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Mechanism and Inhibition of Matrix Metalloproteinases

期刊

CURRENT MEDICINAL CHEMISTRY
卷 26, 期 15, 页码 2609-2633

出版社

BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/0929867325666180326163523

关键词

Matrix metalloproteinases; enzyme; mechanism; collagenolysis; elastolysis; inhibitor

资金

  1. Fondazione Cassa di Risparmio di Firenze, MIUR PRIN [2012SK7ASN]
  2. CERM/CIRMMP Italy center
  3. Instruct-ERIC, a landmark ESFRI project
  4. H2020 West-Life [675858]
  5. University of Florence CERM-TT, Recombinant Proteins JOYNLAB

向作者/读者索取更多资源

Matrix metalloproteinases hydrolyze proteins and glycoproteins forming the extracellular ma- trix, cytokines and growth factors released in the extracellular space, and membrane-bound receptors on the outer cell membrane. The pathological relevance of MMPs has prompted the structural and functional characterization of these enzymes and the development of synthetic inhibitors as possible drug candidates. Recent studies have provided a better understanding of the substrate preference of the different members of the family, and structural data on the mechanism by which these enzymes hydrolyze the substrates. Here, we report the recent advancements in the understanding of the mechanism of collagenolysis and elastolysis, and we discuss the perspectives of new therapeutic strategies for targeting MMPs.

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