Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
about
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.Structural insights into the conformational diversity of ClpP from Bacillus subtilisFunctional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin systemThe YjbH protein of Bacillus subtilis enhances ClpXP-catalyzed proteolysis of SpxRequirement of the zinc-binding domain of ClpX for Spx proteolysis in Bacillus subtilis and effects of disulfide stress on ClpXP activityDiscovery of antibacterial cyclic peptides that inhibit the ClpXP protease.Co-evolution of multipartite interactions between an extended tmRNA tag and a robust Lon protease in Mycoplasma.The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpPClpXP, an ATP-powered unfolding and protein-degradation machineLocation of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker.Deciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX.Roles of adaptor proteins in regulation of bacterial proteolysisClp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpXEngineering synthetic adaptors and substrates for controlled ClpXP degradationACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils.A degradation signal recognition in prokaryotes.Mini review: ATP-dependent proteases in bacteria.Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial speciesA Phosphosignaling Adaptor Primes the AAA+ Protease ClpXP to Drive Cell Cycle-Regulated Proteolysis.Inducible protein degradation in Bacillus subtilis using heterologous peptide tags and adaptor proteins to target substrates to the protease ClpXP.Structural and Functional Insights into Bacillus subtilis Sigma Factor Inhibitor, CsfB.Altered tethering of the SspB adaptor to the ClpXP protease causes changes in substrate delivery.
P2860
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P2860
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
description
2007 nî lūn-bûn
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2007 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մարտին հրատարակված գիտական հոդված
@hy
2007年の論文
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2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@ast
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@en
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@nl
type
label
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@ast
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@en
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@nl
prefLabel
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@ast
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@en
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@nl
P2093
P1476
Structural basis of SspB-tail recognition by the zinc binding domain of ClpX
@en
P2093
Eun Young Park
Hyesung Jeon
Hyung-Wook Kim
Seung-Beom Hong
P304
P356
10.1016/J.JMB.2007.01.003
P407
P577
2007-01-09T00:00:00Z