Identification of VPA0451 as the specific chaperone for the Vibrio parahaemolyticus chromosome 1 type III-secreted effector VPA0450.

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Identification of VPA0451 as the specific chaperone for the Vibrio parahaemolyticus chromosome 1 type III-secreted effector VPA0450.

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http://www.wikidata.org/entity/Q42225106

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2014 nî lūn-bûn

@nan

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

@wuu

2014年论文

@zh

2014年论文

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name

Identification of VPA0451 as t ...... III-secreted effector VPA0450.

@en

Identification of VPA0451 as t ...... III-secreted effector VPA0450.

@nl

type

Item

label

Identification of VPA0451 as t ...... III-secreted effector VPA0450.

@en

Identification of VPA0451 as t ...... III-secreted effector VPA0450.

@nl

prefLabel

Identification of VPA0451 as t ...... III-secreted effector VPA0450.

@en

Identification of VPA0451 as t ...... III-secreted effector VPA0450.

@nl

P1476

Identification of VPA0451 as t ...... III-secreted effector VPA0450.

@en

P2093

Barbara Waddell

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

Carolyn M Southward

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

Neil McKenna

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

Rebekah Devinney

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

P2860

AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling

Expanded roles for multicargo and class 1B effector chaperones in type III secretion

Structural and biochemical characterization of the type III secretion chaperones CesT and SigE

Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion

Mechanism of actin filament nucleation by the bacterial effector VopL

Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation

Structure of the HopA1(21-102)-ShcA Chaperone-Effector Complex of Pseudomonas syringae Reveals Conservation of a Virulence Factor Binding Motif from Animal to Plant Pathogens

Protein structure prediction on the Web: a case study using the Phyre server

Protein delivery into eukaryotic cells by type III secretion machines

Structural and biochemical characterization of SrcA, a multi-cargo type III secretion chaperone in Salmonella required for pathogenic association with a host

P304

141-150

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P31

scholarly article

P356

10.1111/1574-6968.12416

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

P433

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

P478

353

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

P577

2014-03-24T00:00:00Z

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

P5875

260607142

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

P698

24606036

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

P921

molecular chaperones