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Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator
Although trypsin-like serine proteases have flexible surface-exposed loops and are known to adopt higher and lower activity conformations, structural determinants for the different conformations have remained largely obscure. The trypsin-like serine protease, urokinase-type plasminogen activator (uP...
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| Publicado no: | Sci Rep |
|---|---|
| Main Authors: | , , , , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Nature Publishing Group UK
2017
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5469797/ https://ncbi.nlm.nih.gov/pubmed/28611361 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-017-03457-7 |
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