Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication.
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Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2Rotavirus non-structural proteins: structure and functionX-ray Crystal Structure of the Rotavirus Inner Capsid Particle at 3.8 Å ResolutionCrystallographic 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 VirusActivation of the endoplasmic reticulum calcium sensor STIM1 and store-operated calcium entry by rotavirus requires NSP4 viroporin activity.Modular software platform for low-dose electron microscopy and tomography.Dual selection mechanisms drive efficient single-gene reverse genetics for rotavirusRice 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.Electron microscopic analysis of rotavirus assembly-replication intermediates.Histidine triad-like motif of the rotavirus NSP2 octamer mediates both RTPase and NTPase activitiesGenome heterogeneity of SA11 rotavirus due to reassortment with "O" agentVaccine-derived NSP2 segment in rotaviruses from vaccinated children with gastroenteritis in Nicaragua.Diversity and relationships of cocirculating modern human rotaviruses revealed using large-scale comparative genomicsThe formation of viroplasm-like structures by the rotavirus NSP5 protein is calcium regulated and directed by a C-terminal helical domainAutophagy hijacked through viroporin-activated calcium/calmodulin-dependent kinase kinase-β signaling is required for rotavirus replicationStructural insights into the coupling of virion assembly and rotavirus replication.Life cycle of phytoreoviruses visualized by electron microscopy and tomography.An 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.Lipid droplets form complexes with viroplasms and are crucial for rotavirus replication.Sequestration of free tubulin molecules by the viral protein NSP2 induces microtubule depolymerization during rotavirus infection.Single-particle detection of transcription following rotavirus entry.Probing the sites of interactions of rotaviral proteins involved in replication.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.
P2860
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P2860
Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication.
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Cryoelectron microscopy struct ...... ations for genome replication.
@ast
Cryoelectron microscopy struct ...... ations for genome replication.
@en
type
label
Cryoelectron microscopy struct ...... ations for genome replication.
@ast
Cryoelectron microscopy struct ...... ations for genome replication.
@en
prefLabel
Cryoelectron microscopy struct ...... ations for genome replication.
@ast
Cryoelectron microscopy struct ...... ations for genome replication.
@en
P2093
P2860
P356
P1433
P1476
Cryoelectron microscopy struct ...... cations for genome replication
@en
P2093
Hariharan Jayaram
Mary K Estes
Steven J Ludtke
Xiaofang Jiang
P2860
P304
10829-10835
P356
10.1128/JVI.01347-06
P407
P577
2006-08-23T00:00:00Z