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Volumn 79, Issue 4, 2000, Pages 2138-2149

pH- and temperature-dependence of functional modulation in metalloproteinases. A comparison between neutrophil collagenase and gelatinases A and B

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE; GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE; NEUTROPHIL COLLAGENASE; RECOMBINANT ENZYME;

EID: 0033803416     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76461-7     Document Type: Article
Times cited : (61)

References (10)
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    • Aimes, R. T., and J. P. Quigley. 1995. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J. Biol. Chem. 270:5872-5876.
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    • Antonini, E., and P. Ascenzi. 1981. The mechanism of trypsin catalysis at low pH. Proposal for a structural model. J. Biol. Chem. 256: 12449-12455.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12449-12455
    • Antonini, E.1    Ascenzi, P.2
  • 4
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    • Matrix metalloproteinase family
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    • 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., P. Reinemer, R. Huber, T. Kleine, S. Schnierer, and H. Tschesche. 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
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  • 8
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.