of collagenase-tissue inhibitor of metalloproteinases-1 (TIMP-1) complex - Its application for the independent measurements of TIMP- and collagenase activity in culture media and body fluids
    • Yamashita K, Zhang J, Zou L, Hayakawa H, Noguchi T, Kondo I et al. Dissociation of collagenase-tissue inhibitor of metalloproteinases-1 (TIMP-1) complex - its application for the independent measurements of TIMP- and collagenase activity in culture media and body fluids. Matrix 1992; 12: 481-7.
    • (1992) Matrix , vol.12 , pp. 481-487
    • Yamashita, K.1    Zhang, J.2    Zou, L.3    Hayakawa, H.4    Noguchi, T.5    Kondo, I.6
  • 68
    • 0028509288 scopus 로고
    • Collagenase activity and tissue inhibitor of metalloproteinases-1 (TIMP-1) content in human whole saliva from clinically healthy and periodontally diseased subjects
    • Hayakawa H, Yamashita H, Ohwaki K, Sawa M, Noguchi T, Iwata K et al. Collagenase activity and tissue inhibitor of metalloproteinases-1 (TIMP-1) content in human whole saliva from clinically healthy and periodontally diseased subjects. J Periodont Res 1994; 29: 305-8.
    • (1994) J Periodont Res , vol.29 , pp. 305-308
    • Hayakawa, H.1    Yamashita, H.2    Ohwaki, K.3    Sawa, M.4    Noguchi, T.5    Iwata, K.6
  • 69
    • 0025057488 scopus 로고
    • Rapid one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases
    • Kodama S, Iwata K, Iwata H, Yamashita K, Hayakawa T. Rapid one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases. J Immunol Methods 1990; 127: 103-8.
    • (1990) J Immunol Methods , vol.127 , pp. 103-108
    • Kodama, S.1    Iwata, K.2    Iwata, H.3    Yamashita, K.4    Hayakawa, T.5
  • 70
    • 0029154908 scopus 로고
    • Increased levels of stromelysin-1 and tissue inhibitor of metalloproteinase-1 in sera from patients with rheumatoid arthritis
    • Yoshihara Y, Obata K, Fujimoto N, Yamashita K, Hayakawa T, Shimmei M. Increased levels of stromelysin-1 and tissue inhibitor of metalloproteinase-1 in sera from patients with rheumatoid arthritis. Arth Rheum 1995; 38: 969-75.
    • (1995) Arth Rheum , vol.38 , pp. 969-975
    • Yoshihara, Y.1    Obata, K.2    Fujimoto, N.3    Yamashita, K.4    Hayakawa, T.5    Shimmei, M.6
  • 71
    • 0013617514 scopus 로고    scopus 로고
    • Levels of circulating collagenase, stromelysin-1, and tissue inhibitor of matrix metalloproteinases-1 in patients with rheumatoid arthritis
    • Manicourt DH, Fujimoto N, Obata K, Thonar EJ. Levels of circulating collagenase, stromelysin-1, and tissue inhibitor of matrix metalloproteinases-1 in patients with rheumatoid arthritis. Arth Rheum 1996; 39: 884-6.
    • (1996) Arth Rheum , vol.39 , pp. 884-886
    • Manicourt, D.H.1    Fujimoto, N.2    Obata, K.3    Thonar, E.J.4
  • 72
    • 0027268661 scopus 로고
    • Clinical evaluation of serum tissue inhibitor of metalloproteinases-1 levels in patients with liver diseases
    • Muzzillo DA, Imoto M, Fukuda Y, Koyama Y, Saga S, Nagai Y et al. Clinical evaluation of serum tissue inhibitor of metalloproteinases-1 levels in patients with liver diseases. J Gasroenter Hepatol 1993; 8: 437-41.
    • (1993) J Gasroenter Hepatol , vol.8 , pp. 437-441
    • Muzzillo, D.A.1    Imoto, M.2    Fukuda, Y.3    Koyama, Y.4    Saga, S.5    Nagai, Y.6
  • 73
    • 0013588454 scopus 로고
    • Diagnostic value of serum laminin, type IV collagen peptides, collagenase inhibitor and prolylhydroxylase on HCC
    • (JL Sung, DS Chen) eds. Hong Kong: Excerpta Medica Asia Ld
    • Ichida T, Miyagiwa M, Inoue K. Diagnostic value of serum laminin, type IV collagen peptides, collagenase inhibitor and prolylhydroxylase on HCC. In, Viral Hepatitis and Hepatocellular Carcinoma, (JL Sung, DS Chen) eds. Hong Kong: Excerpta Medica Asia Ld, 1988; 579-89.
    • (1988) Viral Hepatitis and Hepatocellular Carcinoma , pp. 579-589
    • Ichida, T.1    Miyagiwa, M.2    Inoue, K.3
  • 74
    • 0028130051 scopus 로고
    • Serum metalloproteinases and their inhibitors; makers for malignant potential
    • Baker T, Tickle S, Wasan H, Docherty A, Isenberg D, Waxman J. Serum metalloproteinases and their inhibitors; makers for malignant potential. Br J Cancer 1994; 70: 506-12.
    • (1994) Br J Cancer , vol.70 , pp. 506-512
    • Baker, T.1    Tickle, S.2    Wasan, H.3    Docherty, A.4    Isenberg, D.5    Waxman, J.6
  • 75
    • 0005419738 scopus 로고
    • Platelet-derived collagenase inhibitor: Characterization and subcellular localization
    • Cooper TW, Eisen AZ, Stricklin GP, Welgus HG. Platelet-derived collagenase inhibitor: characterization and subcellular localization. Proc Natl Acad Sci USA 1985; 82: 2779-83.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2779-2783
    • Cooper, T.W.1    Eisen, A.Z.2    Stricklin, G.P.3    Welgus, H.G.4
  • 76
    • 9844258888 scopus 로고    scopus 로고
    • The production of tissue inhibitors of Metalloproteinases (TIMPs) in megakaryopoiesis: Possible role of, platelet- and megakaryocyte-derived TIMPs in bone marrow fibrosis
    • Murate T, Yamashita K, Isogai C, Suzuki H, Ichihara M, Hatano S et al. The production of tissue inhibitors of Metalloproteinases (TIMPs) in megakaryopoiesis: possible role of, platelet- and megakaryocyte-derived TIMPs in bone marrow fibrosis. Br J Haematol 1997; 99: 181-9.
    • (1997) Br J Haematol , vol.99 , pp. 181-189
    • Murate, T.1    Yamashita, K.2    Isogai, C.3    Suzuki, H.4    Ichihara, M.5    Hatano, S.6
  • 77
    • 0020479995 scopus 로고
    • Growth factors from platelets, monocytes, and endothelium: Their role in cell proliferation
    • Ross R, Reines E, Bowen-Pope D. Growth factors from platelets, monocytes, and endothelium: their role in cell proliferation. Ann NY Acad Sci 1982; 397: 18-24.
    • (1982) Ann NY Acad Sci , vol.397 , pp. 18-24
    • Ross, R.1    Reines, E.2    Bowen-Pope, D.3
  • 78
    • 0024465571 scopus 로고
    • Platelet-derived growth factor concentrations in platelet-poor plasma and urine from patients with myeloproliferative disorders
    • Gersuk GM, Carmel R, Pattengale PK. Platelet-derived growth factor concentrations in platelet-poor plasma and urine from patients with myeloproliferative disorders. Blood 1989; 74: 2330-4.
    • (1989) Blood , vol.74 , pp. 2330-2334
    • Gersuk, G.M.1    Carmel, R.2    Pattengale, P.K.3
  • 79
    • 0027525858 scopus 로고
    • Characterization of an acute micromegakaryocytic leukemia: Evidence for the pathogenesis of meylofibrosis
    • Reilly JT. Characterization of an acute micromegakaryocytic leukemia: evidence for the pathogenesis of meylofibrosis. Br J Haematol 1993; 83: 58-62.
    • (1993) Br J Haematol , vol.83 , pp. 58-62
    • Reilly, J.T.1
  • 80
    • 0021962675 scopus 로고
    • Fibrosis of the bone marrow: Content and causes
    • McCarthy DM. Fibrosis of the bone marrow: content and causes. Br J Haematol 1985; 59: 1-7.
    • (1985) Br J Haematol , vol.59 , pp. 1-7
    • McCarthy, D.M.1
  • 81
    • 0028100745 scopus 로고
    • Pathogenesis of idiopathic myelofibrosis. Present status and future directions
    • Reilly JT. Pathogenesis of idiopathic myelofibrosis. Present status and future directions Br J Haematol 1994; 88: 1-8.
    • (1994) Br J Haematol , vol.88 , pp. 1-8
    • Reilly, J.T.1
  • 82
    • 0029064922 scopus 로고
    • Renal expression of genes that promote interstitial inflammation and fibrosis in rats with protein overload proteinuria
    • Eddy AA, Giachelli CM. Renal expression of genes that promote interstitial inflammation and fibrosis in rats with protein overload proteinuria. Kidney Int 1995; 47: 1546-57.
    • (1995) Kidney Int , vol.47 , pp. 1546-1557
    • Eddy, A.A.1    Giachelli, C.M.2
  • 83
    • 0026090926 scopus 로고
    • Pathogenesis of interstitial fibrosis in chronic purine amino nucleoside nephrosis
    • Jones CL, Buch S, Post M, McCulloch L, Liu E, Eddy AA. Pathogenesis of interstitial fibrosis in chronic purine amino nucleoside nephrosis. Kid Int 1991; 40: 1020-31.
    • (1991) Kid Int , vol.40 , pp. 1020-1031
    • Jones, C.L.1    Buch, S.2    Post, M.3    McCulloch, L.4    Liu, E.5    Eddy, A.A.6
  • 84
    • 0028239792 scopus 로고
    • Expression of 72-kDa gelatinase (MMP-2), collagenase (MMP-1), and TIMP in primary pig skin fibroblast cultures derived from radiation-induced skin
    • Lafuma C, El-Nobout RA, Crechet F, Hovnanian A, Nartin M. Expression of 72-kDa gelatinase (MMP-2), collagenase (MMP-1), and TIMP in primary pig skin fibroblast cultures derived from radiation-induced skin. J Invest Dermatol 1994; 102: 945-50.
    • (1994) J Invest Dermatol , vol.102 , pp. 945-950
    • Lafuma, C.1    El-Nobout, R.A.2    Crechet, F.3    Hovnanian, A.4    Nartin, M.5
  • 86
    • 0025046928 scopus 로고
    • Collagenese production by guinea-pig megakaryocytes in vitro
    • Leven RM, Yee T. Collagenese production by guinea-pig megakaryocytes in vitro. Exp Hematol 1990; 18: 743-7.
    • (1990) Exp Hematol , vol.18 , pp. 743-747
    • Leven, R.M.1    Yee, T.2
  • 88
    • 0030946445 scopus 로고    scopus 로고
    • Release of gelatinase A during platelet activation mediates aggregation
    • Sawicki G, Sales E, Murat J, Miszta-Lane H, Radomski MW. Release of gelatinase A during platelet activation mediates aggregation. Nature 1997; 386: 616-8.
    • (1997) Nature , vol.386 , pp. 616-618
    • Sawicki, G.1    Sales, E.2    Murat, J.3    Miszta-Lane, H.4    Radomski, M.W.5
  • 89
    • 0022339159 scopus 로고
    • Molecular cloning and nucleotide sequence of human pancreatic secretory trypsin inhibitors (PSTI) cDNA
    • Yamamoto T, Nakamura Y, Nishida J, Emi M, Ogawa M, Mori T et al. Molecular cloning and nucleotide sequence of human pancreatic secretory trypsin inhibitors (PSTI) cDNA. Biochem Biophys Res Commun 1985; 132: 605-12.
    • (1985) Biochem Biophys Res Commun , vol.132 , pp. 605-612
    • Yamamoto, T.1    Nakamura, Y.2    Nishida, J.3    Emi, M.4    Ogawa, M.5    Mori, T.6
  • 90
    • 0023024376 scopus 로고
    • Two apparent human endothelial cell growth factors from human hepatoma cells are tumor associated proteinase inhibitors
    • McKeehan WL, Sakagami Y, Hoshi H, McKeehan KA. Two apparent human endothelial cell growth factors from human hepatoma cells are tumor associated proteinase inhibitors. J Biol Chem 1986; 261: 5378-83.
    • (1986) J Biol Chem , vol.261 , pp. 5378-5383
    • McKeehan, W.L.1    Sakagami, Y.2    Hoshi, H.3    McKeehan, K.A.4
  • 91
    • 0023094112 scopus 로고
    • Proteases occurring in the cell membrane: A possible cell receptor for the Bowman-Birk type of protease inhibitors
    • Yavelow J, Caggana M, Beck KA. Proteases occurring in the cell membrane: a possible cell receptor for the Bowman-Birk type of protease inhibitors. Cancer Res 1987; 47: 1598-601.
    • (1987) Cancer Res , vol.47 , pp. 1598-1601
    • Yavelow, J.1    Caggana, M.2    Beck, K.A.3
  • 92
    • 0023129875 scopus 로고
    • Fluorescent visualization of binding and internalization of the anti-carcinogenic Bowman-Birk type protease inhibitors in transformed fibroblasts
    • Yavelow J, Scott CB, Mayer TC. Fluorescent visualization of binding and internalization of the anti-carcinogenic Bowman-Birk type protease inhibitors in transformed fibroblasts. Cancer Res 1987; 47: 1602-7.
    • (1987) Cancer Res , vol.47 , pp. 1602-1607
    • Yavelow, J.1    Scott, C.B.2    Mayer, T.C.3
  • 93
    • 0029825963 scopus 로고    scopus 로고
    • Identification and characterization of a novel collagenase in Xenopus laevis: Possible roles during frog development
    • Stolow MA, Bauzon DD, Li J, Sedgwick T, Liang VCT, Sang QA et al. Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development. Mol Biol Cell 1996; 71: 1471-83.
    • (1996) Mol Biol Cell , vol.71 , pp. 1471-1483
    • Stolow, M.A.1    Bauzon, D.D.2    Li, J.3    Sedgwick, T.4    Liang, V.C.T.5    Sang, Q.A.6
  • 94
    • 0030720933 scopus 로고    scopus 로고
    • Identification and structural and functional characterization of human enamelysin (MMP-20)
    • Llano E, Pendas AM, Knauper V, Sorsa T, Salo T, Salido E et al. Identification and structural and functional characterization of human enamelysin (MMP-20). Biochemistry 1997; 36: 15101-8.
    • (1997) Biochemistry , vol.36 , pp. 15101-15108
    • Llano, E.1    Pendas, A.M.2    Knauper, V.3    Sorsa, T.4    Salo, T.5    Salido, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.