Regulation of Yersinia protein kinase A (YpkA) kinase activity by multisite autophosphorylation and identification of an N-terminal substrate-binding domain in YpkA

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Yersinia type III effectors perturb host innate immune responses Mechanisms of Yersinia YopO kinase substrate specificity.Structural insight into effector proteins of Gram-negative bacterial pathogens that modulate the phosphoproteome of their host.Acting on Actin: Rac and Rho Played by Yersinia.

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P2860

Regulation of Yersinia protein kinase A (YpkA) kinase activity by multisite autophosphorylation and identification of an N-terminal substrate-binding domain in YpkA

Item

http://www.wikidata.org/entity/Q41383773

description

2014 nî lūn-bûn

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2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

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2014年论文

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2014年论文

@zh-cn

name

Regulation of Yersinia protein ...... bstrate-binding domain in YpkA

@en

type

Item

label

Regulation of Yersinia protein ...... bstrate-binding domain in YpkA

@en

prefLabel

Regulation of Yersinia protein ...... bstrate-binding domain in YpkA

@en

P1476

Regulation of Yersinia protein ...... bstrate-binding domain in YpkA

@en

P2093

Khavong Pha

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

Lorena Navarro

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

Matthew E Wright

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

Richard A Eigenheer

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

Tasha M Barr

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

P2860

G-protein signaling through tubby proteins

Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry

Post-translational modification of the deubiquitinating enzyme otubain 1 modulates active RhoA levels and susceptibility to Yersinia invasion

The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases

Regulation of G proteins by covalent modification

The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions

A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant

The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane

The C terminus of YopT is crucial for activity and the N terminus is crucial for substrate binding.

Identification of residues in the N-terminal domain of the Yersinia tyrosine phosphatase that are critical for substrate recognition.

P304

26167-26177

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P31

scholarly article

P356

10.1074/JBC.M114.601153

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

P407

English

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

P478

289

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P577

2014-08-01T00:00:00Z

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P5875

264462297

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P698

25086045

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P932

4176208

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

Regulation of Yersinia protein kinase A (YpkA) kinase activity by multisite autophosphorylation and identification of an N-terminal substrate-binding domain in YpkA

about

P2860

P2860

Regulation of Yersinia protein kinase A (YpkA) kinase activity by multisite autophosphorylation and identification of an N-terminal substrate-binding domain in YpkA

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932