Sort   by:  
 Page size 
The formation of condensates in membraneless organelles is thought to be driven by protein phase separation. Arginine methylation and serine/threonine phosphorylation are important in the phase separation process, however these post-translational modifications are often present in intrinsically diso...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-09-17 | PXD022403 | Pride
Protein methylation is one of the major post-translational modifications (PTMs) in the cell. In Saccharomyces cerevisiae, over twenty protein methyltransferases (MTases) and their respective substrates have been identified. However, the way in which these MTases are modified, and potentially subject...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-12-18 | PXD006767 | Pride
Protein methyltransferases can recognise their substrates through linear sequence motifs and determination of these motifs is critical to understand methyltransferase mechanism, function and drug targeting. Here we describe MT-MAMS (methyltransferase motif analysis by mass spectrometry), a quantitat...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2018-09-03 | PXD009515 | Pride
Disruptor of telomeric silencing (Dot1p) is an exquisitely conserved histone methyltransferase, and is the sole enzyme responsible for H3K79 methylation in the budding yeast, Saccharomyces cerevisiae. It has been shown to be highly phosphorylated in vivo; however, the upstream kinases that act on Do...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2024-01-29 | PXD036747 | Pride
Lysine methylation is widespread on human proteins, however the enzymes that catalyse its addition remain largely unknown. This limits our capacity to study the function and regulation of this modification. Here we report that human METTL21B is a protein methyltransferase, which methylates lysine 16...
ORGANISM(S): Homo sapiens (Human) 
2017-07-03 | PXD005497 | Pride
The methylation of histidine residues is increasingly found to be both prevalent throughout the proteome, and also relevant to human disease. Hpm1p mono-methylates H243 in the ribosomal protein Rpl3 and represents the only histidine methyltransferase in Saccharomyces cerevisiae. Interestingly, the h...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-08-12 | PXD027953 | Pride
Chemical-Crosslinking Mass Spectrometry (XLMS) using MS-cleavable crosslinkers is fast becoming an established technique in the study of protein-protein interactions for both small and large scale samples. With the increased uptake of XLMS as a technique, different combinations of crosslinker types,...
ORGANISM(S): Escherichia coli Saccharomyces cerevisiae (Baker's yeast) 
2018-07-20 | PXD008348 | Pride
Yeast peptides immunoprecipitated with an anti-mono-methylarginine antibody, analysis on Orbitrap Velos with ETD.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-07-03 | PXD002151 | Pride
Here, we apply large scale cross-linking mass spectrometry to profile the interactome of isolated and intact Saccharomyces cerevisiae nuclei. Two independent biological replicates (nuclei isolated from different cultures) were performed.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-03-12 | PXD014584 | Pride
Histone methylation is central to the regulation of eukaryotic transcription. In Saccharomyces cerevisiae, it is controlled by a system of four methyltransferases (Set1p, Set2p, Set5p, and Dot1p) and four demethylases (Jhd1p, Jhd2p, Rph1p, and Gis1p). While the histone targets for these enzymes are ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-12-15 | PXD021214 | Pride
Sort   by:  
 Page size