Recombinant VP4 of human rhinovirus induces permeability in model membranes.
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Viral entry pathways: the example of common cold virusesInsights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsidA sensor-adaptor mechanism for enterovirus uncoating from structures of EV71Picornavirus uncoating intermediate captured in atomic detailPrinciples of Virus Uncoating: Cues and the Snooker BallCapsid protein VP4 of human rhinovirus induces membrane permeability by the formation of a size-selective multimeric poreCryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism.Immunization of N terminus of enterovirus 71 VP4 elicits cross-protective antibody responses.Picornavirus RNA is protected from cleavage by ribonuclease during virion uncoating and transfer across cellular and model membranesThe Rhinovirus subviral a-particle exposes 3'-terminal sequences of its genomic RNA.Role of a single amino acid substitution of VP3 H142D for increased acid resistance of foot-and-mouth disease virus serotype A.Membrane permeabilization of the African horse sickness virus VP5 protein is mediated by two N-terminal amphipathic α-helices.A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid resistance.A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid lability and confer resistance to acid-dependent uncoating inhibition.The conserved N-terminus of human rhinovirus capsid protein VP4 contains membrane pore-forming activity and is a target for neutralizing antibodies.Toll-like receptor 2-expressing macrophages are required and sufficient for rhinovirus-induced airway inflammation.Picornaviruses.The VP4 peptide of hepatitis A virus ruptures membranes through formation of discrete pores.Low pH-triggered beta-propeller switch of the low-density lipoprotein receptor assists rhinovirus infection.Foot-and-mouth disease virus assembly: processing of recombinant capsid precursor by exogenous protease induces self-assembly of pentamers in vitro in a myristoylation-dependent manner.Liposomal nanocontainers as models for viral infection: monitoring viral genomic RNA transfer through lipid membranes.
P2860
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P2860
Recombinant VP4 of human rhinovirus induces permeability in model membranes.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
Recombinant VP4 of human rhinovirus induces permeability in model membranes.
@en
Recombinant VP4 of human rhinovirus induces permeability in model membranes.
@nl
type
label
Recombinant VP4 of human rhinovirus induces permeability in model membranes.
@en
Recombinant VP4 of human rhinovirus induces permeability in model membranes.
@nl
prefLabel
Recombinant VP4 of human rhinovirus induces permeability in model membranes.
@en
Recombinant VP4 of human rhinovirus induces permeability in model membranes.
@nl
P2093
P2860
P356
P1433
P1476
Recombinant VP4 of human rhinovirus induces permeability in model membranes.
@en
P2093
Graham Bottley
Lucy P Beales
Matthew P Davis
Richard A Killington
Tobias J Tuthill
P2860
P304
P356
10.1128/JVI.01070-07
P407
P577
2008-02-06T00:00:00Z