| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M207853200 |
| P698 | PubMed publication ID | 12351638 |
| P2093 | author name string | Jochen Reinstein | |
| Ralf Seidel | |||
| Yvonne Groemping | |||
| Sandra Schlee | |||
| Philipp Beinker | |||
| P2860 | cites work | Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones | Q36390259 |
| Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis | Q38300971 | ||
| Evaluation of human immunodeficiency virus type 1 reverse transcriptase primer tRNA binding by fluorescence spectroscopy: specificity and comparison to primer/template binding | Q38359201 | ||
| The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942. | Q39501582 | ||
| ClpB is the Escherichia coli heat shock protein F84.1. | Q39942271 | ||
| Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. | Q42247311 | ||
| Roles of the two ATP binding sites of ClpB from Thermus thermophilus | Q43821705 | ||
| Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein | Q43975752 | ||
| Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity | Q44078387 | ||
| Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. | Q47239818 | ||
| Spectrophotometric determination of protein concentration in cell extracts containing tRNA's and rRNA's | Q47963332 | ||
| The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system | Q47977616 | ||
| Fluorescence and NMR investigations on the ligand binding properties of adenylate kinases. | Q54710050 | ||
| The structures of HsIU and the ATP-dependent protease HsIU-HsIV | Q27621563 | ||
| Crystal and solution structures of an HslUV protease-chaperone complex | Q27628834 | ||
| Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein | Q27765268 | ||
| Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins | Q27931364 | ||
| AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes | Q28131706 | ||
| Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase | Q28364580 | ||
| Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE. | Q31853089 | ||
| The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites | Q32179819 | ||
| ClpS, a substrate modulator of the ClpAP machine | Q34121960 | ||
| Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones | Q34387445 | ||
| Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains | Q35675169 | ||
| Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli | Q35675179 | ||
| Lon and Clp family proteases and chaperones share homologous substrate-recognition domains | Q36378628 | ||
| P433 | issue | 49 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Thermus thermophilus | Q139470 |
| molecular chaperones | Q422496 | ||
| P304 | page(s) | 47160-47166 | |
| P577 | publication date | 2002-09-25 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity | |
| P478 | volume | 277 |
| Q35840288 | Aggregate reactivation mediated by the Hsp100 chaperones |
| 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 |
| Q36394450 | ClpB N-terminal domain plays a regulatory role in protein disaggregation |
| Q42958498 | ClpL is required for folding of CtsR in Streptococcus mutans. |
| Q41456038 | ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria |
| Q27679257 | Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ |
| Q46750555 | Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding |
| Q28085237 | Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation |
| Q42481588 | Coordinated synthesis of the two ClpB isoforms improves the ability of Escherichia coli to survive thermal stress |
| Q26796603 | Disaggregases, molecular chaperones that resolubilize protein aggregates |
| Q36217287 | 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 |
| 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 |
| Q90009441 | Genome-wide analysis of the HSP101/CLPB gene family for heat tolerance in hexaploid wheat |
| Q42088127 | Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity |
| Q50912212 | Interplay between heat shock proteins HSP101 and HSA32 prolongs heat acclimation memory posttranscriptionally in Arabidopsis. |
| Q38648239 | Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104. |
| Q26766168 | Molecular chaperones: guardians of the proteome in normal and disease states |
| Q34894976 | N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression |
| Q43189809 | Nucleotide utilization requirements that render ClpB active as a chaperone |
| Q28485543 | Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein |
| Q40046476 | Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation. |
| Q44612493 | Poly-L-lysine enhances the protein disaggregation activity of ClpB. |
| Q42733235 | Regulatory circuits of the AAA+ disaggregase Hsp104. |
| Q45344399 | Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control |
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| Q47269574 | Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria |
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| Q27654635 | Structural and Motional Contributions of the Bacillus subtilis ClpC N-Domain to Adaptor Protein Interactions |
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| Q27675957 | The Molecular Mechanism of Hsp100 Chaperone Inhibition by the Prion Curing Agent Guanidinium Chloride |
| Q51386123 | The N-terminal domain of Escherichia coli ClpB enhances chaperone function. |
| 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 |
| Q27642377 | The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state |
| 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 |
| Q64104281 | Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine |
| Q24791943 | Unscrambling an egg: protein disaggregation by AAA+ proteins |
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