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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
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
One of the major additions in mass spectrometry technology has been the irruption of the Orbitrap mass analyzer, which has boosted the proteomics analyses of biological complex samples since its introduction. Here we assessed the performance of the new generation Orbitrap Fusion Lumos Tribrid mass s...
ORGANISM(S): Homo sapiens (Human) 
2017-03-09 | PXD004940 | Pride
A global cPILOT assay developed on an Orbitrap Velos instrument was transitioned to an Orbitrap Fusion Lumos instrument. Parameters such as the LC gradient, m/z isolation window, dynamic exclusion, targeted mass analyses, and SPS-N were optimized. The number of proteins identified on the Fusion Lumo...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-08 | PXD012133 | 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
We compared the performance of multidimensional protein identification (MudPIT) on Velos Pro Orbitrap (VPO) and Velos Orbitrap Elite (VOE) mass spectrometers to single dimension reversed phase (RP) chromatography on a Q Exactive Plus (QE+) and an Orbitrap Fusion™ Lumos™ (OFL). Using a digested HeLa...
ORGANISM(S): Homo sapiens (Human) 
2019-03-04 | PXD009875 | Pride
Here, we report the optimization result of Orbitrap Fusion Lumos acquistion parameters.
ORGANISM(S): Homo Sapiens (human) 
MLL-fusions represent a large group of leukemia drivers, whose diversity originates from the vast molecular heterogeneity of C-terminal fusion partners of MLL protein. While studies of selected MLL-fusions have revealed critical molecular pathways, unifying mechanisms across all MLL-fusions remain p...
ORGANISM(S): Homo sapiens (Human) 
2018-05-25 | PXD009338 | Pride
Protein glycosylation is a post-translational modification (PTM) responsible for many aspects of proteomic diversity and biological regulation. Correlation of the intact glycoform to the protein attachment site is a critical step to assign functional roles to specific glycoproteins. Isotope targeted...
ORGANISM(S): Homo sapiens (Human) 
2017-02-22 | PXD004302 | Pride
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