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UnknownHydrogen bond based smart polymer for highly selective and tunable capture of multiply phosphorylated peptides.
Not available
S-EPMC5587758 | biostudies-literature
ProteomicsAn optimized SP3 sample processing workflow for in-depth phos-phoproteomics and improved identification of multiply phosphory-lated peptides
Protein phosphorylation is a critical and ubiquitous post-translational modification (PTM) found across the kingdoms of life. Advances in high-throughput mass spectrometry have transformed our ability to interrogate the phosphoproteome. However, sample prepara-tion methodologies optimized for phosp...
ORGANISM(S): Homo sapiens (Human) 
2025-08-25 | PXD061013 | Pride
Phosphorylation  multiply phosphorylated  mass spectrometry  ptm  sp3  tio2  c18. 
UnknownSpecific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK.
Not available
S-EPMC2655680 | biostudies-literature
UnknownA Highly Versatile Expression System for the Production of Multiply Phosphorylated Proteins.
Not available
S-EPMC7737670 | biostudies-literature
ProteomicsJPST000090-2 Extended Coverage of Singly and Multiply Phosphorylated Peptides from a Single Titanium Dioxide Microcolumn [Reanalysis: JPST000090]
We developed a novel approach to enlarge phosphoproteome coverage by selective elution depending on the number of phosphoryl group of peptides from a single titanium dioxide (TiO2) microcolumn using hydrophilic interaction chromatography (HILIC). In this approach, acidic methylphosphonate buffer inc...
ORGANISM(S): Homo Sapiens (human) 
2023-04-01 | RPXD034764 | JPOST Repository
ProteomicsJPST000090-1 Extended Coverage of Singly and Multiply Phosphorylated Peptides from a Single Titanium Dioxide Microcolumn [Reanalysis: JPST000090]
We developed a novel approach to enlarge phosphoproteome coverage by selective elution depending on the number of phosphoryl group of peptides from a single titanium dioxide (TiO2) microcolumn using hydrophilic interaction chromatography (HILIC). In this approach, acidic methylphosphonate buffer inc...
ORGANISM(S): Homo Sapiens (human) 
2023-04-01 | RPXD034763 | JPOST Repository
ProteomicsInterferon stimulated changes in the brain phosphoproteome
Type I interferons (IFN-Is) are immunoregulatory cytokines that are essential for normal host antiviral responses. The current understanding is that IFN-Is mediate their effects through the expression of several hundred interferon-regulated genes. Here we identified a novel IFN-I response mechanism ...
ORGANISM(S): Mus musculus (Mouse) 
2021-11-02 | PXD014443 | Pride
Astrocytes Brain Mouse Interferon Microglia Phosphoproteomics Lc-ms/ms 
ProteomicsHiRIEF LC-MS allows for in depth quantitative analysis of the phosphoproteome.
In this project we aimed at improving phosphoproteomics analysis by taking advantage of high resolution isoelectric focusing (HiRIEF) fractionation. We developed a workflow that employs titanium dioxide phospho-enrichment, followed by isobaric labeling with Tandem Mass Tags (TMT) and HiRIEF on a bro...
ORGANISM(S): Homo sapiens (Human) 
2017-07-07 | PXD005410 | Pride
Multiplex Cells Isoelectric point Tmt Phospho-peptides Phospho-sites Fractionation Quantification Networkin Cancer Phosphoproteomics Tyrosine Ipg Proteomics Hirief 10-plex Lc-ms Quantitative Mitosis Mitotic arrest Hela Kinase association Multiply phosphorylated Phosphorylation Pervanadate 
ProteomicsMetal-directed metal oxide chromatography augmented the coverage of phosphoproteome
Phosphosites cluster, a set of co-regulation sites, extends a variety of protein function via the distinct combination of phosphorylation events. The coordination of proximal multisite phosphorylation is a universal mechanism to regulate protein function, activity, and interaction pattern. The commo...
ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse) 
2018-01-11 | PXD005685 | JPOST Repository
ProteomicsSequential Phosphoproteomic Enrichment through Complementary Metal-Directed Immobilized Metal Ion Affinity Chromatography
We developed a tip-based sequential IMAC based on different kinds of metal ion for increasing the coverage of phosphoproteome. This approach not only can be used for singly and multiply phosphopeptides separation but also for acidic, basophilic and Pro-directed phosphopeptides separation.
ORGANISM(S): Homo Sapiens (human) 
2016-09-07 | PXD004903 | JPOST Repository
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