review Open AccessTop 1% cited
Structure and Function of Human Matrix Metalloproteinases
Cells · 2020 · Vol. 9(5) · pp. 1076–1076
Helena Laronha(Escola Superior de Saúde Egas Moniz)Jorge Caldeira✉(Escola Superior de Saúde Egas Moniz)
Abstract
The extracellular matrix (ECM) is a macromolecules network, in which the most abundant molecule is collagen. This protein in triple helical conformation is highly resistant to proteinases degradation, the only enzymes capable of degrading the collagen are matrix metalloproteinases (MMPs). This resistance and maintenance of collagen, and consequently of ECM, is involved in several biological processes and it must be strictly regulated by endogenous inhibitors (TIMPs). The deregulation of MMPs activity leads to development of numerous diseases. This review shows MMPs complexity.
Protease and Inhibitor MechanismsPeptidase Inhibition and AnalysisBlood Coagulation and Thrombosis MechanismsMatrix metalloproteinaseExtracellular matrixCell biologyFunction (biology)Matrix (chemical analysis)ChemistryEnzymeBiochemistryBiology
MeSH terms
CollagenExtracellular MatrixHumansStructure-Activity RelationshipMatrix MetalloproteinasesProteolysisMatrix Metalloproteinase Inhibitors
Funding
- Fundação para a Ciência e a Tecnologia
Citations
560
FWCI
22.18
field-weighted impact
References
36
Percentile
100%
vs. same field & year
Citations per year
References
Structure and function of matrix metalloproteinases and TIMPs
Cardiovascular Research · 2006 · 3,356 citations
Matrix metalloproteinases (MMPs): Chemical–biological functions and (Q)SARs
Bioorganic & Medicinal Chemistry · 2007 · 766 citations
Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases
Circulation Research · 2003 · 4,481 citations
Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances
Sensors · 2018 · 737 citations
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