(Q37175214)

English

Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.

scientific article published on 04 June 2013

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23737532%20AND%20SRC:MED&resulttype=core&format=json

2 March 2020

Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23737532%20AND%20SRC:MED&resulttype=core&format=json

2 March 2020

molecular chaperones

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Sandeep K Sharma

2

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2 March 2020

4

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2 March 2020

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Rayees U H Mattoo

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2 March 2020

Smriti Priya

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2 March 2020

Pierre Goloubinoff

5

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2 March 2020

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4 June 2013

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2 March 2020

Journal of Biological Chemistry

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2 March 2020

288

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2 March 2020

29

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2 March 2020

21399-21411

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2 March 2020

Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Metazoan Hsp70 machines use Hsp110 to power protein disaggregation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Stable α-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Protein folding on the ribosome

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Structure of the Hsp110:Hsc70 nucleotide exchange machine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Progressive disruption of cellular protein folding in models of polyglutamine diseases.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Hsp70 chaperones: cellular functions and molecular mechanism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Modulation of neurodegeneration by molecular chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

On mechanisms that control heat shock transcription factor activity in metazoan cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Coordinated activation of Hsp70 chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Protein folding and misfolding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Macromolecular crowding: obvious but underappreciated

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

The effect of macromolecular crowding on chaperonin-mediated protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Principles that govern the folding of protein chains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

6 September 2017

Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

27 June 2018

Chaperones: A story of thrift unfolds

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

27 June 2018

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

27 June 2018

Hsp110 protects heat-denatured proteins and confers cellular thermoresistance.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

27 June 2018

Interaction of Hsp70 chaperones with substrates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

27 June 2018

Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Hsp110 is a nucleotide-activated exchange factor for Hsp70.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Tuning of DnaK chaperone action by nonnative protein sensor DnaJ and thermosensor GrpE.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Human and yeast Hsp110 chaperones exhibit functional differences

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Influence of GrpE on DnaK-substrate interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Neurodegenerative disease: amyloid pores from pathogenic mutations

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3774407

3 September 2018

Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M113.479253

21 January 2018

Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/23737532

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein folding: Chaperoning protein evolution

1 reference

https://pubmed.ncbi.nlm.nih.gov/23737532

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Functional characterisation of the chaperones DnaK, DnaJ, and GrpE from Clostridium acetobutylicum

1 reference

https://pubmed.ncbi.nlm.nih.gov/23737532

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/23737532

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M113.479253

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23737532%20AND%20SRC:MED&resulttype=core&format=json

2 March 2020

release_ixcelclu5baorfrrakaqod47zm

1 reference

https://api.fatcat.wiki/v0/release/ixcelclu5baorfrrakaqod47zm

24 November 2022

based on heuristic

mapped directly with Wikidata item

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23737532%20AND%20SRC:MED&resulttype=core&format=json

2 March 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23737532%20AND%20SRC:MED&resulttype=core&format=json

2 March 2020

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