(Q36275416)

13 August 2017

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title

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

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13 August 2017

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5

Bernd Bukau

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13 August 2017

1

Jimena Weibezahn

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13 August 2017

4

Axel Mogk

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13 August 2017

3

Peter Tessarz

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13 August 2017

2

Christian Schlieker

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13 August 2017

publication date

1 August 2005

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13 August 2017

number of pages

6

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based on heuristic

inferred from page(s)

published in

Biological Chemistry

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13 August 2017

volume

386

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13 August 2017

issue

8

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13 August 2017

page(s)

739-744

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

13 August 2017

cites work

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

21 January 2018

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Protein misfolding, evolution and disease

21 January 2018

1 reference

ClpS, a substrate modulator of the ClpAP machine

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

AAA superfamily ATPases: common structure--diverse function

21 January 2018

1 reference

Protein disaggregation mediated by heat-shock protein Hsp104.

21 January 2018

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HSP104 required for induced thermotolerance

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

1 reference

Substrate recognition by the AAA chaperone ClpB.

21 January 2018

1 reference

MecA, an adaptor protein necessary for ClpC chaperone activity

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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Mutational studies on HslU and its docking mode with HslV

21 January 2018

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

21 January 2018

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Characterization of a trap mutant of the AAA chaperone ClpB.

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

1 reference

21 January 2018

Identifiers

DOI

10.1515/BC.2005.086

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13 August 2017

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