PpiD is a player in the network of periplasmic chaperones in Escherichia coli. - Wikidata - awgldk - TriplyDB

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

http://www.wikidata.org/entity/Q30156004

about

Environmental Regulation of Yersinia Pathophysiology Mechanism to control the cell lysis and the cell survival strategy in stationary phase under heat stress Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditions The Bam machine: a molecular cooper.Dynamic interaction of the sec translocon with the chaperone PpiD Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.The virulence factor PEB4 (Cj0596) and the periplasmic protein Cj1289 are two structurally related SurA-like chaperones in the human pathogen Campylobacter jejuni NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase.The Periplasmic Chaperone Network of Campylobacter jejuni: Evidence that SalC (Cj1289) and PpiD (Cj0694) Are Involved in Maintaining Outer Membrane Integrity.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Peptidylprolyl cis-trans isomerases of Legionella pneumophila: virulence, moonlighting and novel therapeutic targets.Single-Domain Peptidyl-Prolyl cis/trans Isomerase FkpA from Corynebacterium glutamicum Improves the Biomass Yield at Increased Growth Temperatures.Microbial forensics: predicting phenotypic characteristics and environmental conditions from large-scale gene expression profiles.Rapid label-free quantitative analysis of the E. coli BL21(DE3) inner membrane proteome.Varying dependency of periplasmic peptidylprolyl cis-trans isomerases in promoting Yersinia pseudotuberculosis stress tolerance and pathogenicity.A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.YfgM is an ancillary subunit of the SecYEG translocon in Escherichia coli.Bacterial N-Glycosylation Efficiency Is Dependent on the Structural Context of Target Sequons.Stress responses of Acinetobacter strain Y during phenol degradation.Regulation of Proteolysis in the Gram-Negative Bacterial Envelope.Structural and functional analysis of cyclophilin PpiB mutants supports an in vivo function not limited to prolyl isomerization activity.

P2860

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P2860

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

http://www.wikidata.org/entity/Q30156004

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

@ast

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

@en

type

label

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

@ast

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

@en

prefLabel

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

@ast

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

@en

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P356

1471-2180-10-251

P1433

BMC Microbiology

P1476

PpiD is a player in the network of periplasmic chaperones in Escherichia coli.

@en

P2093

Birgitta Barion

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

Susanne Behrens-Kneip

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

Yvonne Matern

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

P2860

Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins

Structural basis for the regulated protease and chaperone function of DegP

The prolyl isomerase domain of PpiD fromEscherichia colishows a parvulin fold but is devoid of catalytic activity

Clustal W and Clustal X version 2.0

The complete genome sequence of Escherichia coli K-12

How to measure and predict the molar absorption coefficient of a protein

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.

Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili

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1471-2180-10-251

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251

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scholarly article

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10.1186/1471-2180-10-251

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10

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2010-09-29T00:00:00Z

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1020968066

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20920237

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Escherichia coli

molecular chaperones

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2956729

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