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Protein disaggregation mediated by heat-shock protein Hspl04

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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/j.1460-2075.1992.tb05295.xopenalex-snapshot

Hsp104 is required for tolerance to many forms of stress.

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/jcb.240290605openalex-snapshot

Sequence specificity in transcription and translation

inferredcites →https://doi.org/10.1002/yea.320091103openalex-snapshot

Ultrastructural changes in yeast following heat shock and recovery

inferredcites →https://doi.org/10.1016/0003-2697(88)90147-9openalex-snapshot

Current protocols in molecular biology

inferredcites →https://doi.org/10.1016/0076-6879(91)94044-dopenalex-snapshot

[41] Preparation of yeast cells for thin-section electron microscopy

inferredcites →https://doi.org/10.1016/0092-8674(90)90268-jopenalex-snapshot

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

inferredcites →https://doi.org/10.1021/bi00265a025openalex-snapshot

Aggregation equilibria of Escherichia coli RNA polymerase: evidence for anion-linked conformational transitions in the protomers of core and holoenzyme

inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

inferredcites →https://doi.org/10.1038/350165a0openalex-snapshot

Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA

inferredcites →https://doi.org/10.1038/353270a0openalex-snapshot

Hspl04 is a highly conserved protein with two essential nucleotide-binding sites

inferredcites →https://doi.org/10.1038/356683a0openalex-snapshot

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

inferredcites →https://doi.org/10.1073/pnas.86.17.6528openalex-snapshot

Bacterial luciferase alpha beta fusion protein is fully active as a monomer and highly sensitive in vivo to elevated temperature.

inferredcites →https://doi.org/10.1073/pnas.87.9.3513openalex-snapshot

Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes.

inferredcites →https://doi.org/10.1073/pnas.88.18.7903openalex-snapshot

Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin.

inferredcites →https://doi.org/10.1101/gad.6.8.1402openalex-snapshot

The consequences of expressing hsp70 in Drosophila cells at normal temperatures.

inferredcites →https://doi.org/10.1126/science.2188365openalex-snapshot

HSP104 Required for Induced Thermotolerance

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/jb.174.4.1081-1085.1992openalex-snapshot

The Clp proteins: proteolysis regulators or molecular chaperones?

inferredcites →https://doi.org/10.1128/jb.175.20.6484-6491.1993openalex-snapshot

Genetic evidence for a functional relationship between Hsp104 and Hsp70

inferredcites →https://doi.org/10.1128/jb.176.11.3360-3367.1994openalex-snapshot

Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance

inferredcites →https://doi.org/10.1146/annurev.ge.27.120193.002253openalex-snapshot

THE FUNCTION OF HEAT-SHOCK PROTEINS IN STRESS TOLERANCE: DEGRADATION AND REACTIVATION OF DAMAGED PROTEINS

inferredcites →https://doi.org/10.1177/35.3.3546482openalex-snapshot

Immunolocalization of glyceraldehyde-3-phosphate dehydrogenase, hexokinase, and carboxypeptidase Y in yeast cells at the ultrastructural level.

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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The Sequence of 32 kb on the Left Arm of Yeast Chromosome XII Reveals Six Known Genes, a New Member of the Seripauperins Family and a New ABC Transporter Homologous to the Human Multidrug Resistance Protein

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Yeast chaperones and ubiquitin ligases contribute to proteostasis during arsenite stress by preventing or clearing protein aggregates

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Prions as Epigenetic Regulators of Phenotype in Fungi

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Emerging Area: TorsinA, a Novel ATP‐Dependent Factor Linked to Dystonia

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Amyloid Remodeling by Hsp104

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Characterization of ATPase Cycles of Molecular Chaperones by Fluorescence and Transient Kinetic Methods

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Polyglutamine Aggregates as a Model for Protein‐misfolding Diseases

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Conformational stability of the full‐atom hexameric model of the ClpB chaperone from Escherichia coli

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Structure and function of the molecular chaperone Hsp104 from yeast

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Sorghum bicolor S b HSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1 / HSP110 in refolding and disaggregation assays

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Responses of Saccharomyces cerevisiae to thermal stress

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Transient expression of human TorsinA enhances secretion of two functionally distinct proteins in cultured Chinese hamster ovary (CHO) cells

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Degradation of wild‐type alpha‐synuclein by a molecular chaperone leads to reduced aggregate formation

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Yeast Prion‐Protein, Sup35, Fibril Formation Proceeds by Addition and Substraction of Oligomers

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Decoding Skd3 (Human CLPB): A Mitochondrial Protein Disaggregase Critical for Human Health

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How I became a biochemist

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In vivo reactivation of heat‐denatured protein in the endoplasmic reticulum of yeast.

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1995.tb07349.xopenalex-snapshot

Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt‐hsp70.

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Propagation of the yeast prion‐like [psi+] determinant is mediated by oligomerization of the SUP35‐encoded polypeptide chain release factor.

inferred← citeshttps://doi.org/10.1002/j.1460-2075.1996.tb01064.xopenalex-snapshot

Heat shock disassembles the nucleolus and inhibits nuclear protein import and poly(A)+ RNA export.

inferred← citeshttps://doi.org/10.1002/jbt.22344openalex-snapshot

AgsA response to cadmium and copper effects at different temperatures in Escherichia coli

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Genetic and phenotypic characterization of the heat shock response in Pseudomonas putida

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A bipolar functionality of Q/N‐rich proteins: Lsm4 amyloid causes clearance of yeast prions

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Biochemie und Molekulargenetik 1996

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

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Structural mapping of the C lp B ATP ases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design

inferred← citeshttps://doi.org/10.1002/pro.3636openalex-snapshot

Hsp104 facilitates the endoplasmic‐reticulum–associated degradation of disease‐associated and aggregation‐prone substrates

inferred← citeshttps://doi.org/10.1002/pro.4126openalex-snapshot

Drivers of Hsp104 potentiation revealed by scanning mutagenesis of the middle domain

inferred← citeshttps://doi.org/10.1002/yea.888openalex-snapshot

Characterization of a chaperone ClpB homologue ofParacoccidioides brasiliensis

inferred← citeshttps://doi.org/10.1002/yea.985openalex-snapshot

Guanidine reduces stop codon read‐through caused by missense mutations in SUP35 or SUP45

inferred← citeshttps://doi.org/10.1006/abbi.1998.0758openalex-snapshot

Chaperonin Filaments: Their Formation and an Evaluation of Methods for Studying Them

inferred← citeshttps://doi.org/10.1006/anbo.1997.0494openalex-snapshot

Short-term Salinity and High Temperature Stress-associated Ultrastructural Alterations in Young Leaf Cells ofOryza sativaL.

inferred← citeshttps://doi.org/10.1006/bbrc.1997.7339openalex-snapshot

Do Molecular Chaperones Have to Be Proteins?

inferred← citeshttps://doi.org/10.1006/bbrc.1998.9008openalex-snapshot

Hsp104 Responds to Heat and Oxidative Stress with Different Intracellular Localization inSaccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1006/excr.1998.4276openalex-snapshot

Role ofRAS2in Recovery from Chronic Stress: Effect on Yeast Life Span

inferred← citeshttps://doi.org/10.1006/excr.1998.4279openalex-snapshot

Heat Stress-Induced Life Span Extension in Yeast

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Cultured Skin Fibroblasts Isolated from Mice Devoid of the Prion Protein Gene Express Major Heat Shock Proteins in Response to Heat Stress

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Folding pattern of the α-crystallin domain in αA-crystallin determined by site-directed spin labeling

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The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites

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Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein 1 1Edited by M. Yaniv

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Prions of Yeast as Heritable Amyloidoses

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Review: Mechanisms of Disaggregation and Refolding of Stable Protein Aggregates by Molecular Chaperones

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Mechanisms of Active Solubilization of Stable Protein Aggregates by Molecular Chaperones

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Characterization of Interactions Between Misfolding Proteins and Molecular Chaperones by NMR Spectroscopy

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Fungal Prions: Structure, Function and Propagation

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Genetic polymorphism and variation in HSP100 protein and its association with heat tolerance in plants

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Temporary loss of glucocorticoid receptor‐mediated regulation of gene expression in heat‐shocked cells

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HPV 16 E7 oncoprotein induces expression of a 110 kDa heat shock protein

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Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat‐induced protein aggregation

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Understanding and increasing protein stability

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A review of acquired thermotolerance, heat-shock proteins, and molecular chaperones in archaea

inferred← citeshttps://doi.org/10.1016/0168-9525(96)10045-7openalex-snapshot

Maintenance and inheritance of yeast prions

inferred← citeshttps://doi.org/10.1016/0378-1097(96)00204-2openalex-snapshot

Characterization of a barotolerant mutant of the yeast Saccharomyces cerevisiae: importance of trehalose content and membrane fluidity

inferred← citeshttps://doi.org/10.1016/0378-1119(96)00053-4openalex-snapshot

Expression and functional characterisation of the ClpC gene of Mycobacterium leprae: ClpC protein elicits human antibody response

inferred← citeshttps://doi.org/10.1016/0890-6238(95)02001-2openalex-snapshot

Heat shock proteins and teratogenesis

inferred← citeshttps://doi.org/10.1016/b978-0-12-381468-5.00007-5openalex-snapshot

Fermentation

inferred← citeshttps://doi.org/10.1016/b978-0-12-800186-8.00006-7openalex-snapshot

Assembly and Disassembly of Protein Aggregates

inferred← citeshttps://doi.org/10.1016/b978-0-12-803699-0.00020-7openalex-snapshot

Protein Structure and Folding

inferred← citeshttps://doi.org/10.1016/b978-0-12-816118-0.00007-6openalex-snapshot

Fermentation

inferred← citeshttps://doi.org/10.1016/b978-0-12-819460-7.00221-8openalex-snapshot

Protein Folding | Protein Disaggregases – Molecular Chaperones that Resolubilize Protein Aggregates

inferred← citeshttps://doi.org/10.1016/b978-0-12-820780-2.00010-8openalex-snapshot

Genetically Modified Crops and Climate Change Adaptation

inferred← citeshttps://doi.org/10.1016/b978-0-323-95672-7.00017-0openalex-snapshot

Unbiased genome-wide approaches to identify vulnerability factors in Huntington's disease

inferred← citeshttps://doi.org/10.1016/b978-012058785-8/50004-9openalex-snapshot

Posttranslational Modifications

inferred← citeshttps://doi.org/10.1016/b978-012373646-8.50010-xopenalex-snapshot

Fermentation

inferred← citeshttps://doi.org/10.1016/b978-012379062-0/50008-1openalex-snapshot

Fermentation

inferred← citeshttps://doi.org/10.1016/b978-012639011-7/50021-8openalex-snapshot

The Heat Shock Proteins and Hemeoxygenase Response in Central Nervous System Injuries

inferred← citeshttps://doi.org/10.1016/b978-1-4160-5897-7.00076-7openalex-snapshot

Hyperthermia

inferred← citeshttps://doi.org/10.1016/j.abb.2012.01.012openalex-snapshot

Aggregate reactivation mediated by the Hsp100 chaperones

inferred← citeshttps://doi.org/10.1016/j.aspen.2024.102291openalex-snapshot

Identification and expression analysis of four sHsp genes in Sogatella furcifera under abiotic stress

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2006.01.007openalex-snapshot

Hsp78 chaperone functions in restoration of mitochondrial network following heat stress

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2010.02.005openalex-snapshot

Endoplasmic reticulum associated protein degradation: A chaperone assisted journey to hell

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.06.014openalex-snapshot

Structure and function of the AAA+ nucleotide binding pocket

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.07.014openalex-snapshot

The elusive middle domain of Hsp104 and ClpB: Location and function

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.06.031openalex-snapshot

Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system

inferred← citeshttps://doi.org/10.1016/j.bbrc.2005.04.052openalex-snapshot

In vivo induced clpB1 gene of Vibrio cholerae is involved in different stress responses and affects in vivo cholera toxin production

inferred← citeshttps://doi.org/10.1016/j.bbrc.2013.08.064openalex-snapshot

Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum

inferred← citeshttps://doi.org/10.1016/j.bbrc.2013.10.147openalex-snapshot

The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy

inferred← citeshttps://doi.org/10.1016/j.bpj.2019.03.007openalex-snapshot

AAA+ Protein-Based Technologies to Counter Neurodegenerative Disease

inferred← citeshttps://doi.org/10.1016/j.bpj.2019.03.035openalex-snapshot

Hsp104 and Potentiated Variants Can Operate as Distinct Nonprocessive Translocases

inferred← citeshttps://doi.org/10.1016/j.ceb.2016.03.002openalex-snapshot

Protein quality control in the nucleus

inferred← citeshttps://doi.org/10.1016/j.cell.2004.11.018openalex-snapshot

Chaperoned Protein Disaggregation—The ClpB Ring Uses Its Central Channel

inferred← citeshttps://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

inferred← citeshttps://doi.org/10.1016/j.cell.2005.01.016openalex-snapshot

Degradation-Mediated Protein Quality Control in the Nucleus

inferred← citeshttps://doi.org/10.1016/j.cell.2011.11.002openalex-snapshot

Motility and Segregation of Hsp104-Associated Protein Aggregates in Budding Yeast

inferred← citeshttps://doi.org/10.1016/j.cell.2012.09.038openalex-snapshot

Operational Plasticity Enables Hsp104 to Disaggregate Diverse Amyloid and Nonamyloid Clients

inferred← citeshttps://doi.org/10.1016/j.cell.2015.08.041openalex-snapshot

Reversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat Stress

inferred← citeshttps://doi.org/10.1016/j.celrep.2014.12.006openalex-snapshot

Dicer and Hsp104 Function in a Negative Feedback Loop to Confer Robustness to Environmental Stress

inferred← citeshttps://doi.org/10.1016/j.celrep.2019.07.069openalex-snapshot

Mining Disaggregase Sequence Space to Safely Counter TDP-43, FUS, and α-Synuclein Proteotoxicity

inferred← citeshttps://doi.org/10.1016/j.celrep.2020.107680openalex-snapshot

Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions

inferred← citeshttps://doi.org/10.1016/j.celrep.2020.108377openalex-snapshot

Acute Heat Stress Leads to Reversible Aggregation of Nuclear Proteins into Nucleolar Rings in Fission Yeast

inferred← citeshttps://doi.org/10.1016/j.csbj.2022.08.033openalex-snapshot

Quality control of cytoplasmic proteins inside the nucleus

inferred← citeshttps://doi.org/10.1016/j.cub.2003.12.051openalex-snapshot

Molecular Chaperones: Structure of a Protein Disaggregase

inferred← citeshttps://doi.org/10.1016/j.cub.2008.09.003openalex-snapshot

Social Evolution: This Microbe Will Self-Destruct

inferred← citeshttps://doi.org/10.1016/j.cub.2008.09.036openalex-snapshot

Protein Quality Control: On IPODs and Other JUNQ

inferred← citeshttps://doi.org/10.1016/j.devcel.2015.04.015openalex-snapshot

Lipid Droplets Are Essential for Efficient Clearance of Cytosolic Inclusion Bodies

inferred← citeshttps://doi.org/10.1016/j.devcel.2017.12.020openalex-snapshot

A Futile Battle? Protein Quality Control and the Stress of Aging

inferred← citeshttps://doi.org/10.1016/j.ejmech.2016.02.065openalex-snapshot

Structure of amyloid oligomers and their mechanisms of toxicities: Targeting amyloid oligomers using novel therapeutic approaches

inferred← citeshttps://doi.org/10.1016/j.enzmictec.2023.110367openalex-snapshot

Improved titer and stability of selenium nanoparticles produced by engineered Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1016/j.febslet.2005.06.054openalex-snapshot

Coordinated synthesis of the two ClpB isoforms improves the ability of Escherichia coli to survive thermal stress

inferred← citeshttps://doi.org/10.1016/j.febslet.2007.09.010openalex-snapshot

Four members of the HSP101 gene family are differently regulated in Triticum durum Desf

inferred← citeshttps://doi.org/10.1016/j.febslet.2015.07.040openalex-snapshot

Functionality of Class A and Class B J‐protein co‐chaperones with Hsp70

inferred← citeshttps://doi.org/10.1016/j.fgb.2006.06.006openalex-snapshot

Prion proteins as genetic material in fungi

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2014.08.012openalex-snapshot

Regulation of protein turnover by heat shock proteins

inferred← citeshttps://doi.org/10.1016/j.funbio.2025.101598openalex-snapshot

Overview of scientific productivity in the field of fungal stress research

inferred← citeshttps://doi.org/10.1016/j.gene.2016.06.004openalex-snapshot

Nucleopolyhedroviruses (NPV) induce the expression of small heat shock protein 25.4 in Antheraea pernyi

inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e34963openalex-snapshot

The prion-like effect and prion-like protein targeting strategy in amyotrophic lateral sclerosis

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2011.08.027openalex-snapshot

Sugarcane Hsp101 is a hexameric chaperone that binds nucleotides

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2013.05.032openalex-snapshot

Applying chaperones to protein-misfolding disorders: Molecular chaperones against α-synuclein in Parkinson's disease

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.10.024openalex-snapshot

Nanoparticles-protein interaction: Role in protein aggregation and clinical implications

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2017.04.025openalex-snapshot

An overview on molecular chaperones enhancing solubility of expressed recombinant proteins with correct folding

inferred← citeshttps://doi.org/10.1016/j.imbio.2004.12.006openalex-snapshot

Heat shock protein 27 expression in patients with chronic liver damage

inferred← citeshttps://doi.org/10.1016/j.isci.2022.103900openalex-snapshot

Molecular determinants and modifiers of Matrin-3 toxicity, condensate dynamics, and droplet morphology

inferred← citeshttps://doi.org/10.1016/j.isci.2023.108334openalex-snapshot

Solid-to-liquid phase transition in the dissolution of cytosolic misfolded-protein aggregates

inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102533openalex-snapshot

Eisosome protein Pil1 regulates mitochondrial morphology, mitophagy, and cell death in Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1016/j.jbc.2023.105472openalex-snapshot

Contribution of the yeast bi-chaperone system in the restoration of the RNA helicase Ded1 and translational activity under severe ethanol stress

inferred← citeshttps://doi.org/10.1016/j.jbiosc.2017.03.001openalex-snapshot

Efficient antibody production in the methylotrophic yeast Ogataea minuta by overexpression of chaperones

inferred← citeshttps://doi.org/10.1016/j.jbiotec.2018.07.008openalex-snapshot

Enzymatic characterization of a soluble aggregate induced by N-terminal extension to a lipolytic enzyme

inferred← citeshttps://doi.org/10.1016/j.jmb.2003.12.004openalex-snapshot

Silent Prions Lying in Wait: A Two-hit Model of Prion/Amyloid Formation and Infection

inferred← citeshttps://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

inferred← citeshttps://doi.org/10.1016/j.jmb.2004.08.081openalex-snapshot

Structure of Stable Protein Folding Intermediates by Equilibrium ϕ-Analysis: The Apoflavodoxin Thermal Intermediate

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