Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.
about
ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradationEssential functions linked with structural disorder in organisms of minimal genomeAlterations in the E3 ligases Parkin and CHIP result in unique metabolic signaling defects and mitochondrial quality control issues.The epichaperome is an integrated chaperome network that facilitates tumour survivalThe yeast Hsp70 homolog Ssb: a chaperone for general de novo protein folding and a nanny for specific intrinsically disordered protein domains.Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.The remarkable multivalency of the Hsp70 chaperones.Multiple functions of the E3 ubiquitin ligase CHIP in immunity.Non-canonical Interactions between Heat Shock Cognate Protein 70 (Hsc70) and Bcl2-associated Anthanogene (BAG) Co-Chaperones Are Important for Client Release.Mechanistic basis for a molecular triage reactionOn the role, ecology, phylogeny, and structure of dual-family immunophilins.CHIP as a membrane-shuttling proteostasis sensor.Broadening the functionality of a J-protein/Hsp70 molecular chaperone system.Most mutations that cause spinocerebellar ataxia autosomal recessive type 16 (SCAR16) destabilize the protein quality-control E3 ligase CHIP.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Cracking the Chaperone Code: Cellular Roles for Hsp70 Phosphorylation.Hsp70 at the membrane: driving protein translocation.Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes.Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions.Protein cross-linking capillary electrophoresis at increased throughput for a range of protein-protein interactions.Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein Hsp90.Comparative analysis of FKBP family protein: evaluation, structure, and function in mammals and Drosophila melanogaster.Mapping interactions with the chaperone network reveals factors that protect against tau aggregation
P2860
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P2860
Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Specific Binding of Tetratrico ...... Affinity and Phosphorylation.
@en
type
label
Specific Binding of Tetratrico ...... Affinity and Phosphorylation.
@en
prefLabel
Specific Binding of Tetratrico ...... Affinity and Phosphorylation.
@en
P2093
P2860
P1433
P1476
Specific Binding of Tetratrico ...... Affinity and Phosphorylation.
@en
P2093
Daniel R Southworth
Jason E Gestwicki
Victoria A Assimon
P2860
P304
P356
10.1021/ACS.BIOCHEM.5B00801
P407
P577
2015-11-13T00:00:00Z