The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

about

Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Thermotoga maritima NusG: domain interaction mediates autoinhibition and thermostability.

P2860

Q38600139-53150520-409B-468E-938E-7D6E84F58321 Q41145899-760C9D51-8DB8-4E6E-A0A5-84982BD806E4

P2860

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

Item

http://www.wikidata.org/entity/Q54269439

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年学术文章

@wuu

2015年学术文章

@zh-cn

2015年学术文章

@zh-hans

2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

@zh

2015年學術文章

@zh-hant

name

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

@en

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

@nl

type

Item

label

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

@en

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

@nl

prefLabel

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

@en

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

@nl

P1476

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent

@en

P2093

Anne Richter

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

Birgitta M Wöhrl

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

Kristian Schweimer

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

Martin Strauß

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

Paul Rösch

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

Stephanie Güttler

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

P2860

I-TASSER: a unified platform for automated protein structure and function prediction

PROCHECK: a program to check the stereochemical quality of protein structures

Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities

A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants

Structural Basis for Converting a General Transcription Factor into an Operon-Specific Virulence Regulator

Two Structurally Independent Domains of E. coli NusG Create Regulatory Plasticity via Distinct Interactions with RNA Polymerase and Regulators

A NusE:NusG complex links transcription and translation

An α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation Factor

An Autoinhibited State in the Structure of Thermotoga maritima NusG

Protein secondary structure prediction based on position-specific scoring matrices

P304

352-361

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

P31

scholarly article

P356

10.1080/07391102.2015.1031700

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

P433

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

P478

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

P50

Björn M Burmann

P577

2015-05-01T00:00:00Z

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

P5875

275664856

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

P698

25931133

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

P921

Mycobacterium tuberculosis

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

about

P2860

P2860

The two domains of Mycobacterium tuberculosis NusG protein are dynamically independent.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921