Analysis of the posttranslational modifications of the influenza virus M2 protein.
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The human Kv1.1 channel is palmitoylated, modulating voltage sensing: Identification of a palmitoylation consensus sequence.Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channelCharacterization of the 1918 "Spanish" influenza virus matrix gene segmentInteractome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.Ion channel regulation by protein S-acylation.Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins.Analysis of the pore structure of the influenza A virus M(2) ion channel by the substituted-cysteine accessibility methodEffect of cytoplasmic tail truncations on the activity of the M(2) ion channel of influenza A virus.Influenza virus m2 ion channel protein is necessary for filamentous virion formation.Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientationIon selectivity and activation of the M2 ion channel of influenza virusPalmitoylation of SARS-CoV S protein is necessary for partitioning into detergent-resistant membranes and cell-cell fusion but not interaction with M protein.Activation of the M2 ion channel of influenza virus: a role for the transmembrane domain histidine residueInfluenza a virus M2 ion channel activity is essential for efficient replication in tissue culture.Distinct domains of the influenza a virus M2 protein cytoplasmic tail mediate binding to the M1 protein and facilitate infectious virus productionHow do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles.Characterization of inhibition of M2 ion channel activity by BL-1743, an inhibitor of influenza A virusMapping the phosphoproteome of influenza A and B viruses by mass spectrometry.Importance of conserved cysteine residues in the coronavirus envelope protein.Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayersTyrosine 132 phosphorylation of influenza A virus M1 protein is crucial for virus replication by controlling the nuclear import of M1.The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding.Identification of the functional core of the influenza A virus A/M2 proton-selective ion channelPalmitoylation of the influenza A virus M2 protein is not required for virus replication in vitro but contributes to virus virulence.Ion channel regulation by protein palmitoylation.Influenza A Virus NS1 Protein Promotes Efficient Nuclear Export of Unspliced Viral M1 mRNA.Palmitoylation is required for intracellular trafficking of influenza B virus NB protein and efficient influenza B virus growth in vitro.C-terminal juxtamembrane region of full-length M2 protein forms a membrane surface associated amphipathic helix.Intrinsic cytoskeleton-dependent clustering of influenza virus M2 protein with hemagglutinin assessed by FLIM-FRET.Influenza A Virus M2 Protein: Roles from Ingress to Egress.Ubiquitination of the Cytoplasmic Domain of Influenza A Virus M2 Protein is Crucial for Production of Infectious Virus Particles.
P2860
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P2860
Analysis of the posttranslational modifications of the influenza virus M2 protein.
description
1995 nî lūn-bûn
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1995年の論文
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1995年学术文章
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1995年学术文章
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1995年學術文章
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name
Analysis of the posttranslational modifications of the influenza virus M2 protein.
@ast
Analysis of the posttranslational modifications of the influenza virus M2 protein.
@en
type
label
Analysis of the posttranslational modifications of the influenza virus M2 protein.
@ast
Analysis of the posttranslational modifications of the influenza virus M2 protein.
@en
prefLabel
Analysis of the posttranslational modifications of the influenza virus M2 protein.
@ast
Analysis of the posttranslational modifications of the influenza virus M2 protein.
@en
P2093
P2860
P1433
P1476
Analysis of the posttranslational modifications of the influenza virus M2 protein.
@en
P2093
L J Holsinger
M A Shaughnessy
P2860
P304
P407
P577
1995-02-01T00:00:00Z