(Q36275416)

13 August 2017

1 reference

title

Novel insights into the mechanism of chaperone-assisted protein disaggregation (English)

1 reference

13 August 2017

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5

Bernd Bukau

1 reference

13 August 2017

1

Jimena Weibezahn

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13 August 2017

4

Axel Mogk

1 reference

13 August 2017

3

Peter Tessarz

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13 August 2017

2

Christian Schlieker

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13 August 2017

1 August 2005

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13 August 2017

6

1 reference

based on heuristic

inferred from page(s)

published in

Biological Chemistry

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13 August 2017

386

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13 August 2017

8

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13 August 2017

739-744

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

13 August 2017

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Protein misfolding, evolution and disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

ClpS, a substrate modulator of the ClpAP machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Structure and function of the middle domain of ClpB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

AAA+ superfamily ATPases: common structure--diverse function

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Protein disaggregation mediated by heat-shock protein Hsp104.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

HSP104 required for induced thermotolerance

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Sculpting the proteome with AAA(+) proteases and disassembly machines.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Substrate recognition by the AAA+ chaperone ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

MecA, an adaptor protein necessary for ClpC chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

A link between sequence conservation and domain motion within the AAA+ family.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Mutational studies on HslU and its docking mode with HslV

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Characterization of a trap mutant of the AAA+ chaperone ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Conserved Pore Residues in the AAA Protease FtsH Are Important for Proteolysis and Its Coupling to ATP Hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1515%2FBC.2005.086

21 January 2018

Identifiers

DOI

10.1515/BC.2005.086

1 reference

13 August 2017

1 reference

PubMed ID

16201868