Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity.
about
Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferasesInteraction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2The battle between rotavirus and its host for control of the interferon signaling pathwayRotavirus non-structural proteins: structure and functionCrystallographic and Biochemical Analysis of Rotavirus NSP2 with Nucleotides Reveals a Nucleoside Diphosphate Kinase-Like ActivityCrystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5' GG Sequence for RTPase ActivityCrystallographic Analysis Reveals Octamerization of Viroplasm Matrix Protein P9-1 of Rice Black Streaked Dwarf VirusRotaC: a web-based tool for the complete genome classification of group A rotavirusesMultimerization of hepatitis delta antigen is a critical determinant of RNA binding specificity.Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2.Effect of intragenic rearrangement and changes in the 3' consensus sequence on NSP1 expression and rotavirus replicationRotavirus viroplasm proteins interact with the cellular SUMOylation system: implications for viroplasm-like structure formation.Rotavirus glycoprotein NSP4 is a modulator of viral transcription in the infected cell.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.De novo synthesis of minus strand RNA by the rotavirus RNA polymerase in a cell-free system involves a novel mechanism of initiation.Rice black-streaked dwarf virus P6 self-interacts to form punctate, viroplasm-like structures in the cytoplasm and recruits viroplasm-associated protein P9-1.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.Rotavirus replication: plus-sense templates for double-stranded RNA synthesis are made in viroplasmsCryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication.Electron microscopic analysis of rotavirus assembly-replication intermediates.Histidine triad-like motif of the rotavirus NSP2 octamer mediates both RTPase and NTPase activitiesRotavirus variant replicates efficiently although encoding an aberrant NSP3 that fails to induce nuclear localization of poly(A)-binding proteinAn ATPase activity associated with the rotavirus phosphoprotein NSP5.Viroplasm protein P9-1 of Rice black-streaked dwarf virus preferentially binds to single-stranded RNA in its octamer form, and the central interior structure formed by this octamer constitutes the major RNA binding site.Non-structural protein NSP2 induces heterotypic antibody responses during primary rotavirus infection and reinfection in children.Further characterisation of rotavirus cores: Ss(+)RNAs can be packaged in vitro but packaging lacks sequence specificity.Cell-line-induced mutation of the rotavirus genome alters expression of an IRF3-interacting protein.A cypovirus VP5 displays the RNA chaperone-like activity that destabilizes RNA helices and accelerates strand annealing.Reovirus protein sigmaNS binds in multiple copies to single-stranded RNA and shares properties with single-stranded DNA binding proteins.Rotavirus NSP5: mapping phosphorylation sites and kinase activation and viroplasm localization domains.Rotavirus nonstructural protein NSP5 interacts with major core protein VP2.Mammalian reovirus nonstructural protein microNS forms large inclusions and colocalizes with reovirus microtubule-associated protein micro2 in transfected cellsSequestration of free tubulin molecules by the viral protein NSP2 induces microtubule depolymerization during rotavirus infection.Single-particle detection of transcription following rotavirus entry.Hyperphosphorylation of the rotavirus NSP5 protein is independent of serine 67, [corrected] NSP2, or [corrected] the intrinsic insolubility of NSP5 is regulated by cellular phosphatases.A novel form of rotavirus NSP2 and phosphorylation-dependent NSP2-NSP5 interactions are associated with viroplasm assembly.
P2860
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P2860
Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity.
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Multimers formed by the rotavi ...... oside triphosphatase activity.
@ast
Multimers formed by the rotavi ...... oside triphosphatase activity.
@en
type
label
Multimers formed by the rotavi ...... oside triphosphatase activity.
@ast
Multimers formed by the rotavi ...... oside triphosphatase activity.
@en
prefLabel
Multimers formed by the rotavi ...... oside triphosphatase activity.
@ast
Multimers formed by the rotavi ...... oside triphosphatase activity.
@en
P2093
P2860
P1433
P1476
Multimers formed by the rotavi ...... eoside triphosphatase activity
@en
P2093
J T Patton
Z Taraporewala
P2860
P304
P577
1999-12-01T00:00:00Z