Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
about
The apicomplexan plastid and its evolutionStructural and Motional Contributions of the Bacillus subtilis ClpC N-Domain to Adaptor Protein InteractionsStructure and mechanism of the hexameric MecA-ClpC molecular machineStructural Dynamics of the MecA-ClpC Complex: A TYPE II AAA+ PROTEIN UNFOLDING MACHINEMycobacterium tuberculosis ClpC1: characterization and role of the N-terminal domain in its functionAdaptor protein controlled oligomerization activates the AAA+ protein ClpCGenome-wide analysis of rice ClpB/HSP100, ClpC and ClpD genes.A pangenomic analysis of the Nannochloropsis organellar genomes reveals novel genetic variations in key metabolic genesA Clp/Hsp100 chaperone functions in Myxococcus xanthus sporulation and self-organizationDegradation of SsrA-tagged proteins in streptococci.Protein transport in organelles: The composition, function and regulation of the Tic complex in chloroplast protein import.Insights into the Clp/HSP100 chaperone system from chloroplasts of Arabidopsis thaliana.The proteolysis adaptor, NblA, binds to the N-terminus of β-phycocyanin: Implications for the mechanism of phycobilisome degradation.Quantitative analysis of the chloroplast molecular chaperone ClpC/Hsp93 in Arabidopsis reveals new insights into its localization, interaction with the Clp proteolytic core, and functional importance.Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus.NblA, a key protein of phycobilisome degradation, interacts with ClpC, a HSP100 chaperone partner of a cyanobacterial Clp protease.Structure and function of a novel type of ATP-dependent Clp protease.Discovery of a Unique Clp Component, ClpF, in Chloroplasts: A Proposed Binary ClpF-ClpS1 Adaptor Complex Functions in Substrate Recognition and Delivery.ClpL is a chaperone without auxiliary factors.The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments.
P2860
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P2860
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
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2005年学术文章
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2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
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2005年學術文章
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name
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
@en
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
@nl
type
label
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
@en
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
@nl
prefLabel
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
@en
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
@nl
P2093
P2860
P50
P356
P1476
Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity.
@en
P2093
Adrian K Clarke
Fredrik I Andersson
Janine Kirstein
Robert Blakytny
P2860
P304
P356
10.1074/JBC.M509661200
P407
P577
2005-12-16T00:00:00Z