Proteolysis in prokaryotes: protein quality control and regulatory principles.

Transcriptome analysis of Crp-dependent catabolite control of gene expression in Escherichia coli. J Bacteriol (2004) 2.20

Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates. Genes Dev (2004) 2.11

Global regulatory impact of ClpP protease of Staphylococcus aureus on regulons involved in virulence, oxidative stress response, autolysis, and DNA repair. J Bacteriol (2006) 1.58

A peptide signal for adapter protein-mediated degradation by the AAA+ protease ClpCP. Mol Cell (2007) 1.32

Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR. J Bacteriol (2007) 1.11

ClpP of Streptococcus mutans differentially regulates expression of genomic islands, mutacin production, and antibiotic tolerance. J Bacteriol (2009) 1.09

ClpC1, an ATP-dependent Clp protease in plastids, is involved in iron homeostasis in Arabidopsis leaves. Ann Bot (2010) 0.99

The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies. Proc Natl Acad Sci U S A (2011) 0.94

Genome-wide survey of prokaryotic serine proteases: analysis of distribution and domain architectures of five serine protease families in prokaryotes. BMC Genomics (2008) 0.91

Mechanical design of translocating motor proteins. Cell Biochem Biophys (2009) 0.90

Primary metabolism in Lactobacillus sakei food isolates by proteomic analysis. BMC Microbiol (2010) 0.84

The ClpP protease homologue is required for the transmission traits and cell division of the pathogen Legionella pneumophila. BMC Microbiol (2010) 0.84

Transcription of clpP is enhanced by a unique tandem repeat sequence in Streptococcus mutans. J Bacteriol (2008) 0.83

Exploring the genomic traits of fungus-feeding bacterial genus Collimonas. BMC Genomics (2015) 0.80

Distinct features of protein folding by the GroEL system from a psychrophilic bacterium, Colwellia psychrerythraea 34H. Extremophiles (2012) 0.79

Functional expression, purification, and biochemical properties of subtilase SprP from Pseudomonas aeruginosa. Microbiologyopen (2015) 0.77

Novel chaperonins in a prokaryote. J Mol Evol (2005) 0.76

Distribution, classification, domain architectures and evolution of prolyl oligopeptidases in prokaryotic lineages. BMC Genomics (2014) 0.75

The rpoH gene encoding heat shock sigma factor sigma32 of psychrophilic bacterium Colwellia maris. Extremophiles (2005) 0.75

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

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

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

M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell (2007) 1.72

Characterization of a trap mutant of the AAA+ chaperone ClpB. J Biol Chem (2003) 1.65

Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J (2012) 1.62

Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat Struct Mol Biol (2011) 1.54

Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones. Mol Cell (2008) 1.51

Adaptor protein controlled oligomerization activates the AAA+ protein ClpC. EMBO J (2006) 1.49

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

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

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

Structure and function of the molecular chaperone Trigger Factor. Biochim Biophys Acta (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

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

Unscrambling an egg: protein disaggregation by AAA+ proteins. Microb Cell Fact (2004) 1.19

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

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

The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins. Mol Cell Biol (2009) 1.10

Influence of GrpE on DnaK-substrate interactions. J Biol Chem (2004) 1.10

Toc12, a novel subunit of the intermembrane space preprotein translocon of chloroplasts. Mol Biol Cell (2004) 1.09

The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity. J Biol Chem (2006) 1.09

Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc Natl Acad Sci U S A (2008) 1.08

Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins. Biol Chem (2011) 1.04

Reshaping of the conformational search of a protein by the chaperone trigger factor. Nature (2013) 1.01

ClpS is the recognition component for Escherichia coli substrates of the N-end rule degradation pathway. Mol Microbiol (2009) 1.00

Structure and function of a novel type of ATP-dependent Clp protease. J Biol Chem (2009) 1.00

Broad yet high substrate specificity: the challenge of AAA+ proteins. J Struct Biol (2004) 0.99

Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity. J Biol Chem (2005) 0.97

Large-scale purification of ribosome-nascent chain complexes for biochemical and structural studies. FEBS Lett (2009) 0.97

YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein? Structure (2006) 0.95

Structural analysis of the ribosome-associated complex (RAC) reveals an unusual Hsp70/Hsp40 interaction. J Biol Chem (2009) 0.95

Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding. Nat Struct Mol Biol (2013) 0.95

Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding. FEBS J (2008) 0.93

Selective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes. Nat Protoc (2013) 0.93

A PDZ switch for a cellular stress response. Cell (2004) 0.93

The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. J Biol Chem (2010) 0.92

Aha, another regulator for hsp90 chaperones. Mol Cell (2002) 0.88

Molecular chaperones: structure of a protein disaggregase. Curr Biol (2004) 0.86

Principles of general and regulatory proteolysis by AAA+ proteases in Escherichia coli. Res Microbiol (2009) 0.85

Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones. J Biol Chem (2002) 0.85

DegP: a Protein "Death Star". Structure (2008) 0.84

Integrating protein homeostasis strategies in prokaryotes. Cold Spring Harb Perspect Biol (2011) 0.83

Cell biology. When the beginning marks the end. Science (2010) 0.82

Poly-L-lysine enhances the protein disaggregation activity of ClpB. FEBS Lett (2003) 0.81

Nucleotide exchange factors for Hsp70 chaperones. Methods Mol Biol (2011) 0.81

Trigger factor finds new jobs and contacts. Nat Struct Mol Biol (2009) 0.81

Ribosomes catch Hsp70s. Nat Struct Mol Biol (2005) 0.81

Mechanism of Hsp104/ClpB inhibition by prion curing Guanidinium hydrochloride. FEBS Lett (2013) 0.80

Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior. BMC Genomics (2013) 0.78

Global profiling of SRP interaction with nascent polypeptides. Nature (2016) 0.77

Telling right from wrong in life - cellular quality control. Nat Rev Mol Cell Biol (2013) 0.77

Crystallization and preliminary X-ray analysis of the Escherichia coli adaptor protein ClpS, free and in complex with the N-terminal domain of ClpA. Acta Crystallogr D Biol Crystallogr (2002) 0.77

18 The busy life of nascent chains: mechanisms of folding of newly synthesized proteins. J Biomol Struct Dyn (2015) 0.75

[Molecular mechanism of Hsp70 chaperones]. Tanpakushitsu Kakusan Koso (2002) 0.75

A folding machine for many but a master of none. Nat Struct Biol (2003) 0.75