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ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein Aggregation
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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.1460-2075.1993.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/j.1460-2075.1995.tb07179.xopenalex-snapshot
The ClpX heat‐shock protein of Escherichia coli, the ATP‐dependent substrate specificity component of the ClpP‐ClpX protease, is a novel molecular chaperone.
inferredcites →https://doi.org/10.1002/pro.5560041120openalex-snapshot
How to measure and predict the molar absorption coefficient of a protein
inferredcites →https://doi.org/10.1006/jmbi.1995.0399openalex-snapshot
Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds
inferredcites →https://doi.org/10.1016/0003-2697(75)90388-7openalex-snapshot
Assay of inorganic and organic phosphorus in the 0.1–5 nanomole range
inferredcites →https://doi.org/10.1016/0003-2697(79)90115-5openalex-snapshot
An improved assay for nanomole amounts of inorganic phosphate
inferredcites →https://doi.org/10.1016/0076-6879(94)44025-5openalex-snapshot
[23] Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli
inferredcites →https://doi.org/10.1016/s0021-9258(17)39649-7openalex-snapshot
Purification and properties of the dnaJ replication protein of Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(19)88720-3openalex-snapshot
The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase.
inferredcites →https://doi.org/10.1016/s0092-8674(00)81223-4openalex-snapshot
Hsp104, Hsp70, and Hsp40
inferredcites →https://doi.org/10.1016/s0968-0004(96)10038-4openalex-snapshot
HSP100/Clp proteins: a common mechanism explains diverse functions
inferredcites →https://doi.org/10.1016/s1359-0278(98)00002-9openalex-snapshot
Protein aggregation: folding aggregates, inclusion bodies and amyloid
inferredcites →https://doi.org/10.1038/372475a0openalex-snapshot
Protein disaggregation mediated by heat-shock protein Hspl04
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.88.7.2874openalex-snapshot
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
inferredcites →https://doi.org/10.1073/pnas.91.25.12218openalex-snapshot
A molecular chaperone, ClpA, functions like DnaK and DnaJ.
inferredcites →https://doi.org/10.1073/pnas.96.13.7184openalex-snapshot
Heat-inactivated proteins are rescued by the DnaK⋅J-GrpE set and ClpB chaperones
inferredcites →https://doi.org/10.1096/fasebj.10.1.8566529openalex-snapshot
Supervising the fold: functional principles of molecular chaperones
inferredcites →https://doi.org/10.1101/gad.11.7.815openalex-snapshot
Protein quality control: triage by chaperones and proteases.
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.180.19.5165-5172.1998openalex-snapshot
Roles of the Escherichia coli Small Heat Shock Proteins IbpA and IbpB in Thermal Stress Management: Comparison with ClpA, ClpB, and HtpG In Vivo
inferredcites →https://doi.org/10.3168/jds.s0022-0302(98)75861-8openalex-snapshot
Environmental Influences on Purified κ-Casein: Disulfide Interactions
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Crystal Structure of the E. coli Hsp100 ClpB N-Terminal Domain
inferred← citeshttps://doi.org/10.1016/s1369-5274(00)00075-8openalex-snapshot
Protein folding and unfolding by Escherichia coli chaperones and chaperonins
inferred← citeshttps://doi.org/10.1021/acs.biochem.0c00320openalex-snapshot
KLR-70: A Novel Cationic Inhibitor of the Bacterial Hsp70 Chaperone
inferred← citeshttps://doi.org/10.1021/acs.biochem.6b00122openalex-snapshot
Examination of ClpB Quaternary Structure and Linkage to Nucleotide Binding
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.6b01685openalex-snapshot
Accepting the Invitation to Open Innovation in Malaria Drug Discovery: Synthesis, Biological Evaluation, and Investigation on the Structure–Activity Relationships of Benzo[b]thiophene-2-carboxamides as Antimalarial Agents
inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c03039openalex-snapshot
Complementary Role of Co- and Post-Translational Events in De Novo Protein Biogenesis
inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b05963openalex-snapshot
Asymmetric Conformational Transitions in AAA+ Biological Nanomachines Modulate Direction-Dependent Substrate Protein Unfolding Mechanisms
inferred← citeshttps://doi.org/10.1021/acssynbio.9b00291openalex-snapshot
Genetic Circuits To Detect Nanomaterial Triggered Toxicity through Engineered Heat Shock Response Mechanism
inferred← citeshttps://doi.org/10.1021/bi026161sopenalex-snapshot
Site-Directed Mutagenesis of Conserved Charged Amino Acid Residues in ClpB from Escherichia coli ,
inferred← citeshttps://doi.org/10.1021/bi035573dopenalex-snapshot
Structure and Function of the Middle Domain of ClpB fromEscherichia coli
inferred← citeshttps://doi.org/10.1021/bi049490oopenalex-snapshot
Isomerase-Independent Chaperone Function of Cyclophilin Ensures Aggregation Prevention of Adenosine Kinase Both in vitro and under in vivo Conditions
inferred← citeshttps://doi.org/10.1021/bi0606804openalex-snapshot
The Roles of Conserved Amino Acids on Substrate Binding and Conformational Integrity of ClpB N-Terminal Domain
inferred← citeshttps://doi.org/10.1021/bi101670sopenalex-snapshot
A Quantitative Analysis of the Effect of Nucleotides and the M Domain on the Association Equilibrium of ClpB
inferred← citeshttps://doi.org/10.1021/bp0000959openalex-snapshot
Kinetics of Heat-Shock Response and Inclusion Body Formation During Temperature-Induced Production of Basic Fibroblast Growth Factor in High-Cell-Density Cultures of Recombinant Escherichia coli
inferred← citeshttps://doi.org/10.1021/jm400499kopenalex-snapshot
Screening and Evaluation of Small Organic Molecules as ClpB Inhibitors and Potential Antimicrobials
inferred← citeshttps://doi.org/10.1021/pr400603fopenalex-snapshot
Molecular Mechanisms Involved in the Response to Desiccation Stress and Persistence in Acinetobacter baumannii
inferred← citeshttps://doi.org/10.1023/a:1020565701210openalex-snapshot
Role of Hsp70 (DnaK–DnaJ–GrpE) and Hsp100 (ClpA and ClpB) Chaperones in Refolding and Increased Thermal Stability of Bacterial Luciferases in Escherichia coli Cells
inferred← citeshttps://doi.org/10.1023/a:1025024104862openalex-snapshot
Protein aggregation in recombinant bacteria: biological role of inclusion bodies
inferred← citeshttps://doi.org/10.1023/b:mbil.0000032215.53875.f8openalex-snapshot
The Effect of Clp Proteins on DnaK-Dependent Refolding of Bacterial Luciferases
inferred← citeshttps://doi.org/10.1038/nbt1029openalex-snapshot
Recombinant protein folding and misfolding in Escherichia coli
inferred← citeshttps://doi.org/10.1038/nrm3660openalex-snapshot
Protein rescue from aggregates by powerful molecular chaperone machines
inferred← citeshttps://doi.org/10.1038/nrmicro866openalex-snapshot
Minimal protein-folding systems in hyperthermophilic archaea
inferred← citeshttps://doi.org/10.1038/nsmb.1425openalex-snapshot
Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
inferred← citeshttps://doi.org/10.1038/nsmb.2441openalex-snapshot
A tightly regulated molecular toggle controls AAA+ disaggregase
inferred← citeshttps://doi.org/10.1038/nsmb.2442openalex-snapshot
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
inferred← citeshttps://doi.org/10.1038/nsmb1198openalex-snapshot
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity
inferred← citeshttps://doi.org/10.1038/nsmb787openalex-snapshot
Substrate recognition by the AAA+ chaperone ClpB
inferred← citeshttps://doi.org/10.1038/s41467-018-04587-wopenalex-snapshot
Dynamic structural states of ClpB involved in its disaggregation function
inferred← citeshttps://doi.org/10.1038/s41598-017-08917-8openalex-snapshot
Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during 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/10.1038/s41598-018-35286-7openalex-snapshot
Transcriptomic analysis of Bifidobacterium longum subsp. longum BBMN68 in response to oxidative shock
inferred← citeshttps://doi.org/10.1038/sj.emboj.7601811openalex-snapshot
J‐protein co‐chaperone Sis1 required for generation of [RNQ +] seeds necessary for prion propagation
inferred← citeshttps://doi.org/10.1038/sj.emboj.7601970openalex-snapshot
Chaperones in control of protein disaggregation
inferred← citeshttps://doi.org/10.1042/bj20082238openalex-snapshot
Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity
inferred← citeshttps://doi.org/10.1042/bst0360120openalex-snapshot
Common and specific mechanisms of AAA+ proteins involved in protein quality control
inferred← citeshttps://doi.org/10.1046/j.1365-2958.2000.01951.xopenalex-snapshot
ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
inferred← citeshttps://doi.org/10.1046/j.1365-2958.2003.03424.xopenalex-snapshot
C‐terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding
inferred← citeshttps://doi.org/10.1046/j.1365-2958.2003.03696.xopenalex-snapshot
Negative feedback regulation ofdnaK,clpBandlonexpression by the DnaK chaperone machine inStreptomyces coelicolor, identified by transcriptome andin vivoDnaK‐depletion analysis
inferred← citeshttps://doi.org/10.1046/j.1365-2958.2003.03710.xopenalex-snapshot
Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
inferred← citeshttps://doi.org/10.1046/j.1365-2958.2003.03871.xopenalex-snapshot
Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK‐DnaJ‐GrpE system in the management of protein misfolding under severe stress conditions
inferred← citeshttps://doi.org/10.1046/j.1365-313x.2001.01066.xopenalex-snapshot
Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress
inferred← citeshttps://doi.org/10.1063/5.0347970openalex-snapshot
Probing mechanisms of allosteric regulation in AAA+ ATPases for microtubule severing and protein disaggregation
inferred← citeshttps://doi.org/10.1073/pnas.0535717100openalex-snapshot
MecA, an adaptor protein necessary for ClpC chaperone activity
inferred← citeshttps://doi.org/10.1073/pnas.0703980104openalex-snapshot
Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system
inferred← citeshttps://doi.org/10.1073/pnas.1014278108openalex-snapshot
Unfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase
inferred← citeshttps://doi.org/10.1073/pnas.1102828108openalex-snapshot
Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
inferred← citeshttps://doi.org/10.1073/pnas.1207040109openalex-snapshot
Structural basis for intersubunit signaling in a protein disaggregating machine
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.2014407117openalex-snapshot
Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease
inferred← citeshttps://doi.org/10.1073/pnas.2422640122openalex-snapshot
Hsp90, DnaK, and ClpB collaborate in protein reactivation
inferred← citeshttps://doi.org/10.1073/pnas.261693199openalex-snapshot
Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding
inferred← citeshttps://doi.org/10.1073/pnas.97.16.8892openalex-snapshot
Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
inferred← citeshttps://doi.org/10.1073/pnas.97.8.4392openalex-snapshot
Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
inferred← citeshttps://doi.org/10.1074/jbc.275.17.12388openalex-snapshot
Heat-inactivated Proteins Managed by DnaKJ-GrpE-ClpB Chaperones Are Released as a Chaperonin-recognizable Non-native Form
inferred← citeshttps://doi.org/10.1074/jbc.m001293200openalex-snapshot
Size-dependent Disaggregation of Stable Protein Aggregates by the DnaK Chaperone Machinery
inferred← citeshttps://doi.org/10.1074/jbc.m005211200openalex-snapshot
Structure and Activity of ClpB from Escherichia coli
inferred← citeshttps://doi.org/10.1074/jbc.m006288200openalex-snapshot
Substrate Recognition by the ClpA Chaperone Component of ClpAP Protease
inferred← citeshttps://doi.org/10.1074/jbc.m009514200openalex-snapshot
In Vivo Proteolytic Degradation of the Escherichia coli Acyltransferase HlyC
inferred← citeshttps://doi.org/10.1074/jbc.m107580200openalex-snapshot
Cooperative Action of Escherichia coli ClpB Protein and DnaK Chaperone in the Activation of a Replication Initiation Protein
inferred← citeshttps://doi.org/10.1074/jbc.m107832200openalex-snapshot
Catalytic Activity and Chaperone Function of Human Protein-disulfide Isomerase Are Required for the Efficient Refolding of Proinsulin
inferred← citeshttps://doi.org/10.1074/jbc.m109349200openalex-snapshot
Roles of the Two ATP Binding Sites of ClpB from Thermus thermophilus
inferred← citeshttps://doi.org/10.1074/jbc.m112.350082openalex-snapshot
Group A Streptococcus Adheres to Pharyngeal Epithelial Cells with Salivary Proline-rich Proteins via GrpE Chaperone Protein
inferred← citeshttps://doi.org/10.1074/jbc.m112.383091openalex-snapshot
DnaK Chaperone-dependent Disaggregation by Caseinolytic Peptidase B (ClpB) Mutants Reveals Functional Overlap in the N-terminal Domain and Nucleotide-binding Domain-1 Pore Tyrosine
inferred← citeshttps://doi.org/10.1074/jbc.m113.479253openalex-snapshot
Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates
inferred← citeshttps://doi.org/10.1074/jbc.m113.520759openalex-snapshot
Conserved Distal Loop Residues in the Hsp104 and ClpB Middle Domain Contact Nucleotide-binding Domain 2 and Enable Hsp70-dependent Protein Disaggregation
inferred← citeshttps://doi.org/10.1074/jbc.m114.617696openalex-snapshot
Analysis of the Cooperative ATPase Cycle of the AAA+ Chaperone ClpB from Thermus thermophilus by Using Ordered Heterohexamers with an Alternating Subunit Arrangement
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.m201756200openalex-snapshot
A Bichaperone (Hsp70-Hsp78) System Restores Mitochondrial DNA Synthesis following Thermal Inactivation of Mip1p Polymerase
inferred← citeshttps://doi.org/10.1074/jbc.m204998200openalex-snapshot
ATP-dependent Hexameric Assembly of the Heat Shock Protein Hsp101 Involves Multiple Interaction Domains and a Functional C-proximal Nucleotide-binding Domain
inferred← citeshttps://doi.org/10.1074/jbc.m205800200openalex-snapshot
Hsp31, the Escherichia coli yedU Gene Product, Is a Molecular Chaperone Whose Activity Is Inhibited by ATP at High Temperatures
inferred← citeshttps://doi.org/10.1074/jbc.m207152200openalex-snapshot
The ClpB Homolog Hsp78 Is Required for the Efficient Degradation of Proteins in the Mitochondrial Matrix
inferred← citeshttps://doi.org/10.1074/jbc.m207853200openalex-snapshot
The N Terminus of ClpB from Thermus thermophilus Is Not Essential for the Chaperone Activity
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