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ProteomicsHighly reproducible improved label-free quantitative analysis of cellular phosphoproteome by optimization of LC-MS/MS gradient and analytical column construction
Expanding the sequencing depth of the peptides showing a statistically significant quantitative change arising from a biological stimulation is critical. Here we demonstrate that optimization of LC gradient and analytical column construction can reveal over 30,000 unique peptides and 23,000 phosphop...
ORGANISM(S): Homo sapiens (Human) 
2018-10-26 | PXD005650 | Pride
Human T cell Acute leukemia Q exactive Phosphoproteomics Label free 
ProteomicsLabel-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling
Label-free quantification is a powerful method for studying cellular protein phosphorylation dynamics. However, whether current data normalization methods achieve sufficient accuracy has not been examined systematically. Here, we demonstrate that a large uni-directional shift in the phosphopeptide ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080775 | MassIVE
UnknownPhosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer.
Not available
S-EPMC6126612 | biostudies-literature
UnknownHighly reproducible improved label-free quantitative analysis of cellular phosphoproteome by optimization of LC-MS/MS gradient and analytical column construction.
Not available
S-EPMC5542054 | biostudies-literature
ProteomicsLabel-free, quantitative analysis of PKA-dependent phosphoproteome changes in Trypanosoma brucei
Protein kinase A (PKA), the main effector of second messenger cAMP, is highly conserved among eukaryotes and a paradigm for the mechanisms of regulation of protein kinases by ligands. The unique PKA holoenzymes in the phylogenetically distant protozoan parasite Trypanosoma are unresponsive to cAMP i...
ORGANISM(S): Trypanosoma brucei 
2019-02-25 | PXD012245 | Pride
Protein kinase a  pka  trypanosoma  7-cyano-7-deazainosine  label-free quantitative phosphoproteome analysis 
ProteomicsLabel-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling
Label-free quantification is a powerful method for studying cellular protein phosphorylation dynamics. However, whether current data normalization methods achieve sufficient accuracy has not been examined systematically. Here, we demonstrate that a large uni-directional shift in the phosphopeptide ...
ORGANISM(S): Homo sapiens (Human) 
2015-08-24 | PXD001374 | Pride
Mascot Phosphoproteomics Cip2a Hela Okadaic acid Ras Simspectrast Lc-ms/ms 
UnknownIdentification of Phosphorylated Cyclin-Dependent Kinase 1 Associated with Colorectal Cancer Survival Using Label-Free Quantitative Analyses.
Not available
S-EPMC4934865 | biostudies-literature
ProteomicsArabidopsis diurnal LFQ proteome and labelled phosphoproteome
Plant growth and survival depends to a large extent on the diurnal regulation of cellular processes. Although extensively studied at the transcript level, notably less is known about diurnal fluctuations at the protein level. Here, we report a high-resolution quantitative time-course of the Arabidop...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-12-18 | PXD007600 | Pride
Diurnal Phosphoproteome Arabidopsis Proteome 
ProteomicsProbing the global kinome and phosphoproteome in Chlamydomonas reinhardtii via sequential enrichment and quantitative proteomics
Identifying dynamic protein phosphorylation events is critical for understanding kinase/phosphatase regulated signaling pathways. To date, protein phosphorylation and kinase expression have been examined independently in photosynthetic organisms. Presented here is a method to study the global kinome...
ORGANISM(S): Chlamydomonas reinhardtii 
2016-10-05 | PXD004681 | Pride
Phosphoproteomics Quantitative label-free proteomics Kinome Mass spectrometry Chlamydomonas reinhardtii 
ProteomicsDynamic protein phosphorylation in Streptococcus pyogenes during growth, stationary phase and starvation
The proteome and phosphoproteome of Streptococcus pyogenes M49 was investigated at different growth phases of cultures grown in either rich medium (THY), chemically defined medium without carbon source, or chemically defined medium containing 1% fructose. Of the 815 phosphosites identified, 463 were...
ORGANISM(S): Streptococcus pyogenes NZ131 Bacteria 
2024-05-22 | PXD044423 | Pride
Growth phases Phosphoproteome Label-free quantification Pasta kinase Streptococcus pyogenes m49 Proteome 
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