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In this study, we developed an approach using Zirconium (IV)-grafted mesoporous beads to enrich phosphopeptides followed by analysis with a high resolution nanoRPLC-MS/MS system. The new method was first tested with tryptic digests of standard phosphoproteins and HeLa cell lysates, with excellent en...
ORGANISM(S): Homo sapiens (Human) 
2024-06-16 | PXD045146 | Pride
Acute myocardial infarction (AMI) involves complex molecular events, including alterations in protein phosphorylation. In this study, we performed a comparative phosphoproteomic analysis of serum samples from AMI patients and healthy controls to identify AMI-associated phosphorylation signatures. Se...
ORGANISM(S): Homo sapiens (Human) 
2026-05-25 | PXD062749 | Pride
Phosphorylation is the most commonly studied protein post-translational modification (PTM) in biological systems due to its importance in controlling cell division, survival, growth, etc. Despite the thorough research in phosphoproteomics of cells and tissues there is little information on circulati...
ORGANISM(S): Canis lupus x Canis lupus familiaris 
2018-11-13 | PXD010894 | Pride
A protocol for an improved phosphopeptide identification in tryptically digested complex peptide samples is described. The common TiO2 based phoshopeptide enrichment is coupled to a simple peptide fractionation protocol with following LC-MS analysis of the obtained fractions and proteomic identifica...
ORGANISM(S): Homo sapiens (Human) 
2020-08-31 | PXD018663 | Pride
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