At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane.
about
Dissecting Virus Infectious Cycles by Cryo-Electron MicroscopyDynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane FusionFusion of Enveloped Viruses in Endosomes.Broad Spectrum Anti-Influenza Agents by Inhibiting Self-Association of Matrix Protein 1.Zernike phase contrast cryo-electron tomography of whole bacterial cells.Visualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.How cells tune viral mechanics--insights from biophysical measurements of influenza virus.It's what's inside that mattersStepwise priming by acidic pH and a high K+ concentration is required for efficient uncoating of influenza A virus cores after penetration.Nothing to sneeze at: a dynamic and integrative computational model of an influenza A virion.Crystal structures of influenza A virus matrix protein M1: variations on a themeInfluenza virus-mediated membrane fusion: Structural insights from electron microscopy.Identification of an HIV-1 Mutation in Spacer Peptide 1 That Stabilizes the Immature CA-SP1 Lattice.pH-Dependent Formation and Disintegration of the Influenza A Virus Protein Scaffold To Provide Tension for Membrane FusionProtein-lipid interactions critical to replication of the influenza A virus.The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.Palmitoylation contributes to membrane curvature in Influenza A virus assembly and hemagglutinin-mediated membrane fusion.Crystal structure of an orthomyxovirus matrix protein reveals mechanisms for self-polymerization and membrane association.Cryomicroscopy provides structural snapshots of influenza virus membrane fusion.Dynamic changes during acid-induced activation of influenza hemagglutinin.Abnormal Morphological Vesicles in Influenza A Virus Exposed to Acid pH.Influenza A matrix protein M1 multimerizes upon binding to lipid membranes.The inhibitory effect of iridoid glycoside extracted from Fructus Gardeniae on intracellular acidification and extracellular Ca2+ influx induced by influenza A virus.Maintaining pH-dependent conformational flexibility of M1 is critical for efficient influenza A virus replication.Influenza virus Matrix Protein M1 preserves its conformation with pH, changing multimerization state at the priming stage due to electrostatics.Characterization of Hemagglutinin Antigens on Influenza Virus and within Vaccines Using Electron Microscopy.
P2860
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P2860
At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane.
description
2013 nî lūn-bûn
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2013 թուականի Մարտին հրատարակուած գիտական յօդուած
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2013 թվականի մարտին հրատարակված գիտական հոդված
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2013年の論文
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2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
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2013年論文
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2013年论文
@wuu
name
At low pH, influenza virus mat ...... issociating from the membrane.
@ast
At low pH, influenza virus mat ...... issociating from the membrane.
@en
At low pH, influenza virus mat ...... issociating from the membrane.
@en-gb
At low pH, influenza virus mat ...... issociating from the membrane.
@nl
type
label
At low pH, influenza virus mat ...... issociating from the membrane.
@ast
At low pH, influenza virus mat ...... issociating from the membrane.
@en
At low pH, influenza virus mat ...... issociating from the membrane.
@en-gb
At low pH, influenza virus mat ...... issociating from the membrane.
@nl
prefLabel
At low pH, influenza virus mat ...... issociating from the membrane.
@ast
At low pH, influenza virus mat ...... issociating from the membrane.
@en
At low pH, influenza virus mat ...... issociating from the membrane.
@en-gb
At low pH, influenza virus mat ...... issociating from the membrane.
@nl
P2860
P356
P1433
P1476
At low pH, influenza virus mat ...... issociating from the membrane.
@en
P2093
Alasdair C Steven
P2860
P304
P356
10.1128/JVI.00276-13
P407
P50
P5530
P577
2013-03-06T00:00:00Z
P6179
1003459056