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Volumn 81, Issue 5, 2011, Pages 626-635

Inhibition of human leukocyte elastase, plasmin and matrix metalloproteinases by oleic acid and oleoyl-galardin derivative(s)

Author keywords

Leukocyte elastase; Matrix metalloproteinase; Molecular docking; Oleic acid; Oleoyl galardin; Plasmin

Indexed keywords

CARBOXYLIC ACID; COLLAGEN; COLLAGENASE 3; FATTY ACID; GELATINASE A; GELATINASE B; HYDROXAMIC ACID; ILOMASTAT; LEUKOCYTE ELASTASE; MATRIX METALLOPROTEINASE INHIBITOR; OLEIC ACID; PHENYLALANINE; PLASMIN; TYROSINE; VALINE; ZINC;

EID: 79551471783     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.12.001     Document Type: Article
Times cited : (12)

References (54)
  • 1
    • 33847020833 scopus 로고    scopus 로고
    • Inflammation in wound repair: Molecular and cellular mechanisms
    • S.A. Eming, T. Krieg, and J.M. Davidson Inflammation in wound repair: molecular and cellular mechanisms J Invest Dermatol 127 2007 514 525
    • (2007) J Invest Dermatol , vol.127 , pp. 514-525
    • Eming, S.A.1    Krieg, T.2    Davidson, J.M.3
  • 2
    • 59149104284 scopus 로고    scopus 로고
    • Proteinases in cutaneous wound healing
    • M. Toriseva, and V.M. Kähri Proteinases in cutaneous wound healing Cell Mol Life Sci 66 2009 203 224
    • (2009) Cell Mol Life Sci , vol.66 , pp. 203-224
    • Toriseva, M.1    Kähri, V.M.2
  • 3
    • 0033376144 scopus 로고    scopus 로고
    • Analysis of the acute and chronic wound environments: The role of proteases and their inhibitors
    • N.J. Trengove, M.C. Stacey, S. MacAuley, N. Bennett, A.J. Gibson, and F. Burslem Analysis of the acute and chronic wound environments: the role of proteases and their inhibitors Wound Rep Reg 7 6 1999 442 452
    • (1999) Wound Rep Reg , vol.7 , Issue.6 , pp. 442-452
    • Trengove, N.J.1    Stacey, M.C.2    MacAuley, S.3    Bennett, N.4    Gibson, A.J.5    Burslem, F.6
  • 4
    • 43049092274 scopus 로고    scopus 로고
    • Metalloproteinases and their inhibitors: Regulators of wound healing
    • S.E. Gill, and W.C. Parks Metalloproteinases and their inhibitors: regulators of wound healing Int J Biochem Cell Biol 40 2008 1334 1347
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1334-1347
    • Gill, S.E.1    Parks, W.C.2
  • 5
    • 0033396265 scopus 로고    scopus 로고
    • Leukocyte proteinases in wound healing: Roles in physiologic and pathologic processes
    • B. Barrick, E.J. Campbell, and C.A. Owen Leukocyte proteinases in wound healing: roles in physiologic and pathologic processes Wound Rep Reg 7 1999 410 422
    • (1999) Wound Rep Reg , vol.7 , pp. 410-422
    • Barrick, B.1    Campbell, E.J.2    Owen, C.A.3
  • 6
    • 79551474136 scopus 로고    scopus 로고
    • Patterns of MMPs and TIMP expression in chronic wounds
    • U.K. Saarialho-Kere Patterns of MMPs and TIMP expression in chronic wounds Arch Dermatol Res 290 Suppl. 1998 547 554
    • (1998) Arch Dermatol Res , vol.290 , Issue.SUPPL. , pp. 547-554
    • Saarialho-Kere, U.K.1
  • 7
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • H. Nagase, R. Visse, and G. Murphy Structure and function of matrix metalloproteinases and TIMPs Cardiovasc Res 69 2006 562 573
    • (2006) Cardiovasc Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 8
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • A. Page-McCaw, A.J. Ewald, and Z. Werb Matrix metalloproteinases and the regulation of tissue remodelling Nat Rev Mol Cell Biol 8 2007 221 233
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-Mccaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 10
    • 33644859468 scopus 로고    scopus 로고
    • Prolyl endopeptidase inhibitory activity of unsaturated fatty acids
    • Y.S. Park, H.J. Jang, K.H. Lee, T.R. Hahn, and Y.S. Paik Prolyl endopeptidase inhibitory activity of unsaturated fatty acids J Agric Food Chem 54 4 2006 1238 1242
    • (2006) J Agric Food Chem , vol.54 , Issue.4 , pp. 1238-1242
    • Park, Y.S.1    Jang, H.J.2    Lee, K.H.3    Hahn, T.R.4    Paik, Y.S.5
  • 11
    • 0021324318 scopus 로고
    • Inhibition of chymase activity by long chain fatty acids
    • H. Kido, N. Fukusen, and N. Katunama Inhibition of chymase activity by long chain fatty acids Arch Biochem Biophys 230 2 1984 610 614
    • (1984) Arch Biochem Biophys , vol.230 , Issue.2 , pp. 610-614
    • Kido, H.1    Fukusen, N.2    Katunama, N.3
  • 12
    • 67651114144 scopus 로고    scopus 로고
    • Preliminary report: Inhibition of cellular proteasome activity by free fatty acids
    • F.G. Hamel Preliminary report: inhibition of cellular proteasome activity by free fatty acids Metabolism 58 8 2009 1047 1049
    • (2009) Metabolism , vol.58 , Issue.8 , pp. 1047-1049
    • Hamel, F.G.1
  • 13
    • 0031730809 scopus 로고    scopus 로고
    • Inhibitory activity of unsaturated fatty acids and anacardic acids toward soluble tissue factor-factor VIIa complex
    • D. Wang, T.J. Girard, T.P. Kasten, R.M. LaChance, M.A. Miller-Wideman, and R.C. Durley Inhibitory activity of unsaturated fatty acids and anacardic acids toward soluble tissue factor-factor VIIa complex J Nat Prod 61 11 1998 1352 1355
    • (1998) J Nat Prod , vol.61 , Issue.11 , pp. 1352-1355
    • Wang, D.1    Girard, T.J.2    Kasten, T.P.3    Lachance, R.M.4    Miller-Wideman, M.A.5    Durley, R.C.6
  • 14
    • 0022368332 scopus 로고
    • Fatty acid peptide derivatives as model compounds to protect elastin against degradation by elastases
    • W. Hornebeck, E. Moczar, J. Szecsi, and L. Robert Fatty acid peptide derivatives as model compounds to protect elastin against degradation by elastases Biochem Pharmacol 34 18 1985 3315 3321
    • (1985) Biochem Pharmacol , vol.34 , Issue.18 , pp. 3315-3321
    • Hornebeck, W.1    Moczar, E.2    Szecsi, J.3    Robert, L.4
  • 15
    • 0025027737 scopus 로고
    • Inhibitors directed to binding domains in neutrophil elastase
    • S.C. Tyagi, and S.R. Simon Inhibitors directed to binding domains in neutrophil elastase Biochemistry 29 1990 9970 9977
    • (1990) Biochemistry , vol.29 , pp. 9970-9977
    • Tyagi, S.C.1    Simon, S.R.2
  • 16
    • 0025365447 scopus 로고
    • The susceptibility of elastin-fatty acid complexes to elastolytic enzymes
    • A. Shock, H. Baum, M.F. Kapasi, F.M. Bull, and P.J. Quinn The susceptibility of elastin-fatty acid complexes to elastolytic enzymes Matrix 10 3 1990 179 185
    • (1990) Matrix , vol.10 , Issue.3 , pp. 179-185
    • Shock, A.1    Baum, H.2    Kapasi, M.F.3    Bull, F.M.4    Quinn, P.J.5
  • 17
    • 0035827538 scopus 로고    scopus 로고
    • Involvement of fibronectin type II repeats in the efficient inhibition of gelatinases A and B by long-chain unsaturated fatty acids
    • A. Berton, V. Rigot, E. Huet, M. Decarme, Y. Eeckhout, and L. Patthy Involvement of fibronectin type II repeats in the efficient inhibition of gelatinases A and B by long-chain unsaturated fatty acids J Biol Chem 276 23 2001 20458 20465
    • (2001) J Biol Chem , vol.276 , Issue.23 , pp. 20458-20465
    • Berton, A.1    Rigot, V.2    Huet, E.3    Decarme, M.4    Eeckhout, Y.5    Patthy, L.6
  • 18
    • 1642534351 scopus 로고    scopus 로고
    • Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5
    • E. Huet, J.H. Cauchard, A. Berton, A. Robinet, M. Decarme, and W. Hornebeck Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5 Biochem Pharmacol 67 4 2004 643 654 Erratum in: ibid 2004;67(5):1011
    • (2004) Biochem Pharmacol , vol.67 , Issue.4 , pp. 643-654
    • Huet, E.1    Cauchard, J.H.2    Berton, A.3    Robinet, A.4    Decarme, M.5    Hornebeck, W.6
  • 19
    • 0027231888 scopus 로고
    • Inhibition of human leucocyte elastase by fatty acyl-benzisothiazolinone, 1,1-dioxide conjugates (fatty acyl-saccharins)
    • C. Kerneur, W. Hornebeck, L. Robert, and E. Moczar Inhibition of human leucocyte elastase by fatty acyl-benzisothiazolinone, 1,1-dioxide conjugates (fatty acyl-saccharins) Biochem Pharmacol 45 9 1993 1889 1895
    • (1993) Biochem Pharmacol , vol.45 , Issue.9 , pp. 1889-1895
    • Kerneur, C.1    Hornebeck, W.2    Robert, L.3    Moczar, E.4
  • 20
    • 0027493879 scopus 로고
    • Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin
    • A. Baici, C. Diczhazi, A. Neszmelyi, E. Moczar, and W. Hornebeck Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin Biochem Pharmacol 46 9 1993 1545 1549
    • (1993) Biochem Pharmacol , vol.46 , Issue.9 , pp. 1545-1549
    • Baici, A.1    Diczhazi, C.2    Neszmelyi, A.3    Moczar, E.4    Hornebeck, W.5
  • 21
    • 0033550301 scopus 로고    scopus 로고
    • 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methyl-morpholinium chloride: An efficient condensing agent leading to the formation of amides and esters
    • M. Kunishima, C. Kawachi, J. Morita, K. Terao, F. Iwasaki, and S. Tani 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methyl-morpholinium chloride: an efficient condensing agent leading to the formation of amides and esters Tetrahedron 55 1999 13159 13170
    • (1999) Tetrahedron , vol.55 , pp. 13159-13170
    • Kunishima, M.1    Kawachi, C.2    Morita, J.3    Terao, K.4    Iwasaki, F.5    Tani, S.6
  • 22
    • 0028831529 scopus 로고
    • A simple and efficient procedure for the preparation of chiral 2-oxazolidinones from α-amino acids
    • N. Lewis, A. McKillop, R. Taylor, and R. Watson A simple and efficient procedure for the preparation of chiral 2-oxazolidinones from α-amino acids Synth Commun 25 1995 561 568
    • (1995) Synth Commun , vol.25 , pp. 561-568
    • Lewis, N.1    McKillop, A.2    Taylor, R.3    Watson, R.4
  • 23
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • G.M. Morris, D.S. Goodsell, R.S. Halliday, R. Huey, W.E. Hart, and R.K. Belew Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function J Comput Chem 19 1998 1639 1662
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6
  • 24
    • 33947716119 scopus 로고    scopus 로고
    • A semiempirical free energy force field with charge-based desolvation
    • R. Huey, G.M. Morris, A.J. Olson, and D.S. Goodsell A semiempirical free energy force field with charge-based desolvation J Comput Chem 28 6 2007 1145 1152
    • (2007) J Comput Chem , vol.28 , Issue.6 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 26
    • 0022801412 scopus 로고
    • X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor
    • W. Bode, A.Z. Wei, R. Huber, E. Meyer, J. Travis, and S. Neumann X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor EMBO J 5 10 1986 2453 2458
    • (1986) EMBO J , vol.5 , Issue.10 , pp. 2453-2458
    • Bode, W.1    Wei, A.Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 27
    • 0033523040 scopus 로고    scopus 로고
    • Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed
    • E. Morgunova, A. Tuuttila, U. Bergmann, M. Isupov, Y. Lindqvist, and G. Schneider Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed Science 284 5420 1999 1667 1670
    • (1999) Science , vol.284 , Issue.5420 , pp. 1667-1670
    • Morgunova, E.1    Tuuttila, A.2    Bergmann, U.3    Isupov, M.4    Lindqvist, Y.5    Schneider, G.6
  • 28
    • 70350495904 scopus 로고    scopus 로고
    • Solution structure and functional characterization of human plasminogen kringle 5
    • M.D. Battistel, A. Grishaev, S.S. An, F.J. Castellino, and M. Llinás Solution structure and functional characterization of human plasminogen kringle 5 Biochemistry 48 43 2009 10208 10219
    • (2009) Biochemistry , vol.48 , Issue.43 , pp. 10208-10219
    • Battistel, M.D.1    Grishaev, A.2    An, S.S.3    Castellino, F.J.4    Llinás, M.5
  • 30
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • H. Li, A.D. Robertson, and J.H. Jensen Very fast empirical prediction and rationalization of protein pKa values Proteins 61 4 2005 704 721
    • (2005) Proteins , vol.61 , Issue.4 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 31
    • 57349090665 scopus 로고    scopus 로고
    • Very fast prediction and rationalization of pKa values for protein-ligand complexes
    • D.C. Bas, D.M. Rogers, and J.H. Jensen Very fast prediction and rationalization of pKa values for protein-ligand complexes Proteins 73 3 2008 765 783
    • (2008) Proteins , vol.73 , Issue.3 , pp. 765-783
    • Bas, D.C.1    Rogers, D.M.2    Jensen, J.H.3
  • 32
    • 0023729631 scopus 로고
    • Similar binding sites for unsaturated fatty acids and alkyl 2-pyrone inhibitors of human sputum elastase
    • L. Cook, and B. Ternai Similar binding sites for unsaturated fatty acids and alkyl 2-pyrone inhibitors of human sputum elastase Biol Chem Hoppe Seyler 369 7 1988 627 631
    • (1988) Biol Chem Hoppe Seyler , vol.369 , Issue.7 , pp. 627-631
    • Cook, L.1    Ternai, B.2
  • 33
    • 34249780518 scopus 로고    scopus 로고
    • 1 of Ilomastat confers selectivity for gelatinase A (MMP-2) over gelatinase B (MMP-9) inhibition as shown by molecular modelling studies
    • 1 of Ilomastat confers selectivity for gelatinase A (MMP-2) over gelatinase B (MMP-9) inhibition as shown by molecular modelling studies Bioorg Med Chem 15 14 2007 4753 4766
    • (2007) Bioorg Med Chem , vol.15 , Issue.14 , pp. 4753-4766
    • Moroy, G.1    Denhez, C.2    El Mourabit, H.3    Toribio, A.4    Dassonville, A.5    Decarme, M.6
  • 34
    • 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
    • G. Ledour, G. Moroy, M. Rouffet, E. Bourguet, D. Guillaume, and M. Decarme 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 16 18 2008 8745 8759
    • (2008) Bioorg Med Chem , vol.16 , Issue.18 , pp. 8745-8759
    • Ledour, G.1    Moroy, G.2    Rouffet, M.3    Bourguet, E.4    Guillaume, D.5    Decarme, M.6
  • 36
    • 15444343493 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: A structure-activity study
    • D.E. Levy, F. Lapierre, W. Liang, W. Ye, C.W. Lange, and X. Li Matrix metalloproteinase inhibitors: a structure-activity study J Med Chem 41 1998 199 223
    • (1998) J Med Chem , vol.41 , pp. 199-223
    • Levy, D.E.1    Lapierre, F.2    Liang, W.3    Ye, W.4    Lange, C.W.5    Li, X.6
  • 37
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • H. Nagase Activation mechanisms of matrix metalloproteinases Biol Chem 378 1997 151 160
    • (1997) Biol Chem , vol.378 , pp. 151-160
    • Nagase, H.1
  • 38
    • 0025335183 scopus 로고
    • Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl) mercuric acetate
    • H. Nagase, J.J. Enghild, K. Susuki, and G. Salvesen Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl) mercuric acetate Biochemistry 29 324 1990 5783 5789
    • (1990) Biochemistry , vol.29 , Issue.324 , pp. 5783-5789
    • Nagase, H.1    Enghild, J.J.2    Susuki, K.3    Salvesen, G.4
  • 39
    • 50649119519 scopus 로고    scopus 로고
    • Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition
    • J.L. Lauer-Fields, J.K. Whitehead, S. Li, R.P. Hammer, K. Brew, and G.B. Fields Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition J Biol Chem 283 29 2008 20087 20095
    • (2008) J Biol Chem , vol.283 , Issue.29 , pp. 20087-20095
    • Lauer-Fields, J.L.1    Whitehead, J.K.2    Li, S.3    Hammer, R.P.4    Brew, K.5    Fields, G.B.6
  • 40
    • 34547850671 scopus 로고    scopus 로고
    • Inhibition of MMP-2 gelatinolysis by targeting exodomain-substrate interactions
    • X. Xu, Z. Chen, Y. Wang, L. Bonewald, and B. Steffensen Inhibition of MMP-2 gelatinolysis by targeting exodomain-substrate interactions Biochem J 406 2007 147 155
    • (2007) Biochem J , vol.406 , pp. 147-155
    • Xu, X.1    Chen, Z.2    Wang, Y.3    Bonewald, L.4    Steffensen, B.5
  • 41
    • 0347298772 scopus 로고    scopus 로고
    • Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide
    • P.S. Frank, J.T. Douglas, M. Locher, M. Llinas, and J. Schaller Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide Biochemistry 42 4 2003 1078 1085
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 1078-1085
    • Frank, P.S.1    Douglas, J.T.2    Locher, M.3    Llinas, M.4    Schaller, J.5
  • 42
    • 0038146970 scopus 로고    scopus 로고
    • Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2)
    • M. Trexler, K. Briknarova, M. Gehrmann, M. Llinas, and L. Patthy Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2) J Biol Chem 278 14 2003 12241 12246
    • (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
  • 43
    • 67649610424 scopus 로고    scopus 로고
    • Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2
    • X. Xu, M. Mikhailova, U. Ilangovan, Z. Chen, A. Yu, and S. Pal Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2 Biochemistry 48 2009 5822 5831
    • (2009) Biochemistry , vol.48 , pp. 5822-5831
    • Xu, X.1    Mikhailova, M.2    Ilangovan, U.3    Chen, Z.4    Yu, A.5    Pal, S.6
  • 44
    • 0034193629 scopus 로고    scopus 로고
    • Analysis of the ex vivo specificity of human gelatinases A and B towards skin collagen and elastic fibers by computerized morphometry
    • A. Berton, G. Godeau, H. Emonard, K. Baba, P. Bellon, and W. Hornebeck Analysis of the ex vivo specificity of human gelatinases A and B towards skin collagen and elastic fibers by computerized morphometry Matrix Biol 19 2 2000 139 148
    • (2000) Matrix Biol , vol.19 , Issue.2 , pp. 139-148
    • Berton, A.1    Godeau, G.2    Emonard, H.3    Baba, K.4    Bellon, P.5    Hornebeck, W.6
  • 45
    • 0026768692 scopus 로고
    • Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic acids
    • D. Grobelny, L. Poncz, and R.E. Galardy Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic acids Biochemistry 31 31 1992 7152 7154
    • (1992) Biochemistry , vol.31 , Issue.31 , pp. 7152-7154
    • Grobelny, D.1    Poncz, L.2    Galardy, R.E.3
  • 46
    • 0023948731 scopus 로고
    • Effect of sodium oleate on the hydrolysis of human plasma fibronectin by proteinases
    • L. Stanislawski, and W. Hornebeck Effect of sodium oleate on the hydrolysis of human plasma fibronectin by proteinases Biochem Int 16 4 1988 661 670
    • (1988) Biochem Int , vol.16 , Issue.4 , pp. 661-670
    • Stanislawski, L.1    Hornebeck, W.2
  • 49
    • 15244355692 scopus 로고    scopus 로고
    • Hydroxamate-based peptide inhibitors of matrix metalloprotease 2
    • M. Jani, H. Tordai, M. Trexler, L. Banyai, and L. Patthy Hydroxamate-based peptide inhibitors of matrix metalloprotease 2 Biochimie 87 2005 385 392
    • (2005) Biochimie , vol.87 , pp. 385-392
    • Jani, M.1    Tordai, H.2    Trexler, M.3    Banyai, L.4    Patthy, L.5
  • 50
    • 0030895479 scopus 로고    scopus 로고
    • Elastase from polymorphonuclear leukocyte in articular cartilage and synovial fluids of patients with rheumatoid arthritis
    • S. Momohara, S. Kashiwasaki, K. Inoue, S. Saito, and T. Nakagawa Elastase from polymorphonuclear leukocyte in articular cartilage and synovial fluids of patients with rheumatoid arthritis Clin Rheumatol 16 2 1997 133 140
    • (1997) Clin Rheumatol , vol.16 , Issue.2 , pp. 133-140
    • Momohara, S.1    Kashiwasaki, S.2    Inoue, K.3    Saito, S.4    Nakagawa, T.5
  • 51
    • 0035172262 scopus 로고    scopus 로고
    • Stromelysin-1 (MMP-3) in synovial fluid of patients with rheumatoid arthritis has potential to cleave membranes bound Fas ligand
    • H. Matsuno, K. Yudoh, Y. Watanaba, F. Nakazawa, H. Aono, and T. Kimura Stromelysin-1 (MMP-3) in synovial fluid of patients with rheumatoid arthritis has potential to cleave membranes bound Fas ligand J Rheumatol 28 1 2001 22 28
    • (2001) J Rheumatol , vol.28 , Issue.1 , pp. 22-28
    • Matsuno, H.1    Yudoh, K.2    Watanaba, Y.3    Nakazawa, F.4    Aono, H.5    Kimura, T.6
  • 53
    • 33645036393 scopus 로고    scopus 로고
    • Collagen degradation by interleukine 1β-stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine proteinases
    • S.W. Cox, B.M. Eley, M. Kiili, A. Asikainen, T. Tervahartiala, and T. Sorsa Collagen degradation by interleukine 1β-stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine proteinases Oral Dis 12 2006 34 40
    • (2006) Oral Dis , vol.12 , pp. 34-40
    • Cox, S.W.1    Eley, B.M.2    Kiili, M.3    Asikainen, A.4    Tervahartiala, T.5    Sorsa, T.6
  • 54
    • 67651112138 scopus 로고    scopus 로고
    • Control of melanoma invasiveness by anticollagenolytic agents: A reappraisal of an old concept
    • E. Bourguet, J. Sapi, H. Emonard, and W. Hornebeck Control of melanoma invasiveness by anticollagenolytic agents: a reappraisal of an old concept Anticancer Agents Med Chem 9 5 2009 576 579
    • (2009) Anticancer Agents Med Chem , vol.9 , Issue.5 , pp. 576-579
    • Bourguet, E.1    Sapi, J.2    Emonard, H.3    Hornebeck, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.