Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

about

Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2 The formation of viroplasm-like structures by the rotavirus NSP5 protein is calcium regulated and directed by a C-terminal helical domain

P2860

Q24672464-CD769739-3CFC-48D1-B2C4-868D9271AB29 Q36315068-56D5BA49-E9D5-43B4-841F-3D6F8E934F91

P2860

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

Item

http://www.wikidata.org/entity/Q43156418

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

@zh

2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

2006年學術文章

@zh-hant

name

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

@en

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

@nl

type

Item

label

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

@en

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

@nl

prefLabel

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

@en

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

@nl

P1476

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

@en

P2093

Michela Campagna

http://www.w3.org/2001/XMLSchema#string

Oscar R Burrone

http://www.w3.org/2001/XMLSchema#string

P2860

Two non-structural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo

Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2

Phosphorylation generates different forms of rotavirus NSP5

The N- and C-terminal regions of rotavirus NSP5 are the critical determinants for the formation of viroplasm-like structures independent of NSP2

Vaccinia protein kinase 2: a second essential serine/threonine protein kinase encoded by vaccinia virus.

Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation.

The dual-specificity phosphatase encoded by vaccinia virus, VH1, is essential for viral transcription in vivo and in vitro.

Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation.

Analysis of rotavirus nonstructural protein NSP5 phosphorylation.

Rotavirus NSP5: mapping phosphorylation sites and kinase activation and viroplasm localization domains.

P304

8283-4; author reply 8284-5

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1128/JVI.00813-06

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2006-08-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

6913725

http://www.w3.org/2001/XMLSchema#string

P698

16873287

http://www.w3.org/2001/XMLSchema#string

P921

phosphorylation

P932

1563783

http://www.w3.org/2001/XMLSchema#string

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

about

P2860

P2860

Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P932