The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
about
Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXPHuman mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpXCompetence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor.The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging systemCan sequence determine function?Stress Physiology of Lactic Acid BacteriaThe structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triadCrystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolutionCrystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP proteaseCrystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpACrystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritimaCrystal 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 siteNovel dimer structure of a membrane-bound protease with a catalytic Ser–Lys dyad and its linkage to stomatinAn Asymmetric Model for Na + -translocating Glutaconyl-CoA DecarboxylasesStructures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamberAcyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.A conformational switch underlies ClpP protease functionStructural Switching of Staphylococcus aureus Clp Protease: A KEY TO UNDERSTANDING PROTEASE DYNAMICSStructural Insights into the Inactive Subunit of the Apicoplast-localized Caseinolytic Protease Complex of Plasmodium falciparumStructural insights into the conformational diversity of ClpP from Bacillus subtilisMycobacterium 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) ProteinHelix Unfolding/Refolding Characterizes the Functional Dynamics of Staphylococcus aureus Clp ProteaseStructural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triadDiamonds in the rough: a strong case for the inclusion of weak-intensity X-ray diffraction dataSignal transduction and regulatory mechanisms involved in control of the sigma(S) (RpoS) subunit of RNA polymeraseHow high G+C Gram-positive bacteria and in particular bifidobacteria cope with heat stress: protein players and regulatorsUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationThe RssB response regulator directly targets sigma(S) for degradation by ClpXPCharacterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPaseEffects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machineNovel peptide-mediated interactions derived from high-resolution 3-dimensional structuresMycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infectionAdaptor protein controlled oligomerization activates the AAA+ protein ClpCMolecular cloning and characterization of a mouse homolog of bacterial ClpX, a novel mammalian class II member of the Hsp100/Clp chaperone familyGenome-wide analysis of alternative splicing in Volvox carteriAAA+ proteins: have engine, will workPositive Selection in Rapidly Evolving Plastid-Nuclear Enzyme Complexes.
P2860
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P2860
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
description
1997 nî lūn-bûn
@nan
1997 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@ast
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@en
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@nl
type
label
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@ast
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@en
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@nl
prefLabel
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@ast
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@en
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@nl
P2093
P3181
P1433
P1476
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
@en
P2093
J A Hartling
J M Flanagan
P304
P3181
P356
10.1016/S0092-8674(00)80431-6
P407
P577
1997-11-14T00:00:00Z