(Q48216572)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28219929%20AND%20SRC:MED&resulttype=core&format=json

3 April 2020

title

Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28219929%20AND%20SRC:MED&resulttype=core&format=json

3 April 2020

1 reference

2

1 reference

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3 April 2020

Nadinath B Nillegoda

4

1 reference

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3 April 2020

Szymon Ziętkiewicz

6

1 reference

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3 April 2020

Bernd Bukau

7

1 reference

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3 April 2020

Krzysztof Liberek

9

1 reference

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3 April 2020

3

Igor Obuchowski

1 reference

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3 April 2020

8

Axel Mogk

1 reference

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3 April 2020

author name string

Szymon Żwirowski

1

1 reference

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3 April 2020

Artur Piróg

5

1 reference

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3 April 2020

language of work or name

English

0 references

publication date

20 February 2017

1 reference

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3 April 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28219929%20AND%20SRC:MED&resulttype=core&format=json

3 April 2020

volume

36

1 reference

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3 April 2020

issue

6

1 reference

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3 April 2020

page(s)

783-796

1 reference

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describes a project that uses

3 April 2020

ImageQuant

1 reference

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC5350560/fullTextXML

inferred from PubMed Central ID database lookup

ImageJ

1 reference

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC5350560/fullTextXML

inferred from PubMed Central ID database lookup

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A first line of stress defense: small heat shock proteins and their function in protein homeostasis

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23 May 2018

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Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues.

23 May 2018

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An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones

23 May 2018

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23 May 2018

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Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding

23 May 2018

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Alternative bacterial two-component small heat shock protein systems

23 May 2018

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Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach

23 May 2018

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Importance of N- and C-terminal regions of IbpA, Escherichia coli small heat shock protein, for chaperone function and oligomerization

23 May 2018

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Molecular chaperones in protein folding and proteostasis

23 May 2018

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Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation.

23 May 2018

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The heat shock response: life on the verge of death

23 May 2018

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Cellular strategies for controlling protein aggregation

23 May 2018

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The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.

23 May 2018

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23 May 2018

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Quaternary dynamics and plasticity underlie small heat shock protein chaperone function

23 May 2018

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23 May 2018

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Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry

23 May 2018

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Real-time monitoring of protein complexes reveals their quaternary organization and dynamics.

23 May 2018

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Chaperones in control of protein disaggregation

23 May 2018

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Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity

23 May 2018

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23 May 2018

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Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae

23 May 2018

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23 May 2018

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23 May 2018

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

23 May 2018

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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

23 May 2018

1 reference

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

23 May 2018

1 reference

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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

23 May 2018

1 reference

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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

23 May 2018

1 reference

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Kinetics of molecular chaperone action

23 May 2018

1 reference

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Translational control during heat shock

23 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Disruption of the gene for hsp30, an alpha-crystallin-related heat shock protein of Neurospora crassa, causes defects in thermotolerance

23 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis.

23 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

23 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein

23 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation.

23 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction.

23 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70.

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces.

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104.

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state.

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Temperature and concentration-controlled dynamics of rhizobial small heat shock proteins

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock

14 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=5350560

HSP16.6 is involved in the development of thermotolerance and thylakoid stability in the unicellular cyanobacterium, Synechocystis sp. PCC 6803

14 August 2018

1 reference

12 December 2020

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding

1 reference

12 December 2020

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol

1 reference

12 December 2020

Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro

1 reference

12 December 2020

Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

1 reference

12 December 2020

The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

1 reference

12 December 2020

Identifiers

DOI

10.15252/EMBJ.201593378

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28219929%20AND%20SRC:MED&resulttype=core&format=json

3 April 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28219929%20AND%20SRC:MED&resulttype=core&format=json

3 April 2020

1 reference