Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
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Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2Hyperphosphorylation of the hepatitis C virus NS5A protein requires an active NS3 protease, NS4A, NS4B, and NS5A encoded on the same polyproteinExperimental pathways towards developing a rotavirus reverse genetics system: synthetic full length rotavirus ssRNAs are neither infectious nor translated in permissive cells.Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity.Rotavirus viroplasm proteins interact with the cellular SUMOylation system: implications for viroplasm-like structure formation.RNA-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.Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication.Rotavirus increases levels of lipidated LC3 supporting accumulation of infectious progeny virus without inducing autophagosome formation.The N- and C-terminal regions of rotavirus NSP5 are the critical determinants for the formation of viroplasm-like structures independent of NSP2An Inhibitory Motif on the 5'UTR of Several Rotavirus Genome Segments Affects Protein Expression and Reverse Genetics Strategies.The formation of viroplasm-like structures by the rotavirus NSP5 protein is calcium regulated and directed by a C-terminal helical domainAn ATPase activity associated with the rotavirus phosphoprotein NSP5.Further characterisation of rotavirus cores: Ss(+)RNAs can be packaged in vitro but packaging lacks sequence specificity.Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation.Thiazolides, a new class of antiviral agents effective against rotavirus infection, target viral morphogenesis, inhibiting viroplasm formation.Rotavirus replication requires a functional proteasome for effective assembly of viroplasmsRotavirus NSP5: mapping phosphorylation sites and kinase activation and viroplasm localization domains.Rotavirus nonstructural protein NSP5 interacts with major core protein VP2.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.Rotavirus-induced miR-142-5p elicits proviral milieu by targeting non-canonical transforming growth factor beta signalling and apoptosis in cells.Probing the sites of interactions of rotaviral proteins involved in replication.A novel form of rotavirus NSP2 and phosphorylation-dependent NSP2-NSP5 interactions are associated with viroplasm assembly.Fusion of tags induces spurious phosphorylation of rotavirus NSP5.Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes.Role of the histidine triad-like motif in nucleotide hydrolysis by the rotavirus RNA-packaging protein NSP2.Identification of a small molecule that compromises the structural integrity of viroplasms and rotavirus double-layered particles.Molecular characterization of the porcine group A rotavirus NSP2 and NSP5/6 genes from São Paulo State, Brazil, in 2011/12.Cytoplasmic re-localization and colocalization with viroplasms of host cell proteins, and their role in rotavirus infection.
P2860
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P2860
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին 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
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@ast
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@en
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@nl
type
label
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@ast
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@en
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@nl
prefLabel
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@ast
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@en
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@nl
P2093
P1476
Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
@en
P2093
E Fabbretti
I Afrikanova
M C Miozzo
O R Burrone
P304
P356
10.1099/0022-1317-79-11-2679
P407
P478
79 ( Pt 11)
P577
1998-11-01T00:00:00Z