Published in Mol Cell on November 07, 2008
Chaperone machines for protein folding, unfolding and disaggregation. Nat Rev Mol Cell Biol (2013) 2.24
Proteotoxic stress induces a cell-cycle arrest by stimulating Lon to degrade the replication initiator DnaA. Cell (2013) 1.86
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat Chem Biol (2010) 1.59
Multiple controls affect arsenite oxidase gene expression in Herminiimonas arsenicoxydans. BMC Microbiol (2010) 1.59
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Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles. Cell (2014) 1.46
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VapC6, a ribonucleolytic toxin regulates thermophilicity in the crenarchaeote Sulfolobus solfataricus. RNA (2011) 0.96
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A chaperone trap contributes to the onset of cystic fibrosis. PLoS One (2012) 0.93
A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1. Cell Rep (2014) 0.91
Key features of σS required for specific recognition by Crl, a transcription factor promoting assembly of RNA polymerase holoenzyme. Proc Natl Acad Sci U S A (2013) 0.89
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Arabidopsis J-protein J20 delivers the first enzyme of the plastidial isoprenoid pathway to protein quality control. Plant Cell (2013) 0.87
A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli. J Biol Chem (2012) 0.86
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Role of Streptococcus intermedius DnaK chaperone system in stress tolerance and pathogenicity. Cell Stress Chaperones (2011) 0.86
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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
Rehosting of bacterial chaperones for high-quality protein production. Appl Environ Microbiol (2009) 0.84
Analysis of chaperone mRNA expression in the adult mouse brain by meta analysis of the Allen Brain Atlas. PLoS One (2010) 0.84
Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery. Protein Sci (2012) 0.83
Proteolysis in the Escherichia coli heat shock response: a player at many levels. Curr Opin Microbiol (2011) 0.83
Multiple molecules of Hsc70 and a dimer of DjA1 independently bind to an unfolded protein. J Biol Chem (2010) 0.83
Integrating protein homeostasis strategies in prokaryotes. Cold Spring Harb Perspect Biol (2011) 0.83
DnaJ (Hsp40 protein) binding to folded substrate impacts KplE1 prophage excision efficiency. J Biol Chem (2012) 0.82
Molecular mechanism of thermosensory function of human heat shock transcription factor Hsf1. Elife (2016) 0.82
Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. Front Mol Biosci (2014) 0.82
Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome. Mol Biosyst (2012) 0.82
Synergistic binding of DnaJ and DnaK chaperones to heat shock transcription factor σ32 ensures its characteristic high metabolic instability: implications for heat shock protein 70 (Hsp70)-Hsp40 mode of function. J Biol Chem (2012) 0.81
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DnaJ-promoted binding of DnaK to multiple sites on σ32 in the presence of ATP. J Bacteriol (2014) 0.80
Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: binding and remodeling of a native substrate. J Biol Chem (2013) 0.80
Late steps of ribosome assembly in E. coli are sensitive to a severe heat stress but are assisted by the HSP70 chaperone machine. Nucleic Acids Res (2010) 0.80
The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity. PLoS One (2012) 0.80
Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control. Microb Cell Fact (2011) 0.77
Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles. Elife (2017) 0.77
A Novel SRP Recognition Sequence in the Homeostatic Control Region of Heat Shock Transcription Factor σ(32). Sci Rep (2016) 0.76
A structural insight into the prokaryotic heat shock transcription regulatory protein σ(32): an implication of σ(32)-DnaK interaction. Bioinformation (2012) 0.75
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Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell (2004) 4.90
Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol (2010) 3.54
Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol Cell (2010) 3.23
The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat Struct Mol Biol (2009) 3.21
L23 protein functions as a chaperone docking site on the ribosome. Nature (2002) 2.68
The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol (2007) 2.64
Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo. Cell (2011) 2.55
Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J (2006) 2.45
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature (2004) 2.41
Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol (2003) 2.31
ClpS, a substrate modulator of the ClpAP machine. Mol Cell (2002) 2.28
Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J Biol Chem (2003) 2.26
Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing. EMBO J (2010) 2.25
Substrate recognition by the AAA+ chaperone ClpB. Nat Struct Mol Biol (2004) 2.19
AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett (2002) 2.10
Protein interaction networks by proteome peptide scanning. PLoS Biol (2004) 1.92
Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J Biol Chem (2006) 1.90
Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem (2003) 1.89
Allosteric regulation of Hsp70 chaperones by a proline switch. Mol Cell (2006) 1.88
Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol Microbiol (2008) 1.85
Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol Cell (2012) 1.84
Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli. BMC Biotechnol (2007) 1.80
Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation. J Biol Chem (2006) 1.78
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Mol Microbiol (2003) 1.77
MecA, an adaptor protein necessary for ClpC chaperone activity. Proc Natl Acad Sci U S A (2003) 1.76
Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration. J Biol Chem (2004) 1.74
M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell (2007) 1.72
Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity. J Mol Biol (2011) 1.66
Characterization of a trap mutant of the AAA+ chaperone ClpB. J Biol Chem (2003) 1.65
Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. EMBO J (2009) 1.62
Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J (2012) 1.62
A tale of two oxidation states: bacterial colonization of arsenic-rich environments. PLoS Genet (2007) 1.59
Multiple controls affect arsenite oxidase gene expression in Herminiimonas arsenicoxydans. BMC Microbiol (2010) 1.59
A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants. Proc Natl Acad Sci U S A (2002) 1.58
Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat Struct Mol Biol (2011) 1.54
iTRAQ and multiple reaction monitoring as proteomic tools for biomarker search in cerebrospinal fluid of patients with Parkinson's disease dementia. Exp Neurol (2012) 1.52
Allostery in the Hsp70 chaperone proteins. Top Curr Chem (2013) 1.52
Adaptor protein controlled oligomerization activates the AAA+ protein ClpC. EMBO J (2006) 1.49
SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of interleukin-6 signaling through gp130. J Biol Chem (2002) 1.48
WW domain sequence activity relationships identified using ligand recognition propensities of 42 WW domains. Protein Sci (2003) 1.46
Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol (2012) 1.46
Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J Cell Biol (2011) 1.45
Hsp110 is a nucleotide-activated exchange factor for Hsp70. J Biol Chem (2008) 1.45
Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit Rev Biochem Mol Biol (2005) 1.43
Molecular mechanism and structure of Trigger Factor bound to the translating ribosome. EMBO J (2008) 1.41
Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. Mol Cell (2003) 1.40
Recognition of proline-rich motifs by protein-protein-interaction domains. Angew Chem Int Ed Engl (2005) 1.39
Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. J Biol Chem (2003) 1.39
Trigger factor forms a protective shield for nascent polypeptides at the ribosome. J Biol Chem (2006) 1.38
Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat Struct Biol (2002) 1.38
Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat Struct Mol Biol (2008) 1.35
Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology. J Biotechnol (2002) 1.34
Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling. J Biol Chem (2007) 1.33
The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition. J Biol Chem (2005) 1.30
Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor. Proc Natl Acad Sci U S A (2004) 1.28
Dynamics of trigger factor interaction with translating ribosomes. J Biol Chem (2007) 1.28
Correlation of levels of folded recombinant p53 in escherichia coli with thermodynamic stability in vitro. J Mol Biol (2007) 1.27
Peptide arrays: from macro to micro. Curr Opin Biotechnol (2002) 1.26
Structure and function of the molecular chaperone Trigger Factor. Biochim Biophys Acta (2010) 1.26
Asna1/TRC40-mediated membrane insertion of tail-anchored proteins. J Cell Sci (2010) 1.26
Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS One (2008) 1.26
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nat Struct Mol Biol (2012) 1.26
Metabolic diversity among main microorganisms inside an arsenic-rich ecosystem revealed by meta- and proteo-genomics. ISME J (2011) 1.24
Chaperone networks in protein disaggregation and prion propagation. J Struct Biol (2012) 1.23
Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange. J Biol Chem (2003) 1.23
Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett (2005) 1.22
Deuteration distribution estimation with improved sequence coverage for HX/MS experiments. Bioinformatics (2010) 1.22
Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nat Struct Mol Biol (2009) 1.22
Posttranscriptional control of quorum-sensing-dependent virulence genes by DksA in Pseudomonas aeruginosa. J Bacteriol (2003) 1.21
Unscrambling an egg: protein disaggregation by AAA+ proteins. Microb Cell Fact (2004) 1.19
Synthesis of an Array Comprising 837 Variants of the hYAP WW Protein Domain This work was supported by the DFG (INK 16/B1-1), by the Fonds der Chemischen Industrie, and by the Universitätsklinikum Charité Berlin. Angew Chem Int Ed Engl (2001) 1.18
Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochem Cell Biol (2010) 1.18
A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing. Nature (2008) 1.16
Proteolysis in prokaryotes: protein quality control and regulatory principles. Mol Microbiol (2003) 1.14
Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. J Biol Chem (2004) 1.13
Translation suppression promotes stress granule formation and cell survival in response to cold shock. Mol Biol Cell (2012) 1.13
Functional analysis of Hsp70 inhibitors. PLoS One (2013) 1.13
A tightly regulated molecular toggle controls AAA+ disaggregase. Nat Struct Mol Biol (2012) 1.13
Common and specific mechanisms of AAA+ proteins involved in protein quality control. Biochem Soc Trans (2008) 1.13
Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol Chem (2005) 1.12
Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding. Mol Cell (2012) 1.12
SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria. Mol Cell (2011) 1.12
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. FEBS Lett (2004) 1.12
Three-state equilibrium of Escherichia coli trigger factor. Biol Chem (2002) 1.11