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ProteomicsHuman serum glycoproteome - Glyco-Decipher
Identification results of peptide-spectrum matches supporting Glyco-Decipher manuscript (Glyco-Decipher: Glycan database-independent peptide matching enables discovery of new glycans and in-depth characterization of site-specific N-glycosylation). Recently, several elegant bioinformatics tools have ...
ORGANISM(S): Homo sapiens (Human) 
2022-03-04 | PXD031025 | Pride
Glycoproteomics  glycopeptide  glycosylation  n-glycosylation 
ProteomicsRe-analysis of glycoproteomics data with Glyco-Decipher
Reanalysis of submissions PXD005411, PXD005413, PXD005412, PXD005553, PXD005555, PXD005565 and PXD019937 using Glyco-Decipher. Identification results of peptide-spectrum matches supporting Glyco-Decipher manuscript (Glyco-Decipher: glycan database-independent peptide matching enables discovery of ne...
ORGANISM(S): Mus musculus (Mouse) Saccharomyces cerevisiae (Baker's yeast) 
2022-03-04 | PXD031032 | Pride
Glycoproteomics  glycopeptide  reanalysis  glycosylation  n-glycosylation 
ProteomicsArginine dimethylation and liquid-liquid phase separation
Recently, arginine methylation was found to regulate the protein LLPS which drives the formation of MLOs. Here, we developed a chemical enrichment method coupled with LC-MS/MS to analyze dynamic change of arginine di-methylation upon SG formation.
ORGANISM(S): Homo sapiens (Human) 
2022-10-20 | PXD033048 | Pride
Liquid-liquid phase separation Arginine dimethylation Chemical enrichment method Stress granule Rg/rgg motifs 
ProteomicsArginine dimethylation and liquid-liquid phase separation_Supplementary
Recently, arginine methylation was found to regulate the protein LLPS which drives the formation of MLOs. Here, we developed a chemical enrichment method coupled with LC-MS/MS to analyze dynamic change of arginine di-methylation upon SG formation.
ORGANISM(S): Homo sapiens (Human) 
2022-10-20 | PXD035137 | Pride
Liquid-liquid phase separation Arginine dimethylation Chemical enrichment method Stress granule Rg/rgg motifs 
ProteomicsProteome-Wide Deconvolution of Drug Targets and Binding Sites by Lysine Reactivity Profiling
Recently, numerous efforts have been devoted to identifying drug targets and binding sites in complex proteomes, which is of great importance in modern drug discovery. In this study, we developed a robust lysine reactivity profiling method to systematically study drug-binding targets and binding sit...
ORGANISM(S): Homo Sapiens 
2023-09-28 | PXD045749 |
Proteomics[HPP-2.0] Matrix Thermal Shift Assay for Fast Construction of Multidimensional Ligand–Target Space
Existing thermal shift-based mass spectrometry approaches are able to identify target proteins without chemical modification of the ligand, but they are suffering from complicated workflows with limited throughput. Herein, we present a new thermal shift-based method, termed matrix thermal shift assa...
ORGANISM(S): Homo Sapiens 
2023-09-29 | PXD045941 |
ProteomicsSolvent-Induced partial Cellular Fixation Approach enables systematic identification of drug targets and temporal progression of downstream biochemical pathways in living cells
In this study, we introduce a novel approach, the Solvent-Induced Partial Cellular Fixation Approach (SICFA), to monitor drug targets and the temporal progression of downstream biochemical pathways in living cells. We observed that proteins in living cells undergo unfolding and aggregation when expo...
ORGANISM(S): Homo sapiens (Human) 
2025-10-15 | PXD057157 | Pride
Proteomics  protein stability  drug target identification  drug binding potency  downstream effector proteins  living cells analysis 
ProteomicsHuman serum glycoproteome - Glyco-Decipher
Identification results of peptide-spectrum matches supporting Glyco-Decipher manuscript (Glyco-Decipher: Glycan database-independent peptide matching enables discovery of new glycans and in-depth characterization of site-specific N-glycosylation). Recently, several elegant bioinformatics tools have ...
ORGANISM(S): Homo Sapiens 
2023-09-25 | PXD045630 |
UnknownPalladium catalyst imbedded in polymers of intrinsic microporosity for the Suzuki-Miyaura coupling reaction.
Not available
S-EPMC9087636 | biostudies-literature
ProteomicsOne-Step Chemoenzymatic Labeling and Oxime-Reversible Enrichment for O-GlcNAc Profiling in Oxidative Stress
Chemoenzymatic labeling has greatly advanced O-GlcNAc proteomics, yet existing strategies using azide-modified donors (e.g., UDP-GalNAz) require multi-step click-based workflows that introduce substantial sample loss and limit sensitivity toward low-abundance targets. While recent one-step labeling ...
ORGANISM(S): Homo Sapiens 
2026-01-06 | PXD072723 |
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