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Chaperone machines for protein folding, unfolding and disaggregation
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title
Chaperone machines for protein folding, unfolding and disaggregation
(English)
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main subject
cell biology
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protein folding
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molecular chaperones
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author
Helen Saibil
series ordinal
1
object named as
Helen Saibil
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Crossref
language of work or name
English
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PubMed
publication date
October 2013
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PubMed
published in
Nature Reviews Molecular Cell Biology
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PubMed
volume
14
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PubMed
issue
10
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PubMed
page(s)
630-42
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PubMed
cites work
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Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones
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Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolution
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Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein
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Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
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Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones
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The molecular architecture of the eukaryotic chaperonin TRiC/CCT
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ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin
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Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
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Crystal Structure of Group II Chaperonin in the Open State
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Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine
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Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
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Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1
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Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism
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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
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Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
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The crystal structure of the bacterial chaperonin GroEL at 2.8 A
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Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
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Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
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Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
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Structural basis of the unfolded protein response
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The HSP70 chaperone machinery: J proteins as drivers of functional specificity
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Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.
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Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm
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Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling
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Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex
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Gymnastics of molecular chaperones
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Local and global mobility in the ClpA AAA+ chaperone detected by cryo-electron microscopy: functional connotations
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Mechanisms of the Hsp70 chaperone system
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Multiple states of a nucleotide-bound group 2 chaperonin
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
GroEL stimulates protein folding through forced unfolding
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Topologies of a substrate protein bound to the chaperonin GroEL
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Structure of an Hsp90-Cdc37-Cdk4 complex.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Allosteric regulation of chaperonins.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
GHKL, an emergent ATPase/kinase superfamily
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 September 2017
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
Identification of the Cdc48•20S proteasome as an ancient AAA+ proteolytic machine.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
Molecular model of the human 26S proteasome
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
The role of the N-domain in the ATPase activity of the mammalian AAA ATPase p97/VCP.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
Chaperonin complex with a newly folded protein encapsulated in the folding chamber
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
The flexible attachment of the N-domains to the ClpA ring body allows their use on demand.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
An expanded protein folding cage in the GroEL-gp31 complex
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
31 May 2018
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
19 June 2018
Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
A tightly regulated molecular toggle controls AAA+ disaggregase.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Cooperativity in the thermosome.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
GroEL/GroES-mediated folding of a protein too large to be encapsulated
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4340576
retrieved
28 November 2018
Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNRM3658
retrieved
31 March 2020
Identifiers
DOI
10.1038/NRM3658
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
511885
Dimensions Publication ID
1036091575
0 references
OpenCitations bibliographic resource ID
511885
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
511885
PMC publication ID
4340576
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
511885
PubMed publication ID
24026055
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
511885
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