| scholarly article | Q13442814 |
| review article | Q7318358 |
| P356 | DOI | 10.1016/S0065-2911(01)44012-4 |
| P698 | PubMed publication ID | 11407116 |
| P50 | author | Peter A Lund | Q38591014 |
| P2093 | author name string | Lund PA | |
| P2860 | cites work | The complete sequence of the mucosal pathogen Ureaplasma urealyticum | Q22122390 |
| The autoregulatory HspR repressor protein governs chaperone gene transcription in Helicobacter pylori | Q73189500 | ||
| The HspR regulon of Streptomyces coelicolor: a role for the DnaK chaperone as a transcriptional co-repressordagger | Q73312819 | ||
| GroES binding regulates GroEL chaperonin activity under heat shock | Q73374291 | ||
| Positive control of the two-component RcsC/B signal transduction network by DjlA: a member of the DnaJ family of molecular chaperones in Escherichia coli | Q73866641 | ||
| The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network | Q74473349 | ||
| Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP | Q74516881 | ||
| The role of DnaK/DnaJ and GroEL/GroES systems in the removal of endogenous proteins aggregated by heat-shock from Escherichia coli cells | Q74664943 | ||
| Hsc62, a new DnaK homologue of Escherichia coli | Q77293360 | ||
| Structure and function in GroEL-mediated protein folding | Q77366577 | ||
| Purification and characterization of Chromatium vinosum GroEL and GroES proteins overexpressed in Escherichia coli cells lacking the endogenous groESL operon | Q77471933 | ||
| Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor | Q77789106 | ||
| Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains | Q77918974 | ||
| Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers | Q77927053 | ||
| The genetics of disulfide bond metabolism | Q77936221 | ||
| Genome-wide expression profiling in Escherichia coli K-12 | Q24548867 | ||
| The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system | Q24603386 | ||
| Translational induction of heat shock transcription factor sigma32: evidence for a built-in RNA thermosensor | Q24606736 | ||
| Crystal structure of chaperone protein PapD reveals an immunoglobulin fold | Q27690139 | ||
| The crystal structure of the bacterial chaperonin GroEL at 2.8 A | Q27730725 | ||
| Structural analysis of substrate binding by the molecular chaperone DnaK | Q27732810 | ||
| Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK | Q27735852 | ||
| The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex | Q27742747 | ||
| The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis | Q27748258 | ||
| Crystal structure of the signal sequence binding subunit of the signal recognition particle | Q27764928 | ||
| hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures | Q27930675 | ||
| Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins | Q27931364 | ||
| Protein disaggregation mediated by heat-shock protein Hsp104. | Q27940314 | ||
| Principles that govern the folding of protein chains | Q28236872 | ||
| Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains | Q28243957 | ||
| Chaperonins | Q28276039 | ||
| Homologous plant and bacterial proteins chaperone oligomeric protein assembly | Q28283580 | ||
| Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome | Q28294237 | ||
| The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins | Q28302083 | ||
| Regulation of the dnaK operon of Streptomyces coelicolor A3(2) is governed by HspR, an autoregulatory repressor protein | Q28504078 | ||
| Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model | Q28905118 | ||
| Substrate specificity of the SecB chaperone | Q30815173 | ||
| Mycobacteria contain two groEL genes: the second Mycobacterium leprae groEL gene is arranged in an operon with groES. | Q30986453 | ||
| Bacterial genes induced within the nodule during the Rhizobium-legume symbiosis | Q31317183 | ||
| The chaperone/usher pathway: a major terminal branch of the general secretory pathway | Q33538594 | ||
| The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system. | Q33744171 | ||
| Chaperone activity with a redox switch | Q33852523 | ||
| Biochemical characterization of the small heat shock protein IbpB from Escherichia coli. | Q33857365 | ||
| PapD-like chaperones and pilus biogenesis | Q33874589 | ||
| Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. | Q33877945 | ||
| Role of HrcA and CIRCE in the heat shock regulatory network of Bradyrhizobium japonicum | Q33993366 | ||
| The universally conserved GroE (Hsp60) chaperonins | Q33997570 | ||
| Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding | Q34242618 | ||
| Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo | Q34307813 | ||
| Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli | Q42652126 | ||
| Cloning, characterization and functional analysis of groESL operon from thermophilic cyanobacterium Synechococcus vulcanus | Q43025143 | ||
| Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes | Q44169020 | ||
| The activity of sigma 32 is reduced under conditions of excess heat shock protein production in Escherichia coli | Q44527063 | ||
| Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation | Q44653732 | ||
| Heat shock protein GroE of Escherichia coli: key protective roles against thermal stress | Q44843168 | ||
| Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. | Q45975761 | ||
| Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain | Q46375092 | ||
| The Rhizobium meliloti groELc locus is required for regulation of early nod genes by the transcription activator NodD. | Q46489194 | ||
| The ins and outs of a molecular chaperone machine. | Q47289550 | ||
| Streptomyces lividans groES, groEL1 and groEL2 genes | Q48042210 | ||
| Characterization of two groEL genes in Streptomyces coelicolor A3(2). | Q48081654 | ||
| Rhizobium leguminosarum contains multiple chaperonin (cpn60) genes | Q48086658 | ||
| Demonstration by genetic suppression of interaction of GroE products with many proteins | Q50192888 | ||
| A computational approach to simplifying the protein folding alphabet. | Q52133354 | ||
| Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli. | Q53755479 | ||
| Bacterial mutants which block phage assembly. | Q53907471 | ||
| Multivalent binding of nonnative substrate proteins by the chaperonin GroEL. | Q53915559 | ||
| Hyperproduction of recombinant ferredoxins in escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster. | Q53929278 | ||
| Molecular chaperones. Opening and closing the Anfinsen cage. | Q54027466 | ||
| Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli. | Q54059266 | ||
| Trigger factor and DnaK cooperate in folding of newly synthesized proteins. | Q54081409 | ||
| The Escherichia coli chaperonin 60 (groEL) is a potent stimulator of osteoclast formation. | Q54126933 | ||
| In vivo observation of polypeptide flux through the bacterial chaperonin system. | Q54560154 | ||
| Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37 degrees C but not at 43 degrees C. | Q54561981 | ||
| Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro. | Q54577976 | ||
| Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. | Q54582676 | ||
| A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a type III topology. | Q54587487 | ||
| Two different mechanisms are involved in the heat-shock regulation of chaperonin gene expression in Bradyrhizobium japonicum. | Q54594299 | ||
| The functional integration of a polytopic membrane protein of Escherichia coli is dependent on the bacterial signal-recognition particle. | Q54600988 | ||
| Isolation and analysis of mutants of the dnaK operon of Bacillus subtilis. | Q54618437 | ||
| Successive action of Escherichia coli chaperones in vivo. | Q54623330 | ||
| DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli | Q54676319 | ||
| Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat shock protein induction. | Q54690253 | ||
| DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32. | Q54705160 | ||
| GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. | Q54734978 | ||
| Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene. | Q54763507 | ||
| Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli. | Q55060626 | ||
| GroEL under Heat-Shock | Q58660250 | ||
| Protein folding Folding with a two-stroke motor | Q58985812 | ||
| The heat shock response of E. coli is regulated by changes in the concentration of σ32 | Q59067218 | ||
| Identification of in vivo substrates of the chaperonin GroEL | Q59068045 | ||
| GroE is vital for cell-wall synthesis | Q59097794 | ||
| Requirement of the Escherichia coli dnaK gene for thermotolerance and protection against H2O2 | Q68646840 | ||
| The htpR gene product of E. coli is a sigma factor for heat-shock promoters | Q70373280 | ||
| IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock | Q71560881 | ||
| Chaperonins dependent increase of Cu,Zn superoxide dismutase production in Escherichia coli | Q72217252 | ||
| Use of new Escherichia coli/Streptomyces conjugative vectors to probe the functions of the two groEL-like genes of Streptomyces albus G by gene disruption | Q72658672 | ||
| ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli | Q73019220 | ||
| Regulation of the Escherichia coli heat-shock response. | Q34321688 | ||
| Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli | Q34448690 | ||
| Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB. | Q34450730 | ||
| Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli | Q34538968 | ||
| Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli | Q34626779 | ||
| Host participation in bacteriophage lambda head assembly | Q34699367 | ||
| Characterization of twenty-six new heat shock genes of Escherichia coli | Q34729568 | ||
| Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock | Q35593162 | ||
| Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli | Q35608625 | ||
| Cloning and characterization of two groESL operons of Rhodobacter sphaeroides: transcriptional regulation of the heat-induced groESL operon | Q35619035 | ||
| Protein folding in the bacterial periplasm | Q35621918 | ||
| Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo | Q36098016 | ||
| Accumulation of secretory protein precursors in Escherichia coli induces the heat shock response | Q36102319 | ||
| Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli | Q36104983 | ||
| The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export. | Q36174105 | ||
| The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures | Q36174913 | ||
| Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism | Q36176422 | ||
| The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds | Q36177439 | ||
| Delta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures. | Q36184113 | ||
| Ancient heat shock gene is dispensable | Q36207033 | ||
| Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor sigma 32. | Q36211320 | ||
| Escherichia coli dnaK null mutants are inviable at high temperature | Q36226934 | ||
| Isolation and characterization of dnaJ null mutants of Escherichia coli | Q36253137 | ||
| Molecular chaperones and protein translocation across the Escherichia coli inner membrane | Q36490705 | ||
| Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries | Q36857677 | ||
| Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. | Q37697966 | ||
| Disassembly of the Mu transposase tetramer by the ClpX chaperone | Q38291043 | ||
| Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. | Q38316145 | ||
| Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli. | Q38341113 | ||
| Diverse effects of the MalE-LacZ hybrid protein on Escherichia coli cell physiology | Q38350783 | ||
| Nonnative proteins induce expression of the Bacillus subtilis CIRCE regulon. | Q39566254 | ||
| Subcellular localization and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans. | Q39573577 | ||
| Protein unfolding and the energetics of protein translocation across biological membranes | Q39628834 | ||
| An essential role for the Escherichia coli DnaK protein in starvation-induced thermotolerance, H2O2 resistance, and reductive division | Q39837380 | ||
| A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli | Q39837501 | ||
| Regulation of groE expression in Bacillus subtilis: the involvement of the sigma A-like promoter and the roles of the inverted repeat sequence (CIRCE). | Q39838446 | ||
| Induction of heat shock proteins by abnormal proteins results from stabilization and not increased synthesis of sigma 32 in Escherichia coli | Q39897948 | ||
| CIRCE, a novel heat shock element involved in regulation of heat shock operon dnaK of Bacillus subtilis | Q39930774 | ||
| Effects of reduced levels of GroE chaperones on protein metabolism: enhanced synthesis of heat shock proteins during steady-state growth of Escherichia coli | Q39932652 | ||
| A survey of the heat shock response in four Streptomyces species reveals two groEL-like genes and three groEL-like proteins in Streptomyces albus | Q39946461 | ||
| The general concept of molecular chaperones | Q40709976 | ||
| Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12 | Q40790970 | ||
| An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY. | Q40791891 | ||
| DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. | Q40874220 | ||
| Organization and expression of the dnaJ and dnaK genes of Escherichia coli K12 | Q40947479 | ||
| The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. | Q41006640 | ||
| Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES. | Q41042572 | ||
| Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly | Q41068120 | ||
| Purification and properties of groE, a host protein involved in bacteriophage assembly | Q41068128 | ||
| Escherichia coli heat shock gene mutants are defective in proteolysis | Q41392673 | ||
| At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease | Q41633089 | ||
| The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. | Q41633923 | ||
| Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. | Q41634708 | ||
| Chaperonin function: folding by forced unfolding | Q42097312 | ||
| Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. | Q42247311 | ||
| Cloning and characterization of multiple groEL chaperonin-encoding genes in Rhizobium meliloti | Q42601555 | ||
| Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding | Q42608426 | ||
| The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis | Q42625880 | ||
| The dnaK operon of Streptomyces coelicolor encodes a novel heat-shock protein which binds to the promoter region of the operon | Q42638102 | ||
| The Escherichia coli SRP and SecB targeting pathways converge at the translocon | Q42643547 | ||
| P921 | main subject | molecular chaperones | Q422496 |
| P304 | page(s) | 93-140 | |
| P577 | publication date | 2001-01-01 | |
| P1433 | published in | Advances in Microbial Physiology | Q15753070 |
| P1476 | title | Microbial molecular chaperones | |
| P478 | volume | 44 |
| Q36539638 | A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection |
| Q27642847 | A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function |
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| Q34856001 | Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L. |
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