Biophysical characterization of the influence of salt on tetrameric SecB.

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Large-scale evolutionary analyses on SecB subunits of bacterial sec system.

P2860

Q35182130-EE52A812-A298-4DAA-9339-3A4AA27FE46A

P2860

Biophysical characterization of the influence of salt on tetrameric SecB.

Item

http://www.wikidata.org/entity/Q28367695

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2001 nî lūn-bûn

@nan

2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Biophysical characterization of the influence of salt on tetrameric SecB

@nl

Biophysical characterization of the influence of salt on tetrameric SecB.

@ast

Biophysical characterization of the influence of salt on tetrameric SecB.

@en

type

Item

label

Biophysical characterization of the influence of salt on tetrameric SecB

@nl

Biophysical characterization of the influence of salt on tetrameric SecB.

@ast

Biophysical characterization of the influence of salt on tetrameric SecB.

@en

prefLabel

Biophysical characterization of the influence of salt on tetrameric SecB

@nl

Biophysical characterization of the influence of salt on tetrameric SecB.

@ast

Biophysical characterization of the influence of salt on tetrameric SecB.

@en

P1476

Biophysical characterization of the influence of salt on tetrameric SecB.

@en

P2093

Agianian B

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

Dekker C

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Gros P

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

Kroon J

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

Weik M

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

Zaccai G

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de Kruijff B

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P2860

Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques.

Substrate specificity of the SecB chaperone.

Determination of molecular parameters by fitting sedimentation data to finite-element solutions of the Lamm equation.

The Sec system.

Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.

Electrospray mass spectrometric investigation of the chaperone SecB.

The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding.

Molecular chaperones and protein translocation across the Escherichia coli inner membrane.

SecB protein: a cytosolic export factor that associates with nascent exported proteins.

The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein.

P304

455-462

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

P31

scholarly article

P356

10.1016/S0006-3495(01)75713-X

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

P407

English

P433

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

P478

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

P577

2001-07-01T00:00:00Z

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

P698

11423428

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P921

Biofiseg

P932

1301525

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

Biophysical characterization of the influence of salt on tetrameric SecB.

about

P2860

P2860

Biophysical characterization of the influence of salt on tetrameric SecB.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932