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Volumn 2, Issue , 2011, Pages 123-143

Structural Basis of Extracellular Matrix Interactions with Matrix Metalloproteinases

Author keywords

Active Site Cleft; Catalytic Domain; SAXS Data; Tissue Kallikrein; Triple Helix

Indexed keywords


EID: 80155188252     PISSN: 08873224     EISSN: 21911959     Source Type: Book Series    
DOI: 10.1007/978-3-642-16861-1_6     Document Type: Chapter
Times cited : (5)

References (75)
  • 2
    • 0037013250 scopus 로고    scopus 로고
    • Substrate binding of gelatinase b induces its enzymatic activity in the presence of intact propeptide
    • Bannikov GA, Karelina TV, Collier IE, Marmer Bl, Goldberg Gi (2002) Substrate binding of gelatinase b induces its enzymatic activity in the presence of intact propeptide. J Biol Chem 277:16022–16027
    • (2002) J Biol Chem , vol.277 , pp. 16022-16027
    • Bannikov, G.A.1    Karelina, T.V.2    Collier, I.E.3    Bl, M.4    Gi, G.5
  • 3
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagenlike peptide at 1.9 a resolution
    • Bella J, Eaton M, Brodsky B, Berman HM (1994) Crystal and molecular structure of a collagenlike peptide at 1.9 a resolution. Science 266:75–81
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 8
    • 36248991892 scopus 로고    scopus 로고
    • Solution structure of inhibitor-free human metalloelastase (mmp-12) indicates an internal conformational adjustment
    • Bhaskaran R, Palmier Mo, Bagegni Na, Liang X, van Doren Sr (2007) Solution structure of inhibitor-free human metalloelastase (mmp-12) indicates an internal conformational adjustment. J Mol Biol 374:1333–1344
    • (2007) J Mol Biol , vol.374 , pp. 1333-1344
    • Bhaskaran, R.1    Mo, P.2    Na, B.3    Liang, X.4    Sr, D.5
  • 9
    • 52049097313 scopus 로고    scopus 로고
    • Mmp-12 catalytic domain recognizes triple helical peptide models of collagen v with exosites and high activity
    • Bhaskaran R, Palmier Mo, Lauer-Fields Jl, Fields Gb, Van Doren Sr (2008) Mmp-12 catalytic domain recognizes triple helical peptide models of collagen v with exosites and high activity. J Biol Chem 283:21779–21788
    • (2008) J Biol Chem , vol.283 , pp. 21779-21788
    • Bhaskaran, R.1    Mo, P.2    Jl, L.-F.3    Gb, F.4    Sr, V.D.5
  • 10
    • 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
  • 11
    • 33645353328 scopus 로고    scopus 로고
    • Structure and interaction modes of thrombin
    • Bode W (2006) Structure and interaction modes of thrombin. Blood Cells Mol Dis 36:122–130
    • (2006) Blood Cells Mol Dis , vol.36 , pp. 122-130
    • Bode, W.1
  • 12
    • 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, 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
  • 13
    • 0033569704 scopus 로고    scopus 로고
    • The second type ii module from human matrix metalloproteinase 2: Structure, function and dynamics
    • Briknarova K, Grishaev A, Banyai L, Tordai H, Patthy L, Llinas M (1999) The second type ii module from human matrix metalloproteinase 2: structure, function and dynamics. Structure 7: 1235–1245
    • (1999) Structure , vol.7 , pp. 1235-1245
    • Briknarova, K.1    Grishaev, A.2    Banyai, L.3    Tordai, H.4    Patthy, L.5    Llinas, M.6
  • 14
    • 0035920182 scopus 로고    scopus 로고
    • Gelatin-binding region of human matrix metalloproteinase-2: Solution structure, dynamics, and function of the col-23 two-domain construct
    • Briknarova K, Gehrmann M, Banyai L, Tordai H, Patthy L, Llinas M (2001) Gelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the col-23 two-domain construct. J Biol Chem 276:27613–27621
    • (2001) J Biol Chem , vol.276 , pp. 27613-27621
    • Briknarova, K.1    Gehrmann, M.2    Banyai, L.3    Tordai, H.4    Patthy, L.5    Llinas, M.6
  • 15
    • 0026785711 scopus 로고
    • The matrix metalloprotease matrilysin (pump) is expressed in developing human mononuclear phagocytes
    • Busiek Df, Ross Fp, Mcdonnell S, Murphy G, Matrisian Lm, Welgus Hg (1992) The matrix metalloprotease matrilysin (pump) is expressed in developing human mononuclear phagocytes. J Biol Chem 267:9087–9092
    • (1992) J Biol Chem , vol.267 , pp. 9087-9092
    • Df, B.1    Fp, R.2    McDonnell, S.3    Murphy, G.4    Lm, M.5    Hg, W.6
  • 16
    • 0036469507 scopus 로고    scopus 로고
    • Heparin-protein interactions
    • Capila I, Linhardt Rj (2002) Heparin-protein interactions. Angew Chem Int Ed Engl 41:391–412
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 391-412
    • Capila, I.1    Rj, L.2
  • 17
    • 0034703074 scopus 로고    scopus 로고
    • Identification of the (183)rwtnnfrey(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity
    • Chung L, Shimokawa K, Dinakarpandian D, Grams F, Fields Gb, Nagase H (2000) Identification of the (183)rwtnnfrey(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. J Biol Chem 275:29610–29617
    • (2000) J Biol Chem , vol.275 , pp. 29610-29617
    • Chung, L.1    Shimokawa, K.2    Dinakarpandian, D.3    Grams, F.4    Gb, F.5    Nagase, H.6
  • 18
    • 4143066015 scopus 로고    scopus 로고
    • Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis
    • Chung L, Dinakarpandian D, Yoshida N, Lauer-Fields Jl, Fields Gb, Visse R, Nagase H (2004) Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. Embo J 23: 3020–3030
    • (2004) Embo J , vol.23 , pp. 3020-3030
    • Chung, L.1    Dinakarpandian, D.2    Yoshida, N.3    Jl, L.-F.4    Gb, F.5    Visse, R.6    Nagase, H.7
  • 19
    • 0024461448 scopus 로고
    • Fragments of human fibroblast collagenase. Purification and characterization
    • Clark Im, Cawston Te (1989) Fragments of human fibroblast collagenase. Purification and characterization. Biochem J 263:201–206
    • (1989) Biochem J , vol.263 , pp. 201-206
    • Im, C.1    Te, C.2
  • 20
    • 0026656315 scopus 로고
    • Alanine scanning mutagenesis and functional analysis of the fibronectin-like collagen-binding domain from human 92-kda type iv collagenase
    • Collier Ie, Krasnov Pa, Strongin Ay, Birkedal-Hansen H, Goldberg Gi (1992) Alanine scanning mutagenesis and functional analysis of the fibronectin-like collagen-binding domain from human 92-kda type iv collagenase. J Biol Chem 267:6776–6781
    • (1992) J Biol Chem , vol.267 , pp. 6776-6781
    • Ie, C.1    Pa, K.2    Ay, S.3    Birkedal-Hansen, H.4    Gi, G.5
  • 21
    • 0027133565 scopus 로고
    • Human progelatinase a can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the c-terminal domain
    • Crabbe T, Ioannou C, Docherty Aj (1993) Human progelatinase a can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the c-terminal domain. Eur J Biochem 218:431–438
    • (1993) Eur J Biochem , vol.218 , pp. 431-438
    • Crabbe, T.1    Ioannou, C.2    Aj, D.3
  • 22
    • 0028556638 scopus 로고
    • Reciprocated matrix metalloproteinase activation: A process performed by interstitial collagenase and progelatinase a
    • Crabbe T, O’connell Jp, Smith Bj, Docherty Aj (1994) Reciprocated matrix metalloproteinase activation: a process performed by interstitial collagenase and progelatinase a. Biochemistry 33:14419–14425
    • (1994) Biochemistry , vol.33 , pp. 14419-14425
    • Crabbe, T.1    Jp, O.2    Bj, S.3    Aj, D.4
  • 23
    • 0032408076 scopus 로고    scopus 로고
    • Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms
    • Curci JA, Liao S, Huffman MD, Shapiro SD, Thompson RW (1998) Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms. J Clin Invest 102:1900–1910
    • (1998) J Clin Invest , vol.102 , pp. 1900-1910
    • Curci, J.A.1    Liao, S.2    Huffman, M.D.3    Shapiro, S.D.4    Thompson, R.W.5
  • 24
    • 4344710558 scopus 로고    scopus 로고
    • The ternary complex of antithrombinanhydrothrombin-heparin reveals the basis of inhibitor specificity
    • Dementiev A, Petitou M, Herbert Jm, Gettins Pg (2004) The ternary complex of antithrombinanhydrothrombin-heparin reveals the basis of inhibitor specificity. Nat Struct Mol Biol 11: 863–867
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 863-867
    • Dementiev, A.1    Petitou, M.2    Jm, H.3    Pg, G.4
  • 25
    • 63149115283 scopus 로고    scopus 로고
    • Identification and structural analysis of type i collagen sites in complex with fibronectin fragments
    • Erat Mc, Slatter Da, Lowe Ed, Millard Cj, Farndale Rw, Campbell Id, Vakonakis I (2009) Identification and structural analysis of type i collagen sites in complex with fibronectin fragments. Proc Natl Acad Sci U S A 106:4195–4200
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4195-4200
    • Mc, E.1    Da, S.2    Ed, L.3    Cj, M.4    Rw, F.5    Id, C.6    Vakonakis, I.7
  • 26
    • 0035714632 scopus 로고    scopus 로고
    • Cloning, expression, purification, and characterization of rat mmp-12
    • Fu Jy, Lyga A, Shi H, Blue Ml, Dixon B, Chen D (2001) Cloning, expression, purification, and characterization of rat mmp-12. Protein Expr Purif 21:268–274
    • (2001) Protein Expr Purif , vol.21 , pp. 268-274
    • Jy, F.1    Lyga, A.2    Shi, H.3    Ml, B.4    Dixon, B.5    Chen, D.6
  • 27
    • 8744294940 scopus 로고    scopus 로고
    • Modular autonomy, ligand specificity, and functional cooperativity of the three in-tandem fibronectin type ii repeats from human matrix metalloproteinase 2
    • Gehrmann Ml, Douglas Jt, Banyai L, Tordai H, Patthy L, Llinas M (2004) Modular autonomy, ligand specificity, and functional cooperativity of the three in-tandem fibronectin type ii repeats from human matrix metalloproteinase 2. J Biol Chem 279:46921–46929
    • (2004) J Biol Chem , vol.279 , pp. 46921-46929
    • Ml, G.1    Jt, D.2    Banyai, L.3    Tordai, H.4    Patthy, L.5    Llinas, M.6
  • 29
    • 0027772014 scopus 로고
    • Secondary structure and zinc ligation of human recombinant short-form stromelysin by multidimensional nmr
    • Gooley Pr, Johnson Ba, Marcy Ai, Cuca Gc, Salowe Sp, Hagmann Wk, Esser Ck, Springer Jp (1993) Secondary structure and zinc ligation of human recombinant short-form stromelysin by multidimensional nmr. Biochemistry 32:13098–13108
    • (1993) Biochemistry , vol.32 , pp. 13098-13108
    • Pr, G.1    Ba, J.2    Ai, M.3    Gc, C.4    Sp, S.5    Wk, H.6    Ck, E.7    Jp, S.8
  • 30
    • 0028382242 scopus 로고
    • The nmr structure of the inhibited catalytic domain of human stromelysin-1
    • Gooley Pr, O’connell Jf, Marcy Ai, Cuca Gc, Salowe Sp, Bush Bl, Hermes Jd, Esser Ck, Hagmann Wk, Springer Jp, Johnson Ba (1994) The nmr structure of the inhibited catalytic domain of human stromelysin-1. Nat Struct Biol 1:111–118
    • (1994) Nat Struct Biol , vol.1 , pp. 111-118
    • Pr, G.1    Jf, O.2    Ai, M.3    Gc, C.4    Sp, S.5    Bl, B.6    Jd, H.7    Ck, E.8    Wk, H.9    Jp, S.10    Ba, J.11
  • 31
    • 1842416597 scopus 로고    scopus 로고
    • Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase
    • Gronski Tj, Martin Rl Jr, Kobayashi Dk, Walsh Bc, Holman Mc, Huber M, Van Wart He, Shapiro Sd (1997) Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase. J Biol Chem 272:12189–12194
    • (1997) J Biol Chem , vol.272 , pp. 12189-12194
    • Tj, G.1    Jr, M.R.2    Dk, K.3    Bc, W.4    Mc, H.5    Huber, M.6    He, V.W.7    Sd, S.8
  • 32
    • 0028913443 scopus 로고
    • Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties
    • Imai K, Yokohama Y, Nakanishi I, Ohuchi E, Fujii Y, Nakai N, Okada Y (1995) Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties. J Biol Chem 270:6691–6697
    • (1995) J Biol Chem , vol.270 , pp. 6691-6697
    • Imai, K.1    Yokohama, Y.2    Nakanishi, I.3    Ohuchi, E.4    Fujii, Y.5    Nakai, N.6    Okada, Y.7
  • 33
    • 33747610734 scopus 로고    scopus 로고
    • Crystal structure of an active form of human mmp 1
    • Iyer S, Visse R, Nagase H, Acharya Kr (2006) Crystal structure of an active form of human mmp 1. J Mol Biol 362:78–88
    • (2006) J Mol Biol , vol.362 , pp. 78-88
    • Iyer, S.1    Visse, R.2    Nagase, H.3    Kr, A.4
  • 34
    • 0027280459 scopus 로고
    • Fragmentation of human polymorphonuclear-leucocyte collagenase
    • Knauper V, Osthues A, Declerck Ya, Langley Ke, Blaser J, Tschesche H (1993) Fragmentation of human polymorphonuclear-leucocyte collagenase. Biochem J 291(Pt 3):847–854
    • (1993) Biochem J , vol.291 , Issue.3 , pp. 847-854
    • Knauper, V.1    Osthues, A.2    Ya, D.3    Ke, L.4    Blaser, J.5    Tschesche, H.6
  • 35
    • 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
    • Knauper V, Cowell S, Smith B, Lopez-Otin C, O’shea M, Morris H, Zardi L, Murphy G (1997) 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 272:7608–7616
    • (1997) J Biol Chem , vol.272 , 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
  • 36
    • 0035965125 scopus 로고    scopus 로고
    • Substrate specificity determinants of human macrophage elastase (mmp-12) based on the 1.1 a crystal structure
    • Lang R, Kocourek A, Braun M, Tschesche H, Huber R, Bode W, Maskos K (2001) Substrate specificity determinants of human macrophage elastase (mmp-12) based on the 1.1 a crystal structure. J Mol Biol 312:731–742
    • (2001) J Mol Biol , vol.312 , pp. 731-742
    • Lang, R.1    Kocourek, A.2    Braun, M.3    Tschesche, H.4    Huber, R.5    Bode, W.6    Maskos, K.7
  • 37
    • 50649119519 scopus 로고    scopus 로고
    • Selective modulation of matrix metalloproteinase 9 (mmp-9) functions via exosite inhibition
    • Lauer-Fields Jl, Whitehead Jk, Li S, Hammer Rp, Brew K, Fields Gb (2008) Selective modulation of matrix metalloproteinase 9 (mmp-9) functions via exosite inhibition. J Biol Chem 283:20087–20095
    • (2008) J Biol Chem , vol.283 , pp. 20087-20095
    • Jl, L.-F.1    Jk, W.2    Li, S.3    Rp, H.4    Brew, K.5    Gb, F.6
  • 38
    • 69949126360 scopus 로고    scopus 로고
    • Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity
    • Lauer-Fields Jl, Chalmers M, Busby Sa, Minond D, Griffin Pr, Fields Gb (2009) Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity. J Biol Chem 284:24017–24024
    • (2009) J Biol Chem , vol.284 , pp. 24017-24024
    • Jl, L.-F.1    Chalmers, M.2    Sa, B.3    Minond, D.4    Pr, G.5    Gb, F.6
  • 39
    • 0029644935 scopus 로고
    • Structure of full-length porcine synovial collagenase reveals a c-terminal domain containing a calcium-linked, four-bladed ß-propeller
    • Li J, Brick P, O’hare Mc, Skarzynski T, Lloyd Lf, Curry Va, Clark Im, Bigg Hf, Hazleman Bl, Cawston Te, Blow Dm (1995) Structure of full-length porcine synovial collagenase reveals a c-terminal domain containing a calcium-linked, four-bladed ß-propeller. Structure 3:541–549
    • (1995) Structure , vol.3 , pp. 541-549
    • Li, J.1    Brick, P.2    Mc, O.3    Skarzynski, T.4    Lf, L.5    Va, C.6    Im, C.7    Hf, B.8    Bl, H.9    Te, C.10    Dm, B.11
  • 40
    • 4344590703 scopus 로고    scopus 로고
    • Structure of the antithrombin-thrombinheparin ternary complex reveals the antithrombotic mechanism of heparin
    • Li W, Johnson Dj, Esmon Ct, Huntington Ja (2004) Structure of the antithrombin-thrombinheparin ternary complex reveals the antithrombotic mechanism of heparin. Nat Struct Mol Biol 11:857–862
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 857-862
    • Li, W.1    Dj, J.2    Ct, E.3    Ja, H.4
  • 41
    • 42449150052 scopus 로고    scopus 로고
    • Molecular basis of thrombin recognition by protein c inhibitor revealed by the 1.6-a structure of the heparin-bridged complex
    • Li W, Adams Te, Nangalia J, Esmon Ct, Huntington Ja (2008a) Molecular basis of thrombin recognition by protein c inhibitor revealed by the 1.6-a structure of the heparin-bridged complex. Proc Natl Acad Sci U S A 105:4661–4666
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4661-4666
    • Li, W.1    Te, A.2    Nangalia, J.3    Ct, E.4    Ja, H.5
  • 42
    • 52049126668 scopus 로고    scopus 로고
    • The crystal and molecular structures of a cathepsin k: Chondroitin sulfate complex
    • Li Z, Kienetz M, Cherney Mm, James Mn, Bromme D (2008b) The crystal and molecular structures of a cathepsin k: chondroitin sulfate complex. J Mol Biol 383:78–91
    • (2008) J Mol Biol , vol.383 , pp. 78-91
    • Li, Z.1    Kienetz, M.2    Mm, C.3    Mn, J.4    Bromme, D.5
  • 43
    • 77954365306 scopus 로고    scopus 로고
    • Apparent tradeoff of higher activity in mmp-12 for enhanced stability and flexibility in mmp-3
    • Liang X, Arunima A, Zhao Y, Bhaskaran R, Shende A, Byrne Ts, Fleeks J, Palmier Mo, Doren Van Sr (2010) Apparent tradeoff of higher activity in mmp-12 for enhanced stability and flexibility in mmp-3. Biophys J 99:273–283
    • (2010) Biophys J , vol.99 , pp. 273-283
    • Liang, X.1    Arunima, A.2    Zhao, Y.3    Bhaskaran, R.4    Shende, A.5    Ts, B.6    Fleeks, J.7    Mo, P.8    Sr, D.V.9
  • 44
    • 15244343490 scopus 로고    scopus 로고
    • Crystal structures of mmps in complex with physiological and pharmacological inhibitors
    • Maskos K (2005) Crystal structures of mmps in complex with physiological and pharmacological inhibitors. Biochimie 87:249–263
    • (2005) Biochimie , vol.87 , pp. 249-263
    • Maskos, K.1
  • 48
    • 0026640236 scopus 로고
    • The role of the c-terminal domain in collagenase and stromelysin specificity
    • Murphy G, Allan Ja, Willenbrock F, Cockett Mi, O’connell Jp, Docherty Aj (1992) The role of the c-terminal domain in collagenase and stromelysin specificity. J Biol Chem 267:9612–9618
    • (1992) J Biol Chem , vol.267 , pp. 9612-9618
    • Murphy, G.1    Ja, A.2    Willenbrock, F.3    Mi, C.4    Jp, O.5    Aj, D.6
  • 49
    • 0031877083 scopus 로고    scopus 로고
    • The fibronectin-like domain is required for the type v and xi collagenolytic activity of gelatinase b
    • O’farrell Tj, Pourmotabbed T (1998) The fibronectin-like domain is required for the type v and xi collagenolytic activity of gelatinase b. Arch Biochem Biophys 354:24–30
    • (1998) Arch Biochem Biophys , vol.354 , pp. 24-30
    • Tj, O.1    Pourmotabbed, T.2
  • 50
    • 33745181159 scopus 로고    scopus 로고
    • Microfibrillar structure of type i collagen in situ
    • Orgel Jp, Irving Tc, Miller A, Wess Tj (2006) Microfibrillar structure of type i collagen in situ. Proc Natl Acad Sci USA 103:9001–9005
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 9001-9005
    • Jp, O.1    Tc, I.2    Miller, A.3    Tj, W.4
  • 51
    • 0035227706 scopus 로고    scopus 로고
    • Matrix metalloproteinase substrate binding domains, modules and exosites. Overview and experimental strategies
    • Overall Cm (2001) Matrix metalloproteinase substrate binding domains, modules and exosites. Overview and experimental strategies. Methods Mol Biol 151:79–120
    • (2001) Methods Mol Biol , vol.151 , pp. 79-120
    • Cm, O.1
  • 52
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites
    • Overall Cm (2002) Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites. Mol Biotechnol 22:51–86
    • (2002) Mol Biotechnol , vol.22 , pp. 51-86
    • Cm, O.1
  • 53
    • 35148883112 scopus 로고    scopus 로고
    • Protease yoga: Extreme flexibility of a matrix metalloproteinase
    • Overall Cm, Butler Gs (2007) Protease yoga: extreme flexibility of a matrix metalloproteinase. Structure 15:1159–1161
    • (2007) Structure , vol.15 , pp. 1159-1161
    • Cm, O.1    Gs, B.2
  • 54
    • 77957285621 scopus 로고    scopus 로고
    • Nmr and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices
    • Palmier Mo, Fulcher Yg, Bhaskaran R, Duong Vq, Fields Gb, Van Doren Sr (2010) Nmr and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices. J Biol Chem 285(40):30918–30930
    • (2010) J Biol Chem , vol.285 , Issue.40 , pp. 30918-30930
    • Mo, P.1    Yg, F.2    Bhaskaran, R.3    Vq, D.4    Gb, F.5    Sr, V.D.6
  • 55
    • 0035903020 scopus 로고    scopus 로고
    • Specific collagenolysis by gelatinase a, mmp-2, is determined by the hemopexin domain and not the fibronectin-like domain
    • Patterson Ml, Atkinson Sj, Knauper V, Murphy G (2001) Specific collagenolysis by gelatinase a, mmp-2, is determined by the hemopexin domain and not the fibronectin-like domain. FEBS Lett 503:158–162
    • (2001) FEBS Lett , vol.503 , pp. 158-162
    • Ml, P.1    Sj, A.2    Knauper, V.3    Murphy, G.4
  • 56
    • 12544256661 scopus 로고    scopus 로고
    • 0 subsite of matrix metalloproteinase 8 (mmp-8): The role of hydrogen bonding potential of asn188 and tyr189 and the connecting cis bond
    • 0 subsite of matrix metalloproteinase 8 (mmp-8): The role of hydrogen bonding potential of asn188 and tyr189 and the connecting cis bond. J Biol Chem 280:2370–2377
    • (2005) J Biol Chem , vol.280 , pp. 2370-2377
    • Gr, P.1    Cj, M.2    Cm, O.3
  • 57
    • 42949135530 scopus 로고    scopus 로고
    • Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis
    • Perumal S, Antipova O, Orgel Jp (2008) Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis. Proc Natl Acad Sci USA 105:2824–2829
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 2824-2829
    • Perumal, S.1    Antipova, O.2    Jp, O.3
  • 58
    • 70350458704 scopus 로고    scopus 로고
    • Control of promatrilysin (mmp7) activation and substrate-specific activity by sulfated glycosaminoglycans
    • Ra Hj, Harju-Baker S, Zhang F, Linhardt Rj, Wilson Cl, Parks Wc (2009) Control of promatrilysin (mmp7) activation and substrate-specific activity by sulfated glycosaminoglycans. J Biol Chem 284:27924–27932
    • (2009) J Biol Chem , vol.284 , pp. 27924-27932
    • Ra, H.1    Harju-Baker, S.2    Zhang, F.3    Rj, L.4    Cl, W.5    Wc, P.6
  • 59
    • 0034329465 scopus 로고    scopus 로고
    • Crystal structure of the human alpha-thrombin-haemadin complex: An exosite ii-binding inhibitor
    • Richardson Jl, Kroger B, Hoeffken W, Sadler Je, Pereira P, Huber R, Bode W, Fuentes-Prior P (2000) Crystal structure of the human alpha-thrombin-haemadin complex: an exosite ii-binding inhibitor. EMBO J 19:5650–5660
    • (2000) EMBO J , vol.19 , pp. 5650-5660
    • Jl, R.1    Kroger, B.2    Hoeffken, W.3    Je, S.4    Pereira, P.5    Huber, R.6    Bode, W.7    Fuentes-Prior, P.8
  • 60
    • 35148837731 scopus 로고    scopus 로고
    • Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9/gelatinase b
    • Rosenblum G, Van Den Steen Pe, Cohen Sr, Grossmann Jg, Frenkel J, Sertchook R, Slack N, Strange Rw, Opdenakker G, Sagi I (2007) Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9/gelatinase b. Structure 15:1227–1236
    • (2007) Structure , vol.15 , pp. 1227-1236
    • Rosenblum, G.1    Pe, V.D.S.2    Sr, C.3    Jg, G.4    Frenkel, J.5    Sertchook, R.6    Slack, N.7    Rw, S.8    Opdenakker, G.9    Sagi, I.10
  • 61
    • 6044274345 scopus 로고    scopus 로고
    • Interstitial collagenase is a Brownian ratchet driven by proteolysis of collagen
    • Saffarian S, Collier Ie, Marmer Bl, Elson El, Goldberg G (2004) Interstitial collagenase is a Brownian ratchet driven by proteolysis of collagen. Science 306:108–111
    • (2004) Science , vol.306 , pp. 108-111
    • Saffarian, S.1    Ie, C.2    Bl, M.3    El, E.4    Goldberg, G.5
  • 62
    • 44949142150 scopus 로고    scopus 로고
    • Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites
    • Schilling O, Overall Cm (2008) Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites. Nat Biotechnol 26:685–694
    • (2008) Nat Biotechnol , vol.26 , pp. 685-694
    • Schilling, O.1    Cm, O.2
  • 63
    • 0042622380 scopus 로고    scopus 로고
    • Swiss-model: An automated protein homologymodeling server
    • Schwede T, Kopp J, Guex N, Peitsch Nc (2003) Swiss-model: an automated protein homologymodeling server. Nucleic Acids Res 31:3381–3385
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Nc, P.4
  • 64
    • 0027515289 scopus 로고
    • Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
    • Shapiro Sd, Kobayashi Dk, Ley Tj (1993) Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J Biol Chem 268:23824–23829
    • (1993) J Biol Chem , vol.268 , pp. 23824-23829
    • Sd, S.1    Dk, K.2    Tj, L.3
  • 65
    • 0030068937 scopus 로고    scopus 로고
    • Welgus Hg, Senior Rm (1996) The structural basis for the elastolytic activity of the 92-kda and 72-kda gelatinases. Role of the fibronectin type ii-like repeats
    • Shipley Jm, Doyle Ga, Fliszar Cj, Ye Qz, Johnson Ll, Shapiro Sd, Welgus Hg, Senior Rm (1996) The structural basis for the elastolytic activity of the 92-kda and 72-kda gelatinases. Role of the fibronectin type ii-like repeats. J Biol Chem 271:4335–4341
    • J Biol Chem , vol.271 , pp. 4335-4341
    • Jm, S.1    Ga, D.2    Cj, F.3    Qz, Y.4    Ll, J.5    Sd, S.6
  • 66
  • 67
    • 45049083085 scopus 로고    scopus 로고
    • Mapping of macrophage elastase cleavage sites in insoluble human skin elastin
    • Taddese S, Weiss As, Neubert Rh, Schmelzer Ce (2008) Mapping of macrophage elastase cleavage sites in insoluble human skin elastin. Matrix Biol 27:420–428
    • (2008) Matrix Biol , vol.27 , pp. 420-428
    • Taddese, S.1    As, W.2    Neubert, R.3    Ce, S.4
  • 68
    • 76849112691 scopus 로고    scopus 로고
    • Mmp-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type i and type iii
    • Taddese S, Jung Mc, Ihling C, Heinz A, Neubert Rh, Schmelzer Ce (2010) Mmp-12 catalytic domain recognizes and cleaves at multiple sites in human skin collagen type i and type iii. Biochim Biophys Acta 1804:731–739
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 731-739
    • Taddese, S.1    Mc, J.2    Ihling, C.3    Heinz, A.4    Neubert, R.5    Ce, S.6
  • 69
    • 5744251586 scopus 로고    scopus 로고
    • Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase a and mt1-mmp): The differential roles of the mmp hemopexin c domains and the mmp-2 fibronectin type ii modules in collagen triple helicase activities
    • Tam Em, Moore Tr, Butler Gs, Overall Cm (2004) Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase a and mt1-mmp): The differential roles of the mmp hemopexin c domains and the mmp-2 fibronectin type ii modules in collagen triple helicase activities. J Biol Chem 279:43336–43344
    • (2004) J Biol Chem , vol.279 , pp. 43336-43344
    • Em, T.1    Tr, M.2    Gs, B.3    Cm, O.4
  • 70
    • 0027723430 scopus 로고
    • Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3d nmr experiments
    • Van Doren Sr, Kurochkin Av, Ye Qz, Johnson Ll, Hupe Dl, Zuiderweg Erp (1993) Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3d nmr experiments. Biochemistry 32:13109–13122
    • (1993) Biochemistry , vol.32 , pp. 13109-13122
    • Sr, V.D.1    Av, K.2    Ye, Q.3    Ll, J.4    Dl, H.5    Erp, Z.6
  • 71
    • 0028841016 scopus 로고
    • Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor
    • Van Doren Sr, Kurochkin Av, Hu Wd, Ye Qz, Johnson Ll, Hupe Dl, Zuiderweg Erp (1995) Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor. Protein Sci 4:2487–2498
    • (1995) Protein Sci , vol.4 , pp. 2487-2498
    • Sr, V.D.1    Av, K.2    Wd, H.3    Ye, Q.4    Ll, J.5    Dl, H.6    Erp, Z.7
  • 72
    • 67649610424 scopus 로고    scopus 로고
    • Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2
    • Xu X, Mikhailova M, Ilangovan U, Chen Z, Yu A, Pal S, Hinck Ap, Steffensen B (2009) Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2. Biochemistry 48:5822–5831
    • (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    Ap, H.7    Steffensen, B.8
  • 73
    • 0034635483 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
    • Yu Wh, Woessner Jf Jr (2000) Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). J Biol Chem 275:4183–4191
    • (2000) J Biol Chem , vol.275 , pp. 4183-4191
    • Yu, W.1    Jr, W.J.2
  • 74
    • 0035369013 scopus 로고    scopus 로고
    • Heparin-enhanced zymographic detection of matrilysin and collagenases
    • Yu Wh, Woessner Jf Jr (2001) Heparin-enhanced zymographic detection of matrilysin and collagenases. Anal Biochem 293:38–42
    • (2001) Anal Biochem , vol.293 , pp. 38-42
    • Yu, W.1    Jr, W.J.2
  • 75
    • 0036468005 scopus 로고    scopus 로고
    • Cd44 anchors the assembly of matrilysin/mmp-7 with heparin-binding epidermal growth factor precursor and erbb4 and regulates female reproductive organ remodeling
    • Yu Wh, Woessner Jf Jr, Mcneish Jd, Stamenkovic I (2002) Cd44 anchors the assembly of matrilysin/mmp-7 with heparin-binding epidermal growth factor precursor and erbb4 and regulates female reproductive organ remodeling. Genes Dev 16:307–323
    • (2002) Genes Dev , vol.16 , pp. 307-323
    • Yu, W.1    Jr, W.J.2    Jd, M.3    Stamenkovic, I.4


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