Abstract 2927 Identifying Histone Citrullination Sites in vitro via NMR Spectroscopy

Citrullination is a charge-modifying post-translational modification (PTM) whereby arginine is converted to the non-coded amino acid citrulline by calcium-activated protein arginine deiminases (PADs; EC 3.5.3.15). In this enzyme class, there are five known PAD isozymes found in humans (1, 2, 3, 4, and 6) that are differentially expressed and have distinct targets including histones. While some histone citrullination sites are known, a comprehensive investigation of all histone arginine targets by each PAD is lacking.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.110047
Primary Topic
Glycosylation and Glycoproteins Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Abstract 2927 Identifying Histone Citrullination Sites in vitro via NMR Spectroscopy

Emma A. Morrison, Alicja Kowalczyk
Journal of Biological Chemistry
Glycosylation and Glycoproteins Research
article

Abstract 2927 Identifying Histone Citrullination Sites in vitro via NMR Spectroscopy

Emma A. Morrison, Alicja Kowalczyk
article en

Abstract

Citrullination is a charge-modifying post-translational modification (PTM) whereby arginine is converted to the non-coded amino acid citrulline by calcium-activated protein arginine deiminases (PADs; EC 3.5.3.15). In this enzyme class, there are five known PAD isozymes found in humans (1, 2, 3, 4, and 6) that are differentially expressed and have distinct targets including histones. While some histone citrullination sites are known, a comprehensive investigation of all histone arginine targets by each PAD is lacking.

Journal of Biological ChemistryVol. 301(5)
Soka University of America (US)
National Science Foundation
Openalex Percentile: Top 88%
Glycosylation and Glycoproteins Research
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