Signaling complexes control the chemotaxis kinase by altering its apparent rate constant of autophosphorylation.

about

Signaling complexes control the chemotaxis kinase by altering its apparent rate constant of autophosphorylation.

Item

http://www.wikidata.org/entity/Q46836261

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Signaling complexes control th ...... nstant of autophosphorylation.

@en

Signaling complexes control th ...... nstant of autophosphorylation.

@nl

type

Item

label

Signaling complexes control th ...... nstant of autophosphorylation.

@en

Signaling complexes control th ...... nstant of autophosphorylation.

@nl

prefLabel

Signaling complexes control th ...... nstant of autophosphorylation.

@en

Signaling complexes control th ...... nstant of autophosphorylation.

@nl

P1476

Signaling complexes control th ...... nstant of autophosphorylation.

@en

P2093

Frederick W Dahlquist

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

Gerald L Hazelbauer

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

Wenlin Pan

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

P2860

Solution Structure of a Complex of the Histidine Autokinase CheA with Its Substrate CheY

CryoEM and computer simulations reveal a novel kinase conformational switch in bacterial chemotaxis signaling

Structure of CheA, a signal-transducing histidine kinase

Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells.

New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography.

The chemoreceptor dimer is the unit of conformational coupling and transmembrane signaling

Comparison in vitro of a high- and a low-abundance chemoreceptor of Escherichia coli: similar kinase activation but different methyl-accepting activities.

Histidine kinases: diversity of domain organization.

Bacterial chemoreceptors: providing enhanced features to two-component signaling.

Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer

P304

1535-1546

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

P31

scholarly article

P356

10.1002/PRO.3179

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

P433

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

P478

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

P577

2017-04-20T00:00:00Z

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

P698

28425142

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

P921

chemotaxis

P932

5521549

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