메뉴 건너뛰기




Volumn 55, Issue 4, 1999, Pages 639-652

Structural properties of matrix metalloproteinases

Author keywords

Crystal structures; Drug design; Matrix metalloproteinases (MMPs); Proteinases; Tissue inhibitors of metalloproteinases (TIMPs)

Indexed keywords

MATRIX METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 0032951138     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050320     Document Type: Review
Times cited : (315)

References (89)
  • 1
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner J. F. Jr. (1991) Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5: 2145-2155
    • (1991) FASEB J. , vol.5 , pp. 2145-2155
    • Woessner J.F., Jr.1
  • 5
    • 0030293598 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the development of cancer
    • Coussens L. M. and Werb Z. (1996) Matrix metalloproteinases and the development of cancer. Chem. Biol. 3: 895-904
    • (1996) Chem. Biol. , vol.3 , pp. 895-904
    • Coussens, L.M.1    Werb, Z.2
  • 6
    • 0030806173 scopus 로고    scopus 로고
    • Changing views of the role of matrix metalloproteinases in metastasis
    • Chambers A. F. and Matrisian L. M. (1997) Changing views of the role of matrix metalloproteinases in metastasis. J. Natl. Cancer Inst. 89: 1260-1270
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 1260-1270
    • Chambers, A.F.1    Matrisian, L.M.2
  • 7
  • 8
    • 0031799439 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors in arthritis
    • Bottomley K. M., Johnson W. H. and Walter D. S. (1998) Matrix metalloproteinase inhibitors in arthritis. J. Enz. Inhib. 13: 79-101
    • (1998) J. Enz. Inhib. , vol.13 , pp. 79-101
    • Bottomley, K.M.1    Johnson, W.H.2    Walter, D.S.3
  • 9
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution and diversification
    • Massova I., Kotra L. P., Fridman R. and Mobashery S. (1998) Matrix metalloproteinases: structures, evolution and diversification. FASEB J. 12: 1075-1095
    • (1998) FASEB J. , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 10
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings N. D. and Barrett A. J. (1995) Evolutionary families of metallopeptidases. Methods Enzymol. 248: 183-229
    • (1995) Methods Enzymol. , vol.248 , pp. 183-229
    • Rawlings, N.D.1    Barrett, A.J.2
  • 11
    • 0029877524 scopus 로고    scopus 로고
    • Computational sequence analysis of matrix metalloproteinases
    • Sang Q. A. and Douglas D. A. (1996) Computational sequence analysis of matrix metalloproteinases. J. Prot. Chem. 15: 137-160
    • (1996) J. Prot. Chem. , vol.15 , pp. 137-160
    • Sang, Q.A.1    Douglas, D.A.2
  • 12
    • 0025799478 scopus 로고
    • The origin of matrix metalloproteinases and their familial relationships
    • Murphy G. J., Murphy G. and Reynolds J. J. (1991) The origin of matrix metalloproteinases and their familial relationships. FEBS Lett. 289: 4-7
    • (1991) FEBS Lett. , vol.289 , pp. 4-7
    • Murphy, G.J.1    Murphy, G.2    Reynolds, J.J.3
  • 13
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato H., Takino T., Okada Y., Cao J., Shinagawa A., Yamamoto E. et al. (1994) A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370: 61-65
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6
  • 14
    • 0030577022 scopus 로고    scopus 로고
    • Activation of a recombinant membrane type I-matrix metalloproteinase (MTI-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2
    • Sato H., Kinoshita T., Takino T., Nakayama K. and Seiki M. (1996) Activation of a recombinant membrane type I-matrix metalloproteinase (MTI-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2. FEBS Lett. 393: 101-104
    • (1996) FEBS Lett. , vol.393 , pp. 101-104
    • Sato, H.1    Kinoshita, T.2    Takino, T.3    Nakayama, K.4    Seiki, M.5
  • 15
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity
    • Pei D. and Weiss S. J. (1996) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J. Biol. Chem. 271: 9135-9140
    • (1996) J. Biol. Chem. , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 16
    • 0343812072 scopus 로고    scopus 로고
    • Relating matrix metalloproteinase structure to function: Why the 'hemopexin' domain?
    • Murphy G. and Knäuper V. (1997) Relating matrix metalloproteinase structure to function: why the 'hemopexin' domain? Matrix Biol. 15: 511-518
    • (1997) Matrix Biol. , vol.15 , pp. 511-518
    • Murphy, G.1    Knäuper, V.2
  • 17
    • 0022996811 scopus 로고
    • Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein
    • Goldberg G. I., Wilhelm S. M., Kronberger A., Bauer E. A., Grant G. A. and Eisen A. Z. (1986) Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein. J. Biol. Chem. 261: 6600-6605
    • (1986) J. Biol. Chem. , vol.261 , pp. 6600-6605
    • Goldberg, G.I.1    Wilhelm, S.M.2    Kronberger, A.3    Bauer, E.A.4    Grant, G.A.5    Eisen, A.Z.6
  • 18
    • 0004552673 scopus 로고
    • Human skin fibroblast stromelysin: Structure, glycosylation, substrate specificity and differential expression in normal and tumorigenic cells
    • Wilhelm S. M., Collier I. E., Kronberger A., Eisen A. Z., Marmer B. L., Grant G. A. et al. (1987) Human skin fibroblast stromelysin: structure, glycosylation, substrate specificity and differential expression in normal and tumorigenic cells. Proc. Natl. Acad. Sci. USA 84: 6725-6729
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6725-6729
    • Wilhelm, S.M.1    Collier, I.E.2    Kronberger, A.3    Eisen, A.Z.4    Marmer, B.L.5    Grant, G.A.6
  • 21
    • 0028935326 scopus 로고
    • Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast and head and neck carcinomas
    • Okada A., Bellocq J.-P., Royer N., Chenard M.-P., Rio M.-C., Chambon P. et al. (1995) 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: 2730-2734
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2730-2734
    • Okada, A.1    Bellocq, J.-P.2    Royer, N.3    Chenard, M.-P.4    Rio, M.-C.5    Chambon, P.6
  • 22
    • 0032167522 scopus 로고    scopus 로고
    • Crystal structure of the complex formed by the membrane type I-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor
    • Fernandez-Catalan C., Bode W., Huber R., Turk D., Calvete J. J., Lichte A. et al. (1998) Crystal structure of the complex formed by the membrane type I-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. EMBO J. 17: 5238-5248
    • (1998) EMBO J. , vol.17 , pp. 5238-5248
    • Fernandez-Catalan, C.1    Bode, W.2    Huber, R.3    Turk, D.4    Calvete, J.J.5    Lichte, A.6
  • 23
    • 53249090335 scopus 로고    scopus 로고
    • Computational sequence analysis of the tissue inhibitor of metalloproteinase family
    • Douglas D. A., Shi Y. E. and Sang Q. A. (1997) Computational sequence analysis of the tissue inhibitor of metalloproteinase family. J. Prot. Chem. 16: 237-255
    • (1997) J. Prot. Chem. , vol.16 , pp. 237-255
    • Douglas, D.A.1    Shi, Y.E.2    Sang, Q.A.3
  • 24
    • 0030717692 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions
    • Gomez D. E., Alonso D. F., Yoshiji H. and Thorgeirsson U. P. (1997) Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur. J. Cell Biol. 74: 111-122
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 111-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3    Thorgeirsson, U.P.4
  • 25
    • 0031978254 scopus 로고    scopus 로고
    • Matrix metalloproteinases and TIMPs: Properties and implications for the rheumatic diseases
    • Cawston T. (1998) Matrix metalloproteinases and TIMPs: properties and implications for the rheumatic diseases. Mol. Med. Today 4: 130-137
    • (1998) Mol. Med. Today , vol.4 , pp. 130-137
    • Cawston, T.1
  • 26
    • 0031039965 scopus 로고    scopus 로고
    • Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproeinases
    • Butler G. S., Will H., Atkinson S. J. and Murphy G. (1997) Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproeinases. Eur. J. Biochem. 244: 653-657
    • (1997) Eur. J. Biochem. , vol.244 , pp. 653-657
    • Butler, G.S.1    Will, H.2    Atkinson, S.J.3    Murphy, G.4
  • 27
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type I matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autocatalytic activation
    • Will H., Atkinson S. J., Butler G. S., Smyth B. and Murphy G. (1996) The soluble catalytic domain of membrane type I matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autocatalytic activation. J. Biol. Chem. 271: 17119-17123
    • (1996) J. Biol. Chem. , vol.271 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smyth, B.4    Murphy, G.5
  • 28
    • 0031984868 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type I-matrix metalloproteinase I (MTI -MMP)
    • Zucker S., Drews M., Conner C., Foda H. D., DeClerck Y. A., Langley K. E. et al. (1998) Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type I-matrix metalloproteinase I (MTI -MMP). J. Biol. Chem. 273: 1216-1222
    • (1998) J. Biol. Chem. , vol.273 , pp. 1216-1222
    • Zucker, S.1    Drews, M.2    Conner, C.3    Foda, H.D.4    DeClerck, Y.A.5    Langley, K.E.6
  • 29
    • 0029022713 scopus 로고
    • Tissue inhibitors of matrix metalloendopeptidases
    • Murphy G. and Willenbrock F. (1995) Tissue inhibitors of matrix metalloendopeptidases. Methods Enzymol. 248: 496-510
    • (1995) Methods Enzymol. , vol.248 , pp. 496-510
    • Murphy, G.1    Willenbrock, F.2
  • 31
    • 0027172634 scopus 로고
    • Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2
    • Strongin A. Y., Marmer B. L., Grant G. A. and Goldberg G. I. (1993) Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2. J. Biol. Chem. 268: 14033-14039
    • (1993) J. Biol. Chem. , vol.268 , pp. 14033-14039
    • Strongin, A.Y.1    Marmer, B.L.2    Grant, G.A.3    Goldberg, G.I.4
  • 32
    • 0029891956 scopus 로고    scopus 로고
    • Processing of a precursor of 72-kilodalton type IV collagenase/gelatinase A by a recombinant membrane-type I matrix metalloproteinase
    • Kinoshita T., Sato H., Takino T., Itoh M., Akizawa T. and Seiki M. (1996) Processing of a precursor of 72-kilodalton type IV collagenase/gelatinase A by a recombinant membrane-type I matrix metalloproteinase. Cancer Res. 56: 2535-2538
    • (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
  • 33
    • 0030824330 scopus 로고    scopus 로고
    • Mutational study of the amino-terminal domain of human tissue inhibitor of metalloproteinases I (TIMP-1) locates an inhibitory region for matrix metalloproteinases
    • Huang W., Meng Q., Suzuki K., Nagase H. and Brew K. (1997) Mutational study of the amino-terminal domain of human tissue inhibitor of metalloproteinases I (TIMP-1) locates an inhibitory region for matrix metalloproteinases. J. Biol. Chem. 272: 22086-22091
    • (1997) J. Biol. Chem. , vol.272 , pp. 22086-22091
    • Huang, W.1    Meng, Q.2    Suzuki, K.3    Nagase, H.4    Brew, K.5
  • 34
    • 0025944065 scopus 로고
    • The N-terminal domain of human tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
    • Murphy G., Houbrechts A., Cockett M. I., Williamson R. A., O'Shea M. and Docherty A. J. P. (1991) The N-terminal domain of human tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry 30: 8097-8102
    • (1991) Biochemistry , vol.30 , pp. 8097-8102
    • Murphy, G.1    Houbrechts, A.2    Cockett, M.I.3    Williamson, R.A.4    O'Shea, M.5    Docherty, A.J.P.6
  • 35
    • 0028047686 scopus 로고
    • Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor
    • Lovejoy B., Cleasby A., Hassell A. M., Longley K., Luther M. A., Weigl D. et al. (1994) Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science 263: 375-377
    • (1994) Science , vol.263 , pp. 375-377
    • Lovejoy, B.1    Cleasby, A.2    Hassell, A.M.3    Longley, K.4    Luther, M.A.5    Weigl, D.6
  • 38
    • 0028324076 scopus 로고
    • The x-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity
    • Bode W., Reinemer P., Huber R., Kleine T., Schnierer S. and Tschesche H. (1994) The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. 13: 1263-1269
    • (1994) EMBO J. , vol.13 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Tschesche, H.6
  • 39
    • 0028040070 scopus 로고
    • Structural implications for the role of the N-terminus in the 'superactivation' of collagenases - a crystallographic study
    • Reinemer P., Grams F., Huber R., Kleíne T., Schnierer S., Pieper M. et al. (1994) Structural implications for the role of the N-terminus in the 'superactivation' of collagenases - a crystallographic study. FEBS Lett. 338: 227-233
    • (1994) FEBS Lett. , vol.338 , pp. 227-233
    • Reinemer, P.1    Grams, F.2    Huber, R.3    Kleíne, T.4    Schnierer, S.5    Pieper, M.6
  • 41
    • 0028128235 scopus 로고
    • Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself
    • Lovejoy B., Hassell A. M., Luther M. A., Weigl D. and Jordan S. R. (1994) Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself. Biochemistry 33: 8207-8217
    • (1994) Biochemistry , vol.33 , pp. 8207-8217
    • Lovejoy, B.1    Hassell, A.M.2    Luther, M.A.3    Weigl, D.4    Jordan, S.R.5
  • 43
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • Browner M. F., Smith W. W. and Castelhano A. L. (1995) Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry 34: 6602-6610
    • (1995) Biochemistry , vol.34 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 44
    • 0028805811 scopus 로고
    • Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
    • Becker J. W., Marcy A. I., Rokosz L. L., Axel M. G., Burbaum J. J., Fitzgerald P. M. D. et al. (1995) Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Prot. Sci. 4: 1966-1976
    • (1995) Prot. Sci. , vol.4 , pp. 1966-1976
    • Becker, J.W.1    Marcy, A.I.2    Rokosz, L.L.3    Axel, M.G.4    Burbaum, J.J.5    Fitzgerald, P.M.D.6
  • 45
    • 0030584673 scopus 로고    scopus 로고
    • X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily
    • Dhanaraj V., Ye Q.-Z., Johnson L. L., Hupe D. J., Ortwine D. F., Dunbar J. B. et al. (1996) X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily. Structure 4: 375-386
    • (1996) Structure , vol.4 , pp. 375-386
    • Dhanaraj, V.1    Ye, Q.-Z.2    Johnson, L.L.3    Hupe, D.J.4    Ortwine, D.F.5    Dunbar, J.B.6
  • 46
    • 0028841016 scopus 로고
    • Solution structure of the catalytic domain of human stromelysin completed with a hydrophobic inhibitor
    • vanDoren S. R., Kurochkin A. V., Hu W., Ye Q. Z., Johnson L. L., Hupe D. J. et al. (1995) Solution structure of the catalytic domain of human stromelysin completed with a hydrophobic inhibitor. Protein Sci. 4: 2487-2498
    • (1995) Protein Sci. , vol.4 , pp. 2487-2498
    • VanDoren, S.R.1    Kurochkin, A.V.2    Hu, W.3    Ye, Q.Z.4    Johnson, L.L.5    Hupe, D.J.6
  • 47
    • 0030066103 scopus 로고    scopus 로고
    • Roles of the propeptide and metal ions in the folding and stability of the catalytic domain of stromelysin (matrix metalloproteinase 3)
    • Wetmore D. R. and Hardman K. D. (1996) Roles of the propeptide and metal ions in the folding and stability of the catalytic domain of stromelysin (matrix metalloproteinase 3). Biochemistry 35: 6549-6558
    • (1996) Biochemistry , vol.35 , pp. 6549-6558
    • Wetmore, D.R.1    Hardman, K.D.2
  • 48
    • 1842377505 scopus 로고    scopus 로고
    • Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
    • Gomis-Rüth F. X., Maskos K., Betz M., Bergner A., Huber R., Suzuki K. et al. (1997) Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 389: 77-81
    • (1997) Nature , vol.389 , pp. 77-81
    • Gomis-Rüth, F.X.1    Maskos, K.2    Betz, M.3    Bergner, A.4    Huber, R.5    Suzuki, K.6
  • 49
    • 0028915695 scopus 로고
    • X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design
    • Grams F., Reinemer P., Powers J. C., Kleine T., Pieper M., Tschesche H. et al. (1995) X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design. Eur. J. Biochem. 228: 830-841
    • (1995) Eur. J. Biochem. , vol.228 , pp. 830-841
    • Grams, F.1    Reinemer, P.2    Powers, J.C.3    Kleine, T.4    Pieper, M.5    Tschesche, H.6
  • 50
    • 0028838862 scopus 로고
    • Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor
    • Grams F., Crimmin M., Hinnes L., Huxley P., Pieper M., Tschesche H. et al. (1995) Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor. Biochemistry 34: 14012-14020
    • (1995) Biochemistry , vol.34 , pp. 14012-14020
    • Grams, F.1    Crimmin, M.2    Hinnes, L.3    Huxley, P.4    Pieper, M.5    Tschesche, H.6
  • 51
    • 0029644935 scopus 로고
    • Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller
    • Li J.-Y., Brick P., O'Hare M. C., Skarzynski T., Lloyd L. F., Curry V. A. et al. (1995) Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller. Structure 3: 541-549
    • (1995) Structure , vol.3 , pp. 541-549
    • Li, J.-Y.1    Brick, P.2    O'Hare, M.C.3    Skarzynski, T.4    Lloyd, L.F.5    Curry, V.A.6
  • 53
    • 0342502272 scopus 로고    scopus 로고
    • The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): Structural implications for its function
    • Gohlke U., Gomis-Rüth F.-X., Crabbe T., Murphy G., Docherty A. J. P. and Bode W. (1996) The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function. FEBS Lett. 378: 126-130
    • (1996) FEBS Lett. , vol.378 , pp. 126-130
    • Gohlke, U.1    Gomis-Rüth, F.-X.2    Crabbe, T.3    Murphy, G.4    Docherty, A.J.P.5    Bode, W.6
  • 54
    • 0040051981 scopus 로고    scopus 로고
    • The helping hand of collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal haemopexin-like domain
    • Gomis-Rüth F. X., Gohlke U., Betz M., Knäuper V., Murphy G. Lopez-Otin C. et al. (1996) The helping hand of collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal haemopexin-like domain. J. Mol. Biol. 264: 556-566
    • (1996) J. Mol. Biol. , vol.264 , pp. 556-566
    • Gomis-Rüth, F.X.1    Gohlke, U.2    Betz, M.3    Knäuper, V.4    Murphy, G.5    Lopez-Otin, C.6
  • 55
    • 0029644945 scopus 로고
    • A helping hand for collagenases: The haemopexin-like domain
    • Bode W. (1995) A helping hand for collagenases: the haemopexin-like domain. Structure 3: 527-530
    • (1995) Structure , vol.3 , pp. 527-530
    • Bode, W.1
  • 56
    • 0027973352 scopus 로고
    • Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family
    • Williamson R. A., Martorell G., Carr M. D., Murphy G., Docherty A. J., Freedman R. B. et al. (1994) Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family. Biochemistry 33: 11745-11759
    • (1994) Biochemistry , vol.33 , pp. 11745-11759
    • Williamson, R.A.1    Martorell, G.2    Carr, M.D.3    Murphy, G.4    Docherty, A.J.5    Freedman, R.B.6
  • 57
    • 0030666085 scopus 로고    scopus 로고
    • Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation
    • Williamson R. A., Carr M. D., Frenkiel T. A., Feeney J. and Freedman R. B. (1997) Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation. Biochemistry 36: 13882-13889
    • (1997) Biochemistry , vol.36 , pp. 13882-13889
    • Williamson, R.A.1    Carr, M.D.2    Frenkiel, T.A.3    Feeney, J.4    Freedman, R.B.5
  • 58
    • 0032555593 scopus 로고    scopus 로고
    • High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3
    • Muskett F. W., Frenkiel T. A., Feeney J., Freedman R. B., Carr M. D. and Williamson R. (1998) High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3. J. Biol. Chem. 273: 2173-21743
    • (1998) J. Biol. Chem. , vol.273 , pp. 2173-21743
    • Muskett, F.W.1    Frenkiel, T.A.2    Feeney, J.3    Freedman, R.B.4    Carr, M.D.5    Williamson, R.6
  • 60
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXX-HXXGXXII and Met-turn) and topologies and should be grouped into a common family, the 'metzineins'
    • Bode W., Gomis-Rüth F.-X. and Stöcker W. (1993) Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXX-HXXGXXII and Met-turn) and topologies and should be grouped into a common family, the 'metzineins'. FEBS Lett. 331: 134-140
    • (1993) FEBS Lett. , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Rüth, F.-X.2    Stöcker, W.3
  • 61
    • 0028969678 scopus 로고
    • The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stöcker W., Grams F., Baumann U., Reinemer P., Gomis-Rüth F. X., McKay D. B. et al. (1995) The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4: 823-840
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stöcker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Rüth, F.X.5    McKay, D.B.6
  • 62
    • 0031569351 scopus 로고    scopus 로고
    • Solution structure of a type 2 module from fibronectin: Implications for the structure and function of the gelatin-binding domain
    • Pickford A. R., Potts J. R., Bright J. R., Phan I. and Campbell I. D. (1997) Solution structure of a type 2 module from fibronectin: implications for the structure and function of the gelatin-binding domain. Structure 5: 359-370
    • (1997) Structure , vol.5 , pp. 359-370
    • Pickford, A.R.1    Potts, J.R.2    Bright, J.R.3    Phan, I.4    Campbell, I.D.5
  • 63
    • 0030025404 scopus 로고    scopus 로고
    • Activation of human neutrophil procollagenase by stromelysin 2
    • Knäuper V., Murphy G. and Tschesche H. (1996) Activation of human neutrophil procollagenase by stromelysin 2. Eur. J. Biochem. 235: 187-191
    • (1996) Eur. J. Biochem. , vol.235 , pp. 187-191
    • Knäuper, V.1    Murphy, G.2    Tschesche, H.3
  • 64
    • 0025026410 scopus 로고
    • Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin)
    • Suzuki K., Enghild J. J., Morodomi T., Salvesen G. and Nagase H. (1990) Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry 29: 10261-10270
    • (1990) Biochemistry , vol.29 , pp. 10261-10270
    • Suzuki, K.1    Enghild, J.J.2    Morodomi, T.3    Salvesen, G.4    Nagase, H.5
  • 65
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. (1997) Activation mechanisms of matrix metalloproteinases. Biol. Chem. 378: 151-160
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 66
    • 0030852784 scopus 로고    scopus 로고
    • Expression, purification, characterization and X-ray analysis of selenomethionine 215 variant of leukocyte collagenase
    • Pieper M., Betz M., Budisa N., Gomis-Rüth F.-X., Bode W. and Tschesche H. (1997) Expression, purification, characterization and X-ray analysis of selenomethionine 215 variant of leukocyte collagenase. J. Protein Chem. 16: 637-650
    • (1997) J. Protein Chem. , vol.16 , pp. 637-650
    • Pieper, M.1    Betz, M.2    Budisa, N.3    Gomis-Rüth, F.-X.4    Bode, W.5    Tschesche, H.6
  • 68
    • 0027257103 scopus 로고
    • Comparative sequence specificities of human 72-and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin)
    • Netzel-Arnett S., Sang Q. X., Moore W. G. I., Navre M., Birkedal-Hansen H. and van Wart H. E. (1993) Comparative sequence specificities of human 72-and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin). Biochemistry 32: 6427-6432
    • (1993) Biochemistry , vol.32 , pp. 6427-6432
    • Netzel-Arnett, S.1    Sang, Q.X.2    Moore, W.G.I.3    Navre, M.4    Birkedal-Hansen, H.5    Van Wart, H.E.6
  • 69
    • 0027050785 scopus 로고
    • Substrate specificity of the human matrix metalloproteinase stromelysin and the development of continuous fluoremetric assays
    • Niedzwiecki L., Teahan J., Harrison R. K. and Stein R. L. (1992) Substrate specificity of the human matrix metalloproteinase stromelysin and the development of continuous fluoremetric assays. Biochemistry 31: 12618-12623
    • (1992) Biochemistry , vol.31 , pp. 12618-12623
    • Niedzwiecki, L.1    Teahan, J.2    Harrison, R.K.3    Stein, R.L.4
  • 71
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • Matthews B. W. (1988) Structural basis of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 21: 333-340
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 72
    • 0028365763 scopus 로고
    • Mutation of the active site glutamic acid of human gelatinase A: Effects on latency, catalysis and the binding of tissue inhibitor of metalloproteinases-1
    • Crabbe T., Zucker S., Cockett M. I., Willenbrock F., Tickle S., O'Connell J. P. et al. (1994) Mutation of the active site glutamic acid of human gelatinase A: effects on latency, catalysis and the binding of tissue inhibitor of metalloproteinases-1. Biochemistry 33: 6684-6690
    • (1994) Biochemistry , vol.33 , pp. 6684-6690
    • Crabbe, T.1    Zucker, S.2    Cockett, M.I.3    Willenbrock, F.4    Tickle, S.5    O'Connell, J.P.6
  • 73
    • 0028063371 scopus 로고
    • Mutational analysis of residues in and around the active site of human fibroblast-type collagenase
    • Windsor L. J., Bodden M. K., Birkedal-Hansen B., Engler J. A. and Birkedal-Hansen H. (1994) Mutational analysis of residues in and around the active site of human fibroblast-type collagenase. J. Biol. Chem. 269: 26201-26207
    • (1994) J. Biol. Chem. , vol.269 , pp. 26201-26207
    • Windsor, L.J.1    Bodden, M.K.2    Birkedal-Hansen, B.3    Engler, J.A.4    Birkedal-Hansen, H.5
  • 74
    • 0026736225 scopus 로고
    • Structure of astacin and implications for activation of astacins and zinc ligation of collagenases
    • Bode W., Gomis-Rüth F. X., Huber R., Zwilling R. and Stöcker W. (1992) Structure of astacin and implications for activation of astacins and zinc ligation of collagenases. Nature 358: 164-166
    • (1992) Nature , vol.358 , pp. 164-166
    • Bode, W.1    Gomis-Rüth, F.X.2    Huber, R.3    Zwilling, R.4    Stöcker, W.5
  • 76
    • 0029095699 scopus 로고
    • Identification of structural determinants controlling human and mouse stromelysin-3 proteolytic activities
    • Noel A., Santavicca M., Stoll I., L'Hoir C., Staub A., Murphy G. et al. (1995) Identification of structural determinants controlling human and mouse stromelysin-3 proteolytic activities. J. Biol. Chem. 270: 22866-22872
    • (1995) J. Biol. Chem. , vol.270 , pp. 22866-22872
    • Noel, A.1    Santavicca, M.2    Stoll, I.3    L'Hoir, C.4    Staub, A.5    Murphy, G.6
  • 77
    • 0000732609 scopus 로고
    • Grasp-graphical representation and analysis of surface properties
    • Nicholls A., Bharadwaj R. and Honig B. (1993) Grasp-graphical representation and analysis of surface properties. Biophys. J. 64: A166
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 78
    • 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 H. E. and Birkedal-Hansen H. (1990) The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA 87: 5578-5582
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 79
    • 0028813772 scopus 로고
    • 1.8 À crystal structure of the C-terminal domain of rabbit serum haemopexin
    • Faber H. R., Groom C. R., Baker H. M., Morgan W. T., Smith A. and Baker E. N. (1995) 1.8 À crystal structure of the C-terminal domain of rabbit serum haemopexin. Structure 3: 551-559
    • (1995) Structure , vol.3 , pp. 551-559
    • Faber, H.R.1    Groom, C.R.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 81
    • 0027409432 scopus 로고
    • Role of zinc-binding-and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins
    • Sanchez-Lopez R., Alexander C. M., Behrendtsen O., Breathnach R. and Werb Z. (1993) Role of zinc-binding-and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins. J. Biol. Chem. 268: 7238-7247
    • (1993) J. Biol. Chem. , vol.268 , pp. 7238-7247
    • Sanchez-Lopez, R.1    Alexander C, M.2    Behrendtsen, O.3    Breathnach, R.4    Werb, Z.5
  • 82
    • 0027533506 scopus 로고
    • Structure-function relationship of human neutrophil collagenase: Identification of regions responsible for substrate specificity and general proteinase activity
    • Hirose T., Patterson C., Pourmotabbed T., Mainardi C. L. and Hasty K. A. (1993) Structure-function relationship of human neutrophil collagenase: identification of regions responsible for substrate specificity and general proteinase activity. Proc. Natl. Acad. Sci. USA 90: 2569-2573
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2569-2573
    • Hirose, T.1    Patterson, C.2    Pourmotabbed, T.3    Mainardi, C.L.4    Hasty, K.A.5
  • 83
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi E., Imai K., Fujii Y., Sato H., Seiki M. and Okada Y. (1997) Membrane type I matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272: 2446-2451
    • (1997) J. Biol. Chem. , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 84
    • 0030945404 scopus 로고    scopus 로고
    • Analysis of the contribution of the hinge region of human neutrophil collagenase (HNC, MMP-8) to stability and collagenolytic activity by alanine scanning mutagenesis
    • Knäuper V., Docherty A. J. P., Smith B., Tschesche H. and Murphy G. (1997) Analysis of the contribution of the hinge region of human neutrophil collagenase (HNC, MMP-8) to stability and collagenolytic activity by alanine scanning mutagenesis. FEBS Lett. 405: 60-64
    • (1997) FEBS Lett. , vol.405 , pp. 60-64
    • Knäuper, V.1    Docherty, A.J.P.2    Smith, B.3    Tschesche, H.4    Murphy, G.5
  • 85
    • 0030602223 scopus 로고    scopus 로고
    • Design and synthesis of heterotrimeric collagen peptides with a built-in cystine knot
    • Ottl J., Battistuta R., Pieper M .,Tschesche H., Bode W., Kühn K. et al. (1996) Design and synthesis of heterotrimeric collagen peptides with a built-in cystine knot. FEBS Lett. 398: 31-36
    • (1996) FEBS Lett. , vol.398 , pp. 31-36
    • Ottl, J.1    Battistuta, R.2    Pieper, M.3    Tschesche, H.4    Bode, W.5    Kühn, K.6
  • 86
    • 0028924956 scopus 로고
    • The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for progelatinase A activation
    • Cao J., Sato H.,Takino T. and Seiki M. (1995) The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for progelatinase A activation. J. Biol. Chem. 270: 801-805
    • (1995) J. Biol. Chem. , vol.270 , pp. 801-805
    • Cao, J.1    Sato, H.2    Takino, T.3    Seiki, M.4
  • 87
    • 0031985228 scopus 로고    scopus 로고
    • The TIMP2 membrane type I metalloproteinase 'receptor' regulates the concentration and efficient activation of progelatinase A
    • Butler G. S., Butler M. J., Atkinson S. J., Will H., Tamura T., van Westrum S. S. et al. (1998) The TIMP2 membrane type I metalloproteinase 'receptor' regulates the concentration and efficient activation of progelatinase A. J. Biol. Chem. 273: 871-880
    • (1998) J. Biol. Chem. , vol.273 , pp. 871-880
    • Butler, G.S.1    Butler, M.J.2    Atkinson, S.J.3    Will, H.4    Tamura, T.5    Van Westrum, S.S.6
  • 88
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans S. V. (1993) SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11: 134-138
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 89
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G. J. (1993) ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6: 37-40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.