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Molecular Bases of Disease
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- Research ArticleOpen Access
The pattern of apolipoprotein A-I lysine carbamylation reflects its lipidation state and the chemical environment within human atherosclerotic aorta
Journal of Biological ChemistryVol. 298Issue 4101832Published online: March 15, 2022- Shawna Battle
- Valentin Gogonea
- Belinda Willard
- Zeneng Wang
- Xiaoming Fu
- Ying Huang
- and others
Cited in Scopus: 2Protein lysine carbamylation is an irreversible post-translational modification resulting in generation of homocitrulline (N-ε-carbamyllysine), which no longer possesses a charged ε-amino moiety. Two distinct pathways can promote protein carbamylation. One results from urea decomposition, forming an equilibrium mixture of cyanate (CNO−) and the reactive electrophile isocyanate. The second pathway involves myeloperoxidase (MPO)-catalyzed oxidation of thiocyanate (SCN−), yielding CNO− and isocyanate.