Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding (Q43218186)

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scientific article published on 19 October 2008

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English	Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding	scientific article published on 19 October 2008

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scholarly article

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

title

Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding (English)

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

author name string

Andreas Martin

series ordinal

1

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

Tania A Baker

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2

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

Robert T Sauer

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3

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

publication date

19 October 2008

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

published in

Nature Structural & Molecular Biology

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

volume

15

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

issue

11

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

page(s)

1147-1151

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Europe PubMed Central

PMC publication ID

2610342

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16 November 2017

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Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing

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

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

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AAA+ superfamily ATPases: common structure--diverse function

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

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Mutational studies on HslU and its docking mode with HslV

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Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

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The structures of HsIU and the ATP-dependent protease HsIU-HsIV

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AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

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Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates

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Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates.

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Protein unfolding by a AAA+ protease is dependent on ATP-hydrolysis rates and substrate energy landscapes.

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15 August 2018

Characterization of mutants of the Escherichia coli AAA protease, FtsH, carrying a mutation in the central pore region.

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15 August 2018

Substrate specific consequences of central pore mutations in the i-AAA protease Yme1 on substrate engagement

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15 August 2018

Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines

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15 August 2018

Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation

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15 August 2018

Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine.

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Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase

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15 August 2018

Substrate recognition by the AAA+ chaperone ClpB.

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15 August 2018

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

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15 August 2018

Communication between ClpX and ClpP during substrate processing and degradation

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PubMed Central

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15 August 2018

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

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15 August 2018

Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.

1 reference

stated in

PubMed Central

reference URL

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retrieved

15 August 2018

Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing.

1 reference

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PubMed Central

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retrieved

15 August 2018

Identifiers

DOI

10.1038/NSMB.1503

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Europe PubMed Central

PMC publication ID

2610342

retrieved

16 November 2017

Dimensions Publication ID

1003614969

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PMC publication ID

2610342

1 reference

stated in

Europe PubMed Central

PMC publication ID

2610342

retrieved

16 November 2017

PubMed publication ID

18931677

1 reference

stated in

Europe PubMed Central

PMC publication ID

2610342

retrieved

16 November 2017

ResearchGate publication ID

23395268

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