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Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0061(19970915)13:11<1065::aid-yea159>3.0.co;2-kopenalex-snapshot
Heterologous HIS3 Marker and GFP Reporter Modules for PCR‐Targeting in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1002/j.1460-2075.1993.tb06097.xopenalex-snapshot
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat‐induced protein damage.
inferredcites →https://doi.org/10.1002/yea.1142openalex-snapshot
A versatile toolbox for PCR‐based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
inferredcites →https://doi.org/10.1002/yea.1742openalex-snapshot
Hsp70/Hsp90 co‐chaperones are required for efficient Hsp104‐mediated elimination of the yeast [PSI+] prion but not for prion propagation
inferredcites →https://doi.org/10.1007/s002840010251openalex-snapshot
Guanidine Hydrochloride Inhibits Hsp104 Activity In Vivo: A Possible Explanation for Its Effect in Curing Yeast Prions
inferredcites →https://doi.org/10.1007/s12192-011-0312-4openalex-snapshot
Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities
inferredcites →https://doi.org/10.1016/j.bbamcr.2011.07.014openalex-snapshot
The elusive middle domain of Hsp104 and ClpB: Location and function
inferredcites →https://doi.org/10.1016/j.cell.2004.11.027openalex-snapshot
Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB
inferredcites →https://doi.org/10.1016/j.cell.2009.02.044openalex-snapshot
A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins
inferredcites →https://doi.org/10.1016/j.febslet.2004.11.051openalex-snapshot
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
inferredcites →https://doi.org/10.1016/j.febslet.2009.08.020openalex-snapshot
DnaK‐mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface
inferredcites →https://doi.org/10.1016/j.jmb.2003.12.013openalex-snapshot
A Chaperone Network for the Resolubilization of Protein Aggregates: Direct Interaction of ClpB and DnaK
inferredcites →https://doi.org/10.1016/j.jmb.2009.11.059openalex-snapshot
Synergistic Cooperation between Two ClpB Isoforms in Aggregate Reactivation
inferredcites →https://doi.org/10.1016/j.jmb.2010.07.030openalex-snapshot
The M-Domain Controls Hsp104 Protein Remodeling Activity in an Hsp70/Hsp40-Dependent Manner
inferredcites →https://doi.org/10.1016/j.molcel.2006.05.042openalex-snapshot
Destruction or Potentiation of Different Prions Catalyzed by Similar Hsp104 Remodeling Activities
inferredcites →https://doi.org/10.1016/j.molcel.2006.11.008openalex-snapshot
M Domains Couple the ClpB Threading Motor with the DnaK Chaperone Activity
inferredcites →https://doi.org/10.1016/j.molcel.2008.11.003openalex-snapshot
In Vivo Monitoring of the Prion Replication Cycle Reveals a Critical Role for Sis1 in Delivering Substrates to Hsp104
inferredcites →https://doi.org/10.1016/j.ymeth.2006.04.004openalex-snapshot
Application of photobleaching for measuring diffusion of prion proteins in cytosol of yeast cells
inferredcites →https://doi.org/10.1016/s0014-5793(00)02423-6openalex-snapshot
Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding
inferredcites →https://doi.org/10.1016/s0092-8674(00)81223-4openalex-snapshot
Hsp104, Hsp70, and Hsp40
inferredcites →https://doi.org/10.1016/s1097-2765(02)00499-9openalex-snapshot
Defining a Pathway of Communication from the C-Terminal Peptide Binding Domain to the N-Terminal ATPase Domain in a AAA Protein
inferredcites →https://doi.org/10.1038/76819openalex-snapshot
Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
inferredcites →https://doi.org/10.1038/emboj.2009.412openalex-snapshot
Quantitative and spatio‐temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing
inferredcites →https://doi.org/10.1038/nrg1616openalex-snapshot
Prions as adaptive conduits of memory and inheritance
inferredcites →https://doi.org/10.1038/nsmb1198openalex-snapshot
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity
inferredcites →https://doi.org/10.1038/sj.emboj.7600985openalex-snapshot
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study
inferredcites →https://doi.org/10.1038/sj.emboj.7601811openalex-snapshot
J‐protein co‐chaperone Sis1 required for generation of [RNQ +] seeds necessary for prion propagation
inferredcites →https://doi.org/10.1046/j.1365-2958.2001.02224.xopenalex-snapshot
The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion‐like elements [PSI + ] and [PIN + ]
inferredcites →https://doi.org/10.1046/j.1365-2958.2001.02478.xopenalex-snapshot
The elimination of the yeast [ PSI + ] prion by guanidine hydrochloride is the result of Hsp104 inactivation
inferredcites →https://doi.org/10.1046/j.1365-2958.2002.03257.xopenalex-snapshot
In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures
inferredcites →https://doi.org/10.1073/pnas.0703980104openalex-snapshot
Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system
inferredcites →https://doi.org/10.1073/pnas.0808934105openalex-snapshot
Specificity of the J-protein Sis1 in the propagation of 3 yeast prions
inferredcites →https://doi.org/10.1073/pnas.0811571106openalex-snapshot
The yeast Sup35NM domain propagates as a prion in mammalian cells
inferredcites →https://doi.org/10.1073/pnas.1003895107openalex-snapshot
Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation
inferredcites →https://doi.org/10.1073/pnas.1102828108openalex-snapshot
Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
inferredcites →https://doi.org/10.1073/pnas.96.10.5452openalex-snapshot
Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones
inferredcites →https://doi.org/10.1074/jbc.m111.302869openalex-snapshot
Insight into Molecular Basis of Curing of [PSI+] Prion by Overexpression of 104-kDa Heat Shock Protein (Hsp104)
inferredcites →https://doi.org/10.1074/jbc.m303653200openalex-snapshot
Characterization of a Trap Mutant of the AAA+ Chaperone ClpB
inferredcites →https://doi.org/10.1074/jbc.m307996200openalex-snapshot
Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104
inferredcites →https://doi.org/10.1074/jbc.m312403200openalex-snapshot
The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104
inferredcites →https://doi.org/10.1074/jbc.m402405200openalex-snapshot
Successive and Synergistic Action of the Hsp70 and Hsp100 Chaperones in Protein Disaggregation
inferredcites →https://doi.org/10.1074/jbc.m403777200openalex-snapshot
Evidence for an Unfolding/Threading Mechanism for Protein Disaggregation by Saccharomyces cerevisiae Hsp104
inferredcites →https://doi.org/10.1074/jbc.m408159200openalex-snapshot
Hsp104 Binds to Yeast Sup35 Prion Fiber but Needs Other Factor(s) to Sever It
inferredcites →https://doi.org/10.1074/jbc.m505653200openalex-snapshot
The Amino-terminal Domain of ClpB Supports Binding to Strongly Aggregated Proteins
inferredcites →https://doi.org/10.1074/jbc.m706189200openalex-snapshot
DnaJ Recruits DnaK to Protein Aggregates
inferredcites →https://doi.org/10.1083/jcb.201106037openalex-snapshot
Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1091/mbc.e02-08-0502openalex-snapshot
Dominant Gain-of-Function Mutations in Hsp104p Reveal Crucial Roles for the Middle Region
inferredcites →https://doi.org/10.1091/mbc.e08-01-0078openalex-snapshot
Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition
inferredcites →https://doi.org/10.1091/mbc.e09-11-0927openalex-snapshot
Analyzing the Birth and Propagation of Two Distinct Prions, [PSI+] and [Het-s]y, in Yeast
inferredcites →https://doi.org/10.1093/emboj/20.10.2435openalex-snapshot
The role of Sis1 in the maintenance of the [RNQ+] prion
inferredcites →https://doi.org/10.1093/genetics/147.2.507openalex-snapshot
Genetic and Environmental Factors Affecting the de novo Appearance of the [PSI + ] Prion in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1098/rstb.1993.0026openalex-snapshot
The role of heat-shock proteins in thermotolerance
inferredcites →https://doi.org/10.1107/s1744309110004409openalex-snapshot
Crystallization and preliminary X-ray crystallographic analysis of a GroEL1 fragment fromMycobacterium tuberculosisH37Rv
inferredcites →https://doi.org/10.1111/j.1365-2443.2006.01004.xopenalex-snapshot
Dynamics of yeast prion aggregates in single living cells
inferredcites →https://doi.org/10.1111/j.1365-2443.2009.01333.xopenalex-snapshot
Single mother–daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine‐HCl‐treated [PSI+] cells
inferredcites →https://doi.org/10.1111/j.1365-2958.2008.06135.xopenalex-snapshot
Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
inferredcites →https://doi.org/10.1126/science.1098007openalex-snapshot
Hsp104 Catalyzes Formation and Elimination of Self-Replicating Sup35 Prion Conformers
inferredcites →https://doi.org/10.1126/science.2188365openalex-snapshot
HSP104 Required for Induced Thermotolerance
inferredcites →https://doi.org/10.1126/science.273.5275.622openalex-snapshot
Support for the Prion Hypothesis for Inheritance of a Phenotypic Trait in Yeast
inferredcites →https://doi.org/10.1126/science.7754373openalex-snapshot
Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-Like Factor [ psi + ]
inferredcites →https://doi.org/10.1128/jb.172.12.7157-7166.1990openalex-snapshot
Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation
inferredcites →https://doi.org/10.1128/jb.173.14.4254-4262.1991openalex-snapshot
ClpB is the Escherichia coli heat shock protein F84.1
inferredcites →https://doi.org/10.1128/mcb.01292-09openalex-snapshot
Sti1 Regulation of Hsp70 and Hsp90 Is Critical for Curing of Saccharomyces cerevisiae [ PSI + ] Prions by Hsp104
inferredcites →https://doi.org/10.1128/mcb.16.8.4378openalex-snapshot
Functional Interaction of Cytosolic hsp70 and a DnaJ-Related Protein, Ydj1p, in Protein Translocation In Vivo
inferredcites →https://doi.org/10.1128/mcb.19.2.1325openalex-snapshot
Antagonistic Interactions between Yeast Chaperones Hsp104 and Hsp70 in Prion Curing
inferredcites →https://doi.org/10.1128/mcb.20.23.8916-8922.2000openalex-snapshot
[URE3] Prion Propagation in Saccharomyces cerevisiae : Requirement for Chaperone Hsp104 and Curing by Overexpressed Chaperone Ydj1p
inferredcites →https://doi.org/10.1128/mcb.26.2.617-629.2006openalex-snapshot
Modulation of Prion Formation, Aggregation, and Toxicity by the Actin Cytoskeleton in Yeast
inferredcites →https://doi.org/10.1371/journal.pbio.0050024openalex-snapshot
Hsp104-Dependent Remodeling of Prion Complexes Mediates Protein-Only Inheritance
inferredcites →https://doi.org/10.1534/genetics.106.056820openalex-snapshot
N-Terminal Domain of Yeast Hsp104 Chaperone Is Dispensable for Thermotolerance and Prion Propagation but Necessary for Curing Prions by Hsp104 Overexpression
inferredcites →https://doi.org/10.2174/092986609788490078openalex-snapshot
Hsp104 and Prion Propagation
inferredcites →https://doi.org/10.4161/pri.1.1.3992openalex-snapshot
Prion Propagation: The Role of Protein Dynamics
inferredcites →https://doi.org/10.4161/pri.3.2.9134openalex-snapshot
Influence of Hsp70s and their regulators on yeast prion propagation
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Role of J-Domain Proteins in Yeast Physiology and Protein Quality Control
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Protein Folding and Chaperones
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Opposing roles of Ubp3‐dependent deubiquitination regulate replicative life span and heat resistance
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An integrative proteome analysis of different seedling organs in tolerant and sensitive wheat cultivars under drought stress and recovery
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The non‐prion SUP35 preexists in large chaperone‐containing molecular complexes
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HSF1 and Its Role in Huntington’s Disease Pathology
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The Chaperone Networks: A Heat Shock Protein (Hsp)70 Perspective
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Structural and Biochemical Properties of Hsp40/Hsp70 Chaperone System
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General Structural and Functional Features of Molecular Chaperones
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The Role of Malaria Parasite Heat Shock Proteins in Protein Trafficking and Remodelling of Red Blood Cells
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Introduction to Yeast and Fungal Prions
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General Structural and Functional Features of Molecular Chaperones
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Proteomic analysis reveals complex metabolic regulation in Saccharomyces cerevisiae cells against multiple inhibitors stress
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Generalizing a mathematical model of prion aggregation allows strain coexistence and co-stability by including a novel misfolded species
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Dual role of ribosome-associated chaperones in prion formation and propagation
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Differential effects of chaperones on yeast prions: CURrent view
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Three J-proteins impact Hsp104-mediated variant-specific prion elimination: a new critical role for a low-complexity domain
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Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip
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Total propagation of yeast prion conformers in ssz1∆ upf1∆ Hsp104T160M triple mutants
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Deciphering the Roles of Trehalose and Hsp104 in the Inhibition of Aggregation of Mutant Huntingtin in a Yeast Model of Huntington’s Disease
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Mahogunin Ring Finger-1 (MGRN1), a Multifaceted Ubiquitin Ligase: Recent Unraveling of Neurobiological Mechanisms
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Heat shock induced stress tolerance in plants: Physiological, biochemical, and molecular mechanisms of acquired tolerance
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Protein Folding | Protein Disaggregases – Molecular Chaperones that Resolubilize Protein Aggregates
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Role of molecular chaperones and co-chaperones in maintaining proteostasis
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Application of yeast to studying amyloid and prion diseases
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Interaction of substrate-mimicking peptides with the AAA+ ATPase ClpB from Escherichia coli
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Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis
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Organelle-Based Aggregation and Retention of Damaged Proteins in Asymmetrically Dividing Cells
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Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system
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Dynamic Prions Revealed by Magic
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Biochemical characterization of ClpB and DnaK from Anaplasma phagocytophilum
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Mechanism of Hsp104/ClpB inhibition by prion curing Guanidinium hydrochloride
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Basic mechanism of the autonomous ClpG disaggregase
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Using reporters of different misfolded proteins reveals differential strategies in processing protein aggregates
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Structural basis of aggregate binding by the AAA+ disaggregase ClpG
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Spatially Organized Aggregation of Misfolded Proteins as Cellular Stress Defense Strategy
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Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions
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Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104
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Crowding Modulates the Conformation, Affinity, and Activity of the Components of the Bacterial Disaggregase Machinery
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Bacterial and Yeast AAA + Disaggregases ClpB and Hsp104 Operate through Conserved Mechanism Involving Cooperation with Hsp70
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Using Single-Molecule Approaches to Understand the Molecular Mechanisms of Heat-Shock Protein Chaperone Function
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Regulation of Human Hsc70 ATPase and Chaperone Activities by Apg2: Role of the Acidic Subdomain
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Selective Hsp70-Dependent Docking of Hsp104 to Protein Aggregates Protects the Cell from the Toxicity of the Disaggregase
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Tah1, A Key Component of R2TP Complex that Regulates Assembly of snoRNP, is Involved in De Novo Generation and Maintenance of Yeast Prion [URE3]
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Role of J-domain Proteins in Yeast Physiology and Protein Quality Control
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Quantitative proteomics of the yeast Hsp70/Hsp90 interactomes during DNA damage reveal chaperone-dependent regulation of ribonucleotide reductase
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The Hsp104 N-Terminal Domain Enables Disaggregase Plasticity and Potentiation
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Human Hsp70 Disaggregase Reverses Parkinson’s-Linked α-Synuclein Amyloid Fibrils
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Cellular Handling of Protein Aggregates by Disaggregation Machines
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Acclimation response and management strategies to combat heat stress in wheat for sustainable agriculture: A state-of-the-art review
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Protein-based inheritance
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Cell Biology of Prions and Prionoids: A Status Report
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Deciphering the Seed Size-Dependent Cellular Internalization Mechanism for α-Synuclein Fibrils
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Biomolecular Assemblies: Moving from Observation to Predictive Design
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Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification
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Phosphoglycerate Kinase Can Adopt Topologically Misfolded Forms That Are More Stable Than Its Native State
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Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
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Protein rescue from aggregates by powerful molecular chaperone machines
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A tightly regulated molecular toggle controls AAA+ disaggregase
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Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
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Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations
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Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis
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Nuclear Hsp104 safeguards the dormant translation machinery during quiescence
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Amyloid conformation-dependent disaggregation in a reconstituted yeast prion system
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Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation
inferred← citeshttps://doi.org/10.1038/s41598-018-24140-5openalex-snapshot
Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate
inferred← citeshttps://doi.org/10.1039/bk9781839165986-00086openalex-snapshot
Solution NMR Studies of Chaperone–Client Systems
inferred← citeshttps://doi.org/10.1042/bcj20170395openalex-snapshot
Human TorsinA can function in the yeast cytosol as a molecular chaperone
inferred← citeshttps://doi.org/10.1042/bsr20171399openalex-snapshot
Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase
inferred← citeshttps://doi.org/10.1042/bst20253077openalex-snapshot
How does protein aggregate structure affect mechanisms of disaggregation?
inferred← citeshttps://doi.org/10.1063/1.4940149openalex-snapshot
Modeling generic aspects of ideal fibril formation
inferred← citeshttps://doi.org/10.1073/pnas.1217988110openalex-snapshot
Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor
inferred← citeshttps://doi.org/10.1073/pnas.1512783112openalex-snapshot
ClpB N-terminal domain plays a regulatory role in protein disaggregation
inferred← citeshttps://doi.org/10.1073/pnas.1601846113openalex-snapshot
Hsp70 biases the folding pathways of client proteins
inferred← citeshttps://doi.org/10.1073/pnas.1704016114openalex-snapshot
Hsp104 disaggregase at normal levels cures many [ PSI + ] prion variants in a process promoted by Sti1p, Hsp90, and Sis1p
inferred← citeshttps://doi.org/10.1073/pnas.1712051115openalex-snapshot
Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria
inferred← citeshttps://doi.org/10.1073/pnas.1715483115openalex-snapshot
Molecular basis for diversification of yeast prion strain conformation
inferred← citeshttps://doi.org/10.1073/pnas.2318162121openalex-snapshot
Exposed Hsp70-binding site impacts yeast Sup35 prion disaggregation and propagation
inferred← citeshttps://doi.org/10.1074/jbc.m112.387589openalex-snapshot
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
inferred← citeshttps://doi.org/10.1074/jbc.m114.620427openalex-snapshot
Single-molecule Analyses of the Dynamics of Heat Shock Protein 104 (Hsp104) and Protein Aggregates
inferred← citeshttps://doi.org/10.1074/jbc.ra118.006186openalex-snapshot
Prion disease is accelerated in mice lacking stress-induced heat shock protein 70 (HSP70)
inferred← citeshttps://doi.org/10.1074/jbc.ra120.015413openalex-snapshot
Repurposing p97 inhibitors for chemical modulation of the bacterial ClpB–DnaK bichaperone system
inferred← citeshttps://doi.org/10.1074/jbc.rev119.006197openalex-snapshot
Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade
inferred← citeshttps://doi.org/10.1080/0035919x.2025.2515392openalex-snapshot
Clearing the protein clutter in human cells: the role of protein disaggregases
inferred← citeshttps://doi.org/10.1080/10985549.2023.2198181openalex-snapshot
Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [PSI+] Curing by Hsp104 Overexpression
inferred← citeshttps://doi.org/10.1080/19336896.2015.1020268openalex-snapshot
Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity
inferred← citeshttps://doi.org/10.1080/19336896.2015.1027856openalex-snapshot
Yeast prions are useful for studying protein chaperones and protein quality control
inferred← citeshttps://doi.org/10.1080/19336896.2017.1328342openalex-snapshot
Prion-based memory of heat stress in yeast
inferred← citeshttps://doi.org/10.1080/19336896.2017.1412911openalex-snapshot
Curing of [PSI+] by Hsp104 Overexpression: Clues to solving the puzzle
inferred← citeshttps://doi.org/10.1080/19336896.2020.1785659openalex-snapshot
Prion domains as a driving force for the assembly of functional nanomaterials
inferred← citeshttps://doi.org/10.1083/jcb.201505104openalex-snapshot
Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery
inferred← citeshttps://doi.org/10.1083/jcb.201709072openalex-snapshot
Pathways of cellular proteostasis in aging and disease
inferred← citeshttps://doi.org/10.1083/jcb.202410205openalex-snapshot
Fine-tuning stress responses by auxiliary feedback loops that sense damage repair
inferred← citeshttps://doi.org/10.1091/mbc.e14-08-1262openalex-snapshot
Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments
inferred← citeshttps://doi.org/10.1091/mbc.e25-01-0027openalex-snapshot
Hsp70 chaperones, Ssa1 and Ssa2, limit poly(A) binding protein aggregation
inferred← citeshttps://doi.org/10.1093/abbs/gmt052openalex-snapshot
Recent progress in prion and prion-like protein aggregation
inferred← citeshttps://doi.org/10.1093/femsyr/foaa025openalex-snapshot
Quantitative assessment of chaperone binding to amyloid aggregates identifies specificity of Hsp40 interaction with yeast prion fibrils
inferred← citeshttps://doi.org/10.1093/genetics/iyab129openalex-snapshot
Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein
inferred← citeshttps://doi.org/10.1093/jxb/erac514openalex-snapshot
Identification of subfunctionalized aggregate-remodeling J-domain proteins in Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1098/rsob.200282openalex-snapshot
Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit
inferred← citeshttps://doi.org/10.1101/2021.12.28.474324openalex-snapshot
Size-dependent secondary nucleation and amplification of α-synuclein amyloid fibrils
inferred← citeshttps://doi.org/10.1101/2022.09.15.508104openalex-snapshot
The control of protein arginine phosphorylation facilitates proteostasis by an AAA+ chaperone protease system
inferred← citeshttps://doi.org/10.1101/2025.11.08.687377openalex-snapshot
Stress granules and protein aggregates reveal intracellular resource competition
inferred← citeshttps://doi.org/10.1101/cshperspect.a023663openalex-snapshot
Prions, Chaperones, and Proteostasis in Yeast
inferred← citeshttps://doi.org/10.1104/pp.19.00263openalex-snapshot
HSP101 Interacts with the Proteasome and Promotes the Clearance of Ubiquitylated Protein Aggregates
inferred← citeshttps://doi.org/10.1107/s1399004713030629openalex-snapshot
Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor
inferred← citeshttps://doi.org/10.1111/1462-2920.16677openalex-snapshot
When the going gets tough, the tough get going—Novel bacterial AAA + disaggregases provide extreme heat resistance
inferred← citeshttps://doi.org/10.1111/1574-6976.12053openalex-snapshot
Physiological and environmental control of yeast prions
inferred← citeshttps://doi.org/10.1111/gtc.12125openalex-snapshot
Dysregulation of the proteasome increases the toxicity of ALS ‐linked mutant SOD 1
inferred← citeshttps://doi.org/10.1111/mmi.12518openalex-snapshot
Direct assessment in bacteria of prionoid propagation and phenotype selection by Hsp 70 chaperone
inferred← citeshttps://doi.org/10.1111/mmi.12725openalex-snapshot
Structural variants of yeast prions show conformer‐specific requirements for chaperone activity
inferred← citeshttps://doi.org/10.1111/mmi.12960openalex-snapshot
Feedback control of prion formation and propagation by the ribosome‐associated chaperone complex
inferred← citeshttps://doi.org/10.1111/mmi.13076openalex-snapshot
Swa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [ URE 3‐1]
inferred← citeshttps://doi.org/10.1111/mmi.13617openalex-snapshot
Over‐expression of the molecular chaperone H sp104 in S accharomyces cerevisiae results in the malpartition of [ PSI +] propagons
inferred← citeshttps://doi.org/10.1111/mmi.13697openalex-snapshot
To CURe or not to CURe? Differential effects of the chaperone sorting factor Cur1 on yeast prions are mediated by the chaperone Sis1
inferred← citeshttps://doi.org/10.1111/mmi.13966openalex-snapshot
Variant‐specific and reciprocal Hsp40 functions in Hsp104‐mediated prion elimination
inferred← citeshttps://doi.org/10.1111/mmi.14192openalex-snapshot
Forms and abundance of chaperone proteins influence yeast prion variant competition
inferred← citeshttps://doi.org/10.1111/mmi.14528openalex-snapshot
The actin cytoskeletal network plays a role in yeast prion transmission and contributes to prion stability
inferred← citeshttps://doi.org/10.1111/mmi.14643openalex-snapshot
Mutable yeast prion variants are stabilized by a defective Hsp104 chaperone
inferred← citeshttps://doi.org/10.1128/ec.00300-13openalex-snapshot
Hsp104 Overexpression Cures Saccharomyces cerevisiae [ PSI + ] by Causing Dissolution of the Prion Seeds
inferred← citeshttps://doi.org/10.1128/ec.00301-12openalex-snapshot
Schizosaccharomyces pombe Disaggregation Machinery Chaperones Support Saccharomyces cerevisiae Growth and Prion Propagation
inferred← citeshttps://doi.org/10.1128/mcb.00027-17openalex-snapshot
Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1128/mcb.00118-17openalex-snapshot
RETRACTED ARTICLE: Evidence of a Prion-Like Transmission of p53 Amyloid in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1128/mmbr.00041-14openalex-snapshot
Yeast Prions: Structure, Biology, and Prion-Handling Systems
inferred← citeshttps://doi.org/10.1146/annurev-biophys-111622-091309openalex-snapshot
Mechanisms of Protein Quality Control in the Endoplasmic Reticulum by a Coordinated Hsp40-Hsp70-Hsp90 System
inferred← citeshttps://doi.org/10.1146/annurev-genet-080320-023632openalex-snapshot
Quiescence in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1146/annurev-pharmtox-010617-052745openalex-snapshot
Toward Therapy of Human Prion Diseases
inferred← citeshttps://doi.org/10.1177/10815589251366914openalex-snapshot
Exercise-induced stress pathways: Crosstalk between AMPK, HSPs, and inflammation
inferred← citeshttps://doi.org/10.1186/s42397-025-00223-3openalex-snapshot
Impacts of climate change on cotton production and advancements in genomic approaches for stress resilience enhancement
inferred← citeshttps://doi.org/10.1201/b16586-10openalex-snapshot
Heterologous Gln/Asn-Rich Proteins Impede the Propagation of Yeast Prions by Altering Chaperone Availability
inferred← citeshttps://doi.org/10.1242/jcs.220202openalex-snapshot
Misfolding-prone proteins are reversibly sequestered to an Hsp42-associated granule upon chronological aging
inferred← citeshttps://doi.org/10.1242/jcs.263680openalex-snapshot
Mitochondrial protein aggregates recruit key chaperones and are sequestered in a fission- and fusion-dependent process
inferred← citeshttps://doi.org/10.12688/f1000research.7214.1openalex-snapshot
Molecular chaperones: guardians of the proteome in normal and disease states
inferred← citeshttps://doi.org/10.1371/journal.pgen.1003236openalex-snapshot
Heterologous Gln/Asn-Rich Proteins Impede the Propagation of Yeast Prions by Altering Chaperone Availability
inferred← citeshttps://doi.org/10.1371/journal.pgen.1004510openalex-snapshot
Functional Diversification of Hsp40: Distinct J-Protein Functional Requirements for Two Prions Allow for Chaperone-Dependent Prion Selection
inferred← citeshttps://doi.org/10.1371/journal.pgen.1004814openalex-snapshot
Heterologous Aggregates Promote De Novo Prion Appearance via More than One Mechanism
inferred← citeshttps://doi.org/10.1371/journal.pgen.1006324openalex-snapshot
Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport
inferred← citeshttps://doi.org/10.1371/journal.pgen.1006417openalex-snapshot
Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo
inferred← citeshttps://doi.org/10.1371/journal.pgen.1008951openalex-snapshot
Differential role of cytosolic Hsp70s in longevity assurance and protein quality control
inferred← citeshttps://doi.org/10.1371/journal.pgen.1009539openalex-snapshot
Mapping the degradation pathway of a disease-linked aspartoacylase variant
inferred← citeshttps://doi.org/10.1371/journal.pone.0046458openalex-snapshot
The Effects of Amino Acid Composition of Glutamine-Rich Domains on Amyloid Formation and Fragmentation
inferred← citeshttps://doi.org/10.1371/journal.pone.0052099openalex-snapshot
The Type II Hsp40 Sis1 Cooperates with Hsp70 and the E3 Ligase Ubr1 to Promote Degradation of Terminally Misfolded Cytosolic Protein
inferred← citeshttps://doi.org/10.1371/journal.pone.0062454openalex-snapshot
Aggregate-Reactivation Activity of the Molecular Chaperone ClpB from Ehrlichia chaffeensis
inferred← citeshttps://doi.org/10.1371/journal.pone.0148221openalex-snapshot
The Symbiotic Performance of Chickpea Rhizobia Can Be Improved by Additional Copies of the clpB Chaperone Gene
inferred← citeshttps://doi.org/10.1371/journal.ppat.1006695openalex-snapshot
Chaperone functional specificity promotes yeast prion diversity
inferred← citeshttps://doi.org/10.1515/hsz-2020-0187openalex-snapshot
Hsp70-mediated quality control: should I stay or should I go?
inferred← citeshttps://doi.org/10.15252/embj.201899264openalex-snapshot
Substrate relay in an Hsp70‐cochaperone cascade safeguards tail‐anchored membrane protein targeting
inferred← citeshttps://doi.org/10.1534/genetics.119.302237openalex-snapshot
Role of the Cell Asymmetry Apparatus and Ribosome-Associated Chaperones in the Destabilization of aSaccharomyces cerevisiaePrion by Heat Shock
inferred← citeshttps://doi.org/10.1556/0806.43.2015.040openalex-snapshot
Comparative proteomic analysis of wheat developing grains between Chinese Spring and 1Sl/1B substitution line
inferred← citeshttps://doi.org/10.1590/0001-3765201520140671openalex-snapshot
Disaggregases, molecular chaperones that resolubilize protein aggregates
inferred← citeshttps://doi.org/10.18632/oncotarget.20989openalex-snapshot
Toxoplasma gondii Clp family protein: TgClpB1 plays a crucial role in thermotolerance
inferred← citeshttps://doi.org/10.2144/000114452openalex-snapshot
Characterization of Aggregate Load and Pattern in Living Yeast Cells by Flow Cytometry
inferred← citeshttps://doi.org/10.2174/1389201015666141103021035openalex-snapshot
Yeast Prions Help Identify and Define Chaperone Interaction Networks
inferred← citeshttps://doi.org/10.23860/diss-may-shannon-2018openalex-snapshot
ANALYSIS OF ATP-DEPENDENT CHAPERONE PROTEIN INTERACTIONS WITH MISFOLDED PROTEINS, AMYLOIDS, AND AGGREGATED PROTEINS
inferred← citeshttps://doi.org/10.3389/fgene.2012.00247openalex-snapshot
Aging and the aggregating proteome
inferred← citeshttps://doi.org/10.3389/fmicb.2015.00311openalex-snapshot
Engineered bacterial hydrophobic oligopeptide repeats in a synthetic yeast prion, [REP-PSI+]
inferred← citeshttps://doi.org/10.3389/fmolb.2014.00012openalex-snapshot
Structural mechanisms of chaperone mediated protein disaggregation
inferred← citeshttps://doi.org/10.3389/fmolb.2015.00022openalex-snapshot
Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation
inferred← citeshttps://doi.org/10.3389/fmolb.2015.00057openalex-snapshot
Metazoan Hsp70-based protein disaggregases: emergence and mechanisms
inferred← citeshttps://doi.org/10.3389/fmolb.2017.00006openalex-snapshot
Mutant Analysis Reveals Allosteric Regulation of ClpB Disaggregase
inferred← citeshttps://doi.org/10.3389/fmolb.2017.00044openalex-snapshot
Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis
inferred← citeshttps://doi.org/10.3389/fmolb.2021.681439openalex-snapshot
Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation
inferred← citeshttps://doi.org/10.3389/fmolb.2022.915307openalex-snapshot
The Impact of Hidden Structure on Aggregate Disassembly by Molecular Chaperones
inferred← citeshttps://doi.org/10.3389/fmolb.2024.1392608openalex-snapshot
Unique characteristics of the J-domain proximal regions of Hsp70 cochaperone Apj1 in prion propagation/elimination and its overlap with Sis1 function
inferred← citeshttps://doi.org/10.3389/fnmol.2018.00237openalex-snapshot
The Insoluble Protein Deposit (IPOD) in Yeast
inferred← citeshttps://doi.org/10.3389/fnmol.2022.1050472openalex-snapshot
The yeast molecular chaperone, Hsp104, influences transthyretin aggregate formation
inferred← citeshttps://doi.org/10.3390/agronomy11091825openalex-snapshot
Heat Stress in Cotton: A Review on Predicted and Unpredicted Growth-Yield Anomalies and Mitigating Breeding Strategies
inferred← citeshttps://doi.org/10.3390/biology11091266openalex-snapshot
Anti-Prion Systems Block Prion Transmission, Attenuate Prion Generation, Cure Most Prions as They Arise and Limit Prion-Induced Pathology in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.3390/biom11121884openalex-snapshot
Amyloid Fragmentation and Disaggregation in Yeast and Animals
inferred← citeshttps://doi.org/10.3390/biom9120815openalex-snapshot
ClpG Provides Increased Heat Resistance by Acting as Superior Disaggregase
inferred← citeshttps://doi.org/10.3390/cells10102745openalex-snapshot
Unzipping the Secrets of Amyloid Disassembly by the Human Disaggregase
inferred← citeshttps://doi.org/10.3390/genes17060608openalex-snapshot
Genome-Wide Identification and Expression Analysis of the Soybean GmHSP100 Gene Family in Response to Heat and Salt Stresses
inferred← citeshttps://doi.org/10.3390/ijms19082292openalex-snapshot
Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification
inferred← citeshttps://doi.org/10.3390/ijms20235930openalex-snapshot
Small Molecule Inhibitors Targeting the Heat Shock Protein System of Human Obligate Protozoan Parasites
inferred← citeshttps://doi.org/10.3390/ijms21134742openalex-snapshot
How Do Yeast Cells Contend with Prions?
inferred← citeshttps://doi.org/10.3390/ijms24021170openalex-snapshot
Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond
inferred← citeshttps://doi.org/10.3390/ijms24108660openalex-snapshot
Yeast Chaperone Hsp70-Ssb Modulates a Variety of Protein-Based Heritable Elements
inferred← citeshttps://doi.org/10.3390/ijms241310833openalex-snapshot
Overexpression of Hsp104 by Causing Dissolution of the Prion Seeds Cures the Yeast [PSI+] Prion
inferred← citeshttps://doi.org/10.3390/ijms27177762openalex-snapshot
Comparative Characterization of σ32-Dependent Promoters for the Heat-Inducible Expression of FAST-PETase in Escherichia coli
inferred← citeshttps://doi.org/10.3390/jof8020122openalex-snapshot
Differential Interactions of Molecular Chaperones and Yeast Prions
inferred← citeshttps://doi.org/10.3390/molecules24183388openalex-snapshot
Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery
inferred← citeshttps://doi.org/10.3390/ph15111341openalex-snapshot
Structural Basis of Parasitic HSP90 ATPase Inhibition by Small Molecules
inferred← citeshttps://doi.org/10.3390/v11030238openalex-snapshot
Prion Variants of Yeast are Numerous, Mutable, and Segregate on Growth, Affecting Prion Pathogenesis, Transmission Barriers, and Sensitivity to Anti-Prion Systems
inferred← citeshttps://doi.org/10.3390/v11040349openalex-snapshot
Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast
inferred← citeshttps://doi.org/10.3390/v14081635openalex-snapshot
Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures
inferred← citeshttps://doi.org/10.3390/v14091945openalex-snapshot
Anti-Prion Systems in Saccharomyces cerevisiae Turn an Avalanche of Prions into a Flurry
inferred← citeshttps://doi.org/10.3390/v14102160openalex-snapshot
Hsp40/JDP Requirements for the Propagation of Synthetic Yeast Prions
inferred← citeshttps://doi.org/10.3791/50840openalex-snapshot
Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
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