Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
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New aspects of influenza viruses.S acylation of the hemagglutinin of influenza viruses: mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine.Ion channel regulation by protein S-acylation.Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly.Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivityThe transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G proteinHemagglutinin-esterase-fusion (HEF) protein of influenza C virus.Influenza virus M2 protein ion channel activity stabilizes the native form of fowl plague virus hemagglutinin during intracellular transportMutations at palmitylation sites of the influenza virus hemagglutinin affect virus formationEffects of altering palmitylation sites on biosynthesis and function of the influenza virus hemagglutininAlterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.Role of spike protein endodomains in regulating coronavirus entry.Palmitoylation of Sindbis Virus TF Protein Regulates Its Plasma Membrane Localization and Subsequent Incorporation into Virions.The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity.Ion channel regulation by protein palmitoylation.Association of influenza virus proteins with membrane rafts.Two Cytoplasmic Acylation Sites and an Adjacent Hydrophobic Residue, but No Other Conserved Amino Acids in the Cytoplasmic Tail of HA from Influenza A Virus Are Crucial for Virus Replication.Site-specific S-acylation of influenza virus hemagglutinin: the location of the acylation site relative to the membrane border is the decisive factor for attachment of stearate.Dual role of the cysteine-string domain in membrane binding and palmitoylation-dependent sorting of the molecular chaperone cysteine-string protein.Palmitoylation is required for intracellular trafficking of influenza B virus NB protein and efficient influenza B virus growth in vitro.Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin.Apical budding of a recombinant influenza A virus expressing a hemagglutinin protein with a basolateral localization signal.The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles.Palmitoylation of the Autographa californica multicapsid nucleopolyhedrovirus envelope glycoprotein GP64: mapping, functional studies, and lipid rafts.Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation.A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein.Rescue of vector-expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein.Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin.Structure and assembly of hemagglutinin mutants of fowl plague virus with impaired surface transport.Influence of acylation sites of influenza B virus hemagglutinin on fusion pore formation and dilation.Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity.Unusual topological arrangement of structural motifs in the baboon reovirus fusion-associated small transmembrane protein.Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteinsCysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting.Lateral distribution of the transmembrane domain of influenza virus hemagglutinin revealed by time-resolved fluorescence imaging.Hemagglutinin of influenza virus partitions into the nonraft domain of model membranes.Structural requirements for palmitoylation of surfactant protein C precursor.Palmitoylation of cysteine residues on HA in the cis-Golgi networkDeep Sequencing of H7N9 Influenza A Viruses from 16 Infected Patients from 2013 to 2015 in Shanghai Reveals Genetic Diversity and Antigenic Drift
P2860
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P2860
Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
description
1991 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի մայիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1991
@ast
im Mai 1991 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1991/05/01)
@sk
vědecký článek publikovaný v roce 1991
@cs
wetenschappelijk artikel (gepubliceerd op 1991/05/01)
@nl
наукова стаття, опублікована в травні 1991
@uk
مقالة علمية (نشرت في مايو 1991)
@ar
name
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@ast
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@en
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@nl
type
label
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@ast
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@en
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@nl
prefLabel
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@ast
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@en
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@nl
P2093
P2860
P1433
P1476
Site-specific mutagenesis iden ...... influenza virus hemagglutinin
@en
P2093
E. Kretzschmar
M. F. Schmidt
P2860
P304
P577
1991-05-01T00:00:00Z