Cardiovascular disease remains the leading cause of death in United States. Apolipoprotein A-I (apoA-I) is the major protein in high-density lipoprotein (HDL) and plays a vital role during the process of reverse cholesterol transport (RCT). Knowledge of the high-resolution structure of full-length apoA-I is essential for a molecular understanding of the function of HDL at various steps during the RCT pathway. Due to the flexible nature of apoA-I and inherent aggregation properties, the structure of full-length apoA-I has evaded description for over three decades. We use the techniques of modern molecular biophysics and structural biology to study the structure and function of apoA-I. We primarily rely on protein crystallography and molecular modeling coupled with SAXS to study the structure of apoA-I. In addition, circular dichroism, fluorescence microscope, electron microscopy, NMR and cellular assay are used to understand the function of apoA-I.
- Shandong University, MBBS
- Boston University School of Medicine, PhD
- Published on 9/24/2018
Liu M, Mei X, Herscovitz H, Atkinson D. N-terminal mutation of apoA-I and interaction with ABCA1 reveal mechanisms of nascent HDL biogenesis. J Lipid Res. 2019 Jan; 60(1):44-57. PMID: 30249788.
- Published on 12/5/2017
Gorshkova IN, Mei X, Atkinson D. Arginine 123 of apolipoprotein A-I is essential for lecithin:cholesterol acyltransferase activity. J Lipid Res. 2018 Feb; 59(2):348-356. PMID: 29208698.
- Published on 11/13/2017
Melchior JT, Walker RG, Cooke AL, Morris J, Castleberry M, Thompson TB, Jones MK, Song HD, Rye KA, Oda MN, Sorci-Thomas MG, Thomas MJ, Heinecke JW, Mei X, Atkinson D, Segrest JP, Lund-Katz S, Phillips MC, Davidson WS. A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state. Nat Struct Mol Biol. 2017 Dec; 24(12):1093-1099. PMID: 29131142.
- Published on 12/31/2016
Das M, Wilson CJ, Mei X, Wales T, Engen JR, Gursky O. Structural stability and local dynamics in disease-causing mutants of human apolipoprotein a-I: what makes the protein amyloidogenic? Amyloid. 2017 Mar; 24(sup1):11-12. PMID: 28042708.
- Published on 6/17/2016
Mei X, Liu M, Herscovitz H, Atkinson D. Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation. J Lipid Res. 2016 Aug; 57(8):1507-17. PMID: 27317763.
- Published on 11/10/2015
Das M, Wilson CJ, Mei X, Wales TE, Engen JR, Gursky O. Structural Stability and Local Dynamics in Disease-Causing Mutants of Human Apolipoprotein A-I: What Makes the Protein Amyloidogenic? J Mol Biol. 2016 Jan 29; 428(2 Pt B):449-62. PMID: 26562506.
- Published on 6/3/2015
Mei X, Atkinson D. Lipid-free Apolipoprotein A-I Structure: Insights into HDL Formation and Atherosclerosis Development. Arch Med Res. 2015 Jul; 46(5):351-60. PMID: 26048453.
- Published on 6/11/2014
Gorshkova IN, Mei X, Atkinson D. Binding of human apoA-I[K107del] variant to TG-rich particles: implications for mechanisms underlying hypertriglyceridemia. J Lipid Res. 2014 Sep; 55(9):1876-85. PMID: 24919401.
- Published on 4/28/2014
Das M, Mei X, Jayaraman S, Atkinson D, Gursky O. Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis. FEBS J. 2014 Jun; 281(11):2525-42. PMID: 24702826.
- Published on 12/5/2013
Wang L, Mei X, Atkinson D, Small DM. Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces. J Lipid Res. 2014 Mar; 55(3):478-92. PMID: 24308948.
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