(Q38141722)

29 August 2017

title

Protein rescue from aggregates by powerful molecular chaperone machines (English)

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29 August 2017

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3

Sue Wickner

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29 August 2017

Shannon M Doyle

1

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29 August 2017

Olivier Genest

series ordinal

2

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29 August 2017

publication date

1 October 2013

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Nature Reviews Molecular Cell Biology

29 August 2017

published in

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29 August 2017

volume

14

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29 August 2017

issue

10

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29 August 2017

page(s)

617-629

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https://scigraph.springernature.com/pub.10.1038/nrm3660

29 August 2017

exact match

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cites work

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Hsp104 and ClpB: protein disaggregating machines

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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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Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation

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Mapping the road to recovery: the ClpB/Hsp104 molecular chaperone.

31 March 2020

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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.

31 March 2020

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

31 March 2020

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Metazoan Hsp70 machines use Hsp110 to power protein disaggregation

31 March 2020

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

31 March 2020

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Chaperone networks in protein disaggregation and prion propagation

31 March 2020

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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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Protein disaggregation mediated by heat-shock protein Hsp104.

31 March 2020

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HSP104 required for induced thermotolerance

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

31 March 2020

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

31 March 2020

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Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation

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Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

31 March 2020

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Stress and prions: lessons from the yeast model

31 March 2020

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Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]

31 March 2020

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Prions as adaptive conduits of memory and inheritance

31 March 2020

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Amyloids and yeast prion biology

31 March 2020

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Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions

31 March 2020

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HSP101: a key component for the acquisition of thermotolerance in plants

31 March 2020

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

31 March 2020

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Mitochondrial protein homeostasis: the cooperative roles of chaperones and proteases

31 March 2020

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Hsp78 chaperone functions in restoration of mitochondrial network following heat stress.

31 March 2020

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Evolutionary relationships and structural mechanisms of AAA+ proteins

31 March 2020

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AAA+ proteins: have engine, will work

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31 March 2020

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Structure and function of the AAA+ nucleotide binding pocket

31 March 2020

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ClpXP, an ATP-powered unfolding and protein-degradation machine

31 March 2020

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A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases

31 March 2020

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The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine

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31 March 2020

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Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone

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Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase.

31 March 2020

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ClpP: a structurally dynamic protease regulated by AAA+ proteins

31 March 2020

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

31 March 2020

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Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB

31 March 2020

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Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency

31 March 2020

1 reference

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation

31 March 2020

1 reference

Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.

31 March 2020

1 reference

Motor mechanism for protein threading through Hsp104.

31 March 2020

1 reference

Disaggregases in 4 dimensions

31 March 2020

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The elusive middle domain of Hsp104 and ClpB: location and function.

31 March 2020

1 reference

Structural Dynamics of the MecA-ClpC Complex: A TYPE II AAA+ PROTEIN UNFOLDING MACHINE

31 March 2020

1 reference

Adaptor protein controlled oligomerization activates the AAA+ protein ClpC

31 March 2020

1 reference

MecA, an adaptor protein necessary for ClpC chaperone activity

31 March 2020

1 reference

Modeling AAA+ ring complexes from monomeric structures.

31 March 2020

1 reference

Structural basis for intersubunit signaling in a protein disaggregating machine

31 March 2020

1 reference

Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus

31 March 2020

1 reference

Control of substrate gating and translocation into ClpP by channel residues and ClpX binding.

31 March 2020

1 reference

Binding of the ClpA unfoldase opens the axial gate of ClpP peptidase

31 March 2020

1 reference

The role of the ClpA chaperone in proteolysis by ClpAP

31 March 2020

1 reference

Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.

31 March 2020

1 reference

Dynamics of substrate denaturation and translocation by the ClpXP degradation machine

31 March 2020

1 reference

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

31 March 2020

1 reference

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

31 March 2020

1 reference

Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation

31 March 2020

1 reference

Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding

31 March 2020

1 reference

Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates

31 March 2020

1 reference

ClpS, a substrate modulator of the ClpAP machine

31 March 2020

1 reference

Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system

31 March 2020

1 reference

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity

31 March 2020

1 reference

From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery

31 March 2020

1 reference

Hsp70 chaperones: cellular functions and molecular mechanism

31 March 2020

1 reference

The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions.

31 March 2020

1 reference

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

31 March 2020

1 reference

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

31 March 2020

1 reference

Mutations in the interdomain linker region of DnaK abolish the chaperone action of the DnaK/DnaJ/GrpE system

31 March 2020

1 reference

An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones

31 March 2020

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Mechanics of Hsp70 chaperones enables differential interaction with client proteins.

31 March 2020

1 reference

Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding

31 March 2020

1 reference

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

31 March 2020

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

31 March 2020

1 reference

GrpE, a nucleotide exchange factor for DnaK.

31 March 2020

1 reference

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

31 March 2020

1 reference

DnaJ recruits DnaK to protein aggregates

31 March 2020

1 reference

Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ protein

31 March 2020

1 reference

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

31 March 2020

1 reference

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

31 March 2020

1 reference

Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients.

31 March 2020

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M domains couple the ClpB threading motor with the DnaK chaperone activity.

31 March 2020

1 reference

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

31 March 2020

1 reference

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

31 March 2020

1 reference

In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104

31 March 2020

1 reference

The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner

31 March 2020

1 reference

A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK.

31 March 2020

1 reference

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

31 March 2020

1 reference

Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor

31 March 2020

1 reference

A tightly regulated molecular toggle controls AAA+ disaggregase.

31 March 2020

1 reference

ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2.

31 March 2020

1 reference

Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB.

31 March 2020

1 reference

A quantitative analysis of the effect of nucleotides and the M domain on the association equilibrium of ClpB

31 March 2020

1 reference

Regulatory circuits of the AAA+ disaggregase Hsp104.

31 March 2020

1 reference

Nucleotide utilization requirements that render ClpB active as a chaperone

31 March 2020

1 reference

Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions

31 March 2020

1 reference

Aggregate reactivation mediated by the Hsp100 chaperones

31 March 2020

1 reference

Remodeling of protein aggregates by Hsp104.

31 March 2020

1 reference

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

31 March 2020

1 reference

Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation.

31 March 2020

1 reference

Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation

31 March 2020

1 reference

DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface

31 March 2020

1 reference

DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine

31 March 2020

1 reference

Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding

31 March 2020

1 reference

Substrate recognition by the AAA+ chaperone ClpB.

31 March 2020

1 reference

Synergistic cooperation between two ClpB isoforms in aggregate reactivation.

31 March 2020

1 reference

Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.

31 March 2020

1 reference

Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments.

31 March 2020

1 reference

The prion hypothesis: from biological anomaly to basic regulatory mechanism

31 March 2020

1 reference

Support for the prion hypothesis for inheritance of a phenotypic trait in yeast

31 March 2020

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Maintenance and inheritance of yeast prions.

31 March 2020

1 reference

31 March 2020

1 reference

The amyloid state of proteins in human diseases

31 March 2020

1 reference

Mechanism of prion propagation: amyloid growth occurs by monomer addition

31 March 2020

1 reference

Is the prion domain of soluble Ure2p unstructured?

31 March 2020

1 reference

Fungal prions: structure, function and propagation.

31 March 2020

1 reference

Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance

31 March 2020

1 reference

Hsp104 and prion propagation

31 March 2020

1 reference

Influence of Hsp70s and their regulators on yeast prion propagation

31 March 2020

1 reference

Hsp70 structure, function, regulation and influence on yeast prions

31 March 2020

1 reference

Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion

31 March 2020

1 reference

Protein-only inheritance in yeast: something to get [PSI+]-ched about

31 March 2020

1 reference

Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).

31 March 2020

1 reference

Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.

31 March 2020

1 reference

A new perspective on Hsp104-mediated propagation and curing of the yeast prion [PSI (+) ].

31 March 2020

1 reference

Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers

31 March 2020

1 reference

Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it.

31 March 2020

1 reference

Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities

31 March 2020

1 reference

Molecular chaperones and the assembly of the prion Ure2p in vitro

31 March 2020

1 reference

Molecular chaperones and the assembly of the prion Sup35p, an in vitro study

31 March 2020

1 reference

The AAA ATPase spastin links microtubule severing to membrane modelling.

31 March 2020

1 reference

Microtubule-severing enzymes at the cutting edge

31 March 2020

1 reference

Microtubule-severing enzymes

31 March 2020

1 reference

A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis

31 March 2020

1 reference

Opposing activities protect against age-onset proteotoxicity

31 March 2020

1 reference

Discovery and characterization of a mammalian amyloid disaggregation activity

31 March 2020

1 reference

Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans

31 March 2020

1 reference

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

31 March 2020

1 reference

Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding

31 March 2020

1 reference

Human and yeast Hsp110 chaperones exhibit functional differences

31 March 2020

1 reference

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

31 March 2020

1 reference

Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.

31 March 2020

1 reference

Structure of the Hsp110:Hsc70 nucleotide exchange machine

31 March 2020

1 reference

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

31 March 2020

1 reference

Hsp104 is required for tolerance to many forms of stress

31 March 2020

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/24061228

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Analysis of the Generation and Segregation of Propagons: Entities That Propagate the [PSI+] Prion in Yeast

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/24061228

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NRM3660

1 reference

Dimensions Publication ID

29 August 2017

1032814185

0 references

1 reference