Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
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How viruses use the endoplasmic reticulum for entry, replication, and assemblyRotavirus non-structural proteins: structure and functionH5N1 virus-like particle vaccine elicits cross-reactive neutralizing antibodies that preferentially bind to the oligomeric form of influenza virus hemagglutinin in humans.Interactions of rotavirus VP4 spike protein with the endosomal protein Rab5 and the prenylated Rab acceptor PRA1.Rotavirus glycoprotein NSP4 is a modulator of viral transcription in the infected cell.Rafts promote assembly and atypical targeting of a nonenveloped virus, rotavirus, in Caco-2 cellsRotavirus NSP4: Cell type-dependent transport kinetics to the exofacial plasma membrane and release from intact infected cellsAssembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins.Cooperative binding of the yeast Spt10p activator to the histone upstream activating sequences is mediated through an N-terminal dimerization domain.The concentration of Ca2+ that solubilizes outer capsid proteins from rotavirus particles is dependent on the strainThe cytoplasmic tail of NSP4, the endoplasmic reticulum-localized non-structural glycoprotein of rotavirus, contains distinct virus binding and coiled coil domainsSpike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner.Calcium depletion blocks the maturation of rotavirus by altering the oligomerization of virus-encoded proteins in the ERRetention by the endoplasmic reticulum of rotavirus VP7 is controlled by three adjacent amino-terminal residues.Transient expression and mutational analysis of the rotavirus intracellular receptor: the C-terminal methionine residue is essential for ligand binding.Rotavirus protein rearrangements in purified membrane-enveloped intermediate particles.Structural insights into the coupling of virion assembly and rotavirus replication.Novel pentameric structure of the diarrhea-inducing region of the rotavirus enterotoxigenic protein NSP4.Probing the structure of rotavirus NSP4: a short sequence at the extreme C terminus mediates binding to the inner capsid particleRotavirus spike protein VP4 is present at the plasma membrane and is associated with microtubules in infected cells.Trypsin cleavage stabilizes the rotavirus VP4 spike.Selective depletion of stored calcium by thapsigargin blocks rotavirus maturation but not the cytopathic effect.Two proline residues are essential in the calcium-binding activity of rotavirus VP7 outer capsid protein.Intracellular manipulation of disulfide bond formation in rotavirus proteins during assembly.Spike protein VP4 assembly with maturing rotavirus requires a postendoplasmic reticulum event in polarized caco-2 cells.N- and C-terminal cooperation in rotavirus enterotoxin: novel mechanism of modulation of the properties of a multifunctional protein by a structurally and functionally overlapping conformational domainConformational Differences Unfold a Wide Range of Enterotoxigenic Abilities Exhibited by rNSP4 Peptides from Different Rotavirus Strains.Rotavirus gene silencing by small interfering RNAs.Silencing the morphogenesis of rotavirus.
P2860
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P2860
Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
@ast
Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
@en
type
label
Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
@ast
Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
@en
prefLabel
Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
@ast
Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
@en
P2860
P1433
P1476
Rotavirus proteins VP7, NS28, and VP4 form oligomeric structures
@en
P2093
P H Atkinson
P2860
P304
P407
P577
1990-06-01T00:00:00Z