ClpXP, an ATP-powered unfolding and protein-degradation machine
about
Cross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and DiseaseComparing protein folding in vitro and in vivo: foldability meets the fitness challengeAllosteric communication in the dynein motor domainStructural Insights into the Inactive Subunit of the Apicoplast-localized Caseinolytic Protease Complex of Plasmodium falciparumMycobacterium tuberculosis RsdA provides a conformational rationale for selective regulation of -factor activity by proteolysisInsights into Structural Network Responsible for Oligomerization and Activity of Bacterial Virulence Regulator Caseinolytic Protease P (ClpP) ProteinNucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ MachineProteolytic regulation of alginate overproduction in Pseudomonas aeruginosa.Reversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX AssociationMeet the neighbors: Mapping local protein interactomes by proximity-dependent labeling with BioIDMitochondrial protein quality control: the mechanisms guarding mitochondrial healthCooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationDisordered proteinaceous machinesNew insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Viewing protein fitness landscapes through a next-gen lens.Proteolysis-Dependent Remodeling of the Tubulin Homolog FtsZ at the Division Septum in Escherichia coli.Small oligomers of ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase are required for biological activity.Mechanical operation and intersubunit coordination of ring-shaped molecular motors: insights from single-molecule studiesThe Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpPControl of mitochondrial integrity in ageing and diseaseEnvironment determines evolutionary trajectory in a constrained phenotypic spaceSubstrate Discrimination by ClpB and Hsp104.Streptococcus pyogenes polymyxin B-resistant mutants display enhanced ExPortal integrity.Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine.Functional chromatography reveals three natural products that target the same protein with distinct mechanisms of action.Cell cycle-dependent adaptor complex for ClpXP-mediated proteolysis directly integrates phosphorylation and second messenger signalsMu transpososome and RecBCD nuclease collaborate in the repair of simple Mu insertions.Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors.FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP.Adaptor-mediated Lon proteolysis restricts Bacillus subtilis hyperflagellation.Quantitative genome-wide genetic interaction screens reveal global epistatic relationships of protein complexes in Escherichia coliA Streptococcus uberis transposon mutant screen reveals a negative role for LiaR homologue in biofilm formation.Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity.Genome Modification in Enterococcus faecalis OG1RF Assessed by Bisulfite Sequencing and Single-Molecule Real-Time Sequencing.Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpXThe Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1Following the fate of bacterial cells experiencing sudden chromosome loss.Vps4 disassembles an ESCRT-III filament by global unfolding and processive translocation.Transposable Phage MuContributions of tropodithietic acid and biofilm formation to the probiotic activity of Phaeobacter inhibens.
P2860
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P2860
ClpXP, an ATP-powered unfolding and protein-degradation machine
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
ClpXP, an ATP-powered unfolding and protein-degradation machine
@ast
ClpXP, an ATP-powered unfolding and protein-degradation machine
@en
ClpXP, an ATP-powered unfolding and protein-degradation machine
@nl
type
label
ClpXP, an ATP-powered unfolding and protein-degradation machine
@ast
ClpXP, an ATP-powered unfolding and protein-degradation machine
@en
ClpXP, an ATP-powered unfolding and protein-degradation machine
@nl
prefLabel
ClpXP, an ATP-powered unfolding and protein-degradation machine
@ast
ClpXP, an ATP-powered unfolding and protein-degradation machine
@en
ClpXP, an ATP-powered unfolding and protein-degradation machine
@nl
P2860
P1476
ClpXP, an ATP-powered unfolding and protein-degradation machine
@en
P2093
Robert T Sauer
Tania A Baker
P2860
P356
10.1016/J.BBAMCR.2011.06.007
P407
P577
2011-06-27T00:00:00Z