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Conservation of a crystallographic interface suggests a role for β-sheet augmentation in influenza virus NS1 multifunctionality
The effector domain (ED) of the influenza virus virulence factor NS1 is capable of interaction with a variety of cellular and viral targets, although regulation of these events is poorly understood. Introduction of a W187A mutation into the ED abolishes dimer formation; however, strand–strand intera...
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| Hlavní autoři: | , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
International Union of Crystallography
2011
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3151114/ https://ncbi.nlm.nih.gov/pubmed/21821881 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309111019312 |
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