Proteomics

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Cellular ADP-ribosylome characterization with HCD and EThcD


ABSTRACT: Protein ADP-ribosylation is a post-translational modification involved in important physiological and pathological processes. Here, we present an optimized method using the Orbitrap Fusion Tribrid mass spectrometer, which drastically improves the overall ADP-ribosylation site localization score and boosts the identification of ADP-ribosylated peptides. We compared the HCD, ETcaD or EThcD fragmentation methods for the identification of ADP-ribose acceptor sites in a complex cellular sample and further combined them in a product dependent manner, exploiting the unique fragmentation properties of the ADP-ribose moiety as a trigger for a targeted fragmentation of modified peptides.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Prof. Michael O.Hottiger 

PROVIDER: MSV000080008 | MassIVE | Thu Jul 28 06:38:00 BST 2016

SECONDARY ACCESSION(S): PXD004676

REPOSITORIES: MassIVE

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Publications

Combining Higher-Energy Collision Dissociation and Electron-Transfer/Higher-Energy Collision Dissociation Fragmentation in a Product-Dependent Manner Confidently Assigns Proteomewide ADP-Ribose Acceptor Sites.

Bilan Vera V   Leutert Mario M   Nanni Paolo P   Panse Christian C   Hottiger Michael O MO  

Analytical chemistry 20170113 3


Protein adenosine diphosphate (ADP)-ribosylation is a physiologically and pathologically important post-translational modification. Recent technological advances have improved analysis of this complex modification and have led to the discovery of hundreds of ADP-ribosylated proteins in both cultured cells and mouse tissues. Nevertheless, accurate assignment of the ADP-ribose acceptor site(s) within the modified proteins identified has remained a challenging task. This is mainly due to poor fragm  ...[more]

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