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The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3
We investigated whether the affinity of tissue inhibitor of metalloproteinases (TIMP)-3 for adamalysins with thrombospondin motifs (ADAMTS)-4 and ADAMTS-5 is affected by the non-catalytic ancillary domains of the enzymes. For this purpose, we first established a novel method of purifying recombinant...
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| Autori principali: | , , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
2009
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2835468/ https://ncbi.nlm.nih.gov/pubmed/19643179 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.matbio.2009.07.005 |
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