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ProteomicsSystematic characterization of 21 post-translational modification using synthetic peptides
The data presented in this study in the - context of the ProteoemTools project - is based on the synthesis of about 5000 synthetic peptides carrying 21 different post-translational modifications to systematically characterize their chromatographic and mass spectrometric properties using multimodal L...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-04-05 | MSV000091649 | MassIVE
TranscriptomicsA new strategy to identify the long-distance mobile peptides from xylem sap.
Total RNAs were extracted from internodes and roots of 18 day-after-germination soybean plants, and the expression levels of the genes that encode xylem sap associated peptides or proteins were analyzed.
ORGANISM(S): Glycine max 
2015-10-23 | E-MTAB-5052 | biostudies-arrayexpress
ProteomicsDevelopment of a high-throughput (10 minute microflow gradient) platform for quantitation of histone modifications on a new QTOF instrument
Histone post-translational modifications (PTMs) regulate gene expression patterns through epigenetic mechanisms. The 5 histone proteins (H1, H2A, H2B, H3, and H4) are extensively modified, with over 75 distinct modification types spanning more than 200 sites. Despite strong advances in mass spectrom...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-05-06 | MSV000094696 | MassIVE
ProteomicsDevelopment of a high-throughput (10 minute microflow gradient) platform for quantitation of histone modifications on a new QTOF instrument
Histone post-translational modifications (PTMs) regulate gene expression patterns through epigenetic mechanisms. The 5 histone proteins (H1, H2A, H2B, H3, and H4) are extensively modified, with over 75 distinct modification types spanning more than 200 sites. Despite strong advances in mass spectrom...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-05-06 | MSV000094695 | MassIVE
ProteomicsA mass-tolerant database search identifies a large proportion of unassigned spectra in shotgun proteomics as modified peptides
Less than half of all MS/MS spectra acquired in shotgun proteomics typically result in a confident peptide match. Here we present an ultra-tolerant Sequest database search that allowed peptide matching even with modifications of unknown masses up to ±500 Da. From an HEK293 cell proteome-wide datas...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-06-19 | MSV000079841 | MassIVE
ProteomicsDifferences of uniquely identified peptides between ddaPASEF and diaPASEF
Recent advancements in mass spectrometry-based proteomics have made it possible to conduct comprehensive protein analysis. In particular, the emergence of the data-independent acquisition (DIA) method powered by machine learning has significantly improved protein identification effi-ciency. However,...
ORGANISM(S): Homo Sapiens (human) 
2024-12-01 | PXD056754 | JPOST Repository
ProteomicsSystematic characterization of 21 post-translational modification using synthetic peptides
The data presented in this study in the - context of the ProteoemTools project - is based on the synthesis of about 5000 synthetic peptides carrying 21 different post-translational modifications to systematically characterize their chromatographic and mass spectrometric properties using multimodal L...
ORGANISM(S): Homo sapiens (Human) 
2018-06-04 | PXD009449 | Pride
Post-translational modification Acetylation Immonium ion Ptm Proteometools Synthetic standard Phosphorylation Diagnostic ion Neutral loss Synthetic peptides 
UnknownAntiviral peptides against Enterovirus A71 causing hand, foot and mouth disease.
Not available
S-EPMC7648656 | biostudies-literature
ProteomicsPeptide collision cross section of 22 post-translational modifications
The present study investigates the ion mobility characteristics of synthetic peptides carrying 22 different post-translational modifications by Ion Mobility-Mass Spectrometry. Samples were kindly provided by the ProteomeTools project.
ORGANISM(S): Homo sapiens (Human) 
2023-08-25 | PXD042416 | Pride
Tims Ptm Post-translational modifications Collision cross section Ccs Ion mobility 
UnknownOpening a SWATH Window on Posttranslational Modifications: Automated Pursuit of Modified Peptides.
Not available
S-EPMC4813695 | biostudies-literature
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