(Q47332944)

14 January 2018

title

Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones. (English)

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14 January 2018

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Anat Ben-Zvi

1

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14 January 2018

Paolo De Los Rios

series ordinal

2

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14 January 2018

Giovanni Dietler

series ordinal

3

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14 January 2018

Pierre Goloubinoff

series ordinal

4

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14 January 2018

language of work or name

English

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publication date

16 June 2004

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14 January 2018

Journal of Biological Chemistry

published in

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volume

279

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14 January 2018

page(s)

37298-37303

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issue

36

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14 January 2018

Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones

cites work

1 reference

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Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

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Structural analysis of substrate binding by the molecular chaperone DnaK

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Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

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GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

21 January 2018

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Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

21 January 2018

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Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones.

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Chaperone-assisted protein folding.

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The protein import motor of mitochondria

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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

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Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants

21 January 2018

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Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

21 January 2018

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Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

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21 January 2018

Identifiers

DOI

10.1074/JBC.M405627200

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14 January 2018

PubMed ID

15201275

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14 January 2018