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TranscriptomicsWidespread Co-translational RNA Decay Reveals Ribosome Dynamics
It is generally assumed that mRNAs undergoing translation are protected from decay. Here, we show that mRNAs are, in fact, co-translationally degraded. This is a widespread and conserved process affecting most genes, where 5′–3′ transcript degradation follows the last translating ribosome, producing...
ORGANISM(S): Schizosaccharomyces pombe 
2015-06-04 | E-GEOD-63120 | biostudies-arrayexpress
ProteomicsCo-translational and Post-translational protein myristoylation in HeLa cells
Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. In E. Thinon, R. A. Serwa, et al., Nature Communications 2014, doi:10.1038/ncomms5919, we report the global N-myristoylated prote...
ORGANISM(S): Homo sapiens (Human) 
2018-07-31 | PXD002687 | Pride
Co-translational modification Post-translational modification Apoptosis Protein myristoylation 
ProteomicsProteome-wide identification of SUMO2 modification sites
Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated su...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080741 | MassIVE
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 
TranscriptomicsHow post-translational modification of nitrogenase is circumvented in Rhodopseudomonas palustris strains that produce hydrogen gas constitutively
Characterization of post-translational modification of nitrogenase in Rhodopseudomonas palustris strains that produce hydrogen gas constitutively. To characterize the effect of yeast extract as nitrogen source on gene expression under nitrogen fixing conditions, expression profiles of wild-type cell...
ORGANISM(S): Rhodopseudomonas palustris 
2012-03-15 | E-GEOD-32292 | biostudies-arrayexpress
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 
GenomicsWidespread Co-translational RNA Decay Reveals Ribosome Dynamics
Widespread Co-translational RNA Decay Reveals Ribosome Dynamics
PRJNA266705 | ENA
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 2)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0â??SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structuralâ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-04-01 | MSV000080869 | MassIVE
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0â??SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structuralâ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-30 | MSV000080812 | MassIVE
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 
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