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• W1590776622 startingPage "75" @default.
• W1590776622 abstract "The members of the matrix metalloproteinases (MMP) family are key mediators of pericellular proteolysis in many physiological and pathological conditions and in the past 20 years a considerable effort has been put forth to understand their mechanism of action and inhibition. Targeting the MMPs may interfere with the pathogenesis of various human diseases characterized by uncontrolled degradation of the ECM such as cardiovascular diseases, arthritis, and cancer. Therefore, a vast number of synthetic MMP inhibitors were developed and tested in animal models and in human clinical trials for effectiveness. Although some MMP inhibitors have shown promise, the targeting of MMPs is hampered by the structural similarities among the members of the MMP family, which reduces selectivity. The MMPs possess considerable structural similarities in their individual domain structures, in particular in the catalytic and hemopexin-like domain, and with few exceptions, they have a considerable overlap in substrate specificity. MMP-9 (gelatinase B), together with MMP-2 (gelatinase A), belongs to the gelatinase subfamily of MMPs, which comprise a distinct subgroup of MMPs characterized by unique structural features, interactions with tissue inhibitors of metalloproteinases (TIMPs), and substrate specificity. This chapter discusses surface binding of MMP-9 and surface binding of the soluble interstitial collagenases (MMP-1 and MMP-13), as well as surface binding of MMP-7, and surface binding of MMP-19." @default.
• W1590776622 created "2016-06-24" @default.
• W1590776622 creator A5063462261 @default.
• W1590776622 date "2003-01-01" @default.
• W1590776622 modified "2023-09-27" @default.
• W1590776622 title "Surface association of secreted matrix metalloproteinases" @default.
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• W1590776622 doi "https://doi.org/10.1016/s0070-2153(03)54005-4" @default.
• W1590776622 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12696746" @default.
• W1590776622 hasPublicationYear "2003" @default.
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