The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state (Q27642377)

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Mathew E Sowa

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Yo-hei Watanabe

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Paul B Sigler

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Masasuke Yoshida

6

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Francis T F Tsai

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

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language of work or name

English

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publication date

17 October 2003

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published in

Cell

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volume

115

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issue

2

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page(s)

229-40

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cites work

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

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At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease

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Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein

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The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.

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

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ClpS, a substrate modulator of the ClpAP machine

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

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

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Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease

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Translocation pathway of protein substrates in ClpAP protease.

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Bridging the information gap: computational tools for intermediate resolution structure interpretation

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Dynamics of substrate denaturation and translocation by the ClpXP degradation machine

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Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli

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Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

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

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Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP.

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X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil

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Lon and Clp family proteases and chaperones share homologous substrate-recognition domains

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34 Preparation and properties of complex V

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Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

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

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ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

14567920

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Consolidated OpenCitations Corpus – April 2017