Role of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion Protein
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Crystal structure of glycoprotein C from Rift Valley fever virusEarly Events in Chikungunya Virus Infection-From Virus Cell Binding to Membrane FusionEarly Bunyavirus-Host Cell InteractionsA structural and functional perspective of alphavirus replication and assemblyDealing with low pH: entry and exit of alphaviruses and flavivirusesProtonation of Individual Histidine Residues Is Not Required for the pH-Dependent Entry of West Nile Virus: Evaluation of the "Histidine Switch" HypothesisCrystal Structure of the Marburg Virus GP2 Core Domain in Its Postfusion ConformationCrystal structure of glycoprotein E2 from bovine viral diarrhea virusStudies of the "chain reversal regions" of the avian sarcoma/leukosis virus (ASLV) and ebolavirus fusion proteins: analogous residues are important, and a His residue unique to EnvA affects the pH dependence of ASLV entry.pH-triggered conformational switching of the diphtheria toxin T-domain: the roles of N-terminal histidines.Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion.A histidine-rich linker region in peptidylglycine α-amidating monooxygenase has the properties of a pH sensor.Enhancement of cell membrane invaginations, vesiculation and uptake of macromolecules by protonation of the cell surface.Pseudorevertants of a Semliki forest virus fusion-blocking mutation reveal a critical interchain interaction in the core trimerAlphavirus Entry and Membrane Fusion.The domain I-domain III linker plays an important role in the fusogenic conformational change of the alphavirus membrane fusion proteinResidue-level resolution of alphavirus envelope protein interactions in pH-dependent fusion.The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusionEnergetic Calculations to Decipher pH-Dependent Oligomerization and Domain Swapping of Proteins.Critical role of leucine-valine change in distinct low pH requirements for membrane fusion between two related retrovirus envelopes.Identification of a specific region in the e1 fusion protein involved in zinc inhibition of semliki forest virus fusion.Marburg virus glycoprotein GP2: pH-dependent stability of the ectodomain α-helical bundleAcid-activated structural reorganization of the Rift Valley fever virus Gc fusion protein.A key interaction between the alphavirus envelope proteins responsible for initial dimer dissociation during fusionA tyrosine-to-histidine switch at position 18 of the Ross River virus E2 glycoprotein is a determinant of virus fitness in disparate hostsCross-inhibition of chikungunya virus fusion and infection by alphavirus E1 domain III proteins.Role of electrostatic repulsion in controlling pH-dependent conformational changes of viral fusion proteinsCharacterizing a histidine switch controlling pH-dependent conformational changes of the influenza virus hemagglutininMolecular mechanisms of flavivirus membrane fusion.Structural models of the membrane anchors of envelope glycoproteins E1 and E2 from pestiviruses.Hantavirus Gn and Gc envelope glycoproteins: key structural units for virus cell entry and virus assemblyDesigned protein mimics of the Ebola virus glycoprotein GP2 α-helical bundle: stability and pH effects.Characterization of pH-sensitive molecular switches that trigger the structural transition of vesicular stomatitis virus glycoprotein from the postfusion state toward the prefusion state.Autographa californica multiple nucleopolyhedrovirus GP64 protein: roles of histidine residues in triggering membrane fusion and fusion pore expansion.Localization of a region in the fusion protein of avian metapneumovirus that modulates cell-cell fusionA histidine residue of the influenza virus hemagglutinin controls the pH dependence of the conformational change mediating membrane fusion.Distinct roles in folding, CD81 receptor binding and viral entry for conserved histidine residues of hepatitis C virus glycoprotein E1 and E2.New insights into flavivirus biology: the influence of pH over interactions between prM and E proteins.
P2860
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P2860
Role of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion Protein
description
2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@ast
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@en
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@nl
type
label
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@ast
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@en
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@nl
prefLabel
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@ast
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@en
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@nl
P2860
P3181
P356
P1433
P1476
Role of Conserved Histidine Re ...... ki Forest Virus Fusion Protein
@en
P2093
Zhao-Ling Qin
P2860
P304
P3181
P356
10.1128/JVI.02646-08
P577
2009-05-01T00:00:00Z