about
Human Sug1/p45 is involved in the proteasome-dependent degradation of Sp1Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.Architecture and molecular mechanism of PAN, the archaeal proteasome regulatory ATPase.A single ClpS monomer is sufficient to direct the activity of the ClpA hexamerChaperone rings in protein folding and degradation.Multiple homeostatic mechanisms in the control of P1 plasmid replicationClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence.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.Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones.Translocation pathway of protein substrates in ClpAP protease.Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteasesMinimal protein-folding systems in hyperthermophilic archaea.Similarities between the DNA replication initiators of Gram-negative bacteria plasmids (RepA) and eukaryotes (Orc4p)/archaea (Cdc6p)Here's the hook: similar substrate binding sites in the chaperone domains of Clp and Lon.Replication regulation of Vibrio cholerae chromosome II involves initiator binding to the origin both as monomer and as dimer.DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine.Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunitsHeat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperonesThe 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.Disruption and analysis of the clpB, clpC, and clpE genes in Lactococcus lactis: ClpE, a new Clp family in gram-positive bacteriaReplication and control of circular bacterial plasmids.Protein domains and conformational changes in the activation of RepA, a DNA replication initiator.Dislocation of membrane proteins in FtsH-mediated proteolysis.Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone.A single-domain cyclophilin from Leishmania donovani reactivates soluble aggregates of adenosine kinase by isomerase-independent chaperone function.Structural changes in RepA, a plasmid replication initiator, upon binding to origin DNA.Characterization of interactions between Escherichia coli molecular chaperones and immobilized caseins.ClpAP is an auxiliary protease for DnaA degradation in Caulobacter crescentus.The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer.Binding and degradation of heterodimeric substrates by ClpAP and ClpXP.ClpC regulates the fate of a sporulation initiation sigma factor, sigmaH protein, in Bacillus subtilis at elevated temperatures
P2860
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P2860
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Mechanism of protein remodeling by ClpA chaperone.
@ast
Mechanism of protein remodeling by ClpA chaperone.
@en
type
label
Mechanism of protein remodeling by ClpA chaperone.
@ast
Mechanism of protein remodeling by ClpA chaperone.
@en
prefLabel
Mechanism of protein remodeling by ClpA chaperone.
@ast
Mechanism of protein remodeling by ClpA chaperone.
@en
P2860
P356
P1476
Mechanism of protein remodeling by ClpA chaperone.
@en
P2860
P304
P356
10.1073/PNAS.94.10.4901
P407
P577
1997-05-01T00:00:00Z