Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.
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The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging systemRegulation of clpQ⁺Y⁺ (hslV⁺U⁺) gene expression in Escherichia coliMutational studies on HslU and its docking mode with HslVCrystal structure of heat shock locus V (HslV) from Escherichia coliRegulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidineThe ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-terminal serine proteaseEcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli.Membrane proteases and aminoglycoside antibiotic resistancePaddling mechanism for the substrate translocation by AAA+ motor revealed by multiscale molecular simulations.Single-chain Fv phage display propensity exhibits strong positive correlation with overall expression levelsIdentification of a bacterial-like HslVU protease in the mitochondria of Trypanosoma brucei and its role in mitochondrial DNA replication.Metabolic instability of Escherichia coli cyclopropane fatty acid synthase is due to RpoH-dependent proteolysis.The proteasome: a macromolecular assembly designed for controlled proteolysisCharacterization of six lipoproteins in the sigmaE regulon.Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coliRedundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) protease.Physiological basis for conservation of the signal recognition particle targeting pathway in Escherichia coli.Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).Growth substrate- and phase-specific expression of biphenyl, benzoate, and C1 metabolic pathways in Burkholderia xenovorans LB400.Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli.Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system.Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid systemMolecular architecture of the ATP-dependent CodWX protease having an N-terminal serine active site.Nickel-resistance determinants in Acidiphilium sp. PM identified by genome-wide functional screeningDegradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)The Escherichia coli rpoS-dependent htrC gene is not involved in the heat shock response.Stepwise activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates.Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes.Escherichia coli ClpB is a non-processive polypeptide translocase.Characterization of the HslU chaperone affinity for HslV protease.The role of the ClpA chaperone in proteolysis by ClpAPThe replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone.Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent.The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention?The clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteinsIdentification of potential diagnostic and vaccine candidates of Helicobacter pylori by two-dimensional gel electrophoresis, sequence analysis, and serum profiling.ClpB in a cyanobacterium: predicted structure, phylogenetic relationships, and regulation by light and temperature.
P2860
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P2860
Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Identification and characteriz ...... proteins in Escherichia coli.
@ast
Identification and characteriz ...... proteins in Escherichia coli.
@en
Identification and characterization of HsIV HsIU
@nl
type
label
Identification and characteriz ...... proteins in Escherichia coli.
@ast
Identification and characteriz ...... proteins in Escherichia coli.
@en
Identification and characterization of HsIV HsIU
@nl
prefLabel
Identification and characteriz ...... proteins in Escherichia coli.
@ast
Identification and characteriz ...... proteins in Escherichia coli.
@en
Identification and characterization of HsIV HsIU
@nl
P2093
P2860
P1433
P1476
Identification and characteriz ...... d proteins in Escherichia coli
@en
P2093
Georgopoulos C
Missiakas D
Schwager F
P2860
P304
P356
10.1002/J.1460-2075.1996.TB01082.X
P407
P577
1996-12-01T00:00:00Z