(Q46874460)

26 December 2017

title

Direct observation of chaperone-induced changes in a protein folding pathway (English)

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26 December 2017

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5

Nico Nouwen

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26 December 2017

author name string

Philipp Bechtluft

1

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26 December 2017

Ruud G H van Leeuwen

2

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26 December 2017

Matthew Tyreman

3

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26 December 2017

Danuta Tomkiewicz

4

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26 December 2017

Harald L Tepper

6

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26 December 2017

Arnold J M Driessen

7

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26 December 2017

Sander J Tans

8

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26 December 2017

language of work or name

English

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publication date

1 November 2007

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26 December 2017

published in

Science

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26 December 2017

volume

318

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26 December 2017

issue

5855

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26 December 2017

page(s)

1458-1461

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26 December 2017

Molecular chaperones in the cytosol: from nascent chain to folded protein

cites work

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https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Protein folding and misfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Stretching single molecules into novel conformations using the atomic force microscope.

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Direct observation of the three-state folding of a single protein molecule

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Crystal structure of the bacterial protein export chaperone secB

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Substrate specificity of the SecB chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Correlation between requirement for SecA during export and folding properties of precursor polypeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

X-ray structure of a protein-conducting channel

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Effect of signal peptide on the stability and folding kinetics of maltose binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Protein folding and unfolding at atomic resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

Nucleation mechanisms in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1126%2FSCIENCE.1144972

21 January 2018

Identifiers

DOI

10.1126/SCIENCE.1144972

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26 December 2017

1 reference

26 December 2017