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Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.

The proteolytic activity of matrix metalloproteinases (MMPs) towards extracellular matrix components is held in check by the tissue inhibitors of metalloproteinases (TIMPs). The binary complex of TIMP-2 and membrane-type-1 MMP (MT1-MMP) forms a cell surface located 'receptor' involved in p...

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Bibliografische gegevens
Hoofdauteurs: Fernandez-Catalan, C, Bode, W, Huber, R, Turk, D, Calvete, J J, Lichte, A, Tschesche, H, Maskos, K
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 1998
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1170851/
https://ncbi.nlm.nih.gov/pubmed/9724659
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/17.17.5238
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