| scholarly article | Q13442814 |
| P819 | ADS bibcode | 1999PNAS...9613732G |
| P356 | DOI | 10.1073/PNAS.96.24.13732 |
| P932 | PMC publication ID | 24133 |
| P698 | PubMed publication ID | 10570141 |
| P5875 | ResearchGate publication ID | 12731381 |
| P2093 | author name string | P Goloubinoff | |
| B Bukau | |||
| A Mogk | |||
| T Tomoyasu | |||
| A P Zvi | |||
| P2860 | cites work | Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins | Q27931364 |
| Protein disaggregation mediated by heat-shock protein Hsp104. | Q27940314 | ||
| The Hsp70 and Hsp60 chaperone machines | Q29547601 | ||
| Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+] | Q29619693 | ||
| Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. | Q33877945 | ||
| Hsp104 is required for tolerance to many forms of stress | Q33937933 | ||
| Support for the prion hypothesis for inheritance of a phenotypic trait in yeast | Q34384236 | ||
| Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones | Q36351463 | ||
| Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones | Q36390259 | ||
| DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. | Q40874220 | ||
| Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation | Q41295162 | ||
| Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis | Q41478729 | ||
| Deadly conformations--protein misfolding in prion disease | Q41478736 | ||
| Protein self-organization in vitro and in vivo: partitioning between physical biochemistry and cell biology | Q41752356 | ||
| The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase | Q45232404 | ||
| Binding of the dye congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences | Q46920360 | ||
| Two simple methods for quantifying low-affinity dye-substrate binding. | Q54132771 | ||
| Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity. | Q54646986 | ||
| The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network | Q74473349 | ||
| P433 | issue | 24 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | refolding | Q3935998 |
| P304 | page(s) | 13732-13737 | |
| P577 | publication date | 1999-11-01 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network | |
| P478 | volume | 96 |
| Q24673041 | A New Heat Shock Gene,agsA, Which Encodes a Small Chaperone Involved in Suppressing Protein Aggregation inSalmonella entericaSerovar Typhimurium |
| Q27932265 | A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase |
| Q34552766 | A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases |
| Q33493807 | A genome-scale proteomic screen identifies a role for DnaK in chaperoning of polar autotransporters in Shigella. |
| Q43198439 | A stromal heat shock protein 70 system functions in protein import into chloroplasts in the moss Physcomitrella patens |
| Q73905825 | A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone secB |
| Q54323294 | A tightly regulated molecular toggle controls AAA+ disaggregase. |
| Q34693562 | AAA+ ATPases: achieving diversity of function with conserved machinery |
| Q99548905 | AAA+ Molecular Chaperone ClpB in Leptospira interrogans: Its Role and Significance in Leptospiral Virulence and Pathogenesis of Leptospirosis |
| Q29617410 | AAA+ proteins: have engine, will work |
| Q46421288 | 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. |
| Q43817965 | ATP causes small heat shock proteins to release denatured protein |
| Q44085064 | ATP-dependent hexameric assembly of the heat shock protein Hsp101 involves multiple interaction domains and a functional C-proximal nucleotide-binding domain |
| Q34048664 | ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit |
| Q52324439 | Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate. |
| Q47332944 | Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones |
| Q33735193 | Adaptations to High Salt in a Halophilic Protist: Differential Expression and Gene Acquisitions through Duplications and Gene Transfers |
| Q35840288 | Aggregate reactivation mediated by the Hsp100 chaperones |
| Q28487701 | Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis |
| Q28266387 | Allostery in the Hsp70 chaperone proteins |
| Q33969470 | Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. |
| Q39244663 | An overview on molecular chaperones enhancing solubility of expressed recombinant proteins with correct folding |
| Q27931784 | Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding |
| Q39476216 | Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement |
| Q37687090 | Applying Hsp104 to protein-misfolding disorders. |
| Q35628774 | Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity |
| Q36398218 | Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. |
| Q38578280 | Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates |
| Q38729079 | Cadmium Causes Misfolding and Aggregation of Cytosolic Proteins in Yeast. |
| Q28203834 | Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin |
| Q54483490 | Cells lacking ClpB display a prolonged shutoff phase of the heat shock response in Caulobacter crescentus. |
| Q27026110 | Chaperone machines for protein folding, unfolding and disaggregation |
| Q36194355 | Chaperone networks: tipping the balance in protein folding diseases |
| Q33899375 | Chaperone substrates inside the cell |
| Q33287499 | Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli |
| Q36777158 | Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging. |
| Q34740513 | Chaperones in control of protein disaggregation |
| Q33996090 | Characterization of Brucella suis clpB and clpAB mutants and participation of the genes in stress responses |
| Q44477296 | Characterization of a trap mutant of the AAA+ chaperone ClpB. |
| Q24678182 | Characterization of the Staphylococcus aureus heat shock, cold shock, stringent, and SOS responses and their effects on log-phase mRNA turnover |
| Q24811223 | Characterization of the aggregates formed during recombinant protein expression in bacteria |
| Q43715877 | Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses |
| Q34442141 | ClpB chaperone passively threads soluble denatured proteins through its central pore |
| Q38539889 | ClpB/Hsp100 proteins and heat stress tolerance in plants |
| Q91762395 | ClpG Provides Increased Heat Resistance by Acting as Superior Disaggregase |
| Q53236221 | ClpL is a chaperone without auxiliary factors. |
| Q42958498 | ClpL is required for folding of CtsR in Streptococcus mutans. |
| Q34121960 | ClpS, a substrate modulator of the ClpAP machine |
| Q41456038 | ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria |
| Q58765325 | Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium |
| Q36090078 | Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system |
| Q86080142 | Comment on the paper by Isla et al. (2014) |
| Q41220996 | Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions |
| Q74009953 | Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family |
| Q44599864 | Conserved Pore Residues in the AAA Protease FtsH Are Important for Proteolysis and Its Coupling to ATP Hydrolysis |
| Q44078387 | Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity |
| Q37459328 | Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. |
| Q34762197 | Construction and deconstruction of bacterial inclusion bodies |
| Q28085237 | Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation |
| Q54549149 | Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein. |
| Q28344719 | Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants |
| Q33715895 | Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae |
| Q42481588 | Coordinated synthesis of the two ClpB isoforms improves the ability of Escherichia coli to survive thermal stress |
| Q34488383 | Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation |
| Q37687108 | Cryo electron microscopy structures of Hsp100 proteins: crowbars in or out? |
| Q27639122 | Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity |
| Q44352969 | Crystal structure of the E. coli Hsp100 ClpB N-terminal domain |
| Q54473512 | Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity. |
| Q34985224 | Destabilization and recovery of a yeast prion after mild heat shock. |
| Q45211595 | Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding |
| Q42233230 | Direct assessment in bacteria of prionoid propagation and phenotype selection by Hsp70 chaperone |
| Q26796603 | Disaggregases, molecular chaperones that resolubilize protein aggregates |
| Q34461183 | Disruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria |
| Q28346984 | DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteins |
| Q41975228 | Domain stability in the AAA+ ATPase ClpB from Escherichia coli |
| Q33692013 | Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region |
| Q38864924 | Dynamic changes in the leaf proteome of a C3 xerophyte, Citrullus lanatus (wild watermelon), in response to water deficit |
| Q55180166 | Dynamic structural states of ClpB involved in its disaggregation function. |
| Q38351209 | Ectopic over-expression of BhHsf1, a heat shock factor from the resurrection plant Boea hygrometrica, leads to increased thermotolerance and retarded growth in transgenic Arabidopsis and tobacco |
| Q57458045 | Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation |
| Q35756699 | Endoplasmic reticulum stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways |
| Q36406795 | Escherichia coli ClpB is a non-processive polypeptide translocase |
| Q34517353 | Escherichia coli RNA polymerase subunit omega and its N-terminal domain bind full-length beta' to facilitate incorporation into the alpha2beta subassembly |
| Q34402031 | Essential role of TID1 in maintaining mitochondrial membrane potential homogeneity and mitochondrial DNA integrity |
| Q34244942 | Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity |
| Q44885001 | Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. |
| Q41239669 | Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes. |
| Q53370116 | Examination of the dynamic assembly equilibrium for E. coli ClpB. |
| Q38927256 | Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease. |
| Q36365102 | Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency |
| Q36140066 | Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machine |
| Q38198555 | Functional conservation and divergence of J-domain-containing ZUO1/ZRF orthologs throughout evolution |
| Q41447461 | Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation |
| Q81295871 | Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system |
| Q42577050 | Genetic and phenotypic characterization of the heat shock response in Pseudomonas putida |
| Q35913441 | Genome-wide identification of Francisella tularensis virulence determinants |
| Q34040032 | Genome-wide identification of genes essential for the survival of Streptococcus pneumoniae in human saliva |
| Q37596071 | Global transcriptome analysis of the heat shock response of Shewanella oneidensis |
| Q41063503 | GroES/GroEL and DnaK/DnaJ have distinct roles in stress responses and during cell cycle progression in Caulobacter crescentus. |
| Q63610180 | Growth‐driven displacement of protein aggregates along the cell length ensures partitioning to both daughter cells in Caulobacter crescentus |
| Q27683847 | Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation |
| Q99404926 | Heat Shock Responsive Gene Expression Modulated by mRNA Poly(A) Tail Length |
| Q36884034 | Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor |
| Q35210928 | Heat shock proteins in relation to heat stress tolerance of creeping bentgrass at different N levels |
| Q73703980 | Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form |
| Q28257892 | How high G+C Gram-positive bacteria and in particular bifidobacteria cope with heat stress: protein players and regulators |
| Q38356312 | How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions |
| Q48349534 | Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress. |
| Q37175214 | Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. |
| Q38362898 | Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures. |
| Q34533688 | Hsp70 architecture: the formation of novel polymeric structures of Hsp70.1 and Hsc70 after proteotoxic stress. |
| Q46895785 | Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. |
| Q34597309 | Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling |
| Q34572502 | Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+] |
| Q24644472 | Hsp70 chaperones: cellular functions and molecular mechanism |
| Q54323301 | Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. |
| Q44417784 | Identification and characterization of a Hsp70 (DnaK) chaperone system from Meiothermus ruber |
| Q35191976 | Inactivation of clpB in the pathogen Leptospira interrogans reduces virulence and resistance to stress conditions |
| Q37266700 | Influence of Hsp70s and their regulators on yeast prion propagation |
| Q38676181 | Insights into the Clp/HSP100 chaperone system from chloroplasts of Arabidopsis thaliana. |
| Q37858328 | Integrating protein homeostasis strategies in prokaryotes |
| Q42088127 | Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity |
| Q34979488 | Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation |
| Q37636363 | Investigating the Chaperone Properties of a Novel Heat Shock Protein, Hsp70.c, from Trypanosoma brucei |
| Q27302907 | Investigating the spreading and toxicity of prion-like proteins using the metazoan model organism C. elegans |
| Q55038087 | Isolation and Identification of Putative Protein Substrates of the AAA+ Molecular Chaperone ClpB from the Pathogenic Spirochaete Leptospira interrogans. |
| Q35950429 | J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation |
| Q43514492 | Kinetic model of in vivo folding and inclusion body formation in recombinant Escherichia coli |
| Q41811406 | LON is the master protease that protects against protein aggregation in human mitochondria through direct degradation of misfolded proteins |
| Q37294442 | Large scale comparative proteomics of a chloroplast Clp protease mutant reveals folding stress, altered protein homeostasis, and feedback regulation of metabolism. |
| Q24546090 | Large-scale identification of protein-protein interaction of Escherichia coli K-12 |
| Q34804953 | MecA, an adaptor protein necessary for ClpC chaperone activity |
| Q40600379 | Mechanism of an ATP-independent protein disaggregase: II. distinct molecular interactions drive multiple steps during aggregate disassembly |
| Q39459936 | Mechanism of prion loss after Hsp104 inactivation in yeast |
| Q34505905 | Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. |
| Q34300523 | Metazoan Hsp70 machines use Hsp110 to power protein disaggregation |
| Q26779046 | Metazoan Hsp70-based protein disaggregases: emergence and mechanisms |
| Q90168460 | Microbial ageing and longevity |
| Q73568734 | Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding |
| Q42114093 | Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease |
| Q46917870 | Mitochondrial inner membrane protease promotes assembly of presequence translocase by removing a carboxy-terminal targeting sequence. |
| Q46624522 | Modified Clp protease complex in the ClpP3 null mutant and consequences for chloroplast development and function in Arabidopsis |
| Q34081455 | Molecular basis for interactions of the DnaK chaperone with substrates. |
| Q37853789 | Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease |
| Q34411039 | Molecular chaperones and the assembly of the prion Sup35p, an in vitro study |
| Q35676363 | Molecular chaperones and the assembly of the prion Ure2p in vitro |
| Q34038270 | Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins |
| Q38107685 | Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides. |
| Q34793186 | Molecular chaperones as essential mediators of mitochondrial biogenesis |
| Q34165962 | Molecular chaperones--cellular machines for protein folding |
| Q26766168 | Molecular chaperones: guardians of the proteome in normal and disease states |
| Q35686747 | Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones |
| Q28202414 | Mutation processes at the protein level: is Lamarck back? |
| Q34133518 | Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones |
| Q54491998 | Navigating the ClpB channel to solution. |
| Q39505712 | Novel form of ClpB/HSP100 protein in the cyanobacterium Synechococcus |
| Q36275416 | Novel insights into the mechanism of chaperone-assisted protein disaggregation |
| Q43189809 | Nucleotide utilization requirements that render ClpB active as a chaperone |
| Q42069341 | Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB. |
| Q73428710 | Only one dnaK homolog, dnaK2, is active transcriptionally and is essential in Synechocystis |
| Q28485543 | Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein |
| Q38974841 | Oxidative stress protection by exogenous delivery of rhHsp70 chaperone to the retinal pigment epithelium (RPE), a possible therapeutic strategy against RPE degeneration. |
| Q30667048 | Pathways of allosteric regulation in Hsp70 chaperones. |
| Q41820345 | Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding |
| Q47416491 | Plant Hsp100/ClpB-like proteins: poorly-analyzed cousins of yeast ClpB machine |
| Q42664036 | Plasma membrane cyclic nucleotide gated calcium channels control land plant thermal sensing and acquired thermotolerance. |
| Q44612493 | Poly-L-lysine enhances the protein disaggregation activity of ClpB. |
| Q34762204 | Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology |
| Q46905577 | Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate |
| Q41975664 | Production of recombinant proteins in the lon-deficient BL21(DE3) strain of Escherichia coli in the absence of the DnaK chaperone. |
| Q36198227 | Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions |
| Q37423973 | Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding |
| Q54422222 | Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. |
| Q33879856 | Protein folding and unfolding by Escherichia coli chaperones and chaperonins |
| Q38196753 | Protein folding, misfolding, aggregation and their implications in human diseases: discovering therapeutic ways to amyloid-associated diseases |
| Q38141722 | Protein rescue from aggregates by powerful molecular chaperone machines |
| Q34524526 | Protein-misfolding diseases and chaperone-based therapeutic approaches |
| Q44177969 | Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones. |
| Q36743628 | Proteomic Analysis Reveals the Leaf Color Regulation Mechanism in Chimera Hosta "Gold Standard" Leaves |
| Q50510967 | Proteomic analysis of a model unicellular green alga, Chlamydomonas reinhardtii, during short-term exposure to irradiance stress reveals significant down regulation of several heat-shock proteins. |
| Q53855190 | Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. |
| Q39998015 | Quantitative analysis of the chloroplast molecular chaperone ClpC/Hsp93 in Arabidopsis reveals new insights into its localization, interaction with the Clp proteolytic core, and functional importance |
| Q35243430 | RNA-Seq analysis of the multipartite genome of Rhizobium etli CE3 shows different replicon contributions under heat and saline shock. |
| Q36580607 | Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System |
| Q39502948 | Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system |
| Q35940945 | Recombinant protein folding and misfolding in Escherichia coli |
| Q37620229 | Reconciling theories of chaperonin accelerated folding with experimental evidence |
| Q44467161 | Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. |
| Q41888807 | Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation. |
| Q42733235 | Regulatory circuits of the AAA+ disaggregase Hsp104. |
| Q36208424 | Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu transposase |
| Q98771733 | Reversal of Alpha-Synuclein Fibrillization by Protein Disulfide Isomerase |
| Q54529590 | Role of molecular chaperones in inclusion body formation. |
| Q43029508 | Role of the Clp system in stress tolerance, biofilm formation, and intracellular invasion in Porphyromonas gingivalis |
| Q28485555 | Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus |
| Q44353901 | Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity |
| Q43821705 | Roles of the two ATP binding sites of ClpB from Thermus thermophilus |
| Q60232722 | Seasonal and diurnal variations in gene expression in the desert legume Retama raetam |
| Q24795353 | Sequence determinants of protein aggregation: tools to increase protein solubility |
| Q27313921 | Single-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates. |
| Q35749852 | Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli |
| Q47239818 | Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. |
| Q96644599 | Skd3 (human CLPB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations |
| Q45181636 | Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides |
| Q34880608 | Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. |
| Q28552929 | Specific Hsp100 Chaperones Determine the Fate of the First Enzyme of the Plastidial Isoprenoid Pathway for Either Refolding or Degradation by the Stromal Clp Protease in Arabidopsis |
| Q35675179 | Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli |
| Q46058474 | Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity |
| Q34352138 | Stable α-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones |
| Q35031242 | Stress proteins and glial functions: possible therapeutic targets for neurodegenerative disorders |
| Q34504117 | Stress-induced evolution and the biosafety of genetically modified microorganisms released into the environment |
| Q47118931 | Stressed mycobacteria use the chaperone ClpB to sequester irreversibly oxidized proteins asymmetrically within and between cells |
| Q41063466 | Structural and functional conversion of molecular chaperone ClpB from the gram-positive halophilic lactic acid bacterium Tetragenococcus halophilus mediated by ATP and stress |
| Q27670764 | Structural basis for intersubunit signaling in a protein disaggregating machine |
| Q64970320 | Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase. |
| Q44362227 | Structural changes in RepA, a plasmid replication initiator, upon binding to origin DNA. |
| Q38490755 | Structural mechanisms of chaperone mediated protein disaggregation |
| Q35675169 | Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains |
| Q35678007 | Structure and function of the middle domain of ClpB from Escherichia coli |
| Q33734726 | Substrate Discrimination by ClpB and Hsp104. |
| Q27932701 | Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides |
| Q44945731 | Substrate recognition by the AAA+ chaperone ClpB. |
| Q45012676 | Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation |
| Q33653831 | Synergistic cooperation between two ClpB isoforms in aggregate reactivation. |
| Q43528508 | Systems-wide analysis of acclimation responses to long-term heat stress and recovery in the photosynthetic model organism Chlamydomonas reinhardtii. |
| Q55041195 | The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast. |
| Q38335420 | The DnaK-DnaJ-GrpE chaperone system activates inert wild type pi initiator protein of R6K into a form active in replication initiation |
| Q36962268 | The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. |
| Q93117098 | The Hsp70 chaperone network |
| Q34125006 | The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner |
| Q51386123 | The N-terminal domain of Escherichia coli ClpB enhances chaperone function. |
| Q33504161 | The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion |
| Q28487558 | The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis |
| Q58554573 | The amino-terminal domain of ClpB protein plays a crucial role in its substrate disaggregation activity |
| Q46632158 | The amino-terminal domain of ClpB supports binding to strongly aggregated proteins |
| Q38253736 | The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. |
| Q37917880 | The elusive middle domain of Hsp104 and ClpB: location and function. |
| Q54545897 | The heat-shock protein ClpB of Francisella tularensis is involved in stress tolerance and is required for multiplication in target organs of infected mice. |
| Q90131642 | The huntingtin inclusion is a dynamic phase-separated compartment |
| Q45261031 | The importance of having thermosensor control in the DnaK chaperone system |
| Q42856450 | The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase |
| Q34056277 | The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system |
| Q39625992 | The metabolic potential of Escherichia coli BL21 in defined and rich medium |
| Q31523861 | The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli |
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