(Q43189809)

15 November 2017

title

Nucleotide utilization requirements that render ClpB active as a chaperone (English)

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15 November 2017

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5

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15 November 2017

Urko del Castillo

1

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15 November 2017

José Angel Fernández-Higuero

series ordinal

2

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15 November 2017

Sergio Pérez-Acebrón

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3

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15 November 2017

Fernando Moro

series ordinal

4

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15 November 2017

language of work or name

English

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publication date

19 January 2010

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15 November 2017

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15 November 2017

volume

584

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15 November 2017

issue

5

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15 November 2017

page(s)

929-934

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

15 November 2017

cites work

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Common and specific mechanisms of AAA+ proteins involved in protein quality control

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

The amino-terminal domain of ClpB supports binding to strongly aggregated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Interdomain interaction through helices A and B of DnaK peptide binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

A GrpE mutant containing the NH(2)-terminal "tail" region is able to displace bound polypeptide substrate from DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

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/10.1016%2FJ.FEBSLET.2010.01.029

Synchronized domain-opening motion of GroEL is essential for communication between the two rings.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Salt bridges at the inter-ring interface regulate the thermostat of GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Asymmetric nucleotide transactions of the HslUV protease.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2010.01.029

10.1016/J.FEBSLET.2010.01.029

21 January 2018

Identifiers

DOI

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15 November 2017

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