Apolipoprotein A-I (apoA-I) is the major protein component of high density lipoproteins (HDL) and plays a central role in cholesterol metabolism. The lipid-free/lipid-poor form of apoA-I is the preferred substrate for the ATP-binding cassette transporter A1 (ABCA1). The interaction of apoA-I with ABCA1 leads to the formation of cholesterol laden high density lipoprotein (HDL) particles, a key step in reverse cholesterol transport and the maintenance of cholesterol homeostasis. Knowledge of the structure of lipid-free apoA-I is essential to understanding its critical interaction with ABCA1 and the molecular mechanisms underlying HDL biogenesis. We therefore examined the structure of lipid-free apoA-I by electron paramagnetic resonance spectroscopy (EPR). Through site directed spin label EPR, we mapped the secondary structure of apoA-I and identified sites of spin coupling as residues 26, 44, 64, 167, 217 and 226. We capitalize on the fact that lipid-free apoA-I self-associates in an anti-parallel manner in solution. We employed these sites of spin coupling to define the central plane in the dimeric apoA-I complex. Applying both the constraints of dipolar coupling with the EPR-derived pattern of solvent accessibility, we assemble...Continue Reading
Asymmetry of apolipoprotein A-I in solution as assessed from ultracentrifugal, viscometric, and fluorescence polarization studies
Inherited predisposition to generalized amyloidosis. Clinical and pathological study of a family with neuropathy, nephropathy, and peptic ulcer
Circular dichroic spectra of apolipoprotein E in model complexes and cholesterol-rich lipoproteins: lipid contribution
Phospholipid binding and lecithin-cholesterol acyltransferase activation properties of apolipoprotein A-I mutants
Defective removal of cellular cholesterol and phospholipids by apolipoprotein A-I in Tangier Disease
Properties of an N-terminal proteolytic fragment of apolipoprotein AI in solution and in reconstituted high density lipoproteins.
Structural and binding characteristics of the carboxyl terminal fragment of apolipophorin III from Manduca sexta
Synthetic model peptides for apolipoproteins. II. Characterization of the discoidal complexes generated between phospholipids and synthetic model peptides for apolipoproteins
Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state
Effects of deletion of the carboxyl-terminal domain of ApoA-I or of its substitution with helices of ApoA-II on in vitro and in vivo lipoprotein association.
Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation
Structural analysis of apolipoprotein A-I: limited proteolysis of methionine-reduced and -oxidized lipid-free and lipid-bound human apo A-I
The carboxyl-terminal hydrophobic residues of apolipoprotein A-I affect its rate of phospholipid binding and its association with high density lipoprotein.
Structural analysis of apolipoprotein A-I: effects of amino- and carboxy-terminal deletions on the lipid-free structure
A mechanism of protein-mediated fusion: coupling between refolding of the influenza hemagglutinin and lipid rearrangements
Effect of apolipoprotein A-I lipidation on the formation and function of pre-beta and alpha-migrating LpA-I particles
Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments
Folding and stability of the C-terminal half of apolipoprotein A-I examined with a Cys-specific fluorescence probe
A three-dimensional molecular model of lipid-free apolipoprotein A-I determined by cross-linking/mass spectrometry and sequence threading
Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases
Apolipoprotein A-I lysine modification: effects on helical content, lipid binding and cholesterol acceptor activity
Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I
Electron paramagnetic resonance spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of apoA-I in solution
Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme
Interaction between the N- and C-terminal domains modulates the stability and lipid binding of apolipoprotein A-I
Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry
Influence of N-terminal helix bundle stability on the lipid-binding properties of human apolipoprotein A-I
The secondary structure of apolipoprotein A-I on 9.6-nm reconstituted high-density lipoprotein determined by EPR spectroscopy
Lipid-free Apolipoprotein A-I Structure: Insights into HDL Formation and Atherosclerosis Development
High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation
Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation.
New insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolism.
Apolipoprotein A-I exchange is impaired in metabolic syndrome patients asymptomatic for diabetes and cardiovascular disease
Localization of APOL1 protein and mRNA in the human kidney: nondiseased tissue, primary cells, and immortalized cell lines
Molecular crowding impacts the structure of apolipoprotein A-I with potential implications on in vivo metabolism and function
Synchrotron radiation circular dichroism spectroscopy reveals structural divergences in HDL-bound apoA-I variants
ApoE, Lipids & Cholesterol
Serum cholesterol, triglycerides, apolipoprotein B (APOB)-containing lipoproteins (very low-density lipoprotein (VLDL), immediate-density lipoprotein (IDL), and low-density lipoprotein (LDL), lipoprotein A (LPA)) and the total cholesterol/high-density lipoprotein (HDL) cholesterol ratio are all connected in diseases. Here is the latest research.