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.
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Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication.The formation of viroplasm-like structures by the rotavirus NSP5 protein is calcium regulated and directed by a C-terminal helical domainAcetylation of Rb by PCAF is required for nuclear localization and keratinocyte differentiation.Fusion of tags induces spurious phosphorylation of rotavirus NSP5.Molecular characterization of the porcine group A rotavirus NSP2 and NSP5/6 genes from São Paulo State, Brazil, in 2011/12.
P2860
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.
description
2006 nî lūn-bûn
@nan
2006年の論文
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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
2006年论文
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2006年论文
@zh-cn
name
Hyperphosphorylation of the ro ...... ated by cellular phosphatases.
@en
type
label
Hyperphosphorylation of the ro ...... ated by cellular phosphatases.
@en
prefLabel
Hyperphosphorylation of the ro ...... ated by cellular phosphatases.
@en
P2093
P2860
P1433
P1476
Hyperphosphorylation of the ro ...... ated by cellular phosphatases.
@en
P2093
Adrish Sen
Darin Agresti
Erich R Mackow
P2860
P304
P356
10.1128/JVI.80.4.1807-1816.2006
P407
P577
2006-02-01T00:00:00Z