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UnknownComprehensive Evaluation of Different TiO2-Based Phosphopeptide Enrichment and Fractionation Methods for Phosphoproteomics.
Not available
S-EPMC9265536 | biostudies-literature
ProteomicsComprehensive evaluation of different TiO2-based phosphopeptide enrichment and fractionation methods for phosphoproteomics
We performed a comprehensive evaluation of four different TiO2-based phosphopeptide enrichment methods using different non-phosphopeptide excluders. Then, two phosphopeptide fractionation methods, including the ammonia-based and the TEA based high pH reversed-phase fractionation, are also evaluated.
ORGANISM(S): Homo Sapiens 
PXD034264 |
ProteomicsiSPI: A Multi-dimensional, Regenerable, Proteome-scale, Human Phosphopeptide Resource for Phosphoproteomics
Mass spectrometry-based phosphoproteomics has become indispensable for understanding cellular signaling in complex biological systems. Despite the central role of protein phosphorylation, the field still lacks inexpensive, regenerable, and diverse phosphopeptides with ground truth phosphorylation po...
ORGANISM(S): Homo sapiens (Human) 
2022-10-26 | PXD031171 | Pride
Flr Phosphoproteomics Synthetic biology 
ProteomicsCharacterization of phosphopeptide enrichment strategy for mass spectrometry-based proteomic analysis
We attempted to evaluate four strategies for phosphopeptide enrichment, using the titanium dioxide (TiO2) and Phos-tag ligand particles, from in-solution or in-gel digests prior to mass spectrometry-based proteomic analysis.
ORGANISM(S): Homo Sapiens (human) Cellular Organisms 
2021-12-24 | PXD026295 | JPOST Repository
ProteomicsComplementary Phosphoproteomic Approaches Link IL-23R Downstream Signaling with Metabolic Adaptation in Lymphocytes
Interleukin (IL)-23 mediated signal transduction represents a major molecular mechanism underlying the pathology of inflammatory bowel disease (IBD), Crohn's disease (CD) and ulcerative colitis (UC). In addition, emerging evidence supports the role of IL-23-driven Th17 cells in inflammation. Compone...
ORGANISM(S): Homo sapiens (Human) 
2016-04-21 | PXD002990 | Pride
Phosphoproteomics il-23 
ProteomicsModulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy
Although many affinity adsorbents have been developed for phosphopeptides enrichment, high-specifically capturing the multi-phosphopeptides is still a big challenge. Here, we investigated the mechanism of phosphate ions coordination and substitution on affinity adsorbents surfaces and modulated the ...
ORGANISM(S): Homo sapiens (Human) 
2016-08-03 | PXD004252 | Pride
Mass spectrometry Multi-phosphopeptide enrichment Pre-coordination Phosphoproteomics Competitive substitution 
Proteomicsrat neutrophils phosphoproteome analysis
Intestinal ischemia reperfusion injury (iIRI) is a severe clinical condition presenting high morbidity and mortality worldwide. Some of the systemic consequences of iIRI can be prevented by applying ischemic preconditioning (iIPC), a series of short ischemia/reperfusion events preceding the major is...
ORGANISM(S): Rattus Norvegicus (ncbitaxon:10116) 
2019-11-06 | MSV000084545 | MassIVE
UnknownDevelopment of a tandem affinity phosphoproteomic method with motif selectivity and its application in analysis of signal transduction networks.
Not available
S-EPMC4489695 | biostudies-literature
UnknownSex-Dependent Synaptic Remodeling of the Somatosensory Cortex in Mice With Prenatal Methadone Exposure.
Not available
S-EPMC10569410 | biostudies-literature
ProteomicsProteomics profiling of KAIMRC1 in comparison to MDA-MB231 and MCF-7
Proteomics characterization of KAIMRC1 cell line, a naturally immortalized breast cancer cells, is described in comparison to MCF7 and MDA-231 breast cancer cells. Quantitative proteomics analysis using the tandem mass tag (TMT) labeled technique in conjunction with phosphopeptide enrichment method ...
ORGANISM(S): Homo sapiens (Human) 
2020-06-22 | PXD017721 | Pride
Breast cancer  cell lines  tmt  proteomics  phosphoproteomics 
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