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

Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation

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Combining effect size estimates in meta-analysis with repeated measures and independent-groups designs.

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

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

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MUTANT GENES IN FAMILIAL ALZHEIMER'S DISEASE AND TRANSGENIC MODELS

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Peripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis

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Gender differences in the amount and deposition of amyloidβ in APPswe and PS1 double transgenic mice

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Multiple Effects of Aspartate Mutant Presenilin 1 on the Processing and Trafficking of Amyloid Precursor Protein

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Neuroinflammation in Alzheimer's disease

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Immune attack: the role of inflammation in Alzheimer disease

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Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies

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

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

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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

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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

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

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

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

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

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

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

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

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

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

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

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

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

Cromolyn Reduces Levels of the Alzheimer’s Disease-Associated Amyloid β-Protein by Promoting Microglial Phagocytosis

Zhang, C., Griciuc, A., Hudry, E., Wan, Y., Quinti, L., Ward, J., Forte, A. M., Shen, X., Ran, C., Elmaleh, D. R., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-19641-2 · Cited by 99 · 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

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

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

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

Nurr1:RXRα heterodimer activation as monotherapy for Parkinson’s disease

Spathis, A. D., Asvos, X., Ziavra, D., Karampelas, T., Topouzis, S., Cournia, Z., Qing, X., Alexakos, P., Smits, L. M., Dalla, C., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616874114 · 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

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

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

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

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

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

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

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

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

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

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

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 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

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

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

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

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

Rohn, T. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140714908 · Cited by 67 · see citing works

Molecular Signaling Mechanisms of Natural and Synthetic Retinoids for Inhibition of Pathogenesis in Alzheimer’s Disease

Chakrabarti, M., McDonald, A. J., Will Reed, J., Moss, M. A., Das, B. C., & Ray, S. K. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-150450 · Cited by 57 · 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

Neuroprotective Effect of Bexarotene in the SOD1G93A Mouse Model of Amyotrophic Lateral Sclerosis

Riancho, J., Ruiz‐Soto, M., Berciano, M. T., Berciano, J., & Lafarga, M. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00250 · Cited by 56 · see citing works

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

Age-Dependent, Non-Cell-Autonomous Deposition of Amyloid from Synthesis of β-Amyloid by Cells Other Than Excitatory Neurons

Veeraraghavalu, K., Zhang, C. M., Zhang, X., Tanzi, R. E., & Sisodia, S. S. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5079-13.2014 · Cited by 50 · 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

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

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

Yuan, C., Guo, X., Zhou, Q., Du, F., Jiang, W., Zhou, X., Liu, P., Chi, T., Ji, X., Gao, J., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.028 · Cited by 48 · see citing works

Bexarotene normalizes chemotherapy-induced myelin decompaction and reverses cognitive and sensorimotor deficits in mice

Chiang, A. C. A., Seua, A. V., Singhmar, P., Arroyo, L. D., Mahalingam, R., Hu, J., Kavelaars, A., & Heijnen, C. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01061-x · Cited by 26 · see citing works

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

Rotstein, B. H., Hooker, J. M., Woo, J., Collier, T. L., Brady, T. J., Liang, S. H., & Vasdev, N. (2014) · ACS Medicinal Chemistry Letters · doi:10.1021/ml500065q · Cited by 39 · see citing works

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

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The Continuing Failure of Bexarotene in Alzheimer’s Disease Mice

Balducci, C., Paladini, A., Micotti, E., Tolomeo, D., Vitola, P. L., Grigoli, E., Richardson, J. C., & Forloni, G. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150029 · Cited by 37 · see citing works

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

Muñoz-Cabrera, J. M., Sandoval-Hernández, A. G., Niño, A., Báez, T., Bustos-Rangel, A., Cardona‐Gómez, G. P., Múnera, A., & Arboleda, G. (2019) · PLoS ONE · doi:10.1371/journal.pone.0223578 · Cited by 38 · see citing works

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

Lefterov, I. M., Schug, J., Mounier, A., Nam, K. N., Fitz, N. F., & Koldamova, R. P. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.05.019 · Cited by 36 · see citing works

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

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The national biomarker development alliance: confronting the poor productivity of biomarker research and development

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Some Candidate Drugs for Pharmacotherapy of Alzheimer’s Disease

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

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Soluble Gamma-secretase Modulators Attenuate Alzheimer's β-amyloid Pathology and Induce Conformational Changes in Presenilin 1

Raven, F., Ward, J. F., Zoltowska, K., Wan, Y., Bylykbashi, E., Miller, S. J., Shen, X., Choi, S.-H., Rynearson, K. D., Berezovska, O., et al. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.08.028 · Cited by 36 · see citing works

High-Content Microfluidic Screening Platform Used To Identify σ2R/Tmem97 Binding Ligands that Reduce Age-Dependent Neurodegeneration in C. elegans SC_APP Model

Mondal, S., Hegarty, E., Sahn, J. J., Scott, L. L., Gökçe, S. K., Martin, C., Ghorashian, N., Satarasinghe, P., Iyer, S. V., Sae-Lee, W., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00428 · Cited by 33 · see citing works

Retinoic acid receptor-targeted drugs in neurodegenerative disease

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

Pierrot, N., Lhommel, R., Quenon, L., Hanseeuw, B. J., Dricot, L., Sindic, C. J. M., Maloteaux, J., Octavea, J.-N., & Ivanoiu, A. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150405 · Cited by 29 · see citing works

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

Natunen, T., Martiskainen, H., Sarajärvi, T., Helisalmi, S., Pursiheimo, J., Viswanathan, J., Laitinen, M. H., Mäkinen, P. M., Kauppinen, T., Rauramaa, T. H., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080700 · Cited by 26 · see citing works

The novel function of bexarotene for neurological diseases

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

Carter, A. Y., Letronne, F., Fitz, N. F., Mounier, A., Wolfe, C. M., Nam, K. N., Reeves, V. L., Kamboh, H., Lefterov, I. M., & Koldamova, R. P. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172161 · Cited by 25 · see citing works

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

Huy, P. D. Q., Thai, N. Q., Bednáriková, Z., Phuc, L. H., Linh, H. Q., Gažová, Z., & Li, M. S. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00107 · Cited by 25 · see citing works

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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A novel apoE-mimetic increases brain apoE levels, reduces Aβ pathology and improves memory when treated before onset of pathology in male mice that express APOE3

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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

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

Tesseur, I. C., Lo, A. C., Roberfroid, A., Dietvorst, S., Broeck, B. V., Borgers, M., Gijsen, H. J. M., Moechars, D., Mercken, M. H., Kemp, J. A., et al. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-s1-p40 · Cited by 1 · see citing works

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

Rosenthal, J., Belfort, G., & Isaacson, D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153150 · Cited by 8 · see citing works

Comment on “ApoE-Directed Therapeutics Rapidly Clear beta-Amyloid and

Fitz, N. F., Cronican, A. A., Lefterov, I. M., & Koldamova, R. P. (2016)