Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
about
Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2Rotavirus non-structural proteins: structure and functionHuman cytomegalovirus UL97 Kinase is required for the normal intranuclear distribution of pp65 and virion morphogenesisBiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion componentMultimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity.RNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA.Sequencing and sequence analysis of VP7 and NSP5 genes reveal emergence of a new genotype of bovine group B rotaviruses in IndiaThe N- and C-terminal regions of rotavirus NSP5 are the critical determinants for the formation of viroplasm-like structures independent of NSP2The 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.Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation.Phosphorylation events during viral infections provide potential therapeutic targets.Analysis of rotavirus nonstructural protein NSP5 phosphorylation.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 cellsHyperphosphorylation of the rotavirus NSP5 protein is independent of serine 67, [corrected] NSP2, or [corrected] the intrinsic insolubility of NSP5 is regulated by cellular phosphatases.Fusion of tags induces spurious phosphorylation of rotavirus NSP5.
P2860
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P2860
Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
@en
Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
@nl
type
label
Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
@en
Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
@nl
prefLabel
Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
@en
Serine protein kinase activity associated with rotavirus phosphoprotein NSP5.
@nl
P2093
P2860
P1433
P1476
Serine protein kinase activity associated with rotavirus phosphoprotein NSP5
@en
P2093
Blackhall J
Magnusson G
P2860
P304
P407
P577
1997-01-01T00:00:00Z