The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
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Human Sug1/p45 is involved in the proteasome-dependent degradation of Sp1The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitroCompetence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor.Unscrambling an egg: protein disaggregation by AAA+ proteinsExpression of the heat shock gene clpL of Streptococcus thermophilus is induced by both heat and cold shockStructural Switching of Staphylococcus aureus Clp Protease: A KEY TO UNDERSTANDING PROTEASE DYNAMICSThe molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria.Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machineProteomic analysis of free-living Bradyrhizobium diazoefficiens: highlighting potential determinants of a successful symbiosis.Heat resistance mediated by a new plasmid encoded Clp ATPase, ClpK, as a possible novel mechanism for nosocomial persistence of Klebsiella pneumoniae.TasA-tasB, a new putative toxin-antitoxin (TA) system from Bacillus thuringiensis pGI1 plasmid is a widely distributed composite mazE-doc TA system.Proteomic analysis of stationary phase in the marine bacterium "Candidatus Pelagibacter ubique".Genome-wide analysis of rice ClpB/HSP100, ClpC and ClpD genes.Formation of the preprimosome protects lambda O from RNA transcription-dependent proteolysis by ClpP/ClpX.The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpPThe chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathwaysInteractions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP.Chaperone rings in protein folding and degradation.Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone.An essential protease involved in bacterial cell-cycle control.Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Identification and transcriptional control of the genes encoding the Caulobacter crescentus ClpXP protease.The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coliBiochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome.ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence.ClpX contributes to innate defense peptide resistance and virulence phenotypes of Bacillus anthracis.Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli.Subunit interactions influence the biochemical and biological properties of Hsp104Regulation of SOS mutagenesis by proteolysis.Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.Chaperones in control of protein disaggregation.MecA, an adaptor protein necessary for ClpC chaperone activity.Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.Bacteriophage Mu repressor as a target for the Escherichia coli ATP-dependent Clp ProteaseClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis.Here's the hook: similar substrate binding sites in the chaperone domains of Clp and Lon.Roles of molecular chaperones in protein degradation.Nucleotide-dependent oligomerization of ClpB from Escherichia coli.
P2860
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P2860
The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
description
1995 nî lūn-bûn
@nan
1995 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@ast
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@en
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@nl
type
label
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@ast
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@en
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@nl
prefLabel
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@ast
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@en
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@nl
P2093
P2860
P3181
P1433
P1476
The ClpX heat-shock protein of ...... is a novel molecular chaperone
@en
P2093
A Wawrzynow
C Georgopoulos
D Wojtkowiak
J Marszalek
P2860
P304
P3181
P407
P577
1995-05-01T00:00:00Z