Activation of human matrix metalloproteinase 2 by gingival crevicular fluid andPorphyromonas gingivalis

Author:

Grayson R.,Douglas C.W.I.,Heath J.,Rawlinson A.,Evans G.S.

Publisher

Wiley

Subject

Periodontics

Reference45 articles.

1. Biochemical and functional properties of lysine-specific cysteine preoteinase (Lys-gingipain) as a virulence factor of Porphyromonas gingivalis in periodontal disease;Abe;Journal of Biological Chemistry,1988

2. 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.;Aimes;Journal of Biological Chemistry,1995

3. Cell-mediated degradation of type IV collagen and gelatin films is dependent on the activation of matrix metalloproteinases;Atkinson;Biochemical Journal,1992

4. The regulation of matrix metalloproteinase (MMP) production in human fibroblasts;Baugh;Annals of the New York Academy of Sciences,1998

5. Analysis of the ex vivo specificity of human gelatinases A and B towards skin collagen and elastic fibres by computerised morphometry;Berton;Matrix Biology,2000

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