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Volumn 383, Issue 7-8, 2002, Pages 1095-1105

Triple-helical peptide analysis of collagenolytic protease activity

Author keywords

Collagen; Fluorogenic substrates; Matrix metalloproteinases; Triple helix

Indexed keywords

2,4 DINITROPHENOL; COLLAGEN; COLLAGEN TYPE 1; GELATIN; GELATINASE A; HERNIARIN; INTERSTITIAL COLLAGENASE; MATRILYSIN; MATRIX METALLOPROTEINASE; NEUTROPHIL COLLAGENASE; STROMELYSIN; THERMOLYSIN; TRYPSIN; FLUORESCENT DYE; PEPTIDE FRAGMENT;

EID: 0036660865     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.118     Document Type: Review
Times cited : (55)

References (82)
  • 2
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase
    • Aimes, R.T., and Quigley, J.P. (1995). Matrix metalloproteinase-2 is an interstitial collagenase. J. Biol. Chem. 270, 5872-5876.
    • (1995) J. Biol. Chem , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 5
    • 0018959643 scopus 로고
    • Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen
    • Bächinger, H.R., Bruckner, P., Timpl, R., Prockop, D.J., and Engel, J. (1980). Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Eur. J. Biochem. 106, 619-632.
    • (1980) Eur. J. Biochem , vol.106 , pp. 619-632
    • Bächinger, H.R.1    Bruckner, P.2    Timpl, R.3    Prockop, D.J.4    Engel, J.5
  • 6
    • 0030475119 scopus 로고    scopus 로고
    • Recent advances in the field of matrix metalloproteinase inhibitors
    • Beckett, R.P. (1996). Recent advances in the field of matrix metalloproteinase inhibitors. Exp. Opin. Ther. Patents 6, 1305-1315.
    • (1996) Exp. Opin. Ther. Patents , vol.6 , pp. 1305-1315
    • Beckett, R.P.1
  • 7
  • 12
    • 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
  • 13
    • 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
  • 16
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts
    • Brömme, D., Okamoto, K., Wang, B.B., and Biroc, S. (1996). Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. J. Biol. Chem. 271, 2126-2132.
    • (1996) J. Biol. Chem , vol.271 , pp. 2126-2132
    • Brömme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 17
    • 0019880195 scopus 로고
    • Proteolytic enzymes as probes for the triple-helical conformation of procollagen
    • Bruckner, P., and Prockop, D.J. (1981). Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Anal. Biochem. 110, 360-368.
    • (1981) Anal. Biochem , vol.110 , pp. 360-368
    • Bruckner, P.1    Prockop, D.J.2
  • 18
    • 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
  • 19
    • 0034703074 scopus 로고    scopus 로고
    • Mapping the RWTNN-FREY (183-191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity
    • Chung, L., Shimokawa, K., Dinakarpandian, D., Grams, F., Fields, G.B., and Nagase, H. (2000a). Mapping the RWTNN-FREY (183-191) 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    Fields, G.B.5    Nagase, H.6
  • 20
    • 0000916350 scopus 로고    scopus 로고
    • Structural requirements for collagenolytic activity of matrix metalloproteinase 1 (MMP-1)
    • G.B. Fields, J.P. Tam, and G. Barany, eds. (Dordrecht, The Netherlands: Kluwer)
    • Chung, L., Shimokawa, K.-i., and Nagase, H. (2000b). Structural requirements for collagenolytic activity of matrix metalloproteinase 1 (MMP-1). In: Peptides For The New Millennium, G.B. Fields, J.P. Tam, and G. Barany, eds. (Dordrecht, The Netherlands: Kluwer), pp. 438-440.
    • (2000) Peptides For The New Millennium , pp. 438-440
    • Chung, L.1    Shimokawa, K.-I.2    Nagase, H.3
  • 21
    • 0024461448 scopus 로고
    • Fragments of human fibroblast collagenase: Purification and characterization
    • Clark, I.N., and Cawston, T.E. (1989). Fragments of human fibroblast collagenase: purification and characterization. Biochem. J. 263, 201-206.
    • (1989) Biochem. J , vol.263 , pp. 201-206
    • Clark, I.N.1    Cawston, T.E.2
  • 22
    • 0030959540 scopus 로고    scopus 로고
    • cDNA cloning and expression of bovine procollagen I N-proteinase: A new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
    • Colige, A., Li, S.-W., Sieron, A.L., Nusgens, B.V., Prockop, D.J., and Lapiere, C.M. (1997). cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc. Natl. Acad. Sci. USA 94, 2374-2379.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2374-2379
    • Colige, A.1    Li, S.-W.2    Sieron, A.L.3    Nusgens, B.V.4    Prockop, D.J.5    Lapiere, C.M.6
  • 23
    • 0027731043 scopus 로고
    • 15N NMR relaxation and hydrogen-exchange measurements
    • 15N NMR relaxation and hydrogen-exchange measurements. Biochemistry 32, 13299-13309.
    • (1993) Biochemistry , vol.32 , pp. 13299-13309
    • Fan, P.1    Li, M.H.2    Brodsky, B.3    Baum, J.4
  • 24
    • 0026333465 scopus 로고
    • A model for interstitial collagen catabolism by mammalian collagenases
    • Fields, G.B. (1991). A model for interstitial collagen catabolism by mammalian collagenases. J. Theor. Biol. 153, 585-602.
    • (1991) J. Theor. Biol , vol.153 , pp. 585-602
    • Fields, G.B.1
  • 25
    • 0027130489 scopus 로고
    • Solid-phase synthesis and stability of triple-helical peptides incorporating native collagen sequences
    • Fields, C.G., Lovdahl, C.M., Miles, A.J., Matthias-Hagen, V.L., and Fields, G.B. (1993a). Solid-phase synthesis and stability of triple-helical peptides incorporating native collagen sequences. Biopolymers 33, 1695-1707.
    • (1993) Biopolymers , vol.33 , pp. 1695-1707
    • Fields, C.G.1    Lovdahl, C.M.2    Miles, A.J.3    Matthias-Hagen, V.L.4    Fields, G.B.5
  • 26
    • 0027230410 scopus 로고
    • Melanoma cell adhesion and spreading activities of a synthetic 124-residue triple-helical 'mini-colla-gen'
    • Fields, C.G., Mickelson, D.J., Drake, S.L., McCarthy, J.B., and Fields, G.B. (1993b). Melanoma cell adhesion and spreading activities of a synthetic 124-residue triple-helical 'mini-colla-gen'. J. Biol. Chem. 268, 14153-14160.
    • (1993) J. Biol. Chem , vol.268 , pp. 14153-14160
    • Fields, C.G.1    Mickelson, D.J.2    Drake, S.L.3    McCarthy, J.B.4    Fields, G.B.5
  • 27
    • 0011015333 scopus 로고    scopus 로고
    • Triple-helical peptide analysis of collagenolytic protease activity
    • R.A. Houghton and M. Lebl, eds. (San Diego, USA: American Peptide Society)
    • Fields, G.B., Lauer-Fields, J.L., Sritharan, T., and Nagase, H. (2001). Triple-helical peptide analysis of collagenolytic protease activity. In: Peptides: The Wave Of The Future, R.A. Houghton and M. Lebl, eds. (San Diego, USA: American Peptide Society), pp. 975-977.
    • (2001) Peptides: The Wave Of The Future , pp. 975-977
    • Fields, G.B.1    Lauer-Fields, J.L.2    Sritharan, T.3    Nagase, H.4
  • 28
    • 0028322352 scopus 로고
    • Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
    • Freije, J.M.P., Diez-Itza, T., Balbin, M., Sanchez, L.M., Blasco, R., Tolivia, J., and Lopez-Otin, C. (1994). Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J. Biol. Chem. 269, 16766-16773.
    • (1994) J. Biol. Chem , vol.269 , pp. 16766-16773
    • Freije, J.M.P.1    Diez-Itza, T.2    Balbin, M.3    Sanchez, L.M.4    Blasco, R.5    Tolivia, J.6    Lopez-Otin, C.7
  • 29
    • 17544375225 scopus 로고    scopus 로고
    • Promotion of fibroblast adhesion by triple-helical peptide models of type I collagen-derived sequences
    • Grab, B., Miles, A.J., Furcht, L.T., and Fields, G.B. (1996). Promotion of fibroblast adhesion by triple-helical peptide models of type I collagen-derived sequences. J. Biol. Chem. 271, 12234-12240.
    • (1996) J. Biol. Chem , vol.271 , pp. 12234-12240
    • Grab, B.1    Miles, A.J.2    Furcht, L.T.3    Fields, G.B.4
  • 30
    • 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., Huber, R., and Bode, W. (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    Huber, R.7    Bode, W.8
  • 31
    • 0019336174 scopus 로고
    • Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator
    • Grant, G.A., Henderson, K.O., Eisen, A.Z., and Bradshaw, R.A. (1980). Amino acid sequence of a collagenolytic protease from the hepatopancreas of the fiddler crab, Uca pugilator. Biochemistry 19, 4653-4659.
    • (1980) Biochemistry , vol.19 , pp. 4653-4659
    • Grant, G.A.1    Henderson, K.O.2    Eisen, A.Z.3    Bradshaw, R.A.4
  • 32
    • 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
  • 33
    • 0018782475 scopus 로고
    • 1H High power double magnetic resonance investigation of collagen backbone motion in fibrils and in solution
    • 1H High power double magnetic resonance investigation of collagen backbone motion in fibrils and in solution. J. Mol. Biol. 133, 45-65.
    • (1979) J. Mol. Biol , vol.133 , pp. 45-65
    • Jelinski, L.W.1    Torchia, D.A.2
  • 38
    • 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
    • Knäuper, V., Cowell, S., Smith, B., Lopez-Otin, C., O'Shea, M., Morris, H., Zardi, L., and 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
    • Knäuper, 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
  • 39
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple-helical structure
    • Kramer, R.Z., Bella, J., Mayville, P., Brodsky, B., and Berman, H. M. (1999). Sequence dependent conformational variations of collagen triple-helical structure. Nature Struct. Biol. 6, 454-457.
    • (1999) Nature Struct. Biol , vol.6 , pp. 454-457
    • Kramer, R.Z.1    Bella, J.2    Mayville, P.3    Brodsky, B.4    Berman, H.M.5
  • 40
    • 0033665199 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer
    • Lauer-Fields, J.L., and Fields, G.B. (2000). Matrix metalloproteinase inhibitors and cancer. Exp. Opin. Ther. Patents 10, 1873-1884.
    • (2000) Exp. Opin. Ther. Patents , vol.10 , pp. 1873-1884
    • Lauer-Fields, J.L.1    Fields, G.B.2
  • 41
    • 0034683146 scopus 로고    scopus 로고
    • Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases
    • Lauer-Fields, J.L., Nagase, H., and Fields, G.B. (2000a). Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases. J. Chromatogr. A 890, 117-125.
    • (2000) J. Chromatogr. A , vol.890 , pp. 117-125
    • Lauer-Fields, J.L.1    Nagase, H.2    Fields, G.B.3
  • 42
    • 0034607873 scopus 로고    scopus 로고
    • Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases
    • Lauer-Fields, J.L., Tuzinski, K.A., Shimokawa, K., Nagase, H., and Fields, G.B. (2000b). Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases. J. Biol. Chem. 275, 13282-13290.
    • (2000) J. Biol. Chem , vol.275 , pp. 13282-13290
    • Lauer-Fields, J.L.1    Tuzinski, K.A.2    Shimokawa, K.3    Nagase, H.4    Fields, G.B.5
  • 43
    • 0035873874 scopus 로고    scopus 로고
    • Kinetic analysis of matrix metalloproteinase triple-helicase activity using fluorogenic substrates
    • Lauer-Fields, J.L., Broder, T., Sritharan, T., Nagase, H., and Fields, G.B. (2001). Kinetic analysis of matrix metalloproteinase triple-helicase activity using fluorogenic substrates. Biochemistry 40, 5795-5803.
    • (2001) Biochemistry , vol.40 , pp. 5795-5803
    • Lauer-Fields, J.L.1    Broder, T.2    Sritharan, T.3    Nagase, H.4    Fields, G.B.5
  • 44
    • 0023645018 scopus 로고
    • Complete amino acid sequence of the collagenase from the insect Hypoderma lineatum
    • Lecroisey, A., Gilles, A.-M., De Wolf, A., and Keil, B. (1987). Complete amino acid sequence of the collagenase from the insect Hypoderma lineatum. J. Biol. Chem. 262, 7546-7551.
    • (1987) J. Biol. Chem , vol.262 , pp. 7546-7551
    • Lecroisey, A.1    Gilles, A.-M.2    De Wolf, A.3    Keil, B.4
  • 46
    • 0026536653 scopus 로고
    • Cancer cell invasion and metastasis
    • Liotta, L.A. (1992). Cancer cell invasion and metastasis. Scientific American 266, 54-63.
    • (1992) Scientific American , vol.266 , pp. 54-63
    • Liotta, L.A.1
  • 47
    • 0032480755 scopus 로고    scopus 로고
    • Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease
    • Liu, X., Kim, S., Dai, Q.-H., Brodsky, B., and Baum, J. (1998). Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease. Biochemistry 37, 15528-15533.
    • (1998) Biochemistry , vol.37 , pp. 15528-15533
    • Liu, X.1    Kim, S.2    Dai, Q.-H.3    Brodsky, B.4    Baum, J.5
  • 49
    • 0032540170 scopus 로고    scopus 로고
    • The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro
    • Millichip, M.I., Dallas, D.J., Wu, E., Dale, S., and McKie, N. (1998). The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem. Biophys. Res. Commun. 245, 594-598.
    • (1998) Biochem. Biophys. Res. Commun , vol.245 , pp. 594-598
    • Millichip, M.I.1    Dallas, D.J.2    Wu, E.3    Dale, S.4    McKie, N.5
  • 51
    • 0040182518 scopus 로고    scopus 로고
    • Heterotrimeric collagen peptides as fluorogenic collagenase substrates: Synthesis, conformational properties and enzymatic digestion
    • Müller, J.C.D., Ottl, J., and Moroder, L. (2000). Heterotrimeric collagen peptides as fluorogenic collagenase substrates: synthesis, conformational properties and enzymatic digestion. Biochemistry 39, 5111-5116.
    • (2000) Biochemistry , vol.39 , pp. 5111-5116
    • Müller, J.C.D.1    Ottl, J.2    Moroder, L.3
  • 53
    • 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
  • 54
    • 0000736684 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • N.M. Hooper, ed. (London, UK: Taylor & Francis)
    • Nagase, H. (1996). Matrix metalloproteinases. In: Zinc Metalloproteases In Health and Disease, N.M. Hooper, ed. (London, UK: Taylor & Francis), pp. 153-204.
    • (1996) Zinc Metalloproteases In Health and Disease , pp. 153-204
    • Nagase, H.1
  • 55
    • 0028145441 scopus 로고
    • Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3)
    • Nagase, H., Fields, C.G., and Fields, G.B. (1994). Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3). J. Biol. Chem. 269, 20952-20957.
    • (1994) J. Biol. Chem , vol.269 , pp. 20952-20957
    • Nagase, H.1    Fields, C.G.2    Fields, G.B.3
  • 56
    • 0029758751 scopus 로고    scopus 로고
    • Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides
    • Nagase, H., and Fields, G.B. (1996). Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides. Biopolymers 40, 399-416.
    • (1996) Biopolymers , vol.40 , pp. 399-416
    • Nagase, H.1    Fields, G.B.2
  • 57
    • 0033999308 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Biologic acitivity and clinical implications
    • Nelson, A.R., Fingleton, B., Rothenberg, M.L., and Matrisian, L.M. (2000). Matrix metalloproteinases: biologic acitivity and clinical implications. J. Clin. Oncol. 18, 1135-1149.
    • (2000) J. Clin. Oncol , vol.18 , pp. 1135-1149
    • Nelson, A.R.1    Fingleton, B.2    Rothenberg, M.L.3    Matrisian, L.M.4
  • 58
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase digests intersitial 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 intersitial 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
  • 59
    • 0033518557 scopus 로고    scopus 로고
    • Disulfide-bridged heterotrimeric collagen peptides containing the collagenase cleavage site of collagen type I: Synthesis and conformational properties
    • Ottl, J., and Moroder, L. (1999). Disulfide-bridged heterotrimeric collagen peptides containing the collagenase cleavage site of collagen type I: synthesis and conformational properties. J. Am. Chem. Soc. 121, 653-661.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 653-661
    • Ottl, J.1    Moroder, L.2
  • 60
    • 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., and Moroder, L. (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    Moroder, L.7
  • 62
    • 0035227706 scopus 로고    scopus 로고
    • Matrix metalloproteinase substrate binding domains, modules and exosites: Overview and experimental strategies
    • I.M. Clark, ed. (Totowa, USA: Humana Press)
    • Overall, C.M. (2001). Matrix metalloproteinase substrate binding domains, modules and exosites: overview and experimental strategies. In: Methods in Molecular Biology 151: Matrix Metalloproteinase Protocols, I.M. Clark, ed. (Totowa, USA: Humana Press), pp. 79-120.
    • (2001) Methods in Molecular Biology 151: Matrix Metalloproteinase Protocols , pp. 79-120
    • Overall, C.M.1
  • 63
    • 0030916865 scopus 로고    scopus 로고
    • Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix
    • Perona, J.J., Tsu, C.A., Craik, C.S., and Fletterick, R.J. (1997). Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Biochemistry 36, 5381-5392.
    • (1997) Biochemistry , vol.36 , pp. 5381-5392
    • Perona, J.J.1    Tsu, C.A.2    Craik, C.S.3    Fletterick, R.J.4
  • 64
    • 0020348367 scopus 로고
    • Stability of proteins: Proteins which do not present a single cooperative system
    • Privalov, P.L. (1982). Stability of proteins: proteins which do not present a single cooperative system. Adv. Protein Chem. 35, 1-104.
    • (1982) Adv. Protein Chem , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 65
    • 0020612083 scopus 로고
    • Conformational stability of type I collagen triple helix: Evidence for temporary and local relaxation of the protein conformation using a proteolytic probe
    • Ryhänen, L., Zaragoza, E.J., and Uitto, J. (1983). Conformational stability of type I collagen triple helix: evidence for temporary and local relaxation of the protein conformation using a proteolytic probe. Arch. Biochem. Biophys. 223, 562-571.
    • (1983) Arch. Biochem. Biophys , vol.223 , pp. 562-571
    • Ryhänen, L.1    Zaragoza, E.J.2    Uitto, J.3
  • 66
    • 0026760832 scopus 로고
    • Molecular cloning of a cDNA that encodes a serine protease with chymotryptic and collagenolytic activities in the hepatopancreas of the shrimp Penaeus vanameii (Crustacea, Decapoda)
    • Sellos, D., and Van Wormhoudt, A. (1992). Molecular cloning of a cDNA that encodes a serine protease with chymotryptic and collagenolytic activities in the hepatopancreas of the shrimp Penaeus vanameii (Crustacea, Decapoda). FEBS Lett. 309, 219-224.
    • (1992) FEBS Lett , vol.309 , pp. 219-224
    • Sellos, D.1    Van Wormhoudt, A.2
  • 67
    • 0027441145 scopus 로고
    • Deletion of a large domain in recombinant human procollagen II does not alter the thermal stability of the triple helix
    • Sieron, A.L., Fertala, A., Ala-Kokko, L., and Prockop, D.J. (1993). Deletion of a large domain in recombinant human procollagen II does not alter the thermal stability of the triple helix. J. Biol. Chem. 268, 21232-21237.
    • (1993) J. Biol. Chem , vol.268 , pp. 21232-21237
    • Sieron, A.L.1    Fertala, A.2    Ala-Kokko, L.3    Prockop, D.J.4
  • 70
    • 0029825963 scopus 로고    scopus 로고
    • Identification and characterization of a novel collagenase in Xenopus laevis: Possible roles during frog development
    • Stolow, M.A., Bauzon, D.D., Li, J., Sedgwick, T., Liang, V.C., Sang, Q.A., and Shi, Y.B. (1996). Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development. Mol. Biol. Cell 7, 1471-1483.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1471-1483
    • Stolow, M.A.1    Bauzon, D.D.2    Li, J.3    Sedgwick, T.4    Liang, V.C.5    Sang, Q.A.6    Shi, Y.B.7
  • 71
    • 0027980261 scopus 로고
    • The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen clevage sites
    • Tsu, C.A., Persona, J.J., Schellenberger, V., Turck, C.W., and Craik, C.S. (1994). The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen clevage sites. J. Biol. Chem. 269, 19565-19572.
    • (1994) J. Biol. Chem , vol.269 , pp. 19565-19572
    • Tsu, C.A.1    Persona, J.J.2    Schellenberger, V.3    Turck, C.W.4    Craik, C.S.5
  • 72
    • 0017872971 scopus 로고
    • Cleavage of native type III collagen in the collagenase susceptible region by thermolysin
    • Wang, H.-M., Chan, J., Pettigrew, D.W., and Sodek, J. (1978). Cleavage of native type III collagen in the collagenase susceptible region by thermolysin. Biochim. Biophys. Acta 533, 270-277.
    • (1978) Biochim. Biophys. Acta , vol.533 , pp. 270-277
    • Wang, H.-M.1    Chan, J.2    Pettigrew, D.W.3    Sodek, J.4
  • 73
    • 0019312635 scopus 로고
    • Characteristics of the action of human skin fibroblast collagenase on fibrillar collagen
    • Welgus, H.G., Jeffrey, J.J., Stricklin, G.P., Roswit, W.T., and Eisen, A.Z. (1980). Characteristics of the action of human skin fibroblast collagenase on fibrillar collagen. J. Biol. Chem. 255, 6806-6813.
    • (1980) J. Biol. Chem , vol.255 , pp. 6806-6813
    • Welgus, H.G.1    Jeffrey, J.J.2    Stricklin, G.P.3    Roswit, W.T.4    Eisen, A.Z.5
  • 74
    • 0019888405 scopus 로고
    • Human skin fibroblast collagenase: Assessment of activation energy and deuterium isotope effect with collagenous substrates
    • Welgus, H.G., Jeffrey, J.J., and Eisen, A.Z. (1981). Human skin fibroblast collagenase: assessment of activation energy and deuterium isotope effect with collagenous substrates. J. Biol. Chem. 256, 9516-9521.
    • (1981) J. Biol. Chem , vol.256 , pp. 9516-9521
    • Welgus, H.G.1    Jeffrey, J.J.2    Eisen, A.Z.3
  • 75
    • 0020481279 scopus 로고
    • Substrate specificity of the collagenolytic serine protease from Uca pugilator: Studies with collagenous substrates
    • Welgus, H.G., Grant, G.A., Jeffrey, J.J., and Eisen, A.Z. (1982a). Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with collagenous substrates. Biochemistry 21, 5183-5189.
    • (1982) Biochemistry , vol.21 , pp. 5183-5189
    • Welgus, H.G.1    Grant, G.A.2    Jeffrey, J.J.3    Eisen, A.Z.4
  • 76
    • 0020362863 scopus 로고
    • The gelatinolytic activity of human skin fibroblast collagenase
    • Welgus, H.G., Jeffrey, J.J., Stricklin, G.P., and Eisen, A.Z. (1982b). The gelatinolytic activity of human skin fibroblast collagenase. J. Biol. Chem. 257, 11534-11539.
    • (1982) J. Biol. Chem , vol.257 , pp. 11534-11539
    • Welgus, H.G.1    Jeffrey, J.J.2    Stricklin, G.P.3    Eisen, A.Z.4
  • 79
    • 0032504177 scopus 로고    scopus 로고
    • Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts
    • Yang, M., and Kurkinen, M. (1998). Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. J. Biol. Chem. 273, 17893-17900.
    • (1998) J. Biol. Chem , vol.273 , pp. 17893-17900
    • Yang, M.1    Kurkinen, M.2
  • 80
    • 0030482156 scopus 로고    scopus 로고
    • Self-assembling amphiphiles for construction of protein molecular architecture
    • Yu, Y.-C., Berndt, P., Tirrell, M., and Fields, G.B. (1996). Self-assembling amphiphiles for construction of protein molecular architecture. J. Am. Chem. Soc. 118, 12515-12520.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 12515-12520
    • Yu, Y.-C.1    Berndt, P.2    Tirrell, M.3    Fields, G.B.4
  • 81
    • 0032494447 scopus 로고    scopus 로고
    • Minimal lipidation stabilizes protein-like molecular architecture
    • Yu, Y.-C., Tirrell, M., and Fields, G.B. (1998). Minimal lipidation stabilizes protein-like molecular architecture. J. Am. Chem. Soc. 120, 9979-9987.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 9979-9987
    • Yu, Y.-C.1    Tirrell, M.2    Fields, G.B.3
  • 82
    • 0033514426 scopus 로고    scopus 로고
    • Structure and dynamics of peptide-amphiphiles incorporating triple-helical proteinlike molecular architecture
    • Yu, Y.-C., Roontga, V., Daragan, V.A., Mayo, K.H., Tirrell, M., and Fields, G.B. (1999). Structure and dynamics of peptide-amphiphiles incorporating triple-helical proteinlike molecular architecture. Biochemistry 38, 1659-1668.
    • (1999) Biochemistry , vol.38 , pp. 1659-1668
    • Yu, Y.-C.1    Roontga, V.2    Daragan, V.A.3    Mayo, K.H.4    Tirrell, M.5    Fields, G.B.6


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