The Essential Role of ClpXP in Caulobacter crescentus Requires Species Constrained Substrate Specificity.

about

The Essential Role of ClpXP in Caulobacter crescentus Requires Species Constrained Substrate Specificity.

Item

http://www.wikidata.org/entity/Q42283921

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

The Essential Role of ClpXP in ...... trained Substrate Specificity.

@en

The Essential Role of ClpXP in ...... trained Substrate Specificity.

@nl

type

Item

label

The Essential Role of ClpXP in ...... trained Substrate Specificity.

@en

The Essential Role of ClpXP in ...... trained Substrate Specificity.

@nl

prefLabel

The Essential Role of ClpXP in ...... trained Substrate Specificity.

@en

The Essential Role of ClpXP in ...... trained Substrate Specificity.

@nl

P1476

The Essential Role of ClpXP in ...... trained Substrate Specificity.

@en

P2093

Jacob Nascembeni

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

Peter Chien

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

Robert H Vass

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

P2860

The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

Adaptor-Dependent Degradation of a Cell-Cycle Regulator Uses a Unique Substrate Architecture

Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA

An essential protease involved in bacterial cell-cycle control.

Identification and transcriptional control of the genes encoding the Caulobacter crescentus ClpXP protease.

AAA+ proteases: ATP-fueled machines of protein destruction.

ClpXP, an ATP-powered unfolding and protein-degradation machine

C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide.

Cell cycle-dependent adaptor complex for ClpXP-mediated proteolysis directly integrates phosphorylation and second messenger signals

A bacterial toxin inhibits DNA replication elongation through a direct interaction with the β sliding clamp.

P304

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

P31

scholarly article

P356

10.3389/FMOLB.2017.00028

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

P478

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

P577

2017-05-09T00:00:00Z

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

P698

28536693

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

P932

5422525

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