(Q46905577)

26 December 2017

title

Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate (English)

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26 December 2017

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1

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26 December 2017

author name string

Paolo De Los Rios

series ordinal

2

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26 December 2017

Pierre Goloubinoff

series ordinal

3

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26 December 2017

language of work or name

English

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publication date

12 April 2011

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26 December 2017

published in

Proteins

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26 December 2017

volume

79

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26 December 2017

issue

6

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26 December 2017

page(s)

1991-1998

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26 December 2017

Principles that govern the folding of protein chains

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1 reference

https://api.crossref.org/works/10.1002%2FPROT.23024

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Conformational constraints for amyloid fibrillation: the importance of being unfolded

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

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Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

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Prion-like transmission of protein aggregates in neurodegenerative diseases

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Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

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Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

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

21 January 2018

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The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

21 January 2018

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Macromolecular crowding: obvious but underappreciated

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Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging.

21 January 2018

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Protein folding and misfolding

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Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones

21 January 2018

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The factors governing the thermal stability of frataxin orthologues: how to increase a protein's stability

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Potassium ions and the molecular-chaperone activity of DnaK.

21 January 2018

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The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.

21 January 2018

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Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses

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Osmolyte solutions and protein folding

21 January 2018

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Neurodegenerative disease: amyloid pores from pathogenic mutations.

21 January 2018

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Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils

21 January 2018

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Disaggregating chaperones: an unfolding story.

21 January 2018

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Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection

21 January 2018

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Molecular and biochemical mechanisms associated with dormancy and drought tolerance in the desert legume Retama raetam

21 January 2018

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Mechanistic insight into the role of transition-state stabilization in cyclophilin A.

21 January 2018

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Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

21 January 2018

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Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

21 January 2018

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21 January 2018

Identifiers

DOI

10.1002/PROT.23024

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26 December 2017

PubMed ID

21488102

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26 December 2017