Bioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation.
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Diversity of degradation signals in the ubiquitin-proteasome systemThe Molecular Basis of N-End Rule RecognitionStructural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpSMolecular basis of substrate selection by the N-end rule adaptor protein ClpSThe ClpS Adaptor Mediates Staged Delivery of N-End Rule Substrates to the AAA+ ClpAP ProteaseTargeting proteins for degradationThe substrate recognition domains of the N-end rule pathway.KEGG orthology-based annotation of the predicted proteome of Acropora digitifera: ZoophyteBase - an open access and searchable database of a coral genome.The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains.ClpS is an essential component of the N-end rule pathway in Escherichia coli.Protease gene families in Populus and Arabidopsis.A single ClpS monomer is sufficient to direct the activity of the ClpA hexamerThe N-end rule pathway and regulation by proteolysisRemodeling of a delivery complex allows ClpS-mediated degradation of N-degron substrates.Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogenCrystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog.Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogen Plasmodium falciparum.Structural Basis of an N-Degron Adaptor with More Stringent SpecificityModification of PATase by L/F-transferase generates a ClpS-dependent N-end rule substrate in Escherichia coli.The natural history of ubiquitin and ubiquitin-related domains.Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus.The ClpS-like N-domain is essential for the functioning of Ubr11, an N-recognin in Schizosaccharomyces pombe.Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway.ClpS1 is a conserved substrate selector for the chloroplast Clp protease system in Arabidopsis.Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
P2860
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P2860
Bioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Bioinformatic analysis of ClpS ...... ukaryotic protein degradation.
@en
Bioinformatic analysis of ClpS ...... ukaryotic protein degradation.
@nl
type
label
Bioinformatic analysis of ClpS ...... ukaryotic protein degradation.
@en
Bioinformatic analysis of ClpS ...... ukaryotic protein degradation.
@nl
prefLabel
Bioinformatic analysis of ClpS ...... ukaryotic protein degradation.
@en
Bioinformatic analysis of ClpS ...... ukaryotic protein degradation.
@nl
P1476
Bioinformatic analysis of ClpS ...... ukaryotic protein degradation.
@en
P2093
Kristin K Koretke
P356
10.1016/S1047-8477(02)00582-8
P577
2003-01-01T00:00:00Z