(Q54359354)

28 May 2018

title

Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism. (English)

1 reference

28 May 2018

0 references

1 reference

Si Wu

1

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28 May 2018

Xi Ge

2

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28 May 2018

Zhixin Lv

3

1 reference

28 May 2018

Zeyong Zhi

4

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28 May 2018

Zengyi Chang

5

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28 May 2018

Xin Sheng Zhao

6

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28 May 2018

language of work or name

English

0 references

publication date

1 September 2011

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28 May 2018

published in

Biochemical Journal

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28 May 2018

volume

438

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28 May 2018

issue

3

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28 May 2018

page(s)

505-511

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28 May 2018

Advances in understanding bacterial outer-membrane biogenesis

cites work

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Membrane protein architects: the role of the BAM complex in outer membrane protein assembly.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Secondary and tertiary structure formation of the beta-barrel membrane protein OmpA is synchronized and depends on membrane thickness

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

SurA assists the folding of Escherichia coli outer membrane proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

The Periplasmic Molecular Chaperone Protein SurA Binds a Peptide Motif That Is Characteristic of Integral Outer Membrane Proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Structural basis for the regulated protease and chaperone function of DegP

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Base-by-base dynamics in DNA hybridization probed by fluorescence correlation spectroscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Determination of the fraction and stoichiometry of femtomolar levels of biomolecular complexes in an excess of monomer using single-molecule, two-color coincidence detection

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Structure and function of bacterial outer membrane proteins: barrels in a nutshell

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20110264

21 January 2018

Identifiers

DOI

10.1042/BJ20110264

1 reference

28 May 2018

release_vxcahdwrpbhlzlmjpgrfjtuxva

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/vxcahdwrpbhlzlmjpgrfjtuxva

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference

28 May 2018