Published in Proc Natl Acad Sci U S A on November 23, 1999
Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci (2005) 9.75
Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res (2006) 4.25
Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol Mol Biol Rev (2002) 2.80
Characterization of the Staphylococcus aureus heat shock, cold shock, stringent, and SOS responses and their effects on log-phase mRNA turnover. J Bacteriol (2006) 2.50
The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis. J Bacteriol (2001) 2.40
Global transcriptome analysis of the heat shock response of Shewanella oneidensis. J Bacteriol (2004) 2.28
Mechanism of prion loss after Hsp104 inactivation in yeast. Mol Cell Biol (2001) 2.27
Chaperone machines for protein folding, unfolding and disaggregation. Nat Rev Mol Cell Biol (2013) 2.24
Genome-wide identification of Francisella tularensis virulence determinants. Infect Immun (2007) 2.09
Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family. Plant Physiol (2001) 2.09
Chaperones in control of protein disaggregation. EMBO J (2008) 2.01
Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics (2004) 1.90
Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell (2007) 1.82
Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli. BMC Biotechnol (2007) 1.80
Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J (2002) 1.79
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat Struct Mol Biol (2007) 1.77
MecA, an adaptor protein necessary for ClpC chaperone activity. Proc Natl Acad Sci U S A (2003) 1.76
The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One (2011) 1.74
Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J (2012) 1.62
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat Chem Biol (2010) 1.59
J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. EMBO J (2007) 1.57
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell (2007) 1.56
Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding. Mol Cell Biol (2004) 1.55
Allostery in the Hsp70 chaperone proteins. Top Curr Chem (2013) 1.52
Plasma membrane cyclic nucleotide gated calcium channels control land plant thermal sensing and acquired thermotolerance. Plant Cell (2012) 1.49
A stromal heat shock protein 70 system functions in protein import into chloroplasts in the moss Physcomitrella patens. Plant Cell (2010) 1.46
Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc Natl Acad Sci U S A (2006) 1.45
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J (2006) 1.44
A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases. Mol Microbiol (2006) 1.43
Chaperone networks: tipping the balance in protein folding diseases. Neurobiol Dis (2010) 1.42
Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem (2005) 1.38
Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci U S A (2011) 1.37
The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J Mol Biol (2010) 1.36
Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J Biol Chem (2008) 1.34
Transcriptome profiling reveals the importance of plasmid pSymB for osmoadaptation of Sinorhizobium meliloti. J Bacteriol (2006) 1.33
Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. Cell Stress Chaperones (2005) 1.32
Protein rescue from aggregates by powerful molecular chaperone machines. Nat Rev Mol Cell Biol (2013) 1.31
Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system. Proc Natl Acad Sci U S A (2007) 1.30
Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains. J Biol Chem (2000) 1.30
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. Nature (2015) 1.29
Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region. Mol Biol Cell (2004) 1.29
Role of the Clp system in stress tolerance, biofilm formation, and intracellular invasion in Porphyromonas gingivalis. J Bacteriol (2007) 1.28
Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol (2011) 1.27
Large scale comparative proteomics of a chloroplast Clp protease mutant reveals folding stress, altered protein homeostasis, and feedback regulation of metabolism. Mol Cell Proteomics (2009) 1.27
Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J Biol Chem (2013) 1.27
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nat Struct Mol Biol (2012) 1.26
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife (2014) 1.25
Unscrambling an egg: protein disaggregation by AAA+ proteins. Microb Cell Fact (2004) 1.19
Applying Hsp104 to protein-misfolding disorders. Biochem Cell Biol (2010) 1.18
Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system. Plant Cell (2005) 1.17
Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB. Protein Sci (2004) 1.17
The Chlamydomonas genome reveals its secrets: chaperone genes and the potential roles of their gene products in the chloroplast. Photosynth Res (2004) 1.16
ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit. Nat Struct Mol Biol (2010) 1.16
How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. J Mol Biol (2015) 1.15
Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu transposase. Protein Sci (2005) 1.14
Inactivation of clpB in the pathogen Leptospira interrogans reduces virulence and resistance to stress conditions. Infect Immun (2011) 1.14
Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity. Proc Natl Acad Sci U S A (2005) 1.13
A tightly regulated molecular toggle controls AAA+ disaggregase. Nat Struct Mol Biol (2012) 1.13
Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease. Mol Biol Cell (2011) 1.12
Structure and function of the middle domain of ClpB from Escherichia coli. Biochemistry (2003) 1.11
Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor. Proc Natl Acad Sci U S A (2013) 1.10
Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. Cell Stress Chaperones (2010) 1.10
Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proc Natl Acad Sci U S A (2002) 1.10
The elusive middle domain of Hsp104 and ClpB: location and function. Biochim Biophys Acta (2011) 1.09
GroES/GroEL and DnaK/DnaJ have distinct roles in stress responses and during cell cycle progression in Caulobacter crescentus. J Bacteriol (2006) 1.09
Sequence determinants of protein aggregation: tools to increase protein solubility. Microb Cell Fact (2005) 1.09
Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation. Front Mol Biosci (2015) 1.07
Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB. Protein Sci (2009) 1.03
The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies. Microb Cell Fact (2005) 1.02
Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones. J Biol Chem (2010) 1.00
Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli. Protein Sci (2002) 1.00
Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics (2012) 0.99
Influence of Hsp70s and their regulators on yeast prion propagation. Prion (2009) 0.99
Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli. Biochemistry (2002) 0.99
The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942. J Bacteriol (2000) 0.98
Metazoan Hsp70-based protein disaggregases: emergence and mechanisms. Front Mol Biosci (2015) 0.97
The metabolic potential of Escherichia coli BL21 in defined and rich medium. Microb Cell Fact (2014) 0.97
Regulatory circuits of the AAA+ disaggregase Hsp104. J Biol Chem (2011) 0.97
Toward a semisynthetic stress response system to engineer microbial solvent tolerance. MBio (2012) 0.96
Structural basis for intersubunit signaling in a protein disaggregating machine. Proc Natl Acad Sci U S A (2012) 0.96
Molecular chaperones and the assembly of the prion Ure2p in vitro. J Biol Chem (2008) 0.95
Insights into the Clp/HSP100 chaperone system from chloroplasts of Arabidopsis thaliana. J Biol Chem (2011) 0.95
Aggregate reactivation mediated by the Hsp100 chaperones. Arch Biochem Biophys (2012) 0.95
Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones. Front Mol Biosci (2015) 0.95
The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. Microb Cell Fact (2006) 0.95
Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. J Biol Chem (2013) 0.94
Characterization of Brucella suis clpB and clpAB mutants and participation of the genes in stress responses. J Bacteriol (2001) 0.94
The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion. PLoS One (2009) 0.94
Synergistic cooperation between two ClpB isoforms in aggregate reactivation. J Mol Biol (2009) 0.91
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins. Cell Mol Life Sci (2014) 0.89
Heat shock proteins in relation to heat stress tolerance of creeping bentgrass at different N levels. PLoS One (2014) 0.88
Production of recombinant proteins in the lon-deficient BL21(DE3) strain of Escherichia coli in the absence of the DnaK chaperone. Appl Environ Microbiol (2009) 0.88
Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation. J Mol Biol (2014) 0.87
Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machine. J Struct Biol (2012) 0.87
Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis. PLoS One (2013) 0.87
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. J Biol Chem (2014) 0.85
RNA-Seq analysis of the multipartite genome of Rhizobium etli CE3 shows different replicon contributions under heat and saline shock. BMC Genomics (2014) 0.85
Pathways of allosteric regulation in Hsp70 chaperones. Nat Commun (2015) 0.85
Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system. Cell Stress Chaperones (2011) 0.85
Molecular chaperones: guardians of the proteome in normal and disease states. F1000Res (2015) 0.85
The Hsp70 and Hsp60 chaperone machines. Cell (1998) 13.79
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science (1995) 8.66
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell (1998) 7.69
Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science (1996) 7.24
Protein disaggregation mediated by heat-shock protein Hsp104. Nature (1994) 6.27
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature (1999) 4.57
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J (1993) 4.32
Hsp104 is required for tolerance to many forms of stress. EMBO J (1992) 3.72
Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci U S A (1999) 3.30
Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem Cytochem (1989) 3.26
Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci U S A (1999) 2.54
Deadly conformations--protein misfolding in prion disease. Cell (1997) 2.30
The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem (1998) 2.23
The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase. J Biol Chem (1992) 1.92
Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity. J Biol Chem (1993) 1.58
Binding of the dye congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences. J Mol Biol (1992) 1.52
Two simple methods for quantifying low-affinity dye-substrate binding. J Histochem Cytochem (1989) 1.45
Protein self-organization in vitro and in vivo: partitioning between physical biochemistry and cell biology. Biol Chem (1998) 1.03
Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci (2005) 9.75
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J (1993) 4.32
Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J (1997) 4.28
Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32. Cell (1992) 3.46
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc Natl Acad Sci U S A (1994) 3.33
Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci U S A (1999) 3.30
Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J (1999) 3.20
Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. EMBO J (1995) 3.18
The role of ATP in the functional cycle of the DnaK chaperone system. J Mol Biol (1995) 3.00
Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature (1999) 2.95
A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J (1996) 2.55
Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol (2001) 2.54
Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J Biol Chem (1995) 2.53
Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Biol (2000) 2.37
A xylose-inducible Bacillus subtilis integration vector and its application. Gene (1996) 2.36
Interaction of Hsp70 chaperones with substrates. Nat Struct Biol (1997) 2.26
Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Proc Natl Acad Sci U S A (1998) 2.10
ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature (2006) 2.09
The heat shock response of Escherichia coli. Int J Food Microbiol (2000) 2.02
Cell growth and lambda phage development controlled by the same essential Escherichia coli gene, ftsH/hflB. Proc Natl Acad Sci U S A (1993) 1.97
The second step of ATP binding to DnaK induces peptide release. J Mol Biol (1996) 1.96
Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J (2001) 1.94
The dnaK operon of Bacillus subtilis is heptacistronic. J Bacteriol (1997) 1.89
Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria. J Mol Biol (1996) 1.85
Osmoregulation of the maltose regulon in Escherichia coli. J Bacteriol (1986) 1.85
Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol Microbiol (1999) 1.80
The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J (1994) 1.71
Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci U S A (1996) 1.69
Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. J Mol Biol (1999) 1.69
Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli. Mol Microbiol (1998) 1.68
Hsp70 chaperone machines. Adv Protein Chem (2001) 1.67
Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J Biol Chem (2000) 1.65
A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat Struct Biol (1994) 1.64
Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli. Mol Microbiol (1997) 1.62
Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Nat Struct Biol (2001) 1.61
A module of the DnaJ heat shock proteins found in malaria parasites. Trends Biochem Sci (1992) 1.60
Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question. Cell Mol Life Sci (2002) 1.58
Structure and function of the ftsH gene in Escherichia coli. Res Microbiol (1991) 1.56
Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J Biol Chem (2001) 1.52
Hsp70 chaperone systems: diversity of cellular functions and mechanism of action. Biol Chem (1998) 1.51
Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. J Biol Chem (1999) 1.50
Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of sigma32 in vivo. Mol Microbiol (1998) 1.48
GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry (1997) 1.48
The ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion. Mol Microbiol (1997) 1.47
Escherichia coli mutant Y16 is a double mutant carrying thermosensitive ftsH and ftsI mutations. J Bacteriol (1992) 1.45
Binding specificity of Escherichia coli trigger factor. Proc Natl Acad Sci U S A (2001) 1.45
Molecular chaperones: the busy life of Hsp90. Curr Biol (1999) 1.42
Reconstitution of maltose transport in Escherichia coli: conditions affecting import of maltose-binding protein into the periplasm of calcium-treated cells. J Bacteriol (1983) 1.40
The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. J Biol Chem (1995) 1.39
Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J Mol Biol (1996) 1.28
The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J Cell Biol (1997) 1.28
Molecular basis for interactions of the DnaK chaperone with substrates. Biol Chem (2001) 1.28
A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product. Microbiology (1994) 1.27
Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett (2004) 1.23
Post-transcriptional regulation of the Bacillus subtilis dnaK operon. Mol Microbiol (1999) 1.23
SpoVM, a small protein essential to development in Bacillus subtilis, interacts with the ATP-dependent protease FtsH. J Bacteriol (1997) 1.22
Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators. FEBS Lett (1995) 1.21
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J Biol Chem (1997) 1.20
Identification of the prolyl isomerase domain of Escherichia coli trigger factor. FEBS Lett (1996) 1.17
Contrasting mechanisms of envZ control of mal and pho regulon genes in Escherichia coli. J Bacteriol (1986) 1.16
Substrate specificity of the SecB chaperone. J Biol Chem (1999) 1.11
Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. J Mol Biol (2000) 1.11
Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli. EMBO J (1998) 1.09
Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains. J Bacteriol (2004) 1.07
Mechanism of substrate recognition by Hsp70 chaperones. Biochem Soc Trans (2004) 1.05
Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32. J Bacteriol (1999) 1.01
Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins. Biol Chem (2001) 1.01
The Escherichia coli trigger factor. FEBS Lett (1996) 1.01
The Bacillus subtilis htpG gene is not involved in thermal stress management. Mol Gen Genet (1999) 1.00
Protein turnover: a CHIP programmed for proteolysis. Curr Biol (2002) 0.99
Ca2+-induced permeabilization of the Escherichia coli outer membrane: comparison of transformation and reconstitution of binding-protein-dependent transport. J Bacteriol (1985) 0.97
The C terminus of sigma(32) is not essential for degradation by FtsH. J Bacteriol (2001) 0.96
The tolZ gene of Escherichia coli is identified as the ftsH gene. J Bacteriol (1996) 0.92
Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication. J Biol Chem (1999) 0.85
Construction and analysis of hybrid Escherichia coli-Bacillus subtilis dnaK genes. J Bacteriol (1999) 0.82
Integrative vector for constructing single-copy translational fusions between regulatory regions of Bacillus subtilis and the bgaB reporter gene encoding a heat-stable beta-galactosidase. FEMS Microbiol Lett (1997) 0.81
The gene for cadmium metallothionein from a cadmium-resistant yeast appears to be identical to CUP1 in a copper-resistant strain. Curr Genet (1992) 0.80
Low temperature of GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor DnaK. FEBS Lett (2005) 0.78
Chaperone function on Crete: a meeting report. Cell Stress Chaperones (1996) 0.75
Solution synthesis of human peptide YY (hPYY). Chem Pharm Bull (Tokyo) (1990) 0.75