Description
Post-translational modifications (PTMs) involve adding chemical groups to proteins, which modulate their structures and functions. ADP-ribosylation, characterized by the addition of adenosine diphosphate ribose, can occur in both monomeric (MARylation) and polymeric (PARylation) forms. Maintaining the balance between these forms is crucial for regulating cellular processes such as DNA repair, and disruption of this balance can lead to diseases, including cancer, neurodegeneration, and viral infections. Despite its importance, much remains to be learned about the specific contributions of MARylation and PARylation to these processes due to a lack of tools for jointly investigating these individual forms. Here, we present a novel mass spectrometry (MS)-based proteomics approach that preserves information about the native form of ADP-ribosylation associated with the modification site within a single proteomics experiment. Our workflow enables the simplified, binary identification of ADP-ribosylation forms, avoiding some challenges typically presented by PARylated peptides during MS analysis.
[doi:10.25345/C5JS9HK8H]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: ADPr ; Marylation ; PARylation
Contact
Principal Investigators:
(in alphabetical order)
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Benjamin C Orsburn, Johns Hopkins, USA
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ben_orsburn
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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis
of Quantified Analytes" category having a "Protein" column in this dataset.
"N/A" means no results of this type were submitted.
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