Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes.
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Modern analytical ultracentrifugation in protein science: a tutorial reviewInteraction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2Crystallographic and Biochemical Analysis of Rotavirus NSP2 with Nucleotides Reveals a Nucleoside Diphosphate Kinase-Like ActivityRotavirus protein involved in genome replication and packaging exhibits a HIT-like foldCrystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5' GG Sequence for RTPase ActivityStudying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation.Improved measurement of the rotor temperature in analytical ultracentrifugation.Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2.Mechanism of intraparticle synthesis of the rotavirus double-stranded RNA genome.Rotavirus viroplasm proteins interact with the cellular SUMOylation system: implications for viroplasm-like structure formation.Dual selection mechanisms drive efficient single-gene reverse genetics for rotavirusRNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA.Analysis of a temperature-sensitive mutant rotavirus indicates that NSP2 octamers are the functional form of the protein.Rice black-streaked dwarf virus P6 self-interacts to form punctate, viroplasm-like structures in the cytoplasm and recruits viroplasm-associated protein P9-1.Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation.Structure-activity relationships of wheat flavone O-methyltransferase: a homodimer of convenience.Assortment and packaging of the segmented rotavirus genome.Reovirus sigma NS and mu NS proteins form cytoplasmic inclusion structures in the absence of viral infection.Structure-function analysis of rotavirus NSP2 octamer by using a novel complementation system.Tools for the quantitative analysis of sedimentation boundaries detected by fluorescence optical analytical ultracentrifugationHistidine triad-like motif of the rotavirus NSP2 octamer mediates both RTPase and NTPase activitiesA new adaptive grid-size algorithm for the simulation of sedimentation velocity profiles in analytical ultracentrifugationVariable Field Analytical Ultracentrifugation: II. Gravitational Sweep Sedimentation Velocity.Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.Analytical Ultracentrifugation as a Tool for Studying Protein Interactions.Recorded scan times can limit the accuracy of sedimentation coefficients in analytical ultracentrifugation.Infectious bursal disease virus is an icosahedral polyploid dsRNA virusImproving the thermal, radial, and temporal accuracy of the analytical ultracentrifuge through external referencesOn the analysis of sedimentation velocity in the study of protein complexes.Further characterisation of rotavirus cores: Ss(+)RNAs can be packaged in vitro but packaging lacks sequence specificity.Human herpesvirus 7 U21 tetramerizes to associate with class I major histocompatibility complex molecules.Rotavirus NSP5: mapping phosphorylation sites and kinase activation and viroplasm localization domains.Sequestration of free tubulin molecules by the viral protein NSP2 induces microtubule depolymerization during rotavirus infection.Evidence that avian reovirus σNS is an RNA chaperone: implications for genome segment assortment.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.Role of the histidine triad-like motif in nucleotide hydrolysis by the rotavirus RNA-packaging protein NSP2.Differences in the binding capacity of human apolipoprotein E3 and E4 to size-fractionated lipid emulsions.Development of a multipurpose scaffold for the display of peptide loops.Molecular characterization of the porcine group A rotavirus NSP2 and NSP5/6 genes from São Paulo State, Brazil, in 2011/12.
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P2860
Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes.
description
2000 nî lūn-bûn
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2000年の論文
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2000年学术文章
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2000年学术文章
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name
Rotavirus nonstructural protei ...... nduced conformational changes.
@en
Rotavirus nonstructural protei ...... nduced conformational changes.
@nl
type
label
Rotavirus nonstructural protei ...... nduced conformational changes.
@en
Rotavirus nonstructural protei ...... nduced conformational changes.
@nl
prefLabel
Rotavirus nonstructural protei ...... nduced conformational changes.
@en
Rotavirus nonstructural protei ...... nduced conformational changes.
@nl
P2860
P356
P1476
Rotavirus nonstructural protei ...... induced conformational changes
@en
P2093
Taraporewala Z
P2860
P304
P356
10.1074/JBC.M009398200
P407
P577
2000-12-19T00:00:00Z