# Developing Mass Spectrometry-based Approaches to Characterize Mono- and Poly(ADP-ribosyl)ated Proteomes

> **NIH NIH F31** · JOHNS HOPKINS UNIVERSITY · 2021 · $46,036

## Abstract

PROJECT SUMMARY
Post-translational modifications (PTMs) involve the addition of chemical groups to proteins,
modulating the structures or functions of the modified proteins to coordinate cellular processes.
ADP-ribosylation, the addition of adenosine diphosphate ribose to proteins, exists in both a
monomeric (MARylation) and polymeric (PARylation) form, allowing for more complex regulation.
The balance between the synthesis and degradation of ADP-ribosylation forms is fundamental for
regulating cellular processes. Disruption of this balance leads to human diseases like cancer and
neurodegeneration. However, much remains to be learned about the respective contributions of
MARylation and PARylation to the regulation of physiological processes and disease
pathogenesis. Mass spectrometry (MS)-based proteomics methods are the go-to techniques for
investigating PTMs in healthy and disease states. Previously published proteomics methods
studying ADP-ribosylation have been successful in identifying modification sites on amino acids
of varied chemical properties. However, all of these methods fail to identify the ADP-ribosylation
form associated with each site. This proposal aims to develop a MS-based proteomics method to
identify the site and form of ADP-ribosylation on a proteome-wide level. To preserve information
about the form of ADP-ribosylation at modification sites, my method will either (a) keep ADP-
ribosylation intact during enrichment or (b) determine whether the amino acid is MARylated or
PARylated. With a tool to distinguish between the ADP-ribosylation forms at each site, we can
identify potential functional differences of MARylated and PARylated proteins in healthy and
disease states. Ultimately, this workflow will provide valuable insights into the biological functions
of the different forms of ADP-ribosylation in physiological and disease states.

## Key facts

- **NIH application ID:** 10314945
- **Project number:** 1F31GM143918-01
- **Recipient organization:** JOHNS HOPKINS UNIVERSITY
- **Principal Investigator:** Isabel Uribe
- **Activity code:** F31 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2021
- **Award amount:** $46,036
- **Award type:** 1
- **Project period:** 2021-09-01 → 2023-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10314945

## Citation

> US National Institutes of Health, RePORTER application 10314945, Developing Mass Spectrometry-based Approaches to Characterize Mono- and Poly(ADP-ribosyl)ated Proteomes (1F31GM143918-01). Retrieved via AI Analytics 2026-05-23 from https://api.ai-analytics.org/grant/nih/10314945. Licensed CC0.

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