apoE3[K146N/R147W] acts as a dominant negative apoE form that prevents remnant clearance and inhibits the biogenesis of HDL

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Apolipoprotein E Inhibits Platelet-derived Growth Factor-induced Vascular Smooth Muscle Cell Migration and Proliferation by Suppressing Signal Transduction and Preventing Cell Entry to G1 Phase

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Apolipoprotein E Effectively Inhibits Lipoprotein Lipase-mediated Lipolysis of Chylomicron-like Triglyceride-rich Lipid Emulsions and

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Variable heparan sulfate proteoglycan binding of apolipoprotein E variants may modulate the expression of type III hyperlipoproteinemia.

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Defective hepatic lipoprotein receptor binding of beta-very low density lipoproteins from type III hyperlipoproteinemic patients. Importance of apolipoprotein E.

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The Central Helices of ApoA-I Can Promote ATP-binding Cassette Transporter A1 (ABCA1)-mediated Lipid Efflux

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Defective Lipid Delivery Modulates Glucose Tolerance and Metabolic Response to Diet in Apolipoprotein E–Deficient Mice

Hofmann, S. M., Pérez–Tilve, D., Greer, T. M., Coburn, B. A., Grant, E., Basford, J. E., Tschöp, M. H., & Hui, D. Y. (2007) · Diabetes · doi:10.2337/db07-0403 · Cited by 103 · see citing works

Cell-derived Apolipoprotein E (ApoE) Particles Inhibit Vascular Cell Adhesion Molecule-1 (VCAM-1) Expression in Human Endothelial Cells

Stannard, A. K., Riddell, D. R., Sacre, S. M., Tagalakis, A. D., Langer, C., von Eckardstein, A., Cullen, P., Athanasopoulos, T., Dickson, G., & Owen, J. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104812200 · Cited by 101 · see citing works

The Effects of Mutations in Helices 4 and 6 of ApoA-I on Scavenger Receptor Class B Type I (SR-BI)-mediated Cholesterol Efflux Suggest That Formation of a Productive Complex between Reconstituted High Density Lipoprotein and SR-BI Is Required for Efficient Lipid Transport

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The functional characteristics of a human apolipoprotein E variant (cysteine at residue 142) may explain its association with dominant expression of type III hyperlipoproteinemia

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Pathway of biogenesis of apolipoprotein E-containing HDL <i>in vivo</i> with the participation of ABCA1 and LCAT

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Lipoprotein Lipase Binds to Low Density Lipoprotein Receptors and Induces Receptor-mediated Catabolism of Very Low Density Lipoproteins

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Apolipoprotein E4 Impairs Macrophage Efferocytosis and Potentiates Apoptosis by Accelerating Endoplasmic Reticulum Stress*

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Lipoprotein and receptor interactions in vivo

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Genetic Mutations Affecting Human Lipoproteins, Their Receptors, and Their Enzymes

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Probing the pathways of chylomicron and HDL metabolism using adenovirus-mediated gene transfer

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Apolipoprotein E (apoE) isoforms differentially induce nitric oxide production in endothelial cells

Sacre, S. M., Stannard, A. K., & Owen, J. S. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00261-8 · Cited by 73 · see citing works

Domains of Apolipoprotein E Contributing to Triglyceride and Cholesterol Homeostasis in Vivo

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Apolipoprotein E inhibits Toll-like receptor (TLR)-3- and TLR-4-mediated macrophage activation through distinct mechanisms

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Apolipoprotein E Receptor Binding VersusHeparan Sulfate Proteoglycan Binding in Its Regulation of Smooth Muscle Cell Migration and Proliferation

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Nascent very-low-density lipoprotein triacylglycerol hydrolysis by lipoprotein lipase is inhibited by apolipoprotein E in a dose-dependent manner

JONG, C. M., DAHLMANS, E. H. V., HOFKER, H. M., & HAVEKES, M. L. (1997) · Biochemical Journal · doi:10.1042/bj3280745 · Cited by 55 · see citing works

The Receptor Binding Domain of Apolipoprotein E Is Responsible for Its Antioxidant Activity

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SR-BI Mediates Cholesterol Efflux via Its Interactions with Lipid-Bound ApoE. Structural Mutations in SR-BI Diminish Cholesterol Efflux

Chroni, A., Nieland, T. J. F., Kypreos, K. E., Krieger, M., & Zannis, V. I. (2005) · Biochemistry · doi:10.1021/bi051029o · Cited by 52 · see citing works

Antimitogenic effects of HDL and APOE mediated by Cox-2–dependent IP activation

Kothapalli, D., Fuki, I. V., Ali, K., Stewart, S. A., Zhao, L., Yahil, R. J., Kwiatkowski, D. J., Hawthorne, E. A., FitzGerald, G. A., Phillips, M. C., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19097 · Cited by 50 · see citing works

Apolipoprotein A-I _Fin: Dominantly Inherited Hypoalphalipoproteinemia Due to a Single Base Substitution in the Apolipoprotein A-I Gene

Miettinen, H. E., Gylling, H., Miettinen, T. A., Viikari, J., Paulin, L., & Kontula, K. (1997) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.17.1.83 · Cited by 47 · see citing works

LDL receptor deficiency or apoE mutations prevent remnant clearance and induce hypertriglyceridemia in mice

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Apolipoprotein E2 Accentuates Postprandial Inflammation and Diet-Induced Obesity to Promote Hyperinsulinemia in Mice

Kuhel, D. G., Konaniah, E. S., Basford, J. E., McVey, C. M., Goodin, C., Chatterjee, T. K., Weintraub, N. L., & Hui, D. Y. (2012) · Diabetes · doi:10.2337/db12-0390 · Cited by 43 · see citing works

Distinct signaling mechanisms for apoE inhibition of cell migration and proliferation

Hui, D. Y., & Basford, J. E. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.030 · Cited by 40 · see citing works

Point Mutations in Apolipoprotein A-I Mimic the Phenotype Observed in Patients with Classical Lecithin:Cholesterol Acyltransferase Deficiency

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LCAT can Rescue the Abnormal Phenotype Produced by the Natural ApoA-I Mutations (Leu141Arg)_Pisa and (Leu159Arg)_FIN

Koukos, G., Chroni, A., Duka, A., Kardassis, D., & Zannis, V. I. (2007) · Biochemistry · doi:10.1021/bi7003203 · Cited by 33 · see citing works

Molecular Mechanisms of Type III Hyperlipoproteinemia: The Contribution of the Carboxy-Terminal Domain of ApoE Can Account for the Dyslipidemia That Is Associated with the E2/E2 Phenotype

Kypreos, K. E., Li, X., van Dijk, K. W., Havekes, L. M., & Zannis, V. I. (2003) · Biochemistry · doi:10.1021/bi0271796 · Cited by 33 · see citing works

Apolipoprotein E1-Hammersmith (Lys146 → Asn;Arg147 → Trp), due to a dinucleotide substitution, is associated with early manifestation of dominant type III hyperlipoproteinaemia

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Naturally occurring and bioengineered apoA-I mutations that inhibit the conversion of discoidal to spherical HDL: the abnormal HDL phenotypes can be corrected by treatment with LCAT

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Analysis of the structure and function relationship of human apolipoprotein E in vivo, using adenovirus‐mediated gene transfer

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A dominant negative form of the transcription factor c-Jun affects genes that have opposing effects on lipid homeostasis in mice

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Testing the role of apoA-I, HDL, and cholesterol efflux in the atheroprotective action of low-level apoE expression

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Apolipoprotein E inhibition of vascular hyperplasia and neointima formation requires inducible nitric oxide synthase

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The Amino-Terminal 1−185 Domain of ApoE Promotes the Clearance of Lipoprotein Remnants in Vivo. The Carboxy-Terminal Domain Is Required for Induction of Hyperlipidemia in Normal and ApoE-Deficient Mice

Kypreos, K. E., Morani, P., van Dijk, K. W., Havekes, L. M., & Zannis, V. I. (2001) · Biochemistry · doi:10.1021/bi002414a · Cited by 22 · see citing works

High receptor binding affinity of lipoproteins in atypical dysbetalipoproteinemia (type III hyperlipoproteinemia).

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Vascular Apolipoprotein E Expression and Recruitment from Circulation to Modulate Smooth Muscle Cell Response to Endothelial Denudation

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Domains of apoE4 required for the biogenesis of apoE-containing HDL

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Role of the hydrophobic and charged residues in the 218–226 region of apoA-I in the biogenesis of HDL

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Molecular etiology of a dominant form of type III hyperlipoproteinemia caused by R142C substitution in apoE4

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Abstract 584: ApoE3[K146N/R147W] Acts as a Dominant Negative ApoE Form that Prevents Remnant Clearance and Inhibits the Biogenesis of HDL

PanagiotisFotakis, DimitrisKardassis, & VassilisZannis (2014) · Arteriosclerosis Thrombosis and Vascular Biology

Molecular etiology of a dominant form of type III hyperlipoproteinemia caused by R142C substitution in apoE4

Vezeridis, A. M., Drosatos, K., & Zannis, V. I. (2011) · Journal of Lipid Research · doi:10.1194/jlr.m008409 · Cited by 11 · see citing works

Molecular Mechanisms of Type III Hyperlipoproteinemia: The Contribution of the Carboxy-Terminal Domain of ApoE Can Account for the Dyslipidemia That Is Associated with the E2/E2 Phenotype

Kypreos, K. E., Li, X., van Dijk, K. W., Havekes, L. M., & Zannis, V. I. (2003) · Biochemistry · doi:10.1021/bi0271796 · Cited by 33 · see citing works

Dominant expression of type III hyperlipoproteinemia. Pathophysiological insights derived from the structural and kinetic characteristics of ApoE-1 (Lys146--&gt;Glu).

Mann, W. A., Lohse, P., Gregg, R. E., Ronan, R., Hoeg, J. M., Zech, L. A., & Brewer, H. B. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118096 · Cited by 28 · see citing works

Residues Leu261, Trp264, and Phe265 Account for Apolipoprotein E-Induced Dyslipidemia and Affect the Formation of Apolipoprotein E-Containing High-Density Lipoprotein

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