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ProteomicsCo-translational assembly counteracts promiscuous interactions
During the co-translational assembly of protein complexes, a fully synthesized subunit engages with the nascent chain of a newly synthesized interaction partner. Such events are thought to contribute to productive assembly, but their exact physiological relevance remains underexplored. Here, we exam...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-02-11 | PXD030626 | Pride
Co-translational assembly Proteomics 
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 
ProteomicsCo-translational assembly counteracts promiscuous interactions
During the co-translational assembly of protein complexes, a fully synthesized subunit engages with the nascent chain of a newly synthesized interaction partner. Such events are thought to contribute to productive assembly, but their exact physiological relevance remains underexplored. Here, we exam...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-02-11 | PXD028413 | Pride
Protein complex assembly Co-translational assembly Nuclear pore complex 
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 
ProteomicsKetone Bodies-mediated Cysteine Modifications Discovered by Chemical Proteomics
All the studies of ketone body-dependent post-translational modifications (PTMs), notably those mediated by ketone bodies, β-hydroxybutyrate (Bhb) and acetoacetate (Acac), have focused on lysine acylations. However, given the chemically diverse and reactive nature of metabolites generated, it remain...
ORGANISM(S): Homo Sapiens 
2025-07-22 | PXD066371 |
GenomicsNAC promotes co-translational protein folding at the ribosomal tunnel exit
NAC promotes co-translational protein folding at the ribosomal tunnel exit
PRJNA1230285 | ENA
GenomicsCo-translational ribosome pairing enables native assembly of misfolding-prone subunits
Co-translational ribosome pairing enables native assembly of misfolding-prone subunits
PRJNA1191379 | ENA
UnknownStructural basis of co-translational N-myristoylation in humans.
Not available
S-EPMC12858966 | biostudies-literature
ProteomicsTCellXTalk enables the detection of co-modified peptides for the study of protein post-translational modification cross-talk in T cells
Protein function is regulated by post-translational modifications (PTMs) that may act individually or interact with others in a phenomenon termed PTM cross-talk. Multiple databases have been dedicated to PTMs, including recent initiatives oriented to the in silico prediction of PTM interactions. The...
ORGANISM(S): Homo sapiens (Human) 
2018-09-19 | PXD010176 | Pride
Ptms Cross-talk Tcr activation T cells 
ProteomicsThe state transition acetyltransferase GNAT2 interacts with GNAT1 and GNAT3 in independent complexes
The acetylation of amino groups within proteins is one of the major posttranslational modifications (PTMs) in all organisms. N-terminal acetyltransferases (NATs) or lysine acetyltransferases (KATs) catalyze the transfer of the acetyl group from the donor substrate acetyl coenzyme A (Ac-CoA) to the t...
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress) 
2024-08-19 | PXD044167 | JPOST Repository
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