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ProteomicsCo-translational determination of quaternary structures in chaperone factories
The HSP90/R2TP quaternary chaperone assembles key cellular machines, including the three nuclear RNA polymerases and many non-coding RNPs. Here, we show that the R2TP binds many partners co-translationally. Remarkably, its co-translational interactome reveals many novel potential clients, and side-b...
ORGANISM(S): Homo sapiens (Human) 
2026-01-06 | PXD061298 | Pride
Translation factories Chaperone Co-translational assembly 
ProteomicsA specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand
Heat shock protein-90 chaperone machinery is involved in the stability and activity of its client proteins. The chaperone function of Hsp90 is regulated by co-chaperones and post-translational modifications. Although structural evidence exists for Hsp90 interaction with clients, our understanding of...
ORGANISM(S): Homo sapiens (Human) 
2023-05-30 | PXD030486 | Pride
Hsp90 Co-chaperone Chaperone Glucocorticoid receptor Tsc1 Fnip1 Fnip2 Steroid hormone receptors 
ProteomicsHsp70 ATP-dependent dimerization and Chaperone/Co-chaperone Interactions
Eukaryotic protein homeostasis (proteostasis) is largely dependent on the action of highly conserved Hsp70 molecular chaperones. Recent evidence indicates that apart from conserved molecular allostery, Hsp70 proteins retained and adapted throughout the evolution the ability to assemble as functional...
ORGANISM(S): Homo sapiens (Human) 
2018-12-11 | PXD010069 | Pride
Tomm34 Hsp70 Co-chaperone Dimer Chip 
TranscriptomicsCo-chaperone CCRP/DNAJC7-regulated gene regulation in the mouse liver
Co-chaperone protein CAR Cytoplasmic Retention Protein (CCRP) interacts with various nuclear receptors and determines their localization. However, there is limited information about in vivo role of CCRP especially in nuclear receptor-mediated gene regulation. We have generated CCRP global knockout (...
ORGANISM(S): Mus musculus 
2015-01-05 | E-GEOD-56557 | biostudies-arrayexpress
GenomicsProteome-wide determinants of co-translational chaperone binding in bacteria
Proteome-wide determinants of co-translational chaperone binding in bacteria
PRJNA1238275 | ENA
GenomicsCo-translational determination of quaternary structures in chaperone factories
Co-translational determination of quaternary structures in chaperone factories
PRJNA1235270 | ENA
ProteomicsBacterial RF3 Senses Chaperone Function in Co-translational Folding
Molecular chaperones assist in protein folding by interacting with nascent polypeptide chains (NCs) during translation, but whether the ribosome can sense chaperone defects and abort translation of misfolding NCs has not been explored. Here we used quantitative proteomics in E. coli to investigate t...
ORGANISM(S): Escherichia coli 
2022-12-09 | PXD025219 | Pride
Molecular chaperones Co-translational folding 
ProteomicsGlobal Analysis of Protein Folding Thermodynamics for Disease State Characterization, MCF7 vs MDAMB231
Protein biomarkers can be used to characterize and diagnose disease states such as cancer. They can also serve as therapeutic targets. Current methods for protein biomarker discovery, which generally rely on the large-scale analysis of gene and/or protein expression levels, fail to detect protein b...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080761 | MassIVE
ProteomicsGlobal Analysis of Protein Folding Thermodynamics for Disease State Characterization, MCF7 vs MCF10A
Protein biomarkers can be used to characterize and diagnose disease states such as cancer. They can also serve as therapeutic targets. Current methods for protein biomarker discovery, which generally rely on the large-scale analysis of gene and/or protein expression levels, fail to detect protein b...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080760 | MassIVE
OtherProteome-wide determinants of co-translational chaperone binding in bacteria
Chaperones are essential to the co-translational folding of most proteins. However, the principles of co-translational chaperone interaction throughout the proteome are poorly understood, as current methods are restricted to few substrates and cannot capture nascent protein folding or chaperone bind...
ORGANISM(S): Escherichia coli 
2025-03-25 | GSE292386 | GEO
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