(Q44085064)

English

ATP-dependent hexameric assembly of the heat shock protein Hsp101 involves multiple interaction domains and a functional C-proximal nucleotide-binding domain

scientific article published on 31 July 2002

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

ATP-dependent hexameric assembly of the heat shock protein Hsp101 involves multiple interaction domains and a functional C-proximal nucleotide-binding domain (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

author name string

Daniel R Gallie

1

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

David Fortner

2

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

Jamy Peng

3

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

David Puthoff

4

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

language of work or name

0 references

publication date

31 July 2002

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

number of pages

10

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

277

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

42

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

39617-39626

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

Heat-shock proteins as molecular chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Protein quality control: triage by chaperones and proteases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Molecular chaperone functions of heat-shock proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Protein folding in the plant cell

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Protein disaggregation mediated by heat-shock protein Hsp104.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Chaperone rings in protein folding and degradation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

HSP100/Clp proteins: a common mechanism explains diverse functions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

ATP-dependent proteases that also chaperone protein biogenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

The ATPase activity of Hsp104, effects of environmental conditions and mutations.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Subunit interactions influence the biochemical and biological properties of Hsp104

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

The role of the ClpA chaperone in proteolysis by ClpAP

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

ClpB is the Escherichia coli heat shock protein F84.1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Mutational analysis of the two ATP-binding sites in ClpB, a heat shock protein with protein-activated ATPase activity in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

HSP104 required for induced thermotolerance

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

A soybean 101-kD heat shock protein complements a yeast HSP104 deletion mutant in acquiring thermotolerance

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

An Arabidopsis heat shock protein complements a thermotolerance defect in yeast.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Hsp104 is a highly conserved protein with two essential nucleotide-binding sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Developmental and thermal regulation of the maize heat shock protein, HSP101.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Improved method for high efficiency transformation of intact yeast cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

DMSO-enhanced whole cell yeast transformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Isolation and characterization of the 102-kilodalton RNA-binding protein that binds to the 5' and 3' translational enhancers of tobacco mosaic virus RNA.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Mammalian Ras interacts directly with the serine/threonine kinase Raf

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Interactions among the subunits of the G protein involved in Saccharomyces cerevisiae mating.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Nucleotide-dependent oligomerization of ClpB from Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Heat-shock protein 104 expression is sufficient for thermotolerance in yeast

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Characterization of a maize heat-shock protein 101 gene, HSP101, encoding a ClpB/Hsp100 protein homologue

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Predicting coiled coils from protein sequences

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Protein-protein interactions: PDZ domain networks

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Peptide-surface association: the case of PDZ and PTB domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

PDZ domains bind carboxy-terminal sequences of target proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Hsp104 interacts with Hsp90 cochaperones in respiring yeast

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204998200

21 January 2018

Identifiers

10.1074/JBC.M204998200

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 November 2017

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