Litcius/Paper detail

The pattern of apolipoprotein A-I lysine carbamylation reflects its lipidation state and the chemical environment within human atherosclerotic aorta

Shawna Battle, Valentin Gogonea, Belinda Willard, Zeneng Wang, Xiaoming Fu, Ying Huang, Linda M. Graham, Scott J. Cameron, Joseph A. DiDonato, John W. Crabb, Stanley L. Hazen

2022Journal of Biological Chemistry18 citationsDOIOpen Access PDF

Abstract

pathway. Monitoring patterns of apoA-I carbamylation recovered from arterial tissues can provide insights into both apoA-I structure and the chemical environment within human atheroma.

Topics & Concepts

Lipid-anchored proteinLysineAortaApolipoprotein BBiochemistryChemistryInternal medicineCholesterolMedicineAutophagyAmino acidApoptosisDiabetes, Cardiovascular Risks, and LipoproteinsAdipokines, Inflammation, and Metabolic DiseasesAdvanced Glycation End Products research
The pattern of apolipoprotein A-I lysine carbamylation reflects its lipidation state and the chemical environment within human atherosclerotic aorta | Litcius