The relevance of salt bridges for the stability of the influenza virus hemagglutinin.
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Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeCrystal structure of unliganded influenza B virus hemagglutinin.Structural Characterization of an Early Fusion Intermediate of Influenza Virus HemagglutininAcid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus PathogenicityStructural basis for the divergent evolution of influenza B virus hemagglutininCrystal Structures of Beta- and Gammaretrovirus Fusion Proteins Reveal a Role for Electrostatic Stapling in Viral EntryStructural Stability of Influenza A(H1N1)pdm09 Virus HemagglutininsConserved Neutralizing Epitope at Globular Head of Hemagglutinin in H3N2 Influenza VirusesFusion of Enveloped Viruses in Endosomes.Raman spectroscopic signatures of echovirus 1 uncoating.Cleavage of hemagglutinin-bearing lentiviral pseudotypes and their use in the study of influenza virus persistenceStructural differences between the avian and human H7N9 hemagglutinin proteins are attributable to modifications in salt bridge formation: a computational study with implications in viral evolution.Critical role of leucine-valine change in distinct low pH requirements for membrane fusion between two related retrovirus envelopes.Electrostatic Architecture of the Infectious Salmon Anemia Virus (ISAV) Core Fusion Protein Illustrates a Carboxyl-Carboxylate pH Sensor.Viral RNA Degradation and Diffusion Act as a Bottleneck for the Influenza A Virus Infection Efficiency.Potential electrostatic interactions in multiple regions affect human metapneumovirus F-mediated membrane fusion.Antiviral activity of stachyflin on influenza A viruses of different hemagglutinin subtypes.Role of electrostatic repulsion in controlling pH-dependent conformational changes of viral fusion proteinspH-Controlled two-step uncoating of influenza virus.Autographa californica multiple nucleopolyhedrovirus GP64 protein: roles of histidine residues in triggering membrane fusion and fusion pore expansion.Structural insights on the potential significance of the twin Asn-residue found at the base of the hemagglutinin 2 stalk in all influenza A H1N1 strains: a computational study with clinical implicationsDynamic changes during acid-induced activation of influenza hemagglutinin.A histidine residue of the influenza virus hemagglutinin controls the pH dependence of the conformational change mediating membrane fusion.Exploring the early stages of the pH-induced conformational change of influenza hemagglutinin.Egg- or cell culture-derived hemagglutinin mutations impair virus stability and antigen content of inactivated influenza vaccines.A 3.0-Angstrom Resolution Cryo-Electron Microscopy Structure and Antigenic Sites of Coxsackievirus A6-Like Particles.Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk.
P2860
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P2860
The relevance of salt bridges for the stability of the influenza virus hemagglutinin.
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
@zh-hans
2007年学术文章
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2007年学术文章
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2007年學術文章
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name
The relevance of salt bridges for the stability of the influenza virus hemagglutinin.
@en
The relevance of salt bridges for the stability of the influenza virus hemagglutinin.
@nl
type
label
The relevance of salt bridges for the stability of the influenza virus hemagglutinin.
@en
The relevance of salt bridges for the stability of the influenza virus hemagglutinin.
@nl
prefLabel
The relevance of salt bridges for the stability of the influenza virus hemagglutinin.
@en
The relevance of salt bridges for the stability of the influenza virus hemagglutinin.
@nl
P2093
P356
P1433
P1476
The relevance of salt bridges for the stability of the influenza virus hemagglutinin
@en
P2093
Andreas Herrmann
Christoph Böttcher
Kai Ludwig
Michael F G Schmidt
P Sivaramakrishna Rachakonda
Qiang Huang
Thomas Korte
P304
P356
10.1096/FJ.06-7052HYP
P407
P50
P577
2007-01-11T00:00:00Z