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Top-down analysis of intact proteins by mass spectrometry provides an ideal platform for comprehensive proteoform characterization, in particular, for the identification and localization of post-translational modifications (PTM) co-occurring on a protein. One of the main bottlenecks in top-down prot...
ORGANISM(S): Homo sapiens (Human) 
2015-07-16 | PXD001845 | Pride
Confident identification of sites of protein phosphorylation by mass spectrometry (MS) is essential to advance understanding of phosphorylation-mediated signaling events. However, development of novel instrumentation requires that methods for MS data acquisition and its interrogation be evaluated an...
ORGANISM(S): Homo sapiens (Human) 
2019-09-27 | PXD007058 | Pride
A key step in proteomics is the digestion of proteins into peptides, so far largely done by using trypsin. Tryptic digestion leads to peptides that in ESI-MS attain predominantly two charges, via protonation at the free N-terminus and at the C-terminal basic residue Arginine or Lysine. These peptide...
ORGANISM(S): Homo sapiens (Human) 
2016-12-02 | PXD004447 | Pride
Confident identification of sites of protein phosphorylation by mass spectrometry (MS) is essential to advance understanding of phosphorylation-mediated signaling events. However, development of novel instrumentation requires that methods for MS data acquisition and its interrogation be evaluated an...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-03-31 | MSV000085203 | MassIVE
In this study we compared three different fragmentation techniques and two combined fragmentation schemes available on a novel tribrid mass spectrometer (Orbitrap Fusion Lumos, Themro Fisher Scientific) CID, HCD, ETD, ETD with supplemental CID (ETciD) and ETD with supplemental HCD (EThcD) on cross-l...
ORGANISM(S): Homo sapiens (Human) 
2016-08-02 | PXD003737 | Pride
ADP-ribosylation (ADPr) is a post-translational modification that plays pivotal roles in a wide range of cellular processes. Mass spectrometry (MS)-based analysis of ADPr under physiological conditions, without relying on genetic or chemical perturbation, has been hindered by technical limitations. ...
ORGANISM(S): Homo sapiens (Human) 
2020-09-23 | PXD017417 | Pride
Here, we examined the utility of AI-ETD for sequencing of the intact NIST monoclonal antibody on a modified Fusion Lumos Orbitrap platform using direct infusion. We also tested other dissociation techniques including HCD, ETD, and EThcD.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-10-19 | MSV000086331 | MassIVE
H3.1 and H3.3 quadrupole isolated and fragmented by ETD and EThcD on an Orbitrap Fusion Lumos. Comparison of two cell lines.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2015-07-14 | MSV000079191 | MassIVE
Mice were divided in two groups, one group was sedentary while the other were trained by swimming for 5 days a week for 5 months. After 5 months animals were sacrificed and left ventricles isolated for proteomics profiling. Proteins were isolated, fractionated and digested. Peptide fractions were an...
ORGANISM(S): Mus musculus (Mouse) 
2021-08-23 | PXD026558 | Pride
Capillary zone electrophoresis (CZE)-tandem mass spectrometry (MS/MS) has been recognized as an efficient approach for top-down proteomics recently for its high-capacity separation and highly sensitive detection of proteoforms. However, the commonly used collision-based dissociation methods often ca...
ORGANISM(S): Escherichia coli 
2019-06-11 | PXD012247 | Pride
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