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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...

詳細記述

保存先:
書誌詳細
出版年:J Virol
主要な著者: Zurcher, T, Luo, G, Palese, P
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Microbiology (ASM) 1994
主題:
オンライン・アクセス: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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