The 2.8 A structure of a T = 4 animal virus and its implications for membrane translocation of RNA.
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Virus assembly and maturation: auto-regulation through allosteric molecular switchesVirus maturationEvolution in Action: N and C Termini of Subunits in Related T = 4 Viruses Exchange Roles as Molecular SwitchesStructural analysis of the Spiroplasma virus, SpV4: implications for evolutionary variation to obtain host diversity among the MicroviridaeProtruding Features of Viral Capsids Are Clustered on Icosahedral Great CirclesSubunits fold at position-dependent rates during maturation of a eukaryotic RNA virus.Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry.Picornavirus uncoatingMulti-disciplinary studies of viruses: the role of structure in shaping the questions and answers.Small compounds targeted to subunit interfaces arrest maturation in a nonenveloped, icosahedral animal virusNear-atomic resolution reconstructions using a mid-range electron microscope operated at 200 kV.Nucleic acid packaging in virusesVirion swelling is not required for cotranslational disassembly of cowpea chlorotic mottle virus in vitro.Dissecting quasi-equivalence in nonenveloped viruses: membrane disruption is promoted by lytic peptides released from subunit pentamers, not hexamers.Virion Structure of Black Queen Cell Virus, a Common Honeybee Pathogen.Confessions of an icosahedral virus crystallographerCharacterization of large conformational changes and autoproteolysis in the maturation of a T=4 virus capsid.Dynamics and stability in maturation of a T=4 virusDynamics in cryo EM reconstructions visualized with maximum-likelihood derived variance maps.Energetics of quasiequivalence: computational analysis of protein-protein interactions in icosahedral viruses.Large-scale, pH-dependent, quaternary structure changes in an RNA virus capsid are reversible in the absence of subunit autoproteolysis.Membrane partitioning of the cleavage peptide in flock house virus.Folding and particle assembly are disrupted by single-point mutations near the autocatalytic cleavage site of Nudaurelia capensis omega virus capsid protein.Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus.Cardiomyopathy syndrome of atlantic salmon (Salmo salar L.) is caused by a double-stranded RNA virus of the Totiviridae family
P2860
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P2860
The 2.8 A structure of a T = 4 animal virus and its implications for membrane translocation of RNA.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
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1996年學術文章
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1996年學術文章
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name
The 2.8 A structure of a T = 4 ...... membrane translocation of RNA.
@en
The 2.8 A structure of a T = 4 ...... membrane translocation of RNA.
@nl
type
label
The 2.8 A structure of a T = 4 ...... membrane translocation of RNA.
@en
The 2.8 A structure of a T = 4 ...... membrane translocation of RNA.
@nl
prefLabel
The 2.8 A structure of a T = 4 ...... membrane translocation of RNA.
@en
The 2.8 A structure of a T = 4 ...... membrane translocation of RNA.
@nl
P2093
P356
P1476
The 2.8 A structure of a T = 4 ...... membrane translocation of RNA
@en
P2093
P356
10.1006/JMBI.1996.0437
P407
P577
1996-08-01T00:00:00Z