Published in Cell Stress Chaperones on April 01, 1996
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Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature (1999) 2.95
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Chaperone function of Hsp90-associated proteins. Science (1996) 2.66
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Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol (2001) 2.54
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Hsp26: a temperature-regulated chaperone. EMBO J (1999) 2.51
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Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Biol (2000) 2.37
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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
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ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature (2006) 2.09
Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc Natl Acad Sci U S A (1998) 2.04
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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
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Osmoregulation of the maltose regulon in Escherichia coli. J Bacteriol (1986) 1.85
Coordinated ATP hydrolysis by the Hsp90 dimer. J Biol Chem (2001) 1.79
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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
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Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J Biol Chem (2000) 1.65
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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
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
Symmetric complexes of GroE chaperonins as part of the functional cycle. Science (1994) 1.48
GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry (1997) 1.48
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On the role of groES in the chaperonin-assisted folding reaction. Three case studies. J Biol Chem (1994) 1.43
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Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of alpha-glucosidase from yeast. Biochemistry (1991) 1.34
How chaperones fold proteins. Biol Chem (1998) 1.33
The Hsp90 complex--a super-chaperone machine as a novel drug target. Biochem Pharmacol (1998) 1.31
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
Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. J Mol Biol (2001) 1.27
Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett (2004) 1.23
Assessment of the ATP binding properties of Hsp90. J Biol Chem (1996) 1.21
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
The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species. J Biol Chem (1999) 1.20
C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle. J Mol Biol (2000) 1.18
Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. Biochemistry (2001) 1.17
Identification of the prolyl isomerase domain of Escherichia coli trigger factor. FEBS Lett (1996) 1.17
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BiP binding sequences in antibodies. J Biol Chem (1995) 1.16
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An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. J Mol Biol (1999) 1.14
Interaction of GroE with an all-beta-protein. J Biol Chem (1992) 1.12
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
Catalysis of protein folding by symmetric chaperone complexes. Proc Natl Acad Sci U S A (1997) 1.09
Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli. EMBO J (1998) 1.09
Association of antibody chains at different stages of folding: prolyl isomerization occurs after formation of quaternary structure. J Mol Biol (1995) 1.08
Prolyl isomerases catalyze antibody folding in vitro. Protein Sci (1993) 1.08
Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains. J Bacteriol (2004) 1.07
Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function. J Biol Chem (1995) 1.07
Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties. J Biol Chem (2000) 1.07
ATP-binding properties of human Hsp90. J Biol Chem (1997) 1.06
Mechanism of substrate recognition by Hsp70 chaperones. Biochem Soc Trans (2004) 1.05
Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization. J Mol Biol (1999) 1.03
Folding and association of beta-Galactosidase. J Mol Biol (1998) 1.03
Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins. Biol Chem (2001) 1.01
Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32. J Bacteriol (1999) 1.01
Functional characterization of the higher plant chloroplast chaperonins. J Biol Chem (1995) 1.01
BiP and PDI cooperate in the oxidative folding of antibodies in vitro. J Biol Chem (2000) 1.01
The Escherichia coli trigger factor. FEBS Lett (1996) 1.01
The N-terminal region of the 37-kDa translocated fragment of Pseudomonas exotoxin A aborts translocation by promoting its own export after microsomal membrane insertion. Proc Natl Acad Sci U S A (1993) 1.00