Sort   by:  
 Page size 
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 
2022-06-02 | PXD034264 |
UnknownComprehensive Evaluation of Different TiO2-Based Phosphopeptide Enrichment and Fractionation Methods for Phosphoproteomics.
Not available
S-EPMC9265536 | biostudies-literature
ProteomicsFractionation of phosphopeptides using reversed phase microcolumn prior to LC-MS analysis
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
Phosphopeptide fractionation H1299 cell line Phosphorylation 
ProteomicsAUTOMATED PHOSPHOPEPTIDE ENRICHMENT FROM MINUTE QUANTITIES OF FROZEN MALIGNANT MELANOMA TISSUE
To acquire a deeper understanding of malignant melanoma (MM), it is essential to study the proteome of patient tissues. In particular, phosphoproteomics of MM has become of significant importance because of the central role that phosphorylation plays in the development of MM. Investigating clinical ...
ORGANISM(S): Homo sapiens (Human) 
2018-11-23 | PXD011175 | Pride
Bravo assaymap Sensitivity Fe(iii)-imac. Malignant melanoma phosphoproteomics Phosphopeptide enrichment 
ProteomicsOff-line high pH reversed-phase fractionation for in-depth phosphoproteomics
In this study we provide a detailed analysis of the physicochemical characteristics of phosphopeptides, which have been fractionated by off-line high pH chromatography (HpH) before subsequent titanium dioxide (TiO2) enrichment and LC-MS/MS analysis. Our results demonstrate that HpH is superior to st...
ORGANISM(S): Mus musculus (Mouse) 
2014-10-23 | PXD001404 | Pride
Phosphoproteomics  high ph reversed-phase  phosphorylation  peptides  enrichment  fractionation  titanium dioxide  orbitrap 
UnknownGas-phase fractionation DDA promotes in-depth DIA phosphoproteome analysis.
Not available
S-EPMC11787513 | biostudies-literature
ProteomicsMass Spectrometry-compatible Subcellular Fractionation
We developed a mass spectrometry-compatible subcellular fractionation protocol. This method involves separating cells into cytoplasmic, organellar, and nuclear fractions without ultracentrifugation.
ORGANISM(S): Homo Sapiens (human) 
2019-11-15 | PXD013581 | JPOST Repository
ProteomicsReproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines
There is a need for robust phosphopeptide enrichment methods to allow signaling network analysis in cancer cell lines and tissues with minimal fractionation. With recent instrument developments thousands of unique phosphopeptides can be detected by single-shot LC-MS/MS. However, successful phosphopr...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080715 | MassIVE
UnknownFractionation of Enriched Phosphopeptides Using pH/Acetonitrile-Gradient-Reversed-Phase Microcolumn Separation in Combination with LC-MS/MS Analysis.
Not available
S-EPMC7312998 | biostudies-literature
UnknownAutomated phosphopeptide enrichment from minute quantities of frozen malignant melanoma tissue.
Not available
S-EPMC6287822 | biostudies-literature
Sort   by:  
 Page size