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

Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530

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

Morris, S. B., & DeShon, R. P. (2002) · Psychological Methods · doi:10.1037/1082-989x.7.1.105 · Cited by 2,502

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

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

Radde, R., Bolmont, T., Kaeser, S. A., Coomaraswamy, J., Lindau, D., Stoltze, L., Calhoun, M. E., Jäggi, F., Wolburg, H., Gengler, S., et al. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400784 · Cited by 986

Co-expression of multiple transgenes in mouse CNS: a comparison of strategies

Jankowsky, J. L., Slunt, H. H., Ratovitski, T., Jenkins, N. A., Copeland, N. G., & Borchelt, D. R. (2001) · Biomolecular Engineering · doi:10.1016/s1389-0344(01)00067-3 · Cited by 746

MUTANT GENES IN FAMILIAL ALZHEIMER'S DISEASE AND TRANSGENIC MODELS

Price, D. L., & Sisodia, S. S. (1998) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.21.1.479 · Cited by 581

Peripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis

Eisele, Y. S., Obermüller, U., Heilbronner, G., Baumann, F., Kaeser, S. A., Wolburg, H., Walker, L. C., Staufenbiel, M., Heikenwalder, M., & Jucker, M. (2010) · Science · doi:10.1126/science.1194516 · Cited by 568

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

Wang, J., Tanila, H., Puoliväli, J., Kadish, I., & Groen, T. V. (2003) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.08.009 · Cited by 316

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

Kim, S., Leem, J. Y., Lah, J. J., Slunt, H. H., Levey, A. I., Thinakaran, G., & Sisodia, S. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108245200 · Cited by 103

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

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

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

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

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

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

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

Apolipoprotein E in Alzheimer's Disease: An Update

Yu, J.-T., Tan, L., & Hardy, J. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014300 · Cited by 394

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

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

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 293

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 228

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 204

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 211

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

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 201

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 188

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

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

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 172

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

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 173

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 168

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

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

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 123

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 121

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

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 104

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

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 101

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

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

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 98

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

Tai, L. M., Koster, K. P., Luo, J., Lee, S. H., Wang, Y.-T., Collins, N. C., Ben Aissa, M., Thatcher, G. R. J., & LaDu, M. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.600833 · Cited by 89

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 94

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 88

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 95

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 86

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 88

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

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

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

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

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 76

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 75

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 77

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.-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 67

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

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

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 65

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

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

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

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 69

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

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

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 66

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

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 64

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 63

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

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 62

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

Rohn, T. T. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140714908 · Cited by 58

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

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 59

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

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 57

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.-C., Sevin, E., Fenart, L., & Gosselet, F. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-150469 · Cited by 55

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 51

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 54

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 56

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 49

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 52

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 53

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 49

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

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

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

Yamada, S., & Kakuta, H. (2014) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2014.880692 · Cited by 39

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

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 39

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

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

Nam, K. N., Mounier, A., Fitz, N. F., Wolfe, C. M., Schug, J., Lefterov, I. M., & Koldamova, R. P. (2016) · Scientific Reports · doi:10.1038/srep24048 · Cited by 36

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

Poste, G. H., Compton, C. C., & Barker, A. D. (2014) · Expert Review of Molecular Diagnostics · doi:10.1586/14737159.2015.974561 · Cited by 36

Some Candidate Drugs for Pharmacotherapy of Alzheimer’s Disease

Miziak, B., Błaszczyk, B., & Czuczwar, S. J. (2021) · Pharmaceuticals · doi:10.3390/ph14050458 · Cited by 35

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

O‘Hare, E., Jeggo, R., Kim, E., Barbour, B., Walczak, J., Palmer, P., Lyons, T., Page, D., Hanna, D., Meara, J., et al. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.04.020 · Cited by 33

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

Raven, F., Ward, J. F., Zoltowska, K. M., Wan, Y., Bylykbashi, E., Miller, S., Shen, X., Choi, S. H., Rynearson, K. D., Berezovska, O., et al. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.08.028 · Cited by 35

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. N., Iyer, S., Sae-Lee, W., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00428 · Cited by 41

Retinoic acid receptor-targeted drugs in neurodegenerative disease

Clark, J. N., Whiting, A., & McCaffery, P. J. A. (2020) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2020.1811232 · Cited by 35

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

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

The novel function of bexarotene for neurological diseases

Liu, Y., Wang, P., Jin, G., Shi, P., Zhao, Y., Guo, J., Yin, Y., Shao, Q.-H., Li, P., & Yang, P. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102021 · Cited by 30

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

Marshall, P. A., Jurutka, P. W., Wagner, C. E., van der Vaart, A., Kaneko, I., Chavez, P. I., Ma, N., Bhogal, J. S., Shahani, P. H., Swierski, J. C., et al. (2015) · Pharmacology Research & Perspectives · doi:10.1002/prp2.122 · Cited by 26

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., & Koldamova, R. (2017) · PLOS ONE · doi:10.1371/journal.pone.0172161 · Cited by 28

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

Improving the predictive value of interventional animal models data

Zeiss, C. J. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.10.015 · Cited by 25

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

Aicardi, G. (2013) · Rejuvenation Research · doi:10.1089/rej.2013.1497 · Cited by 24

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

Yoon, H., Flores, L. F., & Kim, J. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.04.020 · Cited by 23

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

Rohn, T. T. (2017) · International Journal of Neurology and Neurotherapy · doi:10.23937/2378-3001/1410067 · Cited by 23

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

Valencia‐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

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 75

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

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

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

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