The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
about
Mechanism for Coordinated RNA Packaging and Genome Replication by Rotavirus Polymerase VP1X-ray Crystal Structure of the Rotavirus Inner Capsid Particle at 3.8 Å ResolutionLocation of the dsRNA-Dependent Polymerase, VP1, in Rotavirus ParticlesThree-dimensional structure of the enveloped bacteriophage phi12: an incomplete T = 13 lattice is superposed on an enclosed T = 1 shell.RNA-binding and capping activities of proteins in rotavirus open coresRotavirus RNA replication requires a single-stranded 3' end for efficient minus-strand synthesis.Rotavirus-like particles: a novel nanocarrier for the gut.Mechanism of intraparticle synthesis of the rotavirus double-stranded RNA genome.Regulation of rotavirus polymerase activity by inner capsid proteins.Rotavirus VP2 core shell regions critical for viral polymerase activation.Assortment and packaging of the segmented rotavirus genome.Interactions among capsid proteins orchestrate rotavirus particle functions.Modeling of the rotavirus group C capsid predicts a surface topology distinct from other rotavirus speciesMolecular characterization of a subgroup specificity associated with the rotavirus inner capsid protein VP2.Rotavirus enterotoxin NSP4 has mucosal adjuvant properties.Group A human rotavirus genomics: evidence that gene constellations are influenced by viral protein interactions.Silencing the alarms: Innate immune antagonism by rotavirus NSP1 and VP3Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation.Identification of rotavirus VP6 residues located at the interface with VP2 that are essential for capsid assembly and transcriptase activity.The hydrophilic amino-terminal arm of reovirus core shell protein lambda1 is dispensable for particle assembly.Rotavirus nonstructural protein NSP5 interacts with major core protein VP2.Protein-mediated RNA folding governs sequence-specific interactions between rotavirus genome segmentsA novel form of rotavirus NSP2 and phosphorylation-dependent NSP2-NSP5 interactions are associated with viroplasm assembly.Interaction between a unique minor protein and a major capsid protein of Bluetongue virus controls virus infectivity.Biophysical properties of single rotavirus particles account for the functions of protein shells in a multilayered virus
P2860
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P2860
The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
@ast
The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
@en
type
label
The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
@ast
The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
@en
prefLabel
The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
@ast
The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
@en
P2093
P2860
P1433
P1476
The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3
@en
P2093
P2860
P304
P577
1998-01-01T00:00:00Z