Comment on “ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models”

ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models

Cramer, P. E., Cirrito, J. R., Wesson, D. W., Lee, C. Y. D., Karlo, J. C., Zinn, A. E., Casali, B. T., Restivo, J. L., Goebel, W. D., James, M. J., et al. (2012) · Science · doi:10.1126/science.1217697 · Cited by 1,050 · see citing works

Aβ42‐driven cerebral amyloidosis in transgenic mice reveals early and robust pathology

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APOE is a major susceptibility gene for Alzheimer’s disease

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Neuroinflammation in Alzheimer's disease

Heneka, M. T., Carson, M. J., Khoury, J. E., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)70016-5 · Cited by 6,226 · see citing works

Immune attack: the role of inflammation in Alzheimer disease

Heppner, F. L., Ransohoff, R. M., & Becher, B. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3880 · Cited by 2,134 · see citing works

Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies

Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425 · see citing works

APOE and Alzheimer’s disease: Advances in genetics, pathophysiology, and therapeutic approaches

Serrano-Pozo, A., Das, S., & Hyman, B. T. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30412-9 · Cited by 1,037 · see citing works

Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer’s diseases

Huang, Y., & Mahley, R. W. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.025 · Cited by 829 · see citing works

Amyloid-β-independent regulators of tau pathology in Alzheimer disease

van der Kant, R., Goldstein, L. S. B., & Ossenkoppele, R. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-019-0240-3 · Cited by 580 · see citing works

Central Nervous System Lipoproteins: ApoE and Regulation of Cholesterol Metabolism

Mahley, R. W. (2016) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.116.307023 · Cited by 516 · see citing works

Apolipoprotein E in Alzheimer's Disease: An Update

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Apolipoprotein E, Receptors, and Modulation of Alzheimer’s Disease

Zhao, N., Liu, C.-C., Qiao, W., & Bu, G. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.03.003 · Cited by 370 · see citing works

Beyond the neuron–cellular interactions early in Alzheimer disease pathogenesis

Henstridge, C. M., Hyman, B. T., & Spires-Jones, T. L. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0113-1 · Cited by 348 · see citing works

APOE2: protective mechanism and therapeutic implications for Alzheimer’s disease

Li, Z., Shue, F., Zhao, N., Shinohara, M., & Bu, G. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00413-4 · Cited by 306 · see citing works

Dry Age-Related Macular Degeneration: Mechanisms, Therapeutic Targets, and Imaging

Rickman, C. B., Farsiu, S., Toth, C. A., & Klingeborn, M. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.13-12757 · Cited by 285 · see citing works

Near-infrared fluorescence molecular imaging of amyloid beta species and monitoring therapy in animal models of Alzheimer’s disease

Zhang, X., Tian, Y., Zhang, C. M., Tian, X., Ross, A., Moir, R. D., Sun, H., Tanzi, R. E., Moore, A. V., & Ran, C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505420112 · Cited by 227 · see citing works

TREM2 in the pathogenesis of AD: a lipid metabolism regulator and potential metabolic therapeutic target

Li, R.-Y., Qin, Q., Yang, H.-C., Wang, Y.-Y., Mi, Y.-X., Yin, Y.-S., Wang, M., Yu, C.-J., & Tang, Y. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00542-y · Cited by 204 · see citing works

An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer’s disease

Habchi, J., Arosio, P., Perni, M., Costa, A. R., Yagi‐Utsumi, M., Joshi, P., Chia, S., Cohen, S. I. A., Müller, M. B. D., Linse, S. S., et al. (2016) · Science Advances · doi:10.1126/sciadv.1501244 · Cited by 201 · see citing works

Recent Progress in Alzheimer’s Disease Research, Part 3: Diagnosis and Treatment

Hane, F. T., Robinson, M. J., Lee, B. Y., Bai, O., Leonenko, Z., & Albert, M. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160907 · Cited by 200 · see citing works

The Role of APOE and TREM2 in Alzheimer′s Disease—Current Understanding and Perspectives

Wolfe, C. M., Fitz, N. F., Nam, K. N., Lefterov, I. M., & Koldamova, R. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010081 · Cited by 192 · see citing works

Double-blind, placebo-controlled, proof-of-concept trial of bexarotene in moderate Alzheimer’s disease

Cummings, J. L., Zhong, K., Kinney, J. W., Heaney, C., Moll-Tudla, J., Joshi, A., Pontecorvo, M., Devous, M., Tang, A., & Bena, J. (2016) · Alzheimer's Research & Therapy · doi:10.1186/s13195-016-0173-2 · Cited by 190 · see citing works

HDL and cognition in neurodegenerative disorders

Hottman, D. A., Chernick, D., Cheng, S., Wang, Z., & Li, L. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.07.015 · Cited by 184 · see citing works

Integrative metabolomics‐genomics approach reveals key metabolic pathways and regulators of Alzheimer's disease

Horgusluoglu, E., Neff, R., Song, W., Wang, M., Wang, Q., Arnold, M., Krumsiek, J., Galindo‐Prieto, B., Ming, C., Nho, K., et al. (2022) · Alzheimer's & Dementia · doi:10.1002/alz.12468 · Cited by 175 · see citing works

The sleep–wake Cycle and Alzheimer’s Disease: What do We know?

Lim, M. M., Gerstner, J. R., & Holtzman, D. M. (2014) · Neurodegenerative Disease Management · doi:10.2217/nmt.14.33 · Cited by 168 · see citing works

Complete morphologies of basal forebrain cholinergic neurons in the mouse

Wu, H., Williams, J., & Nathans, J. (2014) · eLife · doi:10.7554/elife.02444 · Cited by 167 · see citing works

Apolipoprotein E as a Therapeutic Target in Alzheimer’s Disease: A Review of Basic Research and Clinical Evidence

Yamazaki, Y., Painter, M. M., Bu, G., & Kanekiyo, T. (2016) · CNS Drugs · doi:10.1007/s40263-016-0361-4 · Cited by 166 · see citing works

Changing Trends in Computational Drug Repositioning

Yella, J., Yaddanapudi, S., Wang, Y., & Jegga, A. G. (2018) · Pharmaceuticals · doi:10.3390/ph11020057 · Cited by 166 · see citing works

Therapeutic approaches targeting Apolipoprotein E function in Alzheimer’s disease

Williams, T., Borchelt, D., & Chakrabarty, P. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-0358-9 · Cited by 166 · see citing works

Interaction of Alzheimer’s β-Amyloid Peptides with Cholesterol: Mechanistic Insights into Amyloid Pore Formation

Scala, C. D., Chahinian, H., Yahi, N., Garmy, N., & Fantini, J. (2014) · Biochemistry · doi:10.1021/bi500373k · Cited by 161 · see citing works

Invited Review: APOE at the interface of inflammation, neurodegeneration and pathological protein spread in Alzheimer's disease

Tzioras, M., Davies, C., Newman, A., Jackson, R., & Spires‐Jones, T. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12529 · Cited by 147 · see citing works

ATP-binding cassette transporter A1: From metabolism to neurodegeneration

Koldamova, R., Fitz, N. F., & Lefterov, I. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.007 · Cited by 144 · see citing works

Editorial: preclinical data reproducibility for R&D - the challenge for neuroscience

Steckler, T. (2015) · SpringerPlus · doi:10.1186/2193-1801-4-1 · Cited by 141 · see citing works

Reversal of apoE4-driven brain pathology and behavioral deficits by bexarotene

Boehm-Cagan, A., & Michaelson, D. M. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.5198-13.2014 · Cited by 134 · see citing works

Molecular Anti-inflammatory Mechanisms of Retinoids and Carotenoids in Alzheimer’s Disease: a Review of Current Evidence

Honarvar, N. M., Saedisomeolia, A., Abdolahi, M., Shayeganrad, A., Sangsari, G. T., Rad, B. H., & Muench, G. W. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0857-x · Cited by 121 · see citing works

Leveraging preclinical models for the development of Alzheimer disease therapeutics

Scearce-Levie, K. A., Sanchez, P. E., & Lewcock, J. W. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0065-9 · Cited by 118 · see citing works

Soluble apoE/Aβ complex: mechanism and therapeutic target for APOE4-induced AD risk

Tai, L. M., Mehra, S., Shete, V., Estus, S., Rebeck, G. W., Bu, G., & LaDu, M. J. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-2 · Cited by 116 · see citing works

Clearing Amyloid-β through PPARγ/ApoE Activation by Genistein is a Treatment of Experimental Alzheimer’s Disease

Bonet-Costa, V., Herranz‐Pérez, V., Blanco-Gandía, M. C., Mas‐Bargues, C., Inglés, M., García-Tárraga, P., Rodríguez‐Arias, M., Miñarro, J., Borrás, C., García‐Verdugo, J. M., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151020 · Cited by 103 · see citing works

Neuronally-directed effects of RXR activation in a mouse model of Alzheimer’s disease

Mariani, M. M., Malm, T., Lamb, R., Jay, T. R., Neilson, L., Casali, B., Medarametla, L., & Landreth, G. E. (2017) · Scientific Reports · doi:10.1038/srep42270 · Cited by 98 · see citing works

High-Density Lipoproteins and Cerebrovascular Integrity in Alzheimer’s Disease

Stukas, S. K., Robert, J., & Wellington, C. L. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.003 · Cited by 96 · see citing works

Nuclear receptors in neurodegenerative diseases

Skerrett, R., Malm, T., & Landreth, G. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.019 · Cited by 94 · see citing works

Probing the Sources of the Apparent Irreproducibility of Amyloid Formation: Drastic Changes in Kinetics and a Switch in Mechanism Due to Micellelike Oligomer Formation at Critical Concentrations of IAPP

Brender, J., Krishnamoorthy, J., Sciacca, M. F. M., Vivekanandan, S., D’Urso, L., Chen, J., Rosa, C. L., & Ramamoorthy, A. (2015) · The Journal of Physical Chemistry B · doi:10.1021/jp511758w · Cited by 94 · see citing works

Amyloid-β Pathology and APOE Genotype Modulate Retinoid X Receptor Agonist Activity in Vivo

Tai, L. M., Koster, K. P., Luo, J., Lee, S., Wang, Y., Collins, N. C., Aissa, M. B., Thatcher, G. R. J., & LaDu, M. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.600833 · Cited by 93 · see citing works

Retinoids as potential targets for Alzheimer's disease

Sodhi, R. K., & Singh, N. (2014) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2014.02.016 · Cited by 91 · see citing works

Emerging Therapeutics for Alzheimer's Disease

Chiang, K., & Koo, E. H. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-135932 · Cited by 88 · see citing works

Adjusting the compass: new insights into the role of angiogenesis in Alzheimer’s disease

Jefferies, W. A., Price, K. A., Biron, K. E., Fenninger, F., Pfeifer, C. G., & Dickstein, D. L. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt230 · Cited by 85 · see citing works

Apolipoproteins E and J interfere with amyloid‐beta uptake by primary human astrocytes and microglia in vitro

Mulder, S. D., Nielsen, H. M., Blankenstein, M. A., Eikelenboom, P., & Veerhuis, R. (2014) · Glia · doi:10.1002/glia.22619 · Cited by 84 · see citing works

Quercetin stabilizes apolipoprotein E and reduces brain Aβ levels in amyloid model mice

Zhang, X., Hu, J., Zhong, L., Wang, N., Yang, L., Liu, C., Li, H., Wang, X., Zhou, Y., Zhang, Y., et al. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.04.032 · Cited by 84 · see citing works

Treatment with bexarotene, a compound that increases apolipoprotein-E, provides no cognitive benefit in mutant APP/PS1 mice

LaClair, K. D., Manaye, K. F., Lee, D. L., Allard, J. S., Savonenko, A. V., Troncoso, J. C., & Wong, P. C. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-18 · Cited by 83 · see citing works

ABCA1‐Mediated Cholesterol Efflux Capacity to Cerebrospinal Fluid Is Reduced in Patients With Mild Cognitive Impairment and Alzheimer's Disease

Yassine, H. N., Feng, Q., Chiang, J., Petrosspour, L. M., Fonteh, A. N., Chui, H. C., & Harrington, M. G. (2016) · Journal of the American Heart Association · doi:10.1161/jaha.115.002886 · Cited by 80 · see citing works

Autophagy Induction by Bexarotene Promotes Mitophagy in Presenilin 1 Familial Alzheimer’s Disease iPSC-Derived Neural Stem Cells

Martín-Maestro, P., Sproul, A. A., Martínez, H., Paquet, D., Gerges, M., Noggle, S., & Starkov, A. A. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-01665-y · Cited by 77 · see citing works

Remembering your A, B, C's: Alzheimer's disease and ABCA1

Lewandowski, C. T., Laham, M. S., & Thatcher, G. R. J. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.011 · Cited by 76 · see citing works

New Therapeutic Approaches for Alzheimer’s Disease and Cerebral Amyloid Angiopathy

Saitô, S., & Ihara, M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00290 · Cited by 76 · see citing works

Therapeutic potential of nuclear receptor agonists in Alzheimer's disease

Moutinho, M., & Landreth, G. E. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075556 · Cited by 75 · see citing works

Response to Comments on “ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models”

Landreth, G. E., Cramer, P. E., Lakner, M. M., Cirrito, J. R., Wesson, D. W., Brunden, K. R., & Wilson, D. A. (2013) · Science · doi:10.1126/science.1234114 · Cited by 73 · see citing works

A randomized controlled study to evaluate the effect of bexarotene on amyloid‐β and apolipoprotein E metabolism in healthy subjects

Ghosal, K., Haag, M., Verghese, P. B., West, T., Veenstra, T., Braunstein, J. B., Bateman, R. J., Holtzman, D. M., & Landreth, G. E. (2016) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2016.06.001 · Cited by 73 · see citing works

Alzheimer's disease pathology in APOE transgenic mouse models: The Who, What, When, Where, Why, and How

Lewandowski, C. T., Maldonado Weng, J., & LaDu, M. J. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104811 · Cited by 72 · see citing works

CSF Apo-E levels associate with cognitive decline and MRI changes

Initiative, F. T. A. D. N., Toledo, J. B., Da, X., Weiner, M. W., Wolk, D. A., Xie, S. X., Arnold, S. E., Davatzikos, C., Shaw, L. M., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1236-0 · Cited by 71 · see citing works

The emerging role of bexarotene in the treatment of Alzheimer’s disease: current evidence

Tousi, B. (2015) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s61309 · Cited by 70 · see citing works

Retinoic Acid Isomers Facilitate Apolipoprotein E Production and Lipidation in Astrocytes through the Retinoid X Receptor/Retinoic Acid Receptor Pathway

Zhao, J., Fu, Y., Liu, C., Shinohara, M., Nielsen, H. M., Dong, Q., Kanekiyo, T., & Bu, G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526095 · Cited by 70 · see citing works

PPARδ activation by bexarotene promotes neuroprotection by restoring bioenergetic and quality control homeostasis

Dickey, A. S., Sanchez, D. N., Arreola, M., Sampat, K. R., Fan, W., Arbez, N., Akimov, S., Kanegan, M. J. V., Ohnishi, K., Gilmore-Hall, S. K., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aal2332 · Cited by 69 · see citing works

Bexarotene Blocks Calcium-Permeable Ion Channels Formed by Neurotoxic Alzheimer’s β-Amyloid Peptides

Fantini, J., Scala, C. D., Yahi, N., Troadec, J., Sadelli, K., Chahinian, H., & Garmy, N. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn400183w · Cited by 68 · see citing works

Targeting Nuclear Receptors in Neurodegeneration and Neuroinflammation

Willems, S., Zaienne, D., & Merk, D. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00186 · Cited by 66 · see citing works

ABCA1 is Necessary for Bexarotene-Mediated Clearance of Soluble Amyloid Beta from the Hippocampus of APP/PS1 Mice

Corona, A. W., Kodoma, N., Casali, B. T., & Landreth, G. E. (2015) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-015-9627-8 · Cited by 66 · see citing works

Activation of RXR/PPARγ underlies neuroprotection by bexarotene in ischemic stroke

Certo, M., Endo, Y., Ohta, K., Sakurada, S., Bagetta, G., & Amantea, D. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.10.009 · Cited by 65 · see citing works

Bexarotene-Activated Retinoid X Receptors Regulate Neuronal Differentiation and Dendritic Complexity

Mounier, A., Georgiev, D., Nam, K. N., Fitz, N. F., Castranio, E. L., Wolfe, C. M., Cronican, A. A., Schug, J., Lefterov, I., & Koldamova, R. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1001-15.2015 · Cited by 64 · see citing works

Dendrimer Architectonics to Treat Cancer and Neurodegenerative Diseases with Implications in Theranostics and Personalized Medicine

Moorthy, H., & Govindaraju, T. (2021) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c01319 · Cited by 64 · see citing works

Current and future implications of basic and translational research on amyloid-β peptide production and removal pathways

Böhm, C., Chen, F., Sévalle, J., Qamar, S., Dodd, R. B., Li, Y., Schmitt‐Ulms, G., Fraser, P. E., & George‐Hyslop, P. S. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.02.016 · Cited by 63 · see citing works

Bexarotene modulates retinoid-X-receptor expression and is protective against neurotoxic endoplasmic reticulum stress response and apoptotic pathway activation

Dheer, Y., Chitranshi, N., Gupta, V., Abbasi, M., Mirzaei, M., You, Y., Chung, R., Graham, S. L., & Gupta, V. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1041-9 · Cited by 63 · see citing works

Cancer Chemotherapy Related Cognitive Impairment and the Impact of the Alzheimer’s Disease Risk Factor APOE

Fernandez, H. R., Varma, A., Flowers, S. A., & Rebeck, G. W. (2020) · Cancers · doi:10.3390/cancers12123842 · Cited by 62 · see citing works

Omega-3 Fatty Acids Augment the Actions of Nuclear Receptor Agonists in a Mouse Model of Alzheimer's Disease

Casali, B. T., Corona, A. W., Mariani, M. M., Karlo, J. C., Ghosal, K., & Landreth, G. E. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1000-15.2015 · Cited by 62 · see citing works

Peripheral Versus Central Nervous System APOE in Alzheimer’s Disease: Interplay across the Blood-Brain Barrier

Chernick, D., Ortiz-Valle, S., Jeong, A., Qu, W., & Li, L. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.134306 · Cited by 54 · see citing works

Bexarotene reduces network excitability in models of Alzheimer's disease and epilepsy

Bomben, V. C., Holth, J. K., Reed, J. G., Cramer, P. E., Landreth, G. E., & Noebels, J. L. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.029 · Cited by 60 · see citing works

Be positive about negatives–recommendations for the publication of negative (or null) results

Bespalov, A., Steckler, T., & Skolnick, P. (2019) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2019.10.007 · Cited by 59 · see citing works

Beta-Amyloid and Tau-Protein: Structure, Interaction, and Prion-Like Properties

Tatarnikova, O. G., Орлов, М. А., & Bobkova, N. V. (2015) · Biochemistry (Moscow) · doi:10.1134/s000629791513012x · Cited by 59 · see citing works

Connecting the Dots Between Hypercholesterolemia and Alzheimer’s Disease: A Potential Mechanism Based on 27-Hydroxycholesterol

Wu, M., Zhai, Y., Liang, X., Chen, W., Lin, R., Ma, L., Huang, Y., Zhao, D., Liang, Y., Zhao, W., et al. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.842814 · Cited by 57 · see citing works

Rescuing effects of RXR agonist bexarotene on aging-related synapse loss depend on neuronal LRP1

Tachibana, M., Shinohara, M., Yamazaki, Y., Liu, C., Rogers, J. T., Bu, G., & Kanekiyo, T. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.12.003 · Cited by 57 · see citing works

Proteolytic Cleavage of Apolipoprotein E4 as the Keystone for the Heightened Risk Associated with Alzheimer’s Disease

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Bexarotene Promotes Cholesterol Efflux and Restricts Apical-to-Basolateral Transport of Amyloid-β Peptides in an In Vitro Model of the Human Blood-Brain Barrier

Kuntz, M., Candela, P., Saint‐Pol, J., Lamartinière, Y., Boucau, M., Sevin, E., Fénart, L., & Gosselet, F. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150469 · Cited by 54 · see citing works

High‐density lipoprotein mimetic peptide 4F mitigates amyloid‐β‐induced inhibition of apolipoprotein E secretion and lipidation in primary astrocytes and microglia

Chernick, D., Ortiz‐Valle, S., Jeong, A., Swaminathan, S. K., Kandimalla, K. K., Rebeck, G. W., & Li, L. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14554 · Cited by 53 · see citing works

Molecular Insight into the Therapeutic Promise of TargetingAPOE4for Alzheimer’s Disease

Mamun, A. A., Uddin, M. S., Bashar, M. F. B., Zaman, S., Begum, Y., Bulbul, I. J., Islam, M. S., Sarwar, M. S., Mathew, B., Amran, M. S., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5086250 · Cited by 53 · see citing works

Alzheimer’s disease: relevant molecular and physiopathological events affecting amyloid-β brain balance and the putative role of PPARs

Zolezzi, J. M., Candia, S. B., Santos, M. J., & Inestrosa, N. C. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00176 · Cited by 52 · see citing works

Astaxanthin exerts protective effects similar to bexarotene in Alzheimer's disease by modulating amyloid-beta and cholesterol homeostasis in blood-brain barrier endothelial cells

Fanaee‐Danesh, E., Gali, C. C., Tadić, J., Zandl‐Lang, M., Kober, A. C., Agujetas, V. R., de Dios, C., Tam‐Amersdorfer, C., Stracke, A., Albrecher, N. M., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.04.019 · Cited by 52 · see citing works

Therapeutic targeting of nuclear receptors, liver X and retinoid X receptors, for Alzheimer's disease

Fitz, N. F., Nam, K. N., Koldamova, R. P., & Lefterov, I. M. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14668 · Cited by 50 · see citing works

OAB-14, a bexarotene derivative, improves Alzheimer's disease-related pathologies and cognitive impairments by increasing β-amyloid clearance in APP/PS1 mice

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Synthesis of [11C]Bexarotene by Cu-Mediated [11C]Carbon Dioxide Fixation and Preliminary PET Imaging

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Retinoid X receptor ligands: a patent review (2007 – 2013)

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Bexarotene therapy ameliorates behavioral deficits and induces functional and molecular changes in very-old Triple Transgenic Mice model of Alzheimer´s disease

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The Continuing Failure of Bexarotene in Alzheimer’s Disease Mice

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RNA-sequencing reveals transcriptional up-regulation of Trem2 in response to bexarotene treatment

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RXR controlled regulatory networks identified in mouse brain counteract deleterious effects of Aβ oligomers

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Lack of support for bexarotene as a treatment for Alzheimer's disease

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Retinoids and motor neuron disease: Potential role in amyotrophic lateral sclerosis

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Targretin Improves Cognitive and Biological Markers in a Patient with Alzheimer’s Disease

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The novel function of bexarotene for neurological diseases

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Effects of NR1H3 Genetic Variation on the Expression of Liver X Receptor α and the Progression of Alzheimer's Disease

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Analysis of differential secondary effects of novel rexinoids: select rexinoid X receptor ligands demonstrate differentiated side effect profiles

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Bexarotene Does Not Clear Amyloid Beta Plaques but Delays Fibril Growth: Molecular Mechanisms

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Liver X receptor agonist treatment significantly affects phenotype and transcriptome of APOE3 and APOE4 Abca1 haplo-deficient mice

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Preclinical data reproducibility for R&D—the challenge for neuroscience

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Improving the predictive value of interventional animal models data

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New Hope from an Old Drug: Fighting Alzheimer's Disease with the Cancer Drug Bexarotene (Targretin)?

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MicroRNAs in brain cholesterol metabolism and their implications for Alzheimer's disease

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Nuclear Localization of Apolipoprotein E4: A New Trick for an Old Protein

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Comment on “ApoE-Directed Therapeutics Rapidly Clear b-Amyloid and Reverse Deficits in AD Mouse Models”

(2012)

Bexarotene treatment does not clear β-Amyloid in an AD mouse model and Beagle dogs

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Response to Comments on “ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models”

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Early Treatment Critical: Bexarotene Reduces Amyloid-Beta Burden In Silico

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Clearing away Alzheimer's disease

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