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Volumn 18, Issue 3, 2011, Pages 392-401

Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX METALLOPROTEINASE 14; PEPTIDE; PEPTIDE LIBRARY;

EID: 79953064715     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.12.017     Document Type: Article
Times cited : (21)

References (70)
  • 1
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 Is an interstitial collagenase
    • R.T. Aimes, and J.P. Quigley Matrix metalloproteinase-2 Is an interstitial collagenase J. Biol. Chem. 270 1995 5872 5876
    • (1995) J. Biol. Chem. , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 2
    • 34447293780 scopus 로고    scopus 로고
    • Membrane type matrix metalloproteinases (MMPs) show differential expression in non-small cell lung cancer (NSCLC) compared to normal lung: Correlation of MMP-14 mRNA expression and proteolytic activity
    • DOI 10.1016/j.ejca.2007.05.009, PII S0959804907004005
    • J.M. Atkinson, C.J. Pennington, S.W. Martin, V.A. Anikin, A.J. Mearns, P.M. Loadman, D.R. Edwards, and J.H. Gill Membrane type matrix metalloproteinases (MMPs) show differential expression in non-small cell lung cancer (NSCLC) compared to normal lung: correlation of MMP-14 mRNA expression and proteolytic activity Eur. J. Cancer 43 2007 1764 1771 (Pubitemid 47042378)
    • (2007) European Journal of Cancer , vol.43 , Issue.11 , pp. 1764-1771
    • Atkinson, J.M.1    Pennington, C.J.2    Martin, S.W.3    Anikin, V.A.4    Mearns, A.J.5    Loadman, P.M.6    Edwards, D.R.7    Gill, J.H.8
  • 4
    • 33646726556 scopus 로고    scopus 로고
    • Protease specificity determination by using cellular libraries of peptide substrates (CLiPS)
    • K.T. Boulware, and P.S. Daugherty Protease specificity determination by using cellular libraries of peptide substrates (CLiPS) Proc. Natl. Acad. Sci. USA 103 2006 7583 7588
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7583-7588
    • Boulware, K.T.1    Daugherty, P.S.2
  • 5
    • 77953570947 scopus 로고    scopus 로고
    • Evolutionary optimization of peptide substrates for proteases that exhibit rapid hydrolysis kinetics
    • K.T. Boulware, A. Jabaiah, and P.S. Daugherty Evolutionary optimization of peptide substrates for proteases that exhibit rapid hydrolysis kinetics Biotechnol. Bioeng. 106 2010 339 346
    • (2010) Biotechnol. Bioeng. , vol.106 , pp. 339-346
    • Boulware, K.T.1    Jabaiah, A.2    Daugherty, P.S.3
  • 6
    • 47949123468 scopus 로고    scopus 로고
    • Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: Dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding
    • G.S. Butler, R.A. Dean, E.M. Tam, and C.M. Overall Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding Mol. Cell. Biol. 28 2008 4896 4914
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4896-4914
    • Butler, G.S.1    Dean, R.A.2    Tam, E.M.3    Overall, C.M.4
  • 8
    • 70350342893 scopus 로고    scopus 로고
    • "Zipper" molecular beacons: A generalized strategy to optimize the performance of activatable protease probes
    • J. Chen, T.W. Liu, P.C. Lo, B.C. Wilson, and G. Zheng "Zipper" molecular beacons: a generalized strategy to optimize the performance of activatable protease probes Bioconjug. Chem. 20 2009 1836 1842
    • (2009) Bioconjug. Chem. , vol.20 , pp. 1836-1842
    • Chen, J.1    Liu, T.W.2    Lo, P.C.3    Wilson, B.C.4    Zheng, G.5
  • 11
    • 1842864784 scopus 로고    scopus 로고
    • Phage display substrate: A blind method for determining protease specificity
    • DOI 10.1515/BC.2002.119
    • D. Deperthes Phage display substrate: a blind method for determining protease specificity Biol. Chem. 383 2002 1107 1112 (Pubitemid 35215055)
    • (2002) Biological Chemistry , vol.383 , Issue.7-8 , pp. 1107-1112
    • Deperthes, D.1
  • 14
    • 5444219883 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: From new functions to improved inhibition
    • DOI 10.1387/ijdb.041811af, Invasion in Cancer and Embryonic Development
    • A.R. Folgueras, A.M. Pendas, L.M. Sanchez, and C. Lopez-Otin Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies Int. J. Dev. Biol. 48 2004 411 424 (Pubitemid 39360392)
    • (2004) International Journal of Developmental Biology , vol.48 , Issue.5-6 , pp. 411-424
    • Folgueras, A.R.1    Pendas, A.M.2    Sanchez, L.M.3    Lopez-Otin, C.4
  • 15
  • 18
    • 0032488895 scopus 로고    scopus 로고
    • Three-dimensional type I collagen lattices induce coordinate expression of matrix metalloproteinases MT1-MMP and MMP-2 in microvascular endothelial cells
    • DOI 10.1074/jbc.273.6.3604
    • T.L. Haas, S.J. Davis, and J.A. Madri Three-dimensional type I collagen lattices induce coordinate expression of matrix metalloproteinases MT1-MMP and MMP-2 in microvascular endothelial cells J. Biol. Chem. 273 1998 3604 3610 (Pubitemid 28109785)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3604-3610
    • Haas, T.L.1    Davis, S.J.2    Madri, J.A.3
  • 23
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • DOI 10.1016/0014-5793(94)01079-X
    • N.M. Hooper Families of zinc metalloproteases FEBS Lett. 354 1994 1 6 (Pubitemid 24331694)
    • (1994) FEBS Letters , vol.354 , Issue.1 , pp. 1-6
    • Hooper, N.M.1
  • 24
    • 0042371856 scopus 로고    scopus 로고
    • Proteolyzed matrix as a template for the regulation of tumor progression
    • DOI 10.1016/S0753-3322(03)00049-0
    • W. Hornebeck, and F.X. Maquart Proteolyzed matrix as a template for the regulation of tumor progression Biomed. Pharmacother. 57 2003 223 230 (Pubitemid 36903199)
    • (2003) Biomedicine and Pharmacotherapy , vol.57 , Issue.5-6 , pp. 223-230
    • Hornebeck, W.1    Maquart, F.X.2
  • 26
    • 3242772983 scopus 로고    scopus 로고
    • MT1-MMP: An enzyme with multidimensional regulation
    • DOI 10.1016/j.tibs.2004.04.001, PII S0968000404000799
    • Y. Itoh, and M. Seiki MT1-MMP: an enzyme with multidimensional regulation Trends Biochem. Sci. 29 2004 285 289 (Pubitemid 38968758)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.6 , pp. 285-289
    • Itoh, Y.1    Seiki, M.2
  • 28
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • DOI 10.1083/jcb.153.5.893
    • M. Kajita, Y. Itoh, T. Chiba, H. Mori, A. Okada, H. Kinoh, and M. Seiki Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration J. Cell Biol. 153 2001 893 904 (Pubitemid 34289231)
    • (2001) Journal of Cell Biology , vol.153 , Issue.5 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 31
    • 0030898796 scopus 로고    scopus 로고
    • The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction
    • DOI 10.1074/jbc.272.12.7608
    • V. Knauper, S. Cowell, B. Smith, C. Lopez-Otin, M. O'Shea, H. Morris, L. Zardi, and G. Murphy The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction J. Biol. Chem. 272 1997 7608 7616 (Pubitemid 27137308)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.12 , pp. 7608-7616
    • Knauper, V.1    Cowell, S.2    Smith, B.3    Lopez-Otin, C.4    O'Shea, M.5    Morris, H.6    Zardi, L.7    Murphy, G.8
  • 32
    • 0037186958 scopus 로고    scopus 로고
    • Refolding of the catalytic and hinge domains of human MT1-MMP expressed in Escherichia coli and its characterization
    • H.M. Koo, J.H. Kim, I.K. Hwang, S.J. Lee, T.H. Kim, K.H. Rhee, and S.T. Lee Refolding of the catalytic and hinge domains of human MT1-mMP expressed in Escherichia coli and its characterization Mol. Cells 13 2002 118 124 (Pubitemid 41583057)
    • (2002) Molecules and Cells , vol.13 , Issue.1 , pp. 118-124
    • Koo, H.M.1    Kim, J.-H.2    Hwang, I.K.3    Lee, S.-J.4    Kim, T.-H.5    Rhee, K.-H.6    Lee, S.-T.7
  • 35
    • 0037189494 scopus 로고    scopus 로고
    • A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases
    • DOI 10.1074/jbc.M111574200
    • S.J. Kridel, H. Sawai, B.I. Ratnikov, E.I. Chen, W. Li, A. Godzik, A.Y. Strongin, and J.W. Smith A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases J. Biol. Chem. 277 2002 23788 23793 (Pubitemid 34952221)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23788-23793
    • Kridel, S.J.1    Sawai, H.2    Ratnikov, B.I.3    Chen, E.I.4    Li, W.5    Godzik, A.6    Strongin, A.Y.7    Smith, J.W.8
  • 37
    • 70349103682 scopus 로고    scopus 로고
    • Proteolysis: A biological process adapted in drug delivery, therapy, and imaging
    • B. Law, and C.H. Tung Proteolysis: a biological process adapted in drug delivery, therapy, and imaging Bioconjug. Chem. 20 2009 1683 1695
    • (2009) Bioconjug. Chem. , vol.20 , pp. 1683-1695
    • Law, B.1    Tung, C.H.2
  • 38
    • 33750495804 scopus 로고    scopus 로고
    • A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis
    • DOI 10.1091/mbc.E06-06-0486
    • H. Lee, C.M. Overall, C.A. McCulloch, and J. Sodek A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis Mol. Biol. Cell 17 2006 4812 4826 (Pubitemid 44665750)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4812-4826
    • Lee, H.1    Overall, C.M.2    McCulloch, C.A.3    Sodek, J.4
  • 39
    • 0036109579 scopus 로고    scopus 로고
    • Increased membrane type 1 matrix metalloproteinase expression from adenoma to colon cancer: A possible mechanism of neoplastic progression
    • DOI 10.1007/s10350-004-6236-7
    • S. Malhotra, E. Newman, D. Eisenberg, J. Scholes, R. Wieczorek, P. Mignatti, and P. Shamamian Increased membrane type 1 matrix metalloproteinase expression from adenoma to colon cancer: a possible mechanism of neoplastic progression Dis. Colon Rectum 45 2002 537 543 (Pubitemid 34407733)
    • (2002) Diseases of the Colon and Rectum , vol.45 , Issue.4 , pp. 537-543
    • Malhotra, S.1    Newman, E.2    Eisenberg, D.3    Scholes, J.4    Wieczorek, R.5    Mignatti, P.6    Shamamian, P.7
  • 40
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • DOI 10.1038/nbt1066
    • A.W. Nguyen, and P.S. Daugherty Evolutionary optimization of fluorescent proteins for intracellular FRET Nat. Biotechnol. 23 2005 355 360 (Pubitemid 41094425)
    • (2005) Nature Biotechnology , vol.23 , Issue.3 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 41
    • 0028022847 scopus 로고
    • A 92 kDa gelatinase (MMP-9) cleavage site in native type v collagen
    • C. Niyibizi, R. Chan, J.J. Wu, and D. Eyre A 92 kDa gelatinase (MMP-9) cleavage site in native type V collagen Biochem. Biophys. Res. Commun. 202 1994 328 333
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 328-333
    • Niyibizi, C.1    Chan, R.2    Wu, J.J.3    Eyre, D.4
  • 42
    • 0033590212 scopus 로고    scopus 로고
    • Identification of substrate sequences for membrane type-1 matrix metalloproteinase using bacteriophage peptide display library
    • DOI 10.1006/bbrc.1999.1816
    • S. Ohkubo, K. Miyadera, Y. Sugimoto, K. Matsuo, K. Wierzba, and Y. Yamada Identification of substrate sequences for membrane type-1 matrix metalloproteinase using bacteriophage peptide display library Biochem. Biophys. Res. Commun. 266 1999 308 313 (Pubitemid 30028664)
    • (1999) Biochemical and Biophysical Research Communications , vol.266 , Issue.2 , pp. 308-313
    • Ohkubo, S.1    Miyadera, K.2    Sugimoto, Y.3    Matsuo, K.-I.4    Wierzba, K.5    Yamada, Y.6
  • 43
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • DOI 10.1074/jbc.272.4.2446
    • E. Ohuchi, K. Imai, Y. Fujii, H. Sato, M. Seiki, and Y. Okada Membrane type 1Matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules J. Biol. Chem. 272 1997 2446 2451 (Pubitemid 27058534)
    • (1997) Journal of Biological Chemistry , 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
  • 44
    • 0028935326 scopus 로고
    • Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas
    • A. Okada, J. Bellocq, N. Rouyer, M. Chenard, M. Rio, P. Chambon, and P. Basset Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas Proc. Natl. Acad. Sci. USA 92 1995 2730 2734
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2730-2734
    • Okada, A.1    Bellocq, J.2    Rouyer, N.3    Chenard, M.4    Rio, M.5    Chambon, P.6    Basset, P.7
  • 45
    • 47749090496 scopus 로고    scopus 로고
    • Visualization of polarized membrane type 1 matrix metalloproteinase activity in live cells by fluorescence resonance energy transfer imaging
    • M. Ouyang, S. Lu, X.-Y. Li, J. Xu, J. Seong, B.N.G. Giepmans, J.Y.J. Shyy, S.J. Weiss, and Y. Wang Visualization of polarized membrane type 1 matrix metalloproteinase activity in live cells by fluorescence resonance energy transfer imaging J. Biol. Chem. 283 2008 17740 17748
    • (2008) J. Biol. Chem. , vol.283 , pp. 17740-17748
    • Ouyang, M.1    Lu, S.2    Li, X.-Y.3    Xu, J.4    Seong, J.5    Giepmans, B.N.G.6    Shyy, J.Y.J.7    Weiss, S.J.8    Wang, Y.9
  • 46
    • 0035903020 scopus 로고    scopus 로고
    • Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain
    • DOI 10.1016/S0014-5793(01)02723-5, PII S0014579301027235
    • M.L. Patterson, S.J. Atkinson, V. Knäuper, and G. Murphy Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain FEBS Lett. 503 2001 158 162 (Pubitemid 32763197)
    • (2001) FEBS Letters , vol.503 , Issue.2-3 , pp. 158-162
    • Patterson, M.L.1    Atkinson, S.J.2    Knauper, V.3    Murphy, G.4
  • 47
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity
    • D. Pei, and S.J. Weiss Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity J. Biol. Chem. 271 1996 9135 9140
    • (1996) J. Biol. Chem. , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 48
    • 33746788650 scopus 로고    scopus 로고
    • Laminar shear stress inhibits cathepsin L activity in endothelial cells
    • DOI 10.1161/01.ATV.0000227470.72109.2b, PII 0004360520060800000016
    • M.O. Platt, R.F. Ankeny, and H. Jo Laminar shear stress inhibits cathepsin L activity in endothelial cells Arterioscler. Thromb. Vasc. Biol. 26 2006 1784 1790 (Pubitemid 44305332)
    • (2006) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.26 , Issue.8 , pp. 1784-1790
    • Platt, M.O.1    Ankeny, R.F.2    Jo, H.3
  • 50
    • 33645507213 scopus 로고    scopus 로고
    • Bacterial display using circularly permuted outer membrane protein OmpX yields high affinity peptide ligands
    • J.J. Rice, A. Schohn, P.H. Bessette, K.T. Boulware, and P.S. Daugherty Bacterial display using circularly permuted outer membrane protein OmpX yields high affinity peptide ligands Protein Sci. 15 2006 825 836
    • (2006) Protein Sci. , vol.15 , pp. 825-836
    • Rice, J.J.1    Schohn, A.2    Bessette, P.H.3    Boulware, K.T.4    Daugherty, P.S.5
  • 52
    • 69249156451 scopus 로고    scopus 로고
    • Secreted versus membrane-anchored collagenases: Relative roles in fibroblast-dependent collagenolysis and invasion
    • F. Sabeh, X.-Y. Li, T.L. Saunders, R.G. Rowe, and S.J. Weiss Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion J. Biol. Chem. 284 2009 23001 23011
    • (2009) J. Biol. Chem. , vol.284 , pp. 23001-23011
    • Sabeh, F.1    Li, X.-Y.2    Saunders, T.L.3    Rowe, R.G.4    Weiss, S.J.5
  • 53
    • 77957281923 scopus 로고    scopus 로고
    • Coordinate action of membrane-type matrix metalloproteinase-1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion
    • H. Sato, and T. Takino Coordinate action of membrane-type matrix metalloproteinase-1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion Cancer Sci. 101 2010 843 847
    • (2010) Cancer Sci. , vol.101 , pp. 843-847
    • Sato, H.1    Takino, T.2
  • 54
    • 20044387216 scopus 로고    scopus 로고
    • Roles of membrane-type matrix metalloproteinase-1 in tumor invasion and metastasis
    • DOI 10.1111/j.1349-7006.2005.00039.x
    • H. Sato, T. Takino, and H. Miyamori Roles of membrane-type matrix metalloproteinase-1 in tumor invasion and metastasis Cancer Sci. 96 2005 212 217 (Pubitemid 40767057)
    • (2005) Cancer Science , vol.96 , Issue.4 , pp. 212-217
    • Sato, H.1    Takino, T.2    Miyamori, H.3
  • 55
    • 44949142150 scopus 로고    scopus 로고
    • Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites
    • DOI 10.1038/nbt1408, PII NBT1408
    • O. Schilling, and C.M. Overall Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites Nat. Biotechnol. 26 2008 685 694 (Pubitemid 351809596)
    • (2008) Nature Biotechnology , vol.26 , Issue.6 , pp. 685-694
    • Schilling, O.1    Overall, C.M.2
  • 56
    • 77951137373 scopus 로고    scopus 로고
    • Positional scanning synthetic combinatorial libraries for substrate profiling
    • E.L. Schneider, and C.S. Craik Positional scanning synthetic combinatorial libraries for substrate profiling Methods Mol. Biol. 539 2009 59 78
    • (2009) Methods Mol. Biol. , vol.539 , pp. 59-78
    • Schneider, E.L.1    Craik, C.S.2
  • 57
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion
    • DOI 10.1016/S0304-3835(02)00699-7
    • M. Seiki Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion Cancer Lett. 194 2003 1 11 (Pubitemid 36428879)
    • (2003) Cancer Letters , vol.194 , Issue.1 , pp. 1-11
    • Seiki, M.1
  • 58
    • 12344258657 scopus 로고    scopus 로고
    • Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors
    • P.A. Snoek-van Beurden, and J.W. Von den Hoff Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors Biotechniques 38 2005 73 83 (Pubitemid 40139420)
    • (2005) BioTechniques , vol.38 , Issue.1 , pp. 73-83
    • Snoek-Van Beurden, P.A.M.1    Von Den Hoff, J.W.2
  • 59
    • 0034472617 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumor invasion and metastasis
    • DOI 10.1006/scbi.2000.0379
    • I. Stamenkovic Matrix metalloproteinases in tumor invasion and metastasis Semin. Cancer Biol. 10 2000 415 433 (Pubitemid 32181912)
    • (2000) Seminars in Cancer Biology , vol.10 , Issue.6 , pp. 415-433
    • Stamenkovic, I.1
  • 61
    • 0028969678 scopus 로고
    • The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • W. Stocker, F. Grams, U. Baumann, P. Reinemer, F.X. Gomis-Ruth, D.B. McKay, and W. Bode The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases Protein Sci. 4 1995 823 840
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Ruth, F.X.5    McKay, D.B.6    Bode, W.7
  • 64
    • 0029938495 scopus 로고    scopus 로고
    • Evidence of involvement of CD44 in endothelial cell proliferation, migration and angiogenesis in vitro
    • DOI 10.1002/(SI CI)1097-02 15(19960529)66:5<6 64::AID-IJ C14>3.0.CO;2-4
    • V. Trochon, C. Mabilat, P. Bertrand, Y. Legrand, F. Smadja-Joffe, C. Soria, B. Delpech, and H. Lu Evidence of involvement of CD44 in endothelial cell proliferation, migration and angiogenesis in vitro Int. J. Cancer 66 1996 664 668 (Pubitemid 26197930)
    • (1996) International Journal of Cancer , vol.66 , Issue.5 , pp. 664-668
    • Trochon, V.1    Mabilat, C.2    Bertrand, P.3    Legrand, Y.4    Smadja-Joffe, F.5    Soria, C.6    Delpech, B.7    Lu, H.8
  • 65
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • DOI 10.1038/90273
    • B.E. Turk, L.L. Huang, E.T. Piro, and L.C. Cantley Determination of protease cleavage site motifs using mixture-based oriented peptide libraries Nat. Biotechnol. 19 2001 661 667 (Pubitemid 32625438)
    • (2001) Nature Biotechnology , vol.19 , Issue.7 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 67
    • 0032937063 scopus 로고    scopus 로고
    • Stratum corneum thiol protease (SCTP): A novel cysteine protease of late epidermal differentiation
    • DOI 10.1007/s004030050406
    • A. Watkinson Stratum corneum thiol protease (SCTP): a novel cysteine protease of late epidermal differentiation Arch. Dermatol. Res. 291 1999 260 268 (Pubitemid 29225051)
    • (1999) Archives of Dermatological Research , vol.291 , Issue.5 , pp. 260-268
    • Watkinson, A.1
  • 68
    • 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
    • DOI 10.1074/jbc.271.29.17119
    • H. Will, S.J. Atkinson, G.S. Butler, B. Smith, and G. Murphy 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. 271 1996 17119 17123 (Pubitemid 26244261)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.29 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 69
    • 4043179911 scopus 로고    scopus 로고
    • In vivo imaging of protease activity in arthritis: A novel approach for monitoring treatment response
    • DOI 10.1002/art.20379
    • A. Wunder, C.H. Tung, U. Muller-Ladner, R. Weissleder, and U. Mahmood In vivo imaging of protease activity in arthritis: a novel approach for monitoring treatment response Arthritis Rheum. 50 2004 2459 2465 (Pubitemid 39062705)
    • (2004) Arthritis and Rheumatism , vol.50 , Issue.8 , pp. 2459-2465
    • Wunder, A.1    Tung, C.-H.2    Muller-Ladner, U.3    Weissleder, R.4    Mahmood, U.5


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