Xiaohu Mei
Instructor
Boston University School of Medicine
Dept of Physiology & Biophysics

MBBS, Shandong University
PhD, Boston University School of Medicine



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.
Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.

  1. 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.View Related Profiles. PMID: 29208698.
     
  2. 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.View Related Profiles. PMID: 29131142.
     
  3. 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.View Related Profiles. PMID: 28042708; DOI: 10.1080/13506129.2016.1269737;.
     
  4. 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.View Related Profiles. PMID: 27317763; PMCID: PMC4959866; DOI: 10.1194/jlr.M068874;.
     
  5. 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.View Related Profiles. PMID: 26562506; PMCID: PMC4744490; DOI: 10.1016/j.jmb.2015.10.029;.
     
  6. 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.View Related Profiles. PMID: 26048453; PMCID: PMC4522339; DOI: 10.1016/j.arcmed.2015.05.012;.
     
  7. 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.View Related Profiles. PMID: 24919401; PMCID: PMC4617355; DOI: 10.1194/jlr.M047241;.
     
  8. 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.View Related Profiles. PMID: 24702826; PMCID: PMC4047191; DOI: 10.1111/febs.12809;.
     
  9. 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.View Related Profiles. PMID: 24308948; PMCID: PMC3934732; DOI: 10.1194/jlr.M044743;.
     
  10. Gursky O, Jones MK, Mei X, Segrest JP, Atkinson D. Structural basis for distinct functions of the naturally occurring Cys mutants of human apolipoprotein A-I. J Lipid Res. 2013 Dec; 54(12):3244-57.View Related Profiles. PMID: 24038317; PMCID: PMC3826673; DOI: 10.1194/jlr.R037911;.
     
Showing 10 of 12 results. Show More

This graph shows the total number of publications by year, by first, middle/unknown, or last author.

Bar chart showing 12 publications over 6 distinct years, with a maximum of 2 publications in 2011 and 2013 and 2014 and 2015 and 2016 and 2017

YearPublications
20112
20132
20142
20152
20162
20172
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700 Albany St Ctr for Adv Biomed Res
Boston MA 02118
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