Olga Gursky, PhD
Professor
Boston University School of Medicine
Dept of Physiology & Biophysics

PhD, Brandeis University
MS, Moscow State University



Our research focus is on protein folding, structure and stability. It includes the analysis of the energetic-structure-function relationship and folding pathways in proteins and peptides by circular dichroism spectroscopy, differential scanning calorimetry, fluorescence, x-ray crystallography, and site-directed mutagenesis.

Our on-going NIH-funded work is aimed at understanding the energetic and structural basis for the conformational plasticity of apolipoproteins. These are protein constituents of lipoproteins that mediate lipid transport and metabolism and are central in the pathogenesis of atherosclerosis, stroke, and certain forms of amyloidosis. Apolipoproteins are distinct in their structural adaptability to various lipoprotein particles and to plasma. We try to understand in molecular detail the energetic and structural basis for this adaptability.

A major focus of our research is on the molecular mechanisms of lipoprotein stabilization and fusion. In 2002 we revealed that lipoprotein stability is determined by kinetic barriers. Similar barriers may modulate in-vivo lipoprotein transformations. Our goal is to obtain key molecular determinants for these energy barriers.

Graduate Faculty (Primary Mentor of Grad Students)
Boston University School of Medicine, Division of Graduate Medical Sciences




Apolipoprotein conformation in amyloid and cardiovascular diseases
09/15/2017 - 08/31/2018 (PI)
NIH/National Institute of General Medica
2R01GM067260-15

Structural Stability and Functional Remodeling of High-density Lipoproteins
07/01/2016 - 09/14/2017 (PI)
NIH/National Institute of General Medica
4R01GM067260-14

Structural Stability and Functional Remodeling of High-density Lipoproteins
09/01/2013 - 06/30/2016 (PI)
NIH/National Institute of General Medica
3R01GM067260-13S1

Structural Thermodynamics of Human Apolipoprotein C-1
12/20/2002 - 05/31/2008 (PI)
NIH/National Institute of General Medical Sciences
3 R01 GM67260 08S1

Structural Thermodynamics of Human Apolipoprotein C-1
12/15/1998 - 11/30/2002 (PI)
NIH/National Heart, Lung, and Blood Institute
5 R29 HL61429 04




Yr Title Project-Sub Proj Pubs
2017 Apolipoprotein conformation in amyloid and cardiovascular diseases 2R01GM067260-15 36
2016 Structural stability and functional remodeling of high-density lipoproteins 4R01GM067260-14 36
2014 Structural stability and functional remodeling of high-density lipoproteins 5R01GM067260-12 36
2013 Structural stability and functional remodeling of high-density lipoproteins 2R01GM067260-11A1 36
2010 Structural stability and fusion of high- and very-low-density lipoproteins contai 5R01GM067260-10 36
2010 Energetics-Structure-Function Relationship in Lipoproteins 5P01HL026335-30-9 225
2009 Structural stability and fusion of high- and very-low-density lipoproteins contai 2R01GM067260-09A1 36
2009 Energetics-Structure-Function Relationship in Lipoproteins 5P01HL026335-29-9 225
2008 Energetics-Structure-Function Relationship in Lipoproteins 5P01HL026335-28-9 225
2007 Structural Thermodynamics of Human Apolipoprotein C-1 3R01GM067260-08S1 36
Showing 10 of 19 results. Show All Results
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. Jayaraman S, Gantz DL, Haupt C, Gursky O. Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis. Proc Natl Acad Sci U S A. 2017 Aug 08; 114(32):E6507-E6515.View Related Profiles. PMID: 28743750.
  2. Klimtchuk ES, Prokaeva TB, Spencer BH, Gursky O, Connors LH. In vitro co-expression of human amyloidogenic immunoglobulin light and heavy chain proteins: a relevant cell-based model of AL amyloidosis. Amyloid. 2017 Jun; 24(2):115-122.View Related Profiles. PMID: 28632419.
  3. Frame NM, Jayaraman S, Gantz DL, Gursky O. Serum amyloid A self-assembles with phospholipids to form stable protein-rich nanoparticles with a distinct structure: A hypothetical function of SAA as a "molecular mop" in immune response. J Struct Biol. 2017 Jun 20.View Related Profiles. PMID: 28645735.
  4. 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;.
  5. Frame NM, Gursky O. Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks. Amyloid. 2017 Mar; 24(sup1):13-14.View Related Profiles. PMID: 28042712; DOI: 10.1080/13506129.2016.1270930;.
  6. Jayaraman S, Sánchez-Quesada JL, Gursky O. Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: Potential implications for treatment of apolipoprotein deposition diseases. Biochim Biophys Acta. 2017 Jan; 1863(1):200-210.View Related Profiles. PMID: 27768903; DOI: 10.1016/j.bbadis.2016.10.010;.
  7. Jayaraman S, Haupt C, Gursky O. Paradoxical effects of SAA on lipoprotein oxidation suggest a new antioxidant function for SAA. J Lipid Res. 2016 Dec; 57(12):2138-2149.View Related Profiles. PMID: 27744369.
  8. Rull A, Jayaraman S, Gantz DL, Rivas-Urbina A, Pérez-Cuellar M, Ordóñez-Llanos J, Sánchez-Quesada JL, Gursky O. Thermal stability of human plasma electronegative low-density lipoprotein: A paradoxical behavior of low-density lipoprotein aggregation. Biochim Biophys Acta. 2016 09; 1861(9 Pt A):1015-24.View Related Profiles. PMID: 27233433; DOI: 10.1016/j.bbalip.2016.05.008;.
  9. Frame NM, Gursky O. Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks. FEBS Lett. 2016 Mar; 590(6):866-79.View Related Profiles. PMID: 26918388; PMCID: PMC4805461; DOI: 10.1002/1873-3468.12116;.
  10. 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;.
Showing 10 of 64 results. Show More

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

Bar chart showing 64 publications over 23 distinct years, with a maximum of 6 publications in 2016

YearPublications
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20055
20062
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20103
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In addition to these self-described keywords below, a list of MeSH based concepts is available here.

calorimetry
energy landscapes
lipoproteins
protein spectroscopy
protein stability
protein structure-function
thermodynamics and kinetics

Available to Mentor as: (Review Mentor Role Definitions):
  • Advisor
  • Career Mentor
  • Co-Mentor or Peer Mentor
  • Research / Scholarly Mentor
Contact for Mentoring:


700 Albany St Ctr for Adv Biomed Res
Boston MA 02118
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