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Site-specific O-glycoproteome mapping in complex biological system provides molecular basis for understanding the structure-function relationships of glycoproteins and their roles in physiological and pathological processes. Previous O-glycoproteome analysis in cerebrospinal fluid (CSF) focused on s...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-04-05 | MSV000087160 | MassIVE
Intact glycopeptide analysis has been of great interest because it can elucidate glycosylation site information and glycan structural composition at the same time. However, mass-spectrometry (MS)-based glycoproteomic analysis is hindered by the low stoichiometry of glycosylation and poor ionization ...
ORGANISM(S): Homo sapiens (Human) 
2022-09-08 | PXD029269 | Pride
Protein glycosylation and phosphorylation are two of the most common post-translational modifications (PTMs), which plays an important role in many biological processes. However, low abundance and poor ionization efficiency of phosphopeptides and glycopeptides make direct MS analysis challenging. Pr...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2023-07-20 | PXD029775 | Pride
Metabolic reprogramming is a hallmark of cancer. Herein we discover that the key glycolytic enzyme pyruvate kinase M2 isoform (PKM2), but not the related isoform PKM1, is methylated by co-activator-associated arginine methyltransferase 1 (CARM1). PKM2 methylation reversibly shifts the balance of met...
2021-07-30 | MTBLS533 | MetaboLights
Protein glycosylation and phosphorylation are two of the most common post-translational modifications (PTMs). Though they have been indicated to play critical roles in various physiological and pathological processes, effective analytical tools are challenged by low PTM abundance and poor ionization...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2026-06-29 | PXD061371 | Pride
Global proteome comparison between breast cancer MCF7 parental cell and PKM2 KO cell
ORGANISM(S): Homo sapiens (Human) 
2018-10-24 | PXD007671 | Pride
Citrullination and homocitrullination are two post-translational modifications (PTMs) that may cause protein structural and functional changes. Although they have been linked to various biological processes and disease development, the understanding is still poor because of limitations to enrich, de...
ORGANISM(S): Mus musculus (Mouse) 
2022-12-05 | PXD023733 | Pride
Post-translational modifications (PTMs) change protein structures and functions. Methods for the simultaneous enrichment of multiple PTM types can maximize coverage in analyses. We present a protocol using dual-functional Ti(IV)-immobilized metal affinity chromatography followed by mass spectrometry...
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD033065 | Pride
Histone lysine methylation is an important post-translational modifications (PTMs) that plays critical roles in numerous biological processes with abnormal histone lysine methylation having been associated with developmental defects and human diseases. The primary amine of all lysine residues can be...
ORGANISM(S): Homo sapiens (Human) 
2022-04-04 | PXD028269 | Pride
This is the raw data and Byonic search results of mouse mouse lung N-glycoproteome, phosphoproteome, and Mannose-6-Phosphate glycoproteome.
ORGANISM(S): Mus musculus (Mouse) 
2022-01-11 | PXD020196 | Pride
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