Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation.
The carboxy terminus of the hemagglutinin (HA) of influenza A viruses contains three cysteine residues which are highly conserved among HA subtypes. It has previously been shown for the H2, H3, and H7 subtypes of HA that these cysteine residues are modified by the covalent attachment of palmitic aci...
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| Pubblicato in: | J Virol |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Microbiology (ASM)
1994
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC236978/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8057456/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.68.9.5748-5754.1994 |
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