Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
about
Rooting the tree of life by transition analysesInsights into the molecular evolution of HslU ATPase through biochemical and mutational analysesCrystal structure of ClpX molecular chaperone from Helicobacter pyloriThe catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active siteStructural insights into the conformational diversity of ClpP from Bacillus subtilisStructural and Biochemical Analyses of the Eukaryotic Heat Shock Locus V (HslV) from Trypanosoma bruceiCharacterization of Rv3868, an essential hypothetical protein of the ESX-1 secretion system in Mycobacterium tuberculosisCharacterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system.AAA+ proteins and substrate recognition, it all depends on their partner in crime.Stepwise activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates.Disruption of a mitochondrial protease machinery in Plasmodium falciparum is an intrinsic signal for parasite cell death.Minimal protein-folding systems in hyperthermophilic archaea.Sculpting the proteome with AAA(+) proteases and disassembly machines.Molecular machines for protein degradation.Characterization of the HslU chaperone affinity for HslV protease.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.HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysisTracing an allosteric pathway regulating the activity of the HslV protease.Archaeal proteasomes and sampylation.Small molecules as activators in medicinal chemistry (2000-2016).Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease.Asymmetric nucleotide transactions of the HslUV protease.Communication between ClpX and ClpP during substrate processing and degradation.Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase.Successive emergence of ceftazidime-avibactam resistance through distinct genomic adaptations in blaKPC-2-harboring Klebsiella pneumoniae ST307.Structural characterization of the bacterial proteasome homolog BPH reveals a tetradecameric double-ring complex with unique inner cavity properties.Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation.
P2860
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P2860
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
@ast
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
@en
Functional interactions of HslV
@nl
type
label
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
@ast
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
@en
Functional interactions of HslV
@nl
prefLabel
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
@ast
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
@en
Functional interactions of HslV
@nl
P2093
P2860
P356
P1476
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY)
@en
P2093
Claudia Hartmann
Ravishankar Ramachandran
Robert Huber
P2860
P304
P356
10.1073/PNAS.102188799
P407
P577
2002-05-01T00:00:00Z