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- W778599536 abstract "Cellular proteins are subject to the post-translational modification known as deimination in which the amino acid arginine is converted into citrulline. Deiminated proteins are widespread in disease states and thought to play a role in Rheumatoid Arthritis, Multiple Sclerosis, Alzheimer's disease, Parkinson's disease, and cancer. Unlike phosphorylation, substrate specificity of the peptidyl-arginine deiminase (PAD) family of enzymes, which are responsible for deimination, remains elusive and ill defined. Our objective was to identify patterns in the sequence primary and secondary structures, which may underpin this modification. We found that deiminated sequences were most likely to be categorized as having a disorganized secondary structure, and we identify trends in how the sequence primary structure influences the likelihood of deimination, based on amino acid property." @default.
- W778599536 created "2016-06-24" @default.
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- W778599536 date "2015-04-01" @default.
- W778599536 modified "2023-09-23" @default.
- W778599536 title "PADlock Cryptanalysis: a Bayesian Approach to Identifying Trends in the Post‐Translational Modification Deimination" @default.
- W778599536 doi "https://doi.org/10.1096/fasebj.29.1_supplement.717.5" @default.
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