| scholarly article | Q13442814 |
| P819 | ADS bibcode | 1999PNAS...96.7184M |
| P356 | DOI | 10.1073/PNAS.96.13.7184 |
| P932 | PMC publication ID | 22047 |
| P698 | PubMed publication ID | 10377389 |
| P50 | author | Masafumi Yohda | Q43017204 |
| Ken Motohashi | Q41853792 | ||
| P2093 | author name string | M Yoshida | |
| Y Watanabe | |||
| P2860 | cites work | Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus | Q43019651 |
| Isolation of the stable hexameric DnaK.DnaJ complex from Thermus thermophilus. | Q43022800 | ||
| Molecular cloning, expression, and characterization of chaperonin-60 and chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8. | Q43023662 | ||
| The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase | Q45232404 | ||
| A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus | Q48062090 | ||
| Hsp104 is a highly conserved protein with two essential nucleotide-binding sites | Q48209588 | ||
| A malachite green colorimetric assay for protein phosphatase activity | Q48831861 | ||
| A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay. | Q50896016 | ||
| K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus. | Q54560329 | ||
| 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 | ||
| Chaperonin from Thermus thermophilus can protect several enzymes from irreversible heat denaturation by capturing denaturation intermediate | Q72212722 | ||
| The role of ATP in the functional cycle of the DnaK chaperone system | Q72300885 | ||
| Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes | Q72772905 | ||
| Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivo | Q24521559 | ||
| Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold | Q24556499 | ||
| Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation | Q27930558 | ||
| Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins | Q27931364 | ||
| HSP104 required for induced thermotolerance | Q27931727 | ||
| The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function | Q27937823 | ||
| Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70 | Q27938048 | ||
| Protein disaggregation mediated by heat-shock protein Hsp104. | Q27940314 | ||
| The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE | Q28239456 | ||
| The Hsp70 and Hsp60 chaperone machines | Q29547601 | ||
| Molecular chaperones in cellular protein folding | Q29547795 | ||
| Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK | Q29618850 | ||
| Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes | Q33568953 | ||
| Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. | Q33736607 | ||
| A molecular chaperone, ClpA, functions like DnaK and DnaJ. | Q35968116 | ||
| Genetic evidence for a functional relationship between Hsp104 and Hsp70. | Q36123014 | ||
| Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32). | Q36148966 | ||
| Mechanism of protein remodeling by ClpA chaperone | Q36762714 | ||
| Efficient site-directed mutagenesis using uracil-containing DNA. | Q37479506 | ||
| Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products | Q38315821 | ||
| ClpB is the Escherichia coli heat shock protein F84.1. | Q39942271 | ||
| DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. | Q40874220 | ||
| HSP100/Clp proteins: a common mechanism explains diverse functions | Q41083709 | ||
| P433 | issue | 13 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | molecular chaperones | Q422496 |
| P304 | page(s) | 7184-7189 | |
| P577 | publication date | 1999-06-01 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones | |
| P478 | volume | 96 |
| Q34552766 | A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases |
| Q54323294 | A tightly regulated molecular toggle controls AAA+ disaggregase. |
| Q73177832 | AAA-ATPases at the crossroads of protein life and death |
| 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. |
| Q44085064 | ATP-dependent hexameric assembly of the heat shock protein Hsp101 involves multiple interaction domains and a functional C-proximal nucleotide-binding domain |
| Q35840288 | Aggregate reactivation mediated by the Hsp100 chaperones |
| Q28487701 | Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis |
| Q33969470 | Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. |
| Q33301479 | Analysis of gene order data supports vertical inheritance of the leukotoxin operon and genome rearrangements in the 5' flanking region in genus Mannheimia |
| Q39476216 | Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement |
| Q47834277 | Arabidopsis hot mutants define multiple functions required for acclimation to high temperatures |
| Q30624879 | Bacterial ClpB heat-shock protein, an antigen-mimetic of the anorexigenic peptide α-MSH, at the origin of eating disorders |
| Q43572431 | Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding |
| 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. |
| Q36949975 | Characterization of a unique ClpB protein of Mycoplasma pneumoniae and its impact on growth |
| Q34442141 | ClpB chaperone passively threads soluble denatured proteins through its central pore |
| Q73019220 | ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli |
| Q38539889 | ClpB/Hsp100 proteins and heat stress tolerance in plants |
| 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 |
| Q36090078 | Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system |
| Q41668832 | Comparison of the RpoH-dependent regulon and general stress response in Neisseria gonorrhoeae. |
| 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. |
| 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. |
| Q42481588 | Coordinated synthesis of the two ClpB isoforms improves the ability of Escherichia coli to survive thermal stress |
| Q33595843 | Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation. |
| Q41975228 | Domain stability in the AAA+ ATPase ClpB from Escherichia coli |
| Q55180166 | Dynamic structural states of ClpB involved in its disaggregation function. |
| Q57458045 | Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation |
| Q36406795 | Escherichia coli ClpB is a non-processive polypeptide translocase |
| Q44631073 | Examination of polypeptide substrate specificity for Escherichia coli ClpB. |
| Q53370116 | Examination of the dynamic assembly equilibrium for E. coli ClpB. |
| Q36140066 | Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machine |
| Q41447461 | Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation |
| Q43015459 | Gene structure and transcriptional regulation of dnaK and dnaJ genes from a psychrophilic bacterium, Colwellia maris |
| Q81295871 | Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system |
| Q33530234 | Genome-wide analysis of rice ClpB/HSP100, ClpC and ClpD genes |
| Q38327830 | Global gene expression responses to cadmium toxicity in Escherichia coli |
| Q34998331 | Global transcriptome analysis of Mesorhizobium alhagi CCNWXJ12-2 under salt stress |
| Q27683847 | Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation |
| Q36884034 | Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor |
| Q52169308 | Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. |
| Q73703980 | Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form |
| Q48349534 | Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress. |
| Q46895785 | Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. |
| Q24644472 | Hsp70 chaperones: cellular functions and molecular mechanism |
| Q54323301 | Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. |
| Q33874246 | In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104 |
| Q37858328 | Integrating protein homeostasis strategies in prokaryotes |
| Q35950429 | J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation |
| Q24546090 | Large-scale identification of protein-protein interaction of Escherichia coli K-12 |
| Q34804953 | MecA, an adaptor protein necessary for ClpC chaperone activity |
| Q34505905 | Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. |
| Q26779046 | Metazoan Hsp70-based protein disaggregases: emergence and mechanisms |
| Q73568734 | Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding |
| Q36496399 | Molecular chaperones and selection against mutations |
| Q35676363 | Molecular chaperones and the assembly of the prion Ure2p in vitro |
| Q26766168 | Molecular chaperones: guardians of the proteome in normal and disease states |
| Q35683924 | Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress |
| Q39505712 | Novel form of ClpB/HSP100 protein in the cyanobacterium Synechococcus |
| Q43189809 | Nucleotide utilization requirements that render ClpB active as a chaperone |
| Q42069341 | Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB. |
| Q28485543 | Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein |
| Q58231674 | Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infection |
| Q47416491 | Plant Hsp100/ClpB-like proteins: poorly-analyzed cousins of yeast ClpB machine |
| Q35190125 | Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP. |
| 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 |
| Q38141722 | Protein rescue from aggregates by powerful molecular chaperone machines |
| Q35564854 | Proteolysis in Bacterial Regulatory Circuits |
| Q36580607 | Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System |
| Q34032570 | Reduced immunopathology and mortality despite tissue persistence in a Mycobacterium tuberculosis mutant lacking alternative sigma factor, SigH |
| Q42733235 | Regulatory circuits of the AAA+ disaggregase Hsp104. |
| Q36208424 | Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu transposase |
| Q43029508 | Role of the Clp system in stress tolerance, biofilm formation, and intracellular invasion in Porphyromonas gingivalis |
| Q46453462 | Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase |
| 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 |
| Q34505864 | Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network |
| 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. |
| 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. |
| Q27723476 | Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation |
| 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 |
| Q55426478 | Stress-related genes promote Edwardsiella ictaluri pathogenesis. |
| 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 |
| 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 |
| Q40424901 | The Escherichia coli heat shock protein ClpB restores acquired thermotolerance to a cyanobacterial clpB deletion mutant |
| Q44155973 | The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity |
| Q28487558 | The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis |
| Q46632158 | The amino-terminal domain of ClpB supports binding to strongly aggregated proteins |
| Q42701051 | The clpB gene is involved in the stress response of Myxococcus xanthus during vegetative growth and development |
| Q37917880 | The elusive middle domain of Hsp104 and ClpB: location and function. |
| Q31523861 | The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli |
| Q54492592 | The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state. |
| Q27642377 | The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state |
| Q39501582 | The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942. |
| Q37687105 | Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation |
| Q42384586 | Transcriptional profiling of the model Archaeon Halobacterium sp. NRC-1: responses to changes in salinity and temperature |
| Q37119684 | Transcriptome analysis of Pseudomonas aeruginosa PAO1 grown at both body and elevated temperatures |
| Q75284993 | Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress converts the former to the latter, and only the latter can do disaggregation in cooperation with ClpB |
| Q30498176 | Unfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase |
| Q59804979 | Universal Stress Proteins Contribute Edwardsiella ictaluri Virulence in Catfish |
| Q46035197 | Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. |
| Q24791943 | Unscrambling an egg: protein disaggregation by AAA+ proteins |
| Q35757826 | Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB |
| Q43097852 | Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB. |
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