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

When the dust settles: what did we learn from the bexarotene discussion?

Tesseur, I. C., & Strooper, B. D. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt218 · Cited by 15

Bexarotene Impairs Cognition and Produces Hypothyroidism in a Mouse Model of Down Syndrome and Alzheimer’s Disease

Vidal, V., Puente, A., García-Cerro, S., García‐Unzueta, M. T., Rueda, N., Riancho, J., & Martínez‐Cué, C. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.613211 · Cited by 16

Bexarotene Binds to the Amyloid Precursor Protein Transmembrane Domain, Alters Its α-Helical Conformation, and Inhibits γ-Secretase Nonselectively in Liposomes

Kamp, F., Scheidt, H. A., Winkler, E., Basset, G., Heinel, H., Hutchison, J. M. S., LaPointe, L. M., Sanders, C. R., Steiner, H., & Huster, D. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00068 · Cited by 15

Nuclear SphK2/S1P signaling is a key regulator of ApoE production and Aβ uptake in astrocytes

Komai, M., Noda, Y., Ikeda, A., Kaneshiro, N., Kamikubo, Y., Sakurai, T., Uehara, T., & Takasugi, N. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100510 · Cited by 13

Molecular dynamics simulations and molecular flooding studies of the retinoid X-receptor ligand binding domain

Gray, G. M., Ma, N., Wagner, C. E., & van der Vaart, A. (2017) · Journal of Molecular Modeling · doi:10.1007/s00894-017-3260-9 · Cited by 13

Relaunching an old drug: the potential role of bexarotene in neurodegenerative diseases

Riancho, J., Berciano, M. T., Berciano, J., & Lafarga, M. (2016) · Journal of Neurology · doi:10.1007/s00415-015-8004-0 · Cited by 13

Brain metabolite clearance: impact on Alzheimer’s disease

Zolezzi, J. M., & Inestrosa, N. C. (2014) · Metabolic Brain Disease · doi:10.1007/s11011-014-9527-2 · Cited by 12

Protective Effects of Bexarotene against Amyloid-β25-35-Induced Dysfunction in Hippocampal Neurons through the Insulin Signaling Pathway

Dai, W., Yang, J., Chen, T., & Yang, Z. R. (2014) · Neurodegenerative Diseases · doi:10.1159/000358397 · Cited by 11

Inhibitory Mechanism of An Anticancer Drug, Bexarotene Against Amyloid β Peptide Aggregation: Repurposing Via Neuroinformatics Approach

Bibi, N., Rizvi, S. M. D., Batool, A., & Kamal, M. A. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190801123235 · Cited by 10

Parkinson's disease: a long and difficult journey.

Casey, G. (2013) · PubMed · Cited by 10

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

Evaluating Novel RXR Agonists That Induce ApoE and Tyrosine Hydroxylase in Cultured Human Glioblastoma Cells

Mallick, S., Marshall, P. A., Wagner, C. E., Heck, M. C., Sabir, Z. L., Sabir, M. S., Dussik, C. M., Grozić, A., Kaneko, I., & Jurutka, P. W. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00707 · Cited by 8

9-cis beta-carotene-enriched diet significantly improved cognition and decreased Alzheimer’s disease neuropathology and neuroinflammation in Alzheimer’s disease-like mouse models

Twitto‐Greenberg, R., Zaltsman, S. L., Michaelson, D. M., Liraz, O., Lubitz, I., Atrakchi, D., Shemesh, C., Ashery, U., Cooper, I., Harari, A., et al. (2023) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2023.09.005 · Cited by 7

Therapeutic Strategies for Neurodegenerative Diseases

Fantini, J., & Yahi, N. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800111-0.00014-x · Cited by 7

Cancer drugs with high repositioning potential for Alzheimer’s disease

Majeed, J., Sabbagh, M. N., Kang, M. H., Lawrence, J. J., Pruitt, K., Bacus, S. S., Reyna, E., Brown, M., & Decourt, B. (2023) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2023.2296079 · Cited by 9

Synthesis of a new fluorine-18-labeled bexarotene analogue for PET imaging of retinoid X receptor

Wang, M., Davis, T., Gao, M., & Zheng, Q. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.02.037 · Cited by 6

Measuring Olfactory Processes in Mus musculus

Schellinck, H. M. (2017) · Behavioural Processes · doi:10.1016/j.beproc.2017.08.009 · Cited by 6

Bexarotene cannot reduce amyloid beta plaques through inhibition of production of amyloid beta peptides: in silico and in vitro study

Huy, P. D. Q., Thai, N. Q., Bednáriková, Z., Linh, H. Q., Gažová, Z., & Li, M. S. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp00049b · Cited by 4

The Impact of Apolipoprotein E Allelic Variants on Alzheimer’s Disease

Serrano, E., Sanz, P. G., & Barrantes, F. J. (2021) · Springer eBooks · doi:10.1007/978-3-030-61721-9_29 · Cited by 4

RXR-Mediated Remodeling of Transcriptional and Chromatin Landscapes in APP Mouse Brain: Insights from Integrated Single-Cell RNA and ATAC Profiling

Yi, L., Wang, X., Girardi, C. S., Fitz, N. F., Koldamova, R. P., & Lefterov, I. M. (2025) · Cells · doi:10.3390/cells14241970 · Cited by 3

Perspectives on the Role of APOE4 as a Therapeutic Target for Alzheimer’s Disease

Patel, K., Srivastava, S., Kushwah, S., & Mani, A. (2021) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-210027 · Cited by 4

Pathogenesis, modulation, and therapy of Alzheimer’s disease: A perspective on roles of liver-X receptors

Štefulj, J., Panzenboeck, U., Hof, P. R., & Šimić, G. (2013) · Translational Neuroscience · doi:10.2478/s13380-013-0136-z · Cited by 3

Brain Single-Cell Transcriptional Responses to Bexarotene-Activated RXR in an Alzheimer’s Disease Model

Girardi, C. S., Yi, L., Fitz, N. F., Gelain, D. P., Lefterov, I. M., & Koldamova, R. P. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052435 · Cited by 2

Studies cast doubt on cancer drug as Alzheimer's treatment

Shen, H. M. (2013) · Nature · doi:10.1038/nature.2013.13058 · Cited by 2

Potential treatment of Alzheimer’s disease astrocyte pathology based on nuclear lipid regulation

Komai, M., & Takasugi, N. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01125 · Cited by 1

Ausgewählte altersbedingte Erkrankungen

Behl, C., & Ziegler, C. (2015) · Springer eBooks · doi:10.1007/978-3-662-48250-6_4 · Cited by 1

Selected Age-Related Disorders

Behl, C., & Ziegler, C. (2013) · SpringerBriefs in molecular medicine · doi:10.1007/978-3-642-45179-9_4

Alzheimer’s Disease Therapeutics Targeting Apolipoprotein E

Liao, F., & Holtzman, D. M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00010-1

Cerebral Innate Immunity

Gate, D., & Town, T. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802851-3.00012-7

Additional file 2 of 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. L., Kavelaars, A., & Heijnen, C. J. (2020) · Figshare · doi:10.6084/m9.figshare.13233153

Additional file 1 of 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. J. (2020) · Figshare · doi:10.6084/m9.figshare.13233150

Impact de l’infection à Helicobacter pylori sur la maladie d’Alzheimer

Baudron, C. R. (2014) · theses.fr (ABES) · doi:10.70675/201f68e4z646cz4e66z80e2zd8a4b726fbe7

The role of the nicotinic receptors in prefrontal cortex spontaneous neuronal activity in the normal and diseased brain

Koukouli, F. (2016) · theses.fr (ABES) · doi:10.70675/83df9f57z48cfz4372z8c94za5f54e4b5e30

Caractérisation du site de liaison du cholestérol sur l'APP : un modulateur de la sécrétion de peptides amyloïdes

Hanbouch, L. (2017) · theses.fr (ABES) · doi:10.70675/c4d2c894zf69dz4ae4z9ab1zf4135d0efa12

BindingDB Entry 50018264: Targeting Nuclear Receptors in Neurodegeneration and Neuroinflammation.

BindingDB (2024) · UC San Diego · doi:10.7270/q27p93md

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)