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ProteomicsSILAC diGlycine proteomics in C. elegans to identify ULP-3 targets upon DNA damage.
We found a conserved role for the deNEDDylating enzyme NEDP1 (ULP-3 in C. elegans) in the DNA damage induced apoptosis. To gain mechanistic insights into the role of ULP-3 in the IR-induced apoptosis, we devised an unbiased proteomics approach to discover potential NEDD8 targets for ULP-3 upon DNA d...
ORGANISM(S): Nematodes (ncbitaxon:333870) 
2019-08-19 | MSV000084214 | MassIVE
UnknownConformational dynamics of the Hsp70 chaperone throughout key steps of its ATPase cycle.
Not available
S-EPMC9889847 | biostudies-literature
ProteomicsAnalysis of reconstituted tripartite complex supports avidity-based recruitment of Hsp70 by substrate bound J-domain protein
Hsp70 are ubiquitous, versatile molecular chaperones that cyclically interact with substrate protein(s). The initial step requires synergistic interaction of a substrate and a J-domain protein (JDP) cochaperone, via its J-domain, with Hsp70 to stimulate hydrolysis of its bound ATP. This hydrolysis d...
ORGANISM(S): Escherichia coli Saccharomyces cerevisiae (Baker's yeast) 
2024-02-19 | PXD044739 | Pride
Hsc20 Hsp70 atpase cycle Substrate delivery Ssq1 Molecular chaperones 
UnknownIntragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains.
Not available
S-EPMC17769 | biostudies-literature
TranscriptomicsExpression data for inbred mouse brains
Prion diseases are fatal neurodegenerative disorders that include bovine spongiform encephalopathy (BSE) and scrapie in animals and Creutzfeldt-Jakob disease (CJD) in humans. They are characterized by long incubation periods, variation in which is determined by many factors including genetic backgro...
ORGANISM(S): Mus musculus 
2012-09-04 | E-GEOD-38205 | biostudies-arrayexpress
UnknownFe-S Cluster Hsp70 Chaperones: The ATPase Cycle and Protein Interactions.
Not available
S-EPMC6287258 | biostudies-literature
UnknownNovel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.
Not available
S-EPMC4858950 | biostudies-literature
ProteomicsStructures of the 26S proteasome in complex with the Hsp70 cochaperone Bag1 reveal a novel mechanism for direct transfer of substrates to the catalytic chamber
Coupling of the degradation and chaperone systems, particularly under cellular stress, is essential for eliminating unfolded proteins. The co-chaperone Bag1 links the Hsp70 chaperone to the 26S proteasome, recruiting Hsp70-bound unfolded proteins for proteasomal degradation. Here, we present cryo-EM...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2025-12-23 | PXD069071 | Pride
Chaperones Degradation Hsp70 Bag1 Proteasome 
UnknownKinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function.
Not available
S-EPMC7148561 | biostudies-literature
ProteomicsStructures of the 26S proteasome in complex with the Hsp70 cochaperone Bag1 reveal a novel mechanism of ubiquitin-independent proteasomal degradation
The 26S proteasome primarily degrades proteins marked by polyubiquitin chains. Although ubiquitin-independent pathways for proteasomal degradation exist, the mechanisms involved remain poorly understood. Bag1 links Hsp70 chaperone to the 26S proteasome, recruiting Hsp70-bound aberrant proteins for d...
ORGANISM(S): Homo sapiens (Human) 
2025-01-27 | PXD058407 | Pride
Chaperones Degradation Hsp70 Bag1 Proteasome 
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