Publication
Structure and function of human matrix metalloproteinases
| datacite.subject.fos | Ciências Médicas | |
| datacite.subject.sdg | 03:Saúde de Qualidade | |
| dc.contributor.author | Laronha, Helena | |
| dc.contributor.author | Caldeira, Jorge | |
| dc.date.accessioned | 2025-07-31T11:27:59Z | |
| dc.date.available | 2025-07-31T11:27:59Z | |
| dc.date.issued | 2020-05 | |
| dc.description.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. | eng |
| dc.identifier.citation | Laronha, H., & Caldeira, J. (2020). Structure and Function of Human Matrix Metalloproteinases. Cells, 9(5), 1076. https://doi.org/10.3390/cells9051076 | |
| dc.identifier.doi | 10.3390/cells9051076 | |
| dc.identifier.issn | 2073-4409 | |
| dc.identifier.uri | http://hdl.handle.net/10400.26/58300 | |
| dc.language.iso | eng | |
| dc.peerreviewed | yes | |
| dc.publisher | MDPI | |
| dc.relation.hasversion | https://doi.org/10.3390/cells9051076 | |
| dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
| dc.subject | matrix metalloproteinases | |
| dc.subject | TIMP | |
| dc.subject | collagen | |
| dc.title | Structure and function of human matrix metalloproteinases | eng |
| dc.type | contribution to journal | |
| dspace.entity.type | Publication | |
| oaire.citation.issue | 5 | |
| oaire.citation.startPage | 1076 | |
| oaire.citation.title | Cells | |
| oaire.citation.volume | 9 | |
| oaire.version | http://purl.org/coar/version/c_970fb48d4fbd8a85 |