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ProteomicsChaperone Activation and Client Binding of a 2-Cysteine Peroxiredoxin
Many 2-Cys-peroxiredoxins (2-Cys-Prxs) serve as dual-function proteins. Active as peroxidases under non-stress conditions, they convert into effective chaperones under stress conditions. While their peroxidase activity has been extensively studied and shown to involve cycles of redox-mediated oligom...
ORGANISM(S): Leishmania infantum Photinus pyralis (Common eastern firefly) (Lampyris pyralis) 
2019-02-19 | PXD010281 | Pride
Cross-linking  chaperone activation  chaperone-client complex 
UnknownA molecular mechanism of chaperone-client recognition.
Not available
S-EPMC5262456 | biostudies-literature
UnknownPan-Cancer Analysis of Mitochondria Chaperone-Client Co-Expression Reveals Chaperone Functional Partitioning.
Not available
S-EPMC7226338 | biostudies-literature
UnknownClient-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.
Not available
S-EPMC3144320 | biostudies-literature
UnknownTight complex formation between Cosmc chaperone and its specific client non-native T-synthase leads to enzyme activity and client-driven dissociation.
Not available
S-EPMC3346102 | biostudies-literature
UnknownChaperone activation and client binding of a 2-cysteine peroxiredoxin.
Not available
S-EPMC6368585 | biostudies-literature
UnknownSwitchable client specificity in a dual functional chaperone coordinates light-harvesting complex biogenesis.
Not available
S-EPMC12164976 | biostudies-literature
ProteomicsA direct interplay between the co-chaperones Hop and p23 regulates cycle progression and client folding in the Hsp70/Hsp90 chaperone machineries
Folding of stringent clients requires transfer from Hsp70 to Hsp90. The co-chaperone Hop physically connects the chaperone machineries. Here we define its role from the remodeling of Hsp70/40-client complexes to the mechanism of client transfer and the conformational switching from stalled to active...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2022-02-24 | PXD027413 | Pride
Hsp90 P23 Hop Hsp70 
UnknownThe Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System.
Not available
S-EPMC5501727 | biostudies-literature
UnknownA Chaperone Lid Ensures Efficient and Privileged Client Transfer during Tail-Anchored Protein Targeting.
Not available
S-EPMC6689467 | biostudies-literature
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