The DOI matches its Crossref record; 87 of the 88 references it cites were found in a registry or an index.
Apolipoprotein E structure: insights into function
Abstract
Human apolipoprotein E (apoE) is a member of the family of soluble apolipoproteins. Through its interaction with members of the low-density lipoprotein receptor family, apoE has a key role in lipid transport both in the plasma and in the central nervous system. Its three common structural isoforms differentially affect the risk of developing atherosclerosis and neurodegenerative disorders, including Alzheimer's disease. Because the function of apoE is dictated by its structure, understanding the structural properties of apoE and its isoforms is required both to determine its role in disease and for the development of therapeutic strategies.
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In the citing paper
“Several biophysical studies have shown that apoE displays low thermodynamic stability and significant conformational plasticity, and allelic differences as well as single point mutations have been shown to affect protein conformation and to hinder physiological function”
From Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy (2018) · cites this paper as [13]
In the citing paper
“Several biophysical studies have shown that apoE displays low thermodynamic stability and significant conformational plasticity, and allelic differences as well as single point mutations have been shown to affect protein conformation and to hinder physiological function”
From Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy (2018) · cites this paper as [13]
In the citing paper
“Inter-domain interactions within apoE have been hypothesized to underlie key conformational changes related to apoE function [44], [45].”
From Biophysical Analysis of Apolipoprotein E3 Variants Linked with Development of Type III Hyperlipoproteinemia (2011) · cites this paper as [44]
In the citing paper
“Several studies have suggested that the structural and biophysical properties of apoE can dictate the function of the protein and have provided insight into the mechanisms by which apoE is involved in cardiovascular and neurological diseases [42], [43], [44], [45], [46], [47], [48], [49].”
From Biophysical Analysis of Apolipoprotein E3 Variants Linked with Development of Type III Hyperlipoproteinemia (2011) · cites this paper as [44]
In the citing paper
“of the second unfolding transition of apoE3 variant (Table 3) that corresponds to the unfolding of the N-terminal domain where the K146E mutation is located [13], [44], [65].”
From Biophysical Analysis of Apolipoprotein E3 Variants Linked with Development of Type III Hyperlipoproteinemia (2011) · cites this paper as [44]
In the citing paper
“Apo E4 isoform is associated with elevated total and LDL-cholesterol levels, due to the higher affinity of apo E4 for VLDL and LDL”
From Description of a Large Family with Autosomal Dominant Hypercholesterolemia Associated with the APOE p.Leu167del Mutation (2013) · cites this paper as Hatters DM et al. 2006
In the citing paper
“Mutated ApoE2 (Arg158Cys) exhibits only 2% affinity to LDL receptor compared to the wide type ApoE3 isoform [13]”
From A case report of youth-onset lipoprotein glomerulopathy with APOE Chicago mutation (2024) · cites this paper as [13]
In the citing paper
“Biophysical and computational analyses suggest that unfolding of the N-terminal domain constitutes a necessary conformational change for lipid binding and apoE function (19).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [19]
In the citing paper
“ApoE variants with lower thermodynamic stability and changes in conformational plasticity have been shown to have altered interdomain interactions and defective physiological functions (19, 24 -28).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [19]
In the citing paper
“First, apoE4 preferentially forms a “molten globule state” that ultimately reduces the in vitro stability of apoE4 relative to the other isoforms.”
From Impact of Apolipoprotein E (ApoE) Polymorphism on Brain ApoE Levels (2008) · cites this paper as Hatters et al., 2006
In the citing paper
“Second, apoE4 forms a unique salt bridge interaction between Arg-61 in the N terminal and Glu-255 in the carboxy-terminal domain.”
From Impact of Apolipoprotein E (ApoE) Polymorphism on Brain ApoE Levels (2008) · cites this paper as Hatters et al., 2006
In the citing paper
“ApoE contains two independently folded functional domains; these are a 22-kDa N-terminal domain (residues 1–191) and a 10-kDa C-terminal domain (residues 216–299) linked by a hinge region (18, 19).”
From Role of the N- and C-Terminal Domains in Binding of Apolipoprotein E Isoforms to Heparan Sulfate and Dermatan Sulfate: A Surface Plasmon Resonance Study (2008) · cites this paper as [19]
In the citing paper
“This domain interaction mediated by a salt bridge formation between Arg-61 and Glu-255 is unique to apoE4 (Fig. 1) [15].”
From Apolipoprotein E4, inhibitory network dysfunction, and Alzheimer’s disease (2019) · cites this paper as [15]
Citations
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Research works printed but not linked: 1
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Items 301–400 of 583
Xiao, H., Gao, Y., Liu, L., & Li, Y. (2017) · EXCLI journal · doi:10.17179/excli2017-289 · Cited by 17
“The APOE gene that encodes apolipoprotein E (ApoE) located on human chromosome 19 is a multifunctional protein and is a major cholesterol carrier with central roles in lipid metabolism, neurobiology, and neurodegenerative diseases (Carrasquillo et al., 2013; Hatters et al., 2006).”
BackgroundValencia‐Olvera, A. C., Balu, D., Bellur, S., McNally, T. P., Saleh, Y., Pham, D., Ghura, S., York, J. M., Johansson, J. O., LaDu, M. J., et al. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01353-z · Cited by 18
“All data is from the same cohort of mice; the n ’s differ because of study design, technical issues, and outlier tests compared to apoE3-lipoproteins in vitro and in vivo [17, 32, 77].”
BackgroundPablo, G. C., Cruz, M., Moral-Hernández, Ó. D., Leyva‐Vázquez, M. A., Antúnez-Ortiz, D. L., Cahua‐Pablo, J. Á., Alarcón‐Romero, L. D. C., Ortuño‐Pineda, C., Moreno‐Godínez, M. E., Hernández‐Sotelo, D., et al. (2015) · Clinical and Applied Thrombosis/Hemostasis · doi:10.1177/1076029614568714 · Cited by 16
Sakai‐Kato, K., Sakurai, M., Takechi‐Haraya, Y., Nanjo, K., & Goda, Y. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.09.005 · Cited by 16
Apolipoprotein E isoform dependently affects Tat-mediated HIV-1 LTR transactivation
Khan, N., Datta, G., Geiger, J. D., & Chen, X. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1129-1 · Cited by 16
“In addition, both structure and functional analyses have shown that ApoE3, but not ApoE4, preferentially binds and transports HDL, and the binding of HDL lipids opens the hinge region between N- and C-terminal domain of ApoEs allowing receptor-binding domain free access to ApoE receptors [6, 83, 84].”
Kulminski, A. M., Barochia, A. V., Loika, Y., Raghavachari, N., Arbeev, K. G., Wojczynski, M. K., Thyagarajan, B., Vardarajan, B. N., Christensen, K., Yashin, A. I., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0206873 · Cited by 16
Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4
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“However, the finding that the stabilizing interaction of the C-terminal segment with the N-terminal helix bundle in apoE3 is less pronounced in apoE4 does not support the proposed model in which the salt-bridge between the N- and C-terminal domains in apoE4 leads to more pronounced domain-domain interaction [50].”
BackgroundA Review of APOE Genotype-Dependent Autophagic Flux Regulation in Alzheimer’s Disease
Chen, H., Chen, F., Zhang, M., Chen, Y., Cui, L., & Liang, C. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210602 · Cited by 15
“Fourth, ApoE4 deformation has been found to affect lipid content [113, 119, 120] and to reveal the relative position of Arg112 in ApoE4-CLEAR sequence modeling [38].”
InfluentialAssociation of statins use and genetic susceptibility with incidence of Alzheimer's disease
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Pathophysiology of Lipoprotein Oxidation
Jairam, V., Uchida, K., & Narayanaswami, V. (2012) · InTech eBooks · doi:10.5772/50622 · Cited by 15
“It is a major cholesterol transport protein in the plasma and the CNS (Hatters et al., 2006).”
BackgroundLiu, Q., Lin, K., Yang, L., Dai, L., Wang, L., Sun, Y., Qian, C., Wei, G., Liu, D.-R., Zhu, B., et al. (2014) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.21210 · Cited by 15
Pande, A. H., Tripathy, R. K., & Nankar, S. A. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.03.020 · Cited by 15
“Apo E is an exchangeable apolipoprotein component of plasma lipoprotein particles and interaction of apoE with lipid regulates its structure and functions [1–5].”
BackgroundInfluentialGorshkova, I. N., Kypreos, K. E., Gantz, D., Zannis, V. I., & Atkinson, D. (2008) · Biochemistry · doi:10.1021/bi8015857 · Cited by 15
“Previous studies have shown that the structural and biophysical properties of apoE dictate the function of the protein (15,16,19).”
BackgroundApolipoprotein E Levels in the Cerebrospinal Fluid of North Indian Patients With Alzheimer’s Disease
Kandimalla, R. J. L., Wani, W. Y., Anand, R., Kaushal, A., Prabhakar, S. K., Grover, V. K., Bharadwaj, N., Jain, K., & Gill, K. D. (2013) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317513481097 · Cited by 15
An update on medium- and low-abundant blood plasma proteome of horse
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“encodes a 34 KDa glycoprotein containing 299 amino acids [2].”
Villeneuve, S., Brisson, D., & Gaudet, D. (2015) · Journal of Lipids · doi:10.1155/2015/742408 · Cited by 15
“Furthermore, ApoE3 and ApoE2 display a preference for highdensity lipoproteins (HDL), whereas ApoE4 prefers LDL and very-low-density lipoproteins (VLDL) [7–9].”
BackgroundÇetinkalp, Ş., Karadeniz, M., Erdoğan, M., Zengi, A., Çetintaş, V. B., Vardarli, A. T., Eroğlu, Z., Kosova, B., Özgen, G., Saygılı, F., et al. (2008) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-008-9280-8 · Cited by 15
“ApoE4 is connected with decreased longevity, increased plasma lipid and ApoB levels and higher prevalence of cardiovascular illness and also of Alzheimer’s [8, 9].”
BackgroundPhenotype and genotype predictors of BMI variability among European adults
Goñi, L., García‐Granero, M., Milagro, F. I., Cuervo, M., & Martínez, J. A. (2018) · Nutrition and Diabetes · doi:10.1038/s41387-018-0041-1 · Cited by 15
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“Apolipoprotein E (ApoE) is a 34-kDa glycosylated protein that was originally identified for its involvement in cholesterol transport (1).”
BackgroundApolipoprotein ε in Brain and Retinal Neurodegenerative Diseases
Abyadeh, M., Gupta, V., Paulo, J. A., Sheriff, S., Shadfar, S., Fitzhenry, M. J., Amirkhani, A., Gupta, V. B., Salekdeh, G. H., Haynes, P. A., et al. (2023) · Aging and Disease · doi:10.14336/ad.2023.0312-1 · Cited by 15
“glycoprotein with a molecular weight of ̴ 34 kDa, which plays a key role in lipid and cholesterol transport [27, 28].”
RECENT ADVANCES IN ALZHEIMER'S DISEASE: CAUSES AND TREATMENT
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Apolipoproteins as context-dependent regulators of lung inflammation
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“Alabaster, AL), as described previously [20].”
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Hidden Aggregation Hot-Spots on Human Apolipoprotein E: A Structural Study
Tsiolaki, P. L., Katsafana, A. D., Baltoumas, F. A., Louros, N. N., & Iconomidou, V. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092274 · Cited by 15
Apolipoprotein E4 exhibits intermediates with domain interaction
Dolai, S., Cherakara, S., & Garai, K. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140535 · Cited by 13
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“However, unlipidated APO peptides in the extracellular matrix have the potential to initiate Aβ aggregation [42].”
BackgroundPapaioannou, I., Simons, J. P., & Owen, J. S. (2012) · Cardiology Research and Practice · doi:10.1155/2012/148796 · Cited by 15
“ApoE protein comprises an N-terminal domain (1–191 residues) of four amphipathic α-helices linked to the Cterminus by a protease-sensitive loop [17].”
BackgroundZhao, X., Liu, L., Guo, C., Shen, W.-W., Cao, J., Du, F., Wu, D., & Yu, H. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-682 · Cited by 13
“It also promotes cholesterol efflux from macrophages and exerts a protective effect on oxidative processes and inflammation (39).”
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Apolipophorin III lysine modification: Effect on structure and lipid binding
Vásquez, L. J., Abdullahi, G. E., Wan, C.-P. L., & Weers, P. M. M. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.05.006 · Cited by 13
“Such an inverse correlation between protein stability and lipid binding has been reported for human apoE isoforms as well [3,17].”
Determinants of paraoxonase activity in healthy adults
Boesch, C., Rimbach, G. H., Schrader, C., Kofler, B. M., Armah, C. K., & Minihane, A. M. (2010) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201000190 · Cited by 13
Lipoprotein Glomerulopathy Associated with a Mutation in Apolipoprotein E
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“APOEproteinhastwomainregions:thelipid-binding regionattheC-terminaldomainandthereceptor-bindingregionattheN-terminaldomain,wherea flexiblehingejoinsthem[26].”
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“Both domains form α-helical bundles [24] with the critical allelic positions C112 and C158, which are located on the side of the fourth and third α-helixes in the ApoE-LD domain.”
BackgroundTiwari, D., Srivastava, G., Indari, O., Tripathi, V. S., Siddiqi, M. I., & Jha, H. C. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2138978 · Cited by 12
Apolipoprotein E O-glycosylation is associated with amyloid plaques and APOE genotype
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Meuret, C., Hu, Y.-M., Smadi, S., Bantugan, M. A., Xian, H., Martinez, A. E., Krauss, R., Ma, Q.-L., Nedelkov, D., & Yassine, H. N. (2023) · Alzheimer's Research & Therapy · doi:10.1186/s13195-023-01239-0 · Cited by 12
“Of the three apoE isoforms, apoE4 on larger particles binds with the highest affinity to LDLR and LRP1, which competes with Aβ binding [32].”
BackgroundCorsetti, J. P., Gansevoort, R. T., Bakker, S. J. L., & Dullaart, R. P. F. (2016) · Journal of clinical lipidology · doi:10.1016/j.jacl.2016.03.003 · Cited by 12
Hypothesis on ontogenesis and pathophysiology of Alzheimer’s disease
Schwab, E. D. P., Queiroz, R., Fiebrantz, A. K. B., Bastos, M., Bonini, J. S., & da Silva, W. C. F. N. (2022) · Einstein (São Paulo) · doi:10.31744/einstein_journal/2022rw0170 · Cited by 13
“The three isoforms differ from each other by replacing one or two amino acids at positions 112 and 158, as follows: ApoE2 has a cysteine residue at both positions; ApoE3 has an arginine at position 158; while type 4 has an arginine residue at both positions.(76) The polymorphisms presented by the ApoE protein are the…”
BackgroundGenetic association of apolipoprotein E polymorphisms with inflammatory bowel disease
Al-Meghaiseeb, E. S., Al-Otaibi, M. M., Al-Robayan, A. A., Al-Amro, R., Al-Malki, A. S., Arfin, M., & Al-Asmari, A. K. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i3.897 · Cited by 13
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“11 15 – 17 Despite remarkable progress towards understanding apoE function in lipid metabolism, the role of LF-apoE remains poorly understood.”
BackgroundMethodCrosstalk between Thyroid Carcinoma and Tumor-Correlated Immune Cells in the Tumor Microenvironment
Song, M., Liu, Q., Sun, W., & Zhang, H. (2023) · Cancers · doi:10.3390/cancers15102863 · Cited by 12
“It is commonly believed to be linked to Alzheimer’s disease and atherosclerosis [80].”
BackgroundShvetcov, A., Thomson, S., Cho, A., Wilkins, H., Reed, J. H., Swerdlow, R. H., Brown, D. A., Initiative, T. A. D. N., & Finney, C. A. (2024) · Aging Cell · doi:10.1111/acel.14439 · Cited by 11
“For example, murine ApoE does not show N-and C-terminal domain interactions (Hatters et al., 2006; Raffai et al., 2001 ) and there are APOE gene promoter differences between mice and humans (Maloney et al., 2007).”
Biase, E. D., Connolly, K. J., Crumpton, I. S., Cooper, O., Hallett, P. J., & Ole Isacson, A. (2025) · Scientific Reports · doi:10.1038/s41598-025-96531-4 · Cited by 15
“Structural differences between ApoE4 vs. ApoE2 and ApoE3 have also been postulated to impact protein stability, with ApoE4 appearing less stable and prone to degradation 9,10,84 .”
Hossain, M. M., Adhikari, J., Dutta, A., Khandaker, A., Islam, S., Rahman, M. M., & Shibly, A. Z. (2025) · PLOS One · doi:10.1371/journal.pone.0331339 · Cited by 11
“1, it includes additional N-terminal residues that may influence structural integrity and ligand binding [17].”
Dose, J., Nebel, A., Piegholdt, S., Rimbach, G. H., & Huebbe, P. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.031 · Cited by 11
“It mediates the binding of lipoproteins to cell-surface receptors, thereby facilitating the uptake of lipids into cells and thus the hepatic clearance of lipoproteins [1].”
BackgroundPreferential binding of apolipoprotein E derived peptides with oxidized phospholipid
Pande, A. H., & Tripathy, R. K. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.029 · Cited by 11
Apolipoprotein E, a Crucial Cellular Protein in the Lifecycle of Hepatitis Viruses
Tréguier, Y., Bull-Maurer, A., & Roingeard, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073676 · Cited by 14
Lipoprotein sialylation in atherosclerosis: Lessons from mice
Yu, L., Peng, J., & Mineo, C. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.953165 · Cited by 12
Innate immune responses to HIV infection in the central nervous system
Geffin, R., & McCarthy, M. (2013) · Immunologic Research · doi:10.1007/s12026-013-8445-4 · Cited by 10
Li, M., Kwok, M.-K., & Schooling, C. M. (2021) · Nutrients · doi:10.3390/nu13072215 · Cited by 10
Potential Peptides in Atherosclerosis Therapy
Marleau, S., Mellal, K., Huynh, D. N., & Ong, H. (2014) · Frontiers of hormone research · doi:10.1159/000360568 · Cited by 10
Gordon, S. E., & Perugini, M. A. (2016) · Springer eBooks · doi:10.1007/978-4-431-55985-6_16 · Cited by 10
Dolai, S., Pal, S., Deepa, S. M., & Garai, K. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c04738 · Cited by 8
APOE4 drives widespread changes to the hepatic proteome and alters metabolic function
Lysaker, C. R., Johnson, C. N., Csikós, V., Franczak, E., Tetlow, A. L., Benson, M. N., Thyfault, J. P., Geiger, P. C., Morris, J. K., & Wilkins, H. (2026) · iScience · doi:10.1016/j.isci.2026.115035 · Cited by 9
Chapter 14 Real Time Investigation of Protein Folding, Structure, and Dynamics in Living Cells
Li, Q., Huang, Y., Xiao, N., Murray, V. L., Chen, J., & Wang, J. (2008) · Methods in cell biology · doi:10.1016/s0091-679x(08)00814-5 · Cited by 9
Beppu, T., Gil-Bernabe, P., Boveda-Ruiz, D., D’Alessandro‐Gabazza, C. N., MATSUDA, Y., Toda, M., MIYAKE, Y., SHIRAKI, K., MURATA, M., Murata, T., et al. (2010) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2010.04023.x · Cited by 9
Kato, I., Land, S. J., Barnholtz‐Sloan, J. S., & Severson, R. K. (2011) · Cholesterol · doi:10.1155/2011/896360 · Cited by 9
“Hindawi Publishing Corporation Cholesterol Volume 2011, Article ID 896360, 9 pages doi:10.1155/2011/896360”
BackgroundInfluentialCorsetti, J. P., Sparks, C. E., Bakker, S. J. L., Gruppen, E. G., & Dullaart, R. P. F. (2017) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2017.11.010 · Cited by 9
Apolipoprotein E binds to and reduces serum levels of DNA-mimicking, pyrrolated proteins
Hirose, S., Hioki, Y., Miyashita, H., Hirade, N., Yoshitake, J., Shibata, T., Kikuchi, R., Matsushita, T., Chikazawa, M., Itakura, M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006629 · Cited by 9
“apoE contains two independently folded functional domains, a 22-kDa N-terminal domain (amino acids 1–191) and a 10-kDa C-terminal domain (amino acids 225–299), separated by a hinge region (15).”
BackgroundMicro RNAs Promoting Growth and Metastasis in Preclinical In Vivo Models of Subcutaneous Melanoma
Weidle, U. H., Ausländer, S., & Brinkmann, U. (2020) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20221 · Cited by 10
A Model of Lipid-Free Apolipoprotein A-I Revealed by Iterative Molecular Dynamics Simulation
Zhang, X., Lei, D., Zhang, L., Rames, M. J., & Zhang, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120233 · Cited by 9
“A similar more compact structure has also been found in lipid-free apo E [56] and apo A-IV [57].”
BackgroundApolipoprotein E is associated with blood lipids and inflammation in Taiwanese older adults
Vasunilashorn, S. M., Glei, D. A., Lan, C.-Y., Brookmeyer, R., Weinstein, M., & Goldman, N. (2011) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2011.07.100 · Cited by 9
Horn, J. V. C., Ellena, R. A., Tran, J. J., Beck, W. H. J., Narayanaswami, V., & Weers, P. M. M. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.04.017 · Cited by 9
“This is remarkably similar to the structural and functional organization of human apoE [47].”
Apolipoprotein E: the resilience gene
James, L. M., Engdahl, B. E., & Georgopoulos, A. P. (2017) · Experimental Brain Research · doi:10.1007/s00221-017-4941-4 · Cited by 9
Sousa, M. O., Corbella, E., Alia, P. J., Cámara, J., Castro, M. J., Pintó, X., & Navarro, M. Á. (2008) · Medicina Clínica · doi:10.1157/13117852 · Cited by 9
Apolipoprotein E Stimulates Bone Formation on Titanium in Vitro
Kodama, T. S., Goto, T., Ishibe, T., Kobayashi, S., & Takahashi, T. (2007) · Asian Journal of Oral and Maxillofacial Surgery · doi:10.1016/s0915-6992(07)80023-9 · Cited by 9
Lin, C., Liao, H.-Y., Lane, H., & Chen, C. (2023) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyad061 · Cited by 8
“Intensive research has uncovered potential mechanisms by which APOE isoforms contribute to AD development, including A β binding and plaque formation, induction of membrane disruption, and increased neuronal sensitivity to injury (Hatters et al., 2006).”
BackgroundLipoprotein Metabolism and the Treatment of Lipid Disorders
Freeman, M. W., & Walford, G. A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-323-18907-1.00041-x · Cited by 10
Estalayo-Adrián, S., Garnir, K., & Moucheron, C. (2017) · Chemical Communications · doi:10.1039/c7cc06542f · Cited by 8
Kang, Z., Cao, Y., Li, L., & Zhang, G. (2020) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2020.105424 · Cited by 8
Correlation between genetic polymorphisms in apolipoprotein E and atrial fibrillation
Wang, Y., Lou, H., Wang, M., Mei, J., Xing, T., Wang, F., Dong, Z., Wang, L., Cao, R., Yao, L., et al. (2022) · Revista Portuguesa de Cardiologia · doi:10.1016/j.repc.2021.03.013 · Cited by 8
“We therefore hypothesized that ApoE may increase the risk of AF by degrading LDL.13,14 ApoE is involved in and has significant effects on all aspects of blood lipid metabolism, including the synthesis, secretion, transport, and metabolism of lipoproteins.15 Therefore, there is likely to be a correlation between ApoE a…”
BackgroundBi, Q., Zhou, X., Lu, Y., Wang, F., Wang, Y., Wang, F., & Wang, J. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1024014 · Cited by 8
Disrupted fatty acid distribution in HDL and LDL according to apolipoprotein E allele
Dang, T. M., Conway, V., & Plourde, M. (2014) · Nutrition · doi:10.1016/j.nut.2014.11.019 · Cited by 8
“The higher u-6/u-3 ratio in the LDL of E4þ subjects is therefore a potential contributor to higher CVD risk as reported in the Literature [4,11,26], but this needs to be investigated in another trial.”
BackgroundKim, S. H., Kothari, S., Patel, A., Bielicki, J. K., & Narayanaswami, V. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.05.071 · Cited by 7
“ApoE3 is composed of several amphipathic a-helices that are folded into an N-terminal domain (1–191) and a C-terminal domain (201–299) bearing high affinity binding sites for lipids [9].”
Chen, J., & Wang, J. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9526-0 · Cited by 8
“Human apoE is a 299-residue lipid transport protein that is critical to several major human diseases including heart disease and Alzheimer’s disease (Weisgraber 1994; Huang et al. 2004; Hatters et al. 2006 ).”
BackgroundInfluentialConway, V., Allard, M., Minihane, A. M., Jackson, K. G., Lovegrove, J. A., & Plourde, M. (2014) · Lipids in Health and Disease · doi:10.1186/1476-511x-13-148 · Cited by 8
“The differencial affinity of APOE isoform for its clearence receptors, the preferential incorporation of apoE4 within TG-rich lipoproteins (TRL), and its modulating action on size and lipid composition of plasma TRL may all explain part of the APOE genotype-induce variability in lipid metabolism [6,10].”
Apolipoprotein E Expression and Purification
Newhouse, Y., & Weisgraber, K. H. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-744-0_10 · Cited by 8
Self-citationBiomarkers for Alzheimer’s Disease
Farooqui, A. A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809937-7.00007-0 · Cited by 9
Tang, K.-F., Cai, L., & Zhou, J. (2009) · Neuroscience Bulletin · doi:10.1007/s12264-009-0324-6 · Cited by 8
Pharmaceutical induction of ApoE secretion by multipotent mesenchymal stromal cells (MSCs)
Zeitouni, S., Ford, B. S., Harris, S. M., Whitney, M. J., Gregory, C. A., & Prockop, D. J. (2008) · BMC Biotechnology · doi:10.1186/1472-6750-8-75 · Cited by 8
“Although the isoforms vary only at two amino acid residues, the changes are sufficient to profoundly alter the tertiary structure and affect lipid binding properties of the protein [3,5].”
BackgroundApolipoprotein E polymorphisms and their protective effect on hepatitis E virus replication
Weller, R., Tödt, D., Engelmann, M., Friesland, M., Wedemeyer, H. H., Pietschmann, T., & Steinmann, E. (2016) · Hepatology · doi:10.1002/hep.28788 · Cited by 8
“In the literature three allelic isoforms of the ApoE gene are described (ε2, ε3, and ε4) (2).”
Calabuig-Navarro, V., Jackson, K. G., Kemp, C. F., Leake, D. S., Walden, C. M., Lovegrove, J. A., & Minihane, A. M. (2017) · Scientific Reports · doi:10.1038/srep44119 · Cited by 8
“…at positions 112 and 158 of the apoE protein are not within the receptor binding region (amino acids 136–150), it has been demonstrated that amino acid changes at these sites impact on the salt bridge formation and the 3D protein conformation which is likely to affect receptor binding activity 38 .”
Impact of allele‐specific peptides in proteome quantification
Wu, L., & Snyder, M. P. (2015) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400126 · Cited by 7
“Allelic polymorphism of the ApoE gene results in three protein isoforms (ApoE2, ApoE3, and ApoE4) that differ by only 1 or 2 amino acids [16].”
BackgroundConformational Reorganization of Apolipoprotein E Triggered by Phospholipid Assembly
Prakashchand, D. D., & Mondal, J. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c03011 · Cited by 7
Wang, L., Liu, X., Wang, H., He, H., Li, Z., & Chen, L. (2012) · Molecular Biology Reports · doi:10.1007/s11033-012-2315-3 · Cited by 7
Apolipoprotein E polymorphisms status in Iranian patients with multiple sclerosis
Rafiei, M., Yeganeh, M. Z., Sheikholeslami, S., Gozalpour, E., Ghaffarpour, M., & Hedayati, M. (2012) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2012.05.050 · Cited by 7
“APOE is postulated to play a critical role in repairing injuredneurons, modulation of neurite outgrowth, synaptic plasticity, synapse formation, and scavenging of toxins [13,48,49].”
BackgroundAn Integrative Overview of Non-Amyloid and Non-Tau Pathologies in Alzheimer’s Disease
Menta, B. W., & Swerdlow, R. H. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2603-y · Cited by 7
Takechi‐Haraya, Y., Ohgita, T., Usui, A., Nishitsuji, K., Uchimura, K., Abe, Y., Kawano, R., Konaklieva, M. I., Reimund, M., Remaley, A. T., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-46754-0 · Cited by 6
“An amphipathic ARP peptide—named A2-17—was designed based on the gly-ocosaminoglycan-binding region of human apolipoprotein E 9,16,17 , a structural protein found on lipoproteins.”
BackgroundUnraveling APOE4: The dual role in CNS and peripheral inflammation in Alzheimer's disease
Li, X., Li, Z., Chen, H., Guo, H., Ge, Y., Dong, F., Zhang, F., & Zhang, F. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115199 · Cited by 7
Krishnarjuna, B., Anantharamaiah, G. M., & Ramamoorthy, A. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148668 · Cited by 6
Mo, Y., Liu, H., Keszei, A. F. A., Dai, D. L., Makky, A., Ding, L., Pan, A., Bu, J., Mazhab‐Jafari, M. T., Chen, J., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c16025 · Cited by 6
Metadata
- Authors
- Hatters, D. M., Peters-Libeu, C. A., & Weisgraber, K. H.
- Affiliations
- Gladstone Institutes (US)
- Corresponding author
- Weisgraber, Karl H.
- ORCID
- Hatters, Danny M.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2006-08
- Volume
- 31
- Issue
- 8
- Pages
- 445-454
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2051394059
- Cited by
- 583
- References
- 88
- Citations by year
- 2026: 25 · 2025: 32 · 2024: 26 · 2023: 32 · 2022: 34 · 2021: 37 · 2020: 22 · 2019: 21 · 2018: 24 · 2017: 25 · 2016: 32 · 2015: 32 · 2014: 42 · 2013: 24 · 2012: 42
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01AG020235, P01AG022074)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Keywords
- apolipoprotein E, protein structure, APOE isoforms, low-density lipoprotein receptor family, lipid transport, atherosclerosis, Alzheimer's disease, neurodegenerative diseases, central nervous system, treatment options
- MeSH terms
- Animals, Apolipoproteins E, Humans, Models, Molecular, Protein Binding, Protein Folding, Neurodegenerative Diseases, Protein Isoforms, Atherosclerosis
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