Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.

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What macromolecular crowding can do to a protein Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA.Protein folding in the cell envelope of Escherichia coli.A Fatal Case of Necrotizing Fasciitis Caused by a Highly Virulent Escherichia coli Strain

P2860

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P2860

Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.

Item

http://www.wikidata.org/entity/Q41583523

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.

@en

type

Item

label

Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.

@en

prefLabel

Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.

@en

P1476

Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.

@en

P2093

Cui Ye

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

Meng Zhong

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

Qian Chai

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

Yinan Wei

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

P2860

Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site

Macromolecular crowding increases binding of DNA polymerase to DNA: an adaptive effect

Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences

High-resolution structure of the OmpA membrane domain

Structure of outer membrane protein A transmembrane domain by NMR spectroscopy

Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding

Effects of macromolecular crowding on protein conformational changes

The Bam machine: a molecular cooper.

The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel.

The transition state for folding of an outer membrane protein.

P304

239-245

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

P31

scholarly article

P356

10.1002/PRO.2205

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

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

P478

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

P577

2012-12-29T00:00:00Z

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

P698

23225740

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

P921

refolding

P932

3588920

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

Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.

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P2860

P2860

Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P921

P932