Structure and function of human matrix metalloproteinases

Helena Laronha; Jorge Caldeira

doi:10.3390/cells9051076

Structure and function of human matrix metalloproteinases

Helena Laronha
, Jorge Caldeira

Resultado de pesquisa: ???type-name??? › ???researchoutput.researchoutputtypes.contributiontojournal.systematicreview??? › revisão de pares

509 Citações (Scopus)

Resumo

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.

Idioma original	???core.languages.en_GB???
Número do artigo	1076
Revista	Cells
Volume	9
Número de emissão	5
DOIs	https://doi.org/10.3390/cells9051076
Estado da publicação	???researchoutput.status.published??? - mai. 2020

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title = "Structure and function of human matrix metalloproteinases",

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.",

keywords = "Collagen, Matrix metalloproteinases, TIMP",

author = "Helena Laronha and Jorge Caldeira",

note = "Publisher Copyright: {\textcopyright} 2020 by the authors.",

year = "2020",

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doi = "10.3390/cells9051076",

language = "English",

volume = "9",

journal = "Cells",

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T1 - Structure and function of human matrix metalloproteinases

AU - Laronha, Helena

AU - Caldeira, Jorge

PY - 2020/5

Y1 - 2020/5

N2 - 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.

AB - 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.

KW - Collagen

KW - Matrix metalloproteinases

KW - TIMP

UR - https://www.scopus.com/pages/publications/85084888047

U2 - 10.3390/cells9051076

DO - 10.3390/cells9051076

M3 - Review article

C2 - 32357580

AN - SCOPUS:85084888047

SN - 2073-4409

VL - 9

JO - Cells

JF - Cells

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M1 - 1076

ER -

Structure and function of human matrix metalloproteinases

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