O. Gursky

Publications91
h-index28
Citations1,976
Highly Influential Citations49
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Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state.
  • O. Gursky, D. Atkinson
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 2 April 1996
Apolipoprotein A-1 (apoA-1) in complex with high-density lipoprotein is critically involved in the transport and metabolism of cholesterol and in the pathogenesis of atherosclerosis. We reexamined… Expand
  • 148
  • 8
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The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment.
Apolipoprotein A-I (apoA-I) is the main protein of plasma high-density lipoproteins (HDL, or good cholesterol) that remove excess cell cholesterol and protect against atherosclerosis. In hereditary… Expand
  • 58
  • 5
Amyloidogenic mutations in human apolipoprotein A‐I are not necessarily destabilizing – a common mechanism of apolipoprotein A‐I misfolding in familial amyloidosis and atherosclerosis
High‐density lipoproteins and their major protein, apolipoprotein A‐I (apoA‐I), remove excess cellular cholesterol and protect against atherosclerosis. However, in acquired amyloidosis, nonvariant… Expand
  • 41
  • 4
  • PDF
Folded functional lipid-poor apolipoprotein A-I obtained by heating of high-density lipoproteins: relevance to high-density lipoprotein biogenesis.
HDL (high-density lipoproteins) remove cell cholesterol and protect from atherosclerosis. The major HDL protein is apoA-I (apolipoprotein A-I). Most plasma apoA-I circulates in lipoproteins, yet ~5%… Expand
  • 28
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Crystal structure of Δ(185-243)ApoA-I suggests a mechanistic framework for the protein adaptation to the changing lipid load in good cholesterol: from flatland to sphereland via double belt, belt…
  • O. Gursky
  • Chemistry, Medicine
  • Journal of molecular biology
  • 9 January 2013
Apolipoprotein A-I (apoA-I) is the major protein of plasma high-density lipoproteins (HDLs), macromolecular assemblies of proteins and lipids that remove cell cholesterol and protect against… Expand
  • 35
  • 3
Kinetic stabilization and fusion of apolipoprotein A-2:DMPC disks: comparison with apoA-1 and apoC-1.
Denaturation studies of high-density lipoproteins (HDL) containing human apolipoprotein A-2 (apoA-2) and dimyristoyl phosphatidylcholine indicate kinetic stabilization. Circular dichroism (CD) and… Expand
  • 40
  • 2
Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights.
Apolipoproteins are protein constituents of lipoproteins that transport cholesterol and fat in circulation and are central to cardiovascular health and disease. Soluble apolipoproteins can… Expand
  • 40
  • 2
Monitoring protein aggregation during thermal unfolding in circular dichroism experiments
Thermal unfolding monitored by spectroscopy or calorimetry is widely used to determine protein stability. Equilibrium thermodynamic analysis of such unfolding is often hampered by its… Expand
  • 160
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Temperature-dependent β-sheet formation in β-amyloid Aβ1–40 peptide in water: uncoupling β-structure folding from aggregation
To probe the role of temperature in the conversion of soluble Alzheimer's beta-amyloid peptide (Abeta) to insoluble beta-sheet rich aggregates, we analyzed the solution conformation of Abeta(1-40)… Expand
  • 105
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Human plasma high-density lipoproteins are stabilized by kinetic factors.
High-density lipoproteins (HDL) are heterogeneous complexes of proteins and lipids that mediate cholesterol removal from the body. Our thermal and chemical denaturation studies of mature spherical… Expand
  • 68
  • 1