Nuclear receptors as therapeutic targets for Alzheimer's disease

Mandrekar-Colucci, Shweta; Landreth, Gary E

doi:10.1517/14728222.2011.594043

Cited by 126Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

Nuclear receptors as therapeutic targets for Alzheimer's disease

Open access

Mandrekar-Colucci, Shweta, Landreth, Gary E·2011·Expert Opinion on Therapeutic Targets

DOI 10.1517/14728222.2011.594043PMC PMC3156324

Open this paper in CoChat — free account

Abstract

INTRODUCTION: Alzheimer's disease (AD) is characterized by the accumulation and extensive deposition of amyloid β (Aβ) in the parenchyma of the brain. This accumulation of amyloid is associated with perturbations in synaptic function, impairments in energy metabolism and induction of a chronic inflammatory response which acts to promote neuronal loss and cognitive impairment. AREAS COVERED: Currently, there are no drugs that target the underlying mechanisms of AD. Here, we propose a class of nuclear receptors as novel and promising new therapeutic targets for AD. This review summarizes the literature on nuclear receptors and their effects on AD-related pathophysiology. EXPERT OPINION: Nuclear receptors are attractive targets for the treatment of AD due to their ability to facilitate degradation of Aβ, affect microglial activation and suppress the inflammatory milieu of the brain. Liver X receptor agonists have proven difficult to move into clinical trials as long-term treatment results in hepatic steatosis. It is our view that PPAR-γ activation remains a promising avenue for the treatment for AD; however, the poor BBB permeability of the currently available agonists and the negative outcome of the Phase III clinical trials are likely to diminish interest in pursuing this target.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1517/14728222.2011.594043

Cites

110 of 110 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

LXR is a member of a group of nuclear receptors, PPARs, each of which upon activation heterodimerizes with RXR to form a functional transcription factor along with coactivators that regulate expression of many genes, including those involved in AD pathogenesis.
“LXR is a member of a group of nuclear receptors, peroxisome proliferator-activated receptors (PPARs; other members are PPARγ and PPARδ), each of which upon activation heterodimerizes with retinoid X receptor (RXR) to form a functional transcription factor along with coactivators that act to regulate expression of many genes, including those involved in AD pathogenesis [34].”
From Genome-wide analysis identifies novel loci influencing plasma apolipoprotein E concentration and Alzheimer’s disease risk (2023) · cites this paper as [34]
Split into 2 atoms — 0 confirmed, 1 partially supported, 1 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measured
Independent associations of two APOE promoter SNPs (rs769446, rs405509) with ApoE level are most likely due to their close proximity to the LXR/RXR response element.
“The independent associations of two APOE promoter SNPs (rs769446, rs405509) with ApoE level are most likely due to their close proximity to LXR/RXR response element, as APOE expression is regulated by LXR/RXR.”
From Genome-wide analysis identifies novel loci influencing plasma apolipoprotein E concentration and Alzheimer’s disease risk (2023) · cites this paper as [34]
Section 4.0 states that LXRs induce ApoE expression, and section 5.0 reports that RXR activation increases ApoE levels. The paper does not identify rs769446 or rs405509, report their independent associations with ApoE levels, or locate them near an LXR/RXR response element. The proposed explanation for those associations is therefore not supported by this source. (LLM, conf=0.87)
Experimental — accuracy not yet measured
A number of studies of thiazolidinedione PPARγ agonists pioglitazone and rosiglitazone reported salutary effects in murine models of AD.
“A number of studies of the thiazolidinedione agonists of PPARγ, pioglitazone (Actos) and rosiglitazone (Avandia), reported salutary effects of these drugs in murine models of AD (Mandrekar-Colucci and Landreth, 2011).”
From Mechanisms Underlying the Rapid Peroxisome Proliferator-Activated Receptor-γ-Mediated Amyloid Clearance and Reversal of Cognitive Deficits in a Murine Model of Alzheimer's Disease (2012) · cites this paper as Mandrekar-Colucci and Landreth, 2011

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

Peroxisome Proliferator-activated Receptor γ Ligands Suppress the Transcriptional Activation of Cyclooxygenase-2
Subbaramaiah, K., Lin, D. T., Hart, J. C., & Dannenberg, A. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007237200 · Cited by 275 · see citing works
Retracted
Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo
Nimmerjahn, A., Kirchhoff, F., & Helmchen, F. (2005) · Science · doi:10.1126/science.1110647 · Cited by 5,827 · see citing works
Fate Mapping Analysis Reveals That Adult Microglia Derive from Primitive Macrophages
Ginhoux, F., Greter, M., Leboeuf, M., Nandi, S., See, P., Gokhan, S., Mehler, M. F., Conway, S. J., Ng, L. G., Stanley, E. R., et al. (2010) · Science · doi:10.1126/science.1194637 · Cited by 5,175 · see citing works
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514 · see citing works
An Antidiabetic Thiazolidinedione Is a High Affinity Ligand for Peroxisome Proliferator-activated Receptor γ (PPARγ)
Lehmann, J. M., Moore, L. B., Smith-Oliver, T. A., Wilkison, W. O., Willson, T. M., & Kliewer, S. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.12953 · Cited by 3,626 · see citing works
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160 · see citing works
The RXR heterodimers and orphan receptors
Mangelsdorf, D. J., & Evans, R. M. (1995) · Cell · doi:10.1016/0092-8674(95)90200-7 · Cited by 3,133 · see citing works
Alternative Activation of Macrophages: An Immunologic Functional Perspective
Martinez, F. O., Helming, L., & Gordon, S. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132532 · Cited by 2,745 · see citing works
Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors α and δ
Forman, B. M., Chen, J., & Evans, R. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4312 · Cited by 2,116 · see citing works
Macrophage-specific PPARγ controls alternative activation and improves insulin resistance
Odegaard, J. I., Ricardo-Gonzalez, R. R., Goforth, M. H., Morel, C. R., Subramanian, V., Mukundan, L., Eagle, A. R., Vats, D., Brombacher, F., Ferrante, A. W., et al. (2007) · Nature · doi:10.1038/nature05894 · Cited by 2,107 · cited 2× · see citing works
“Studies have shown disruption of PPARɣ or PPARδ in myeloid cells results in impaired maturation of alternative macrophage activation [107-109].”
Background
Decreased Clearance of CNS β-Amyloid in Alzheimer’s Disease
Mawuenyega, K. G., Sigurdson, W., Ovod, V., Munsell, L., Kasten, T., Morris, J. C., Yarasheski, K. E., & Bateman, R. J. (2010) · Science · doi:10.1126/science.1197623 · Cited by 2,078 · see citing works
Roles of PPARs in health and disease
Kersten, S., Desvergne, B., & Wahli, W. (2000) · Nature · doi:10.1038/35013000 · Cited by 1,956 · see citing works
Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective
Tanzi, R. E., & Bertram, L. (2005) · Cell · doi:10.1016/j.cell.2005.02.008 · Cited by 1,849 · see citing works
9-cis retinoic acid is a high affinity ligand for the retinoid X receptor
Heyman, R. A., Mangelsdorf, D. J., Dyck, J. A., Stein, R. B., Eichele, G., Evans, R. M., & Thaller, C. (1992) · Cell · doi:10.1016/0092-8674(92)90479-v · Cited by 1,780 · cited 1× · see citing works
“Ligands for RXRs include 9-cis retinoic acid, all-trans retinoic acid (ATRA), endogenous fatty acids and synthetic agonists, termed rexinoids [33,34].”
Background
Differential expression and activation of a family of murine peroxisome proliferator-activated receptors.
Kliewer, S. A., FORMAN, B. M., Blumberg, B., Ong, E. S., Borgmeyer, U., Mangelsdorf, D. J., Umesono, K., & Evans, R. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7355 · Cited by 1,400 · see citing works
A PPARγ-LXR-ABCA1 Pathway in Macrophages Is Involved in Cholesterol Efflux and Atherogenesis
Chawla, A., Boisvert, W. A., Lee, C.-H., Laffitte, B. A., Barak, Y., Joseph, S. B., Liao, D., Nagy, L., Edwards, P. A., Curtiss, L. K., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00164-2 · Cited by 1,347 · see citing works
A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-γ
Pascual, G., Fong, A. L., Ogawa, S., Gamliel, A., Li, A. C., Perissi, V., Rose, D. W., Willson, T. M., Rosenfeld, M. G., & Glass, C. K. (2005) · Nature · doi:10.1038/nature03988 · Cited by 1,251 · see citing works
Activation of the Nuclear Receptor LXR by Oxysterols Defines a New Hormone Response Pathway
Lehmann, J. M., Kliewer, S. A., Moore, L. B., Smith-Oliver, T. A., Oliver, B. B., Su, J.-L., Sundseth, S. S., Winegar, D. A., Blanchard, D. E., Spencer, T. A., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3137 · Cited by 1,233 · see citing works
Aβ Oligomer-Induced Aberrations in Synapse Composition, Shape, and Density Provide a Molecular Basis for Loss of Connectivity in Alzheimer's Disease
Lacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188 · see citing works
A selective peroxisome proliferator-activated receptor δ agonist promotes reverse cholesterol transport
Oliver, W. R., Shenk, J. L., Snaith, M. R., RUSSELL, C. S., Plunket, K. D., Bodkin, N. L., Lewis, M. C., Winegar, D. A., Sznaidman, M. L., Lambert, M. H., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091021198 · Cited by 1,048 · see citing works
Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease
El Khoury, J., Toft, M., Hickman, S. E., Means, T. K., Terada, K., Geula, C., & Luster, A. D. (2007) · Nature Medicine · doi:10.1038/nm1555 · Cited by 915 · see citing works
Transcriptional Regulation of Metabolism
Desvergne, B., Michalik, L., & Wahli, W. (2006) · Physiological Reviews · doi:10.1152/physrev.00025.2005 · Cited by 889 · see citing works
ApoE Promotes the Proteolytic Degradation of Aβ
Jiang, Q., Lee, C. Y. D., Mandrekar, S., Wilkinson, B., Cramer, P., Zelcer, N., Mann, K., Lamb, B., Willson, T. M., Collins, J. L., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.04.010 · Cited by 876 · see citing works
Self-citation
Alzheimer's disease: the cholesterol connection
Puglielli, L., Tanzi, R. E., & Kovacs, D. M. (2003) · Nature Neuroscience · doi:10.1038/nn0403-345 · Cited by 864 · see citing works
Alternative M2 Activation of Kupffer Cells by PPARδ Ameliorates Obesity-Induced Insulin Resistance
Odegaard, J. I., Ricardo-González, R. R., Eagle, A. R., Vats, D., Morel, C. R., Goforth, M. H., Subramanian, V., Mukundan, L., Ferrante, A. W., & Chawla, A. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.04.003 · Cited by 840 · see citing works
Adipocyte-Derived Th2 Cytokines and Myeloid PPARδ Regulate Macrophage Polarization and Insulin Sensitivity
Kang, K., Reilly, S. M., Karabacak, V., Gangl, M. R., Fitzgerald, K., Hatano, B., & Lee, C.-H. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.04.002 · Cited by 699 · see citing works
Efficacy of rosiglitazone in a genetically defined population with mild-to-moderate Alzheimer’s disease
Risner, M. E., Saunders, A. M., Altman, J. F. B., Ormandy, G. C., Craft, S., Foley, I. M., Zvartau-Hind, M. E., Hosford, D. A., Roses, A. D., & for the Rosiglitazone in Alzheimer's Disease Study Group (2006) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500369 · Cited by 686 · see citing works
Apoptotic Cells Promote Their Own Clearance and Immune Tolerance through Activation of the Nuclear Receptor LXR
A-González, N., Bensinger, S. J., Hong, C., Beceiro, S., Bradley, M. N., Zelcer, N., Deniz, J. M., Ramírez, C. M., Díaz, M., Gallardo, G., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.06.018 · Cited by 674 · see citing works
PPAR : a dagger in the heart of the metabolic syndrome
Barish, G. D. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27955 · Cited by 641 · see citing works
Nuclear receptor transrepression pathways that regulate inflammation in macrophages and T cells
Glass, C. K., & Saijo, K. (2010) · Nature Reviews Immunology · doi:10.1038/nri2748 · Cited by 619 · see citing works
Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo
Bateman, R. J., Munsell, L. Y., Morris, J. C., Swarm, R., Yarasheski, K. E., & Holtzman, D. M. (2006) · Nature Medicine · doi:10.1038/nm1438 · Cited by 599 · see citing works
CD14 and Toll-Like Receptors 2 and 4 Are Required for Fibrillar Aβ-Stimulated Microglial Activation
Reed-Geaghan, E. G., Savage, J. C., Hise, A. G., & Landreth, G. E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3158-09.2009 · Cited by 591 · see citing works
Self-citation
Acute treatment with the PPARγ agonist pioglitazone and ibuprofen reduces glial inflammation and Aβ1–42 levels in APPV717I transgenic mice
Heneka, M. T., Sastre, M., Dumitrescu-Ozimek, L., Hanke, A., Dewachter, I., Kuiperi, C., O'Banion, K., Klockgether, T., Van Leuven, F., & Landreth, G. E. (2005) · Brain · doi:10.1093/brain/awh452 · Cited by 565 · see citing works
Self-citation
Anti-inflammatory actions of PPAR ligands: new insights on cellular and molecular mechanisms
Straus, D. S., & Glass, C. K. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.09.003 · Cited by 553 · see citing works
Retinoid X receptor gamma signaling accelerates CNS remyelination
Huang, J. K., Jarjour, A. A., Nait Oumesmar, B., Kerninon, C., Williams, A., Krezel, W., Kagechika, H., Bauer, J., Zhao, C., Evercooren, A. B.-V., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2702 · Cited by 547 · see citing works
Protective effects of NSAIDs on the development of Alzheimer disease
Vlad, S. C., Miller, D. R., Kowall, N. W., & Felson, D. T. (2008) · Neurology · doi:10.1212/01.wnl.0000311269.57716.63 · Cited by 535 · see citing works
Control of Macrophage Activation and Function by PPARs
Chawla, A. (2010) · Circulation Research · doi:10.1161/circresaha.110.216523 · Cited by 531 · see citing works
Dynamics of the Microglial/Amyloid Interaction Indicate a Role in Plaque Maintenance
Bolmont, T., Haiss, F., Eicke, D., Radde, R., Mathis, C. A., Klunk, W. E., Kohsaka, S., Jucker, M., & Calhoun, M. E. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4814-07.2008 · Cited by 526 · see citing works
A Cell Surface Receptor Complex for Fibrillar β-Amyloid Mediates Microglial Activation
Bamberger, M. E., Harris, M. E., McDonald, D. R., Husemann, J., & Landreth, G. E. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02665.2003 · Cited by 501 · see citing works
Self-citation
Apolipoprotein E is essential for amyloid deposition in the APP V717F transgenic mouse model of Alzheimer's disease
Bales, K. R., Verina, T., Cummins, D. J., Du, Y., Dodel, R. C., Saura, J., Fishman, C. E., DeLong, C. A., Piccardo, P., Petegnief, V., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.15233 · Cited by 486 · see citing works
Microglial Phagocytosis Induced by Fibrillar β-Amyloid and IgGs Are Differentially Regulated by Proinflammatory Cytokines
Koenigsknecht-Talboo, J., & Landreth, G. E. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1808-05.2005 · Cited by 477 · see citing works
Self-citation
Anti-Inflammatory Drug Therapy Alters β-Amyloid Processing and Deposition in an Animal Model of Alzheimer's Disease
Yan, Q., Zhang, J., Liu, H., Babu-Khan, S., Vassar, R., Biere, A. L., Citron, M., & Landreth, G. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-20-07504.2003 · Cited by 469 · see citing works
Self-citation
Microglial Phagocytosis of Fibrillar β-Amyloid through a β1Integrin-Dependent Mechanism
Koenigsknecht-Talboo, J., & Landreth, G. E. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2557-04.2004 · Cited by 444 · see citing works
Self-citation
Inflammation, microglia, and alzheimer's disease
Cameron, B., & Landreth, G. E. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.10.006 · Cited by 440 · see citing works
Self-citation
Microglia and Inflammation in Alzheimers Disease
Mandrekar-Colucci, S., & Landreth, G. E. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791012071 · Cited by 421 · see citing works
Self-citation
Expression profiles for macrophage alternative activation genes in AD and in mouse models of AD.
(2006) · Journal of Neuroinflammation · doi:10.1186/1742-2094-3-27 · Cited by 393 · see citing works
Deletion of tumor necrosis factor death receptor inhibits amyloid β generation and prevents learning and memory deficits in Alzheimer's mice
He, P., Zhong, Z., Lindholm, K., Berning, L., Lee, W., Lemere, C., Staufenbiel, M., Li, R., & Shen, Y. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200705042 · Cited by 390 · see citing works
Efficacy of PPAR-γ agonist pioglitazone in mild Alzheimer disease
Sato, T., Hanyu, H., Hirao, K., Kanetaka, H., Sakurai, H., & Iwamoto, T. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.10.009 · Cited by 387 · see citing works
Peroxisome Proliferator-Activated Receptor γ-Dependent Repression of the Inducible Nitric Oxide Synthase Gene
Li, M., Pascual, G., & Glass, C. K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.13.4699-4707.2000 · Cited by 377 · see citing works
Overexpression of ABCA1 reduces amyloid deposition in the PDAPP mouse model of Alzheimer disease
Wahrle, S. E., Jiang, H., Parsadanian, M., Kim, J., Li, A., Knoten, A., Jain, S., Hirsch-Reinshagen, V., Wellington, C. L., Bales, K. R., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33622 · Cited by 370 · cited 1× · see citing works
“Conversely, overexpression of ABCA1 in a mouse model of AD was shown to decrease both soluble and fibrillar pools of Ab in 12-month-old mice and reduce plaque burden [53].”
Background
PPAR-δ senses and orchestrates clearance of apoptotic cells to promote tolerance
Mukundan, L., Odegaard, J. I., Morel, C. R., Heredia, J. E., Mwangi, J. W., Ricardo-Gonzalez, R. R., Goh, Y. P. S., Eagle, A. R., Dunn, S. E., Awakuni, J. U. H., et al. (2009) · Nature Medicine · doi:10.1038/nm.2048 · Cited by 368 · see citing works
Interferon-γ and Tumor Necrosis Factor-α Regulate Amyloid-β Plaque Deposition and β-Secretase Expression in Swedish Mutant APP Transgenic Mice
Yamamoto, M., Kiyota, T., Horiba, M., Buescher, J. L., Walsh, S. M., Gendelman, H. E., & Ikezu, T. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.060378 · Cited by 367 · see citing works
Rosiglitazone Monotherapy in Mild-to-Moderate Alzheimer’s Disease: Results from a Randomized, Double-Blind, Placebo-Controlled Phase III Study
Gold, M., Alderton, C., Zvartau-Hind, M., Egginton, S., Saunders, A. M., Irizarry, M., Craft, S., Landreth, G., Linnamägi, Ü., & Sawchak, S. (2010) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000318845 · Cited by 361 · see citing works
Self-citation
Attenuation of neuroinflammation and Alzheimer's disease pathology by liver x receptors
Zelcer, N., Khanlou, N., Clare, R., Jiang, Q., Reed-Geaghan, E. G., Landreth, G. E., Vinters, H. V., & Tontonoz, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701096104 · Cited by 358 · see citing works
Self-citation
Lack of ABCA1 Considerably Decreases Brain ApoE Level and Increases Amyloid Deposition in APP23 Mice
Koldamova, R., Staufenbiel, M., & Lefterov, I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504513200 · Cited by 350 · see citing works
Association of Microglia with Amyloid Plaques in Brains of APP23 Transgenic Mice
Stalder, M., Phinney, A., Probst, A., Sommer, B., Staufenbiel, M., & Jucker, M. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65423-5 · Cited by 345 · see citing works
Deletion of Abca1 Increases Aβ Deposition in the PDAPP Transgenic Mouse Model of Alzheimer Disease
Wahrle, S. E., Jiang, H., Parsadanian, M., Hartman, R. E., Bales, K. R., Paul, S. M., & Holtzman, D. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508780200 · Cited by 325 · see citing works
PPARs in the brain
HENEKA, M., & LANDRETH, G. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.04.016 · Cited by 317 · see citing works
Self-citation
Chemokine monocyte chemoattractant protein-1 is expressed by astrocytes after mechanical injury to the brain
Glabinski, A. R., Balasingam, V., Tani, M., Kunkel, S. L., Strieter, R. M., Yong, V. W., & Ransohoff, R. M. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.11.4363 · Cited by 309 · see citing works
Retinoid X receptors: X-ploring their (patho)physiological functions
Szántó, A., Narkar, V. A., Shen, Q., Uray, I. P., Davies, P. J., & Nagy, L. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401533 · Cited by 304 · see citing works
Liver X Receptor Signaling Pathways and Atherosclerosis
Calkin, A. C., & Tontonoz, P. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.191197 · Cited by 294 · see citing works
Activation of Wnt signaling by lithium and rosiglitazone reduced spatial memory impairment and neurodegeneration in brains of an APPswe/PSEN1ΔE9 mouse model of Alzheimer's disease
Toledo, E. M., & Inestrosa, N. C. (2009) · Molecular Psychiatry · doi:10.1038/mp.2009.72 · Cited by 290 · see citing works
Human and Murine ApoE Markedly Alters Aβ Metabolism before and after Plaque Formation in a Mouse Model of Alzheimer's Disease
Fagan, A. M., Watson, M., Parsadanian, M., Bales, K. R., Paul, S. M., & Holtzman, D. M. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0483 · Cited by 290 · see citing works
Liver X receptors in the central nervous system: From lipid homeostasis to neuronal degeneration
Wang, L., Schuster, G. U., Hultenby, K. R., Zhang, Q., Andersson, S., & Gustafsson, J.-Α. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172510899 · Cited by 286 · see citing works
The Liver X Receptor Ligand T0901317 Decreases Amyloid β Production in Vitro and in a Mouse Model of Alzheimer's Disease
Koldamova, R. P., Lefterov, I. M., Staufenbiel, M., Wolfe, D., Huang, S., Glorioso, J. C., Walter, M., Roth, M. G., & Lazo, J. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411420200 · Cited by 279 · see citing works
PPARγ Agonists as Therapeutics for the Treatment of Alzheimer's Disease
Landreth, G. E., Jiang, Q., Mandrekar, S., & Heneka, M. T. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.003 · Cited by 277 · see citing works
Self-citation
Slow Degradation of Aggregates of the Alzheimer's Disease Amyloid β-Protein by Microglial Cells
Paresce, D. M., Chung, H., & Maxfield, F. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.29390 · Cited by 269 · see citing works
Retinoic Acid Attenuates β-Amyloid Deposition and Rescues Memory Deficits in an Alzheimer's Disease Transgenic Mouse Model
Ding, Y., Qiao, A., Wang, Z., Goodwin, J. S., Lee, E.-S., Block, M. L., Allsbrook, M., McDonald, M. P., & Fan, G.-H. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3153-08.2008 · Cited by 269 · see citing works
Role of the β‐amyloid protein in Alzheimer's disease
Sisodia, S. S., & Price, D. L. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.5.7896005 · Cited by 262 · see citing works
Complete Rescue of Cerebrovascular Function in Aged Alzheimer's Disease Transgenic Mice by Antioxidants and Pioglitazone, a Peroxisome Proliferator-Activated Receptor γ Agonist
Nicolakakis, N., Aboulkassim, T., Ongali, B., Lecrux, C., Fernandes, P., Rosa-Neto, P., Tong, X.-K., & Hamel, E. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3348-08.2008 · Cited by 262 · see citing works
Coordination of inflammation and metabolism by PPAR and LXR nuclear receptors
Hong, C., & Tontonoz, P. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.07.016 · Cited by 253 · see citing works
The LXR agonist TO901317 selectively lowers hippocampal Aβ42 and improves memory in the Tg2576 mouse model of Alzheimer's disease
Riddell, D. R., Zhou, H., Comery, T. A., Kouranova, E., Lo, C. F., Warwick, H. K., Ring, R. H., Kirksey, Y., Aschmies, S., Xu, J., et al. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.01.011 · Cited by 244 · see citing works
Rosiglitazone rescues memory impairment in Alzheimer’s transgenic mice: Mechanisms involving a reduced amyloid and tau pathology
Escribano, L., Simón, A.-M., Gimeno, E., Cuadrado-Tejedor, M., López de Maturana, R., García-Osta, A., Ricobaraza, A., Pérez-Mediavilla, A., Del Río, J., & Frechilla, D. (2010) · Neuropsychopharmacology · doi:10.1038/npp.2010.32 · Cited by 235 · see citing works
The absence of ABCA1 decreases soluble ApoE levels but does not diminish amyloid deposition in two murine models of Alzheimer disease
Hirsch-Reinshagen, V., Maia, L. F., Burgess, B. L., Blain, J.-F., Naus, K. E., McIsaac, S. A., Parkinson, P. F., Chan, J. Y., Tansley, G. H., Hayden, M. R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508781200 · Cited by 233 · see citing works
Powerful beneficial effects of macrophage colony-stimulating factor on -amyloid deposition and cognitive impairment in Alzheimer's disease
Boissonneault, V., Filali, M., Lessard, M., Relton, J., Wong, G., & Rivest, S. (2008) · Brain · doi:10.1093/brain/awn331 · Cited by 221 · see citing works
Uptake, Degradation, and Release of Fibrillar and Soluble Forms of Alzheimer's Amyloid β-Peptide by Microglial Cells
Chung, H., Brazil, M. I., Soe, T. T., & Maxfield, F. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32301 · Cited by 212 · see citing works
CC Chemokine Receptor 2 deficiency aggravates cognitive impairments and amyloid pathology in a transgenic mouse model of Alzheimer's disease
Naert, G., & Rivest, S. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0299-11.2011 · Cited by 207 · cited 1× · see citing works
“Its receptor, CCR2, is also expressed by microglia and it is thought that that the upregulation of CCL2 in the vicinity of plaques results in the recruitment of microglia from adjacent regions to these deposits [83,84].”
Background
ATP-binding Cassette Transporter A1 Mediates the Beneficial Effects of the Liver X Receptor Agonist GW3965 on Object Recognition Memory and Amyloid Burden in Amyloid Precursor Protein/Presenilin 1 Mice*
Donkin, J. J., Stukas, S., Hirsch-Reinshagen, V., Namjoshi, D., Wilkinson, A., May, S., Chan, J., Fan, J., Collins, J., & Wellington, C. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.108100 · Cited by 200 · see citing works
Purification of Apolipoprotein E Attenuates Isoform-specific Binding to β-Amyloid
LaDu, M. J., Pederson, T. M., Frail, D. E., Reardon, C. A., Getz, G. S., & Falduto, M. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9039 · Cited by 189 · see citing works
Role of microglia in senile plaque formation
Mackenzie, I. R. A., Hao, C., & Munoz, D. G. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00092-s · Cited by 183 · see citing works
Critical Role of Astroglial Apolipoprotein E and Liver X Receptor-α Expression for Microglial Aβ Phagocytosis
Terwel, D., Steffensen, K. R., Verghese, P. B., Kummer, M. P., Gustafsson, J.-Å., Holtzman, D. M., & Heneka, M. T. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6546-10.2011 · Cited by 181 · see citing works
Liver X Receptor Agonist Treatment Ameliorates Amyloid Pathology and Memory Deficits Caused by High-Fat Diet in APP23 Mice
Fitz, N. F., Cronican, A., Pham, T., Fogg, A., Fauq, A. H., Chapman, R., Lefterov, I., & Koldamova, R. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1051-10.2010 · Cited by 175 · see citing works
Mechanisms of microglia accumulation in Alzheimer’s disease: therapeutic implications
Khoury, J. E., & Luster, A. D. (2008) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.08.004 · Cited by 171 · see citing works
Anti-inflammatory actions of peroxisome proliferator-activated receptor gamma agonists in Alzheimer's disease
Landreth, G. E. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00296-2 · Cited by 169 · see citing works
Self-citation
Inactivation of liver X receptor β leads to adult-onset motor neuron degeneration in male mice
Andersson, S., Gustafsson, N., Warner, M. N., & Gustafsson, J.-Α. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500634102 · Cited by 168 · see citing works
Activation of specific RXR heterodimers by an antagonist of RXR homodimers
Lala, D. S., Mukherjee, R., Schulman, I. G., Koch, S. S. C., Dardashti, L. J., Nadzan, A. M., Croston, G. E., Evans, R. M., & Heyman, R. A. (1996) · Nature · doi:10.1038/383450a0 · Cited by 164 · see citing works
PIOGLITAZONE IMPROVED COGNITION IN A PILOT STUDY ON PATIENTS WITH ALZHEIMER'S DISEASE AND MILD COGNITIVE IMPAIRMENT WITH DIABETES MELLITUS
Hanyu, H., Sato, T., Kiuchi, A., Sakurai, H., & Iwamoto, T. (2008) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.2009.02067.x · Cited by 158 · see citing works
Neuroprotective effect of honokiol and magnolol, compounds from Magnolia officinalis, on beta‐amyloid‐induced toxicity in PC12 cells
Hoi, C. P., Ho, Y. P., Baum, L., & Chow, A. H. L. (2010) · Phytotherapy Research · doi:10.1002/ptr.3178 · Cited by 154 · see citing works
Liver X receptor activation restores memory in aged AD mice without reducing amyloid
Vanmierlo, T., Rutten, K., Dederen, J., Bloks, V. W., van Vark-van der Zee, L. C., Kuipers, F., Kiliaan, A., Blokland, A., Sijbrands, E. J. G., Steinbusch, H., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.07.005 · Cited by 154 · see citing works
Arginase I Induction by Modified Lipoproteins in Macrophages: A Peroxisome Proliferator-Activated Receptor-γ/δ-Mediated Effect that Links Lipid Metabolism and Immunity
Gallardo, A., Gómez-Nieto, C., Campo, M. L., Marathe, C., Tontonoz, P., Castrillo, A., & Corraliza, I. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0525 · Cited by 151 · see citing works
ABCA1 modulates CSF cholesterol levels and influences the age at onset of Alzheimer's disease
Wollmer, M. A. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00094-5 · Cited by 147 · see citing works
Retinoic Acid Receptor-Mediated Induction of ABCA1 in Macrophages
Costet, P., Lalanne, F., Gerbod-Giannone, M. C., Molina, J. R., Fu, X., Lund, E. G., Gudas, L. J., & Tall, A. R. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7756-7766.2003 · Cited by 136 · see citing works
Retinoid X receptor α controls innate inflammatory responses through the up-regulation of chemokine expression
Núñez, V., Alameda, D., Rico, D., Mota, R., Gonzalo, P., Cedenilla, M., Fischer, T., Boscá, L., Glass, C. K., Arroyo, A. G., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913545107 · Cited by 133 · see citing works
Knock-out and transgenic mouse models of tauopathies
Denk, F., & Wade‐Martins, R. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.05.010 · Cited by 120 · see citing works
Insulin resistance contributes to aberrant stress responses in the Tg2576 mouse model of Alzheimer's disease
PEDERSEN, W., & FLYNN, E. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.08.003 · Cited by 108 · see citing works
A PPARdelta Agonist Reduces Amyloid Burden and Brain Inflammation in a Transgenic Mouse Model of Alzheimers Disease
Kalinin, S., Richardson, J. C., & Feinstein, D. L. (2009) · Current Alzheimer Research · doi:10.2174/156720509789207949 · Cited by 107 · see citing works
The effects of ABCA1 on cholesterol efflux and Aβ levels in vitro and in vivo
Burns, M. P., Vardanian, L., Pajoohesh‐Ganji, A., Wang, L., Cooper, M., Harris, D. C., Duff, K., & Rebeck, G. W. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03925.x · Cited by 106 · see citing works
Role of human placental apical membrane transporters in the efflux of glyburide, rosiglitazone, and metformin
Hemauer, S. J., Patrikeeva, S. L., Nanovskaya, T. N., Hankins, G. D. V., & Ahmed, M. S. (2010) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2010.01.035 · Cited by 103 · see citing works
Regulation of β-amyloid stimulated proinflammatory responses by peroxisome proliferator-activated receptor α
Combs, C. K., Bates, P., Karlo, J. C., & Landreth, G. E. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00052-3 · Cited by 100 · see citing works
Self-citation
Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E
Fisher, C. A., & Ryan, R. O. (1999) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33343-5 · Cited by 95 · see citing works
Degradation of fibrillar forms of Alzheimer's amyloid β-peptide by macrophages
Majumdar, A., Chung, H., Dolios, G., Wang, R., Asamoah, N., Lobel, P., & Maxfield, F. R. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.12.001 · Cited by 92 · see citing works
Temporal expression pattern of peripheral myelin protein 22 during in vivo and in vitro myelination
Notterpek, L. M., Snipes, G. J., & Shooter, E. M. (1999) · Glia · doi:10.1002/(sici)1098-1136(19990215)25:4 · Cited by 89 · see citing works
Interleukin-4 mediates the neuroprotective effects of rosiglitazone in the aged brain
Loane, D. J., Deighan, B. F., Clarke, R. M., Griffin, R. J., Lynch, A. M., & Lynch, M. A. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.09.001 · Cited by 87 · see citing works
Rosiglitazone reversal of Tg2576 cognitive deficits is independent of peripheral gluco-regulatory status
Rodriguez-Rivera, J., Denner, L. A., & Dineley, K. T. (2010) · Behavioural Brain Research · doi:10.1016/j.bbr.2010.08.002 · Cited by 86 · see citing works
Binding of type II nuclear receptors and estrogen receptor to full and half-site estrogen response elements in vitro
Klinge, C. M. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.10.1903 · Cited by 74 · see citing works
Identification of a Naturally Occurring Rexinoid, Honokiol, That Activates the Retinoid X Receptor
Kotani, H., Tanabe, H., Mizukami, H., Makishima, M., & Inoue, M. (2010) · Journal of Natural Products · doi:10.1021/np100120c · Cited by 69 · see citing works
Macrophage-Mediated Degradation of β-Amyloid via an Apolipoprotein E Isoform-Dependent Mechanism
Zhao, L.-Z., Lin, S.-Z., Bales, K., Gelfanova, V., Koger, D., Delong, C., Hale, J., Liu, F., Hunter, J. M., & Paul, S. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5302-08.2009 · Cited by 68 · see citing works
The RXR agonists PA024 and HX630 have different abilities to activate LXR/RXR and to induce ABCA1 expression in macrophage cell lines
Nishimaki‐Mogami, T., Tamehiro, N., Sato, Y., Okuhira, K., Sai, K., Kagechika, H., Shudo, K., Abe-Dohmae, S., Yokoyama, S., Ohno, Y., et al. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.08.005 · Cited by 41 · see citing works
Honokiol Increases ABCA1 Expression Level by Activating Retinoid X Receptor Beta
Jung, C., Horike, H., Cha, B., Uhm, K., Yamauchi, R., Yamaguchi, T., Hosono, T., Iida, K., Woo, J., & Michikawa, M. (2010) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.33.1105 · Cited by 39 · see citing works
Normal hematopoiesis after conditional targeting of RXRα in murine hematopoietic stem/progenitor cells
Ricote, M., Snyder, C. S., Leung, H., Chen, J., Chien, K. R., & Glass, C. K. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0206097 · Cited by 35 · see citing works

Flagged first, then by citations

2 of the 112 references couldn’t be matched to a known paper.

Research works printed but not linked: 2

[1]2010 Alzheimer’s disease facts and figures Alzheimers Dement 2010 6 2 158 94 20298981
[7]Akiyama H Mori H Saido T Occurrence of the diffuse amyloid beta-protein (Abeta) deposits with numerous Abeta-containing glial cells in the cerebral cortex of patients with Alzheimer’s disease Glia 1999 25 4 324 31 10028915

Sorted by citations

Neuroinflammation and microglial activation in Alzheimer disease: where do we go from here?
Leng, F., & Edison, P. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-020-00435-y · Cited by 3,179 · see citing works
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
Self-citation
Microglia: Scapegoat, saboteur, or something else?
Aguzzi, A., Barres, B. A., & Bennett, M. L. (2013) · Science · doi:10.1126/science.1227901 · Cited by 836 · see citing works
Mitochondrial Dysfunction in Neurodegenerative Diseases
Johri, A., & Beal, M. F. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.192138 · Cited by 806 · see citing works
Mechanisms Underlying the Rapid Peroxisome Proliferator-Activated Receptor-γ-Mediated Amyloid Clearance and Reversal of Cognitive Deficits in a Murine Model of Alzheimer's Disease
Mandrekar-Colucci, S., Karlo, J. C., & Landreth, G. E. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5268-11.2012 · Cited by 355 · see citing works
“A number of studies of the thiazolidinedione agonists of PPAR , pioglitazone (Actos) and rosiglitazone (Avandia), reported salutary effects of these drugs in murine models of AD (Mandrekar-Colucci and Landreth, 2011).”
BackgroundSelf-citation
Microglia and Neuroinflammation: Crucial Pathological Mechanisms in Traumatic Brain Injury-Induced Neurodegeneration
Shao, F., Wang, X., Wu, H., Wu, Q., & Zhang, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.825086 · Cited by 250 · see citing works
Targeting Neuroinflammation to Treat Alzheimer’s Disease
Ardura-Fabregat, A., Boddeke, E., Boza‐Serrano, A., Brioschi, S., Castro‐Gomez, S., Ceyzériat, K., Dansokho, C., Dierkes, T., Gelders, G., Heneka, M. T., et al. (2017) · CNS Drugs · doi:10.1007/s40263-017-0483-3 · Cited by 236 · see citing works
Self-citation
Multi-Target-Directed Ligands and other Therapeutic Strategies in the Search of a Real Solution for Alzheimer’s Disease
Agis-Torres, A., Sollhuber, M., Fernandez, M., & Sanchez-Montero, J. M. (2014) · Current Neuropharmacology · doi:10.2174/1570159x113116660047 · Cited by 202 · see citing works
The role of lipid-activated nuclear receptors in shaping macrophage and dendritic cell function: From physiology to pathology
Kiss, M., Czimmerer, Z., & Nagy, L. (2013) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2013.05.044 · Cited by 163 · see citing works
ApoE4 Alters ABCA1 Membrane Trafficking in Astrocytes
Rawat, V., Wang, S., Sima, J., Bar, R., Liraz, O., Gundimeda, U., Parekh, T., Chan, J., Johansson, J. O., Tang, C., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.1400-19.2019 · Cited by 165 · see citing works
NR4A nuclear receptors support memory enhancement by histone deacetylase inhibitors
Hawk, J. D., Bookout, A. L., Poplawski, S. G., Bridi, M. S., Rao, A. J., Sulewski, M. E., Kroener, B., Manglesdorf, D. J., & Abel, T. G. (2012) · Journal of Clinical Investigation · doi:10.1172/jci64145 · Cited by 147 · see citing works
Microglial activation states and their implications for Alzheimer's Disease
Valiukas, Z., Tangalakis, K., Apostolopoulos, V., & Feehan, J. (2025) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2024.100013 · Cited by 155 · see citing works
Comment on “ApoE-directed therapeutics rapidly clear β-amyloid and reverse deficits in AD mouse models.”
Price, A. R., Xu, G., Siemienski, Z. B., Smithson, L. A., Borchelt, D. R., Golde, T. E., & Felsenstein, K. M. (2013) · Science · doi:10.1126/science.1234089 · Cited by 138 · see citing works
Involvement of inflammation in Alzheimer’s disease pathogenesis and therapeutic potential of anti-inflammatory agents
Shadfar, S., Hwang, C. J., Lim, M., Choi, D., & Hong, J. T. (2015) · Archives of Pharmacal Research · doi:10.1007/s12272-015-0648-x · Cited by 130 · see citing works
Insulin resistance in Alzheimer's disease
Dineley, K. T., Jahrling, J. B., & Denner, L. A. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.09.001 · Cited by 124 · see citing works
Precision pharmacology for Alzheimer’s disease
Hampel, H. J., Vergallo, A., Aguilar, L. F., Benda, N., Broich, K., Cuello, A. C., Cummings, J. L., Dubois, B., Federoff, H. J., Fiandaca, M. S., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.02.014 · Cited by 112 · see citing works
Inhibition of FAAH and activation of PPAR: New approaches to the treatment of cognitive dysfunction and drug addiction
Panlilio, L. V., Justinová, Z., & Goldberg, S. R. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.003 · Cited by 106 · 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
Impact of Apolipoprotein E on Alzheimer’s Disease
Hauser, P. S., & Ryan, R. O. (2013) · Current Alzheimer Research · doi:10.2174/15672050113109990156 · Cited by 101 · see citing works
Receptor-based Targeting of Therapeutics
Mehra, N. K., Mishra, V. K., & Jain, N. K. (2013) · Therapeutic Delivery · doi:10.4155/tde.13.6 · Cited by 97 · 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
Self-citation
PPARγ Agonist Pioglitazone Reverses Memory Impairment and Biochemical Changes in a Mouse Model of Type 2 Diabetes Mellitus
Jiang, L., Tang, S., Wang, X., Liu, L., Long, Y., Hu, M. Y., Liao, M. X., Qi-long, D., Hu, W. M., Li, J., et al. (2012) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2012.00341.x · Cited by 96 · see citing works
EFAD transgenic mice as a human APOE relevant preclinical model of Alzheimerŉs disease
Tai, L. M., Balu, D., Avila-Munoz, E., Abdullah, L., Thomas, R., Collins, N., Valencia-Olvera, A. C., & LaDu, M. J. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r076315 · Cited by 93 · see citing works
Current Progress on Peroxisome Proliferator-activated Receptor Gamma Agonist as an Emerging Therapeutic Approach for the Treatment of Alzheimer's Disease: An Update
Khan, M. A., Alam, Q., Haque, A., Ashafaq, M., Khan, M. J., Ashraf, G. M., & Ahmad, M. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180828100002 · Cited by 90 · see citing works
Ginsenoside Re reduces Aβ production by activating PPARγ to inhibit BACE1 in N2a/APP695 cells
Cao, G., Su, P., Zhang, S., Guo, L., Zhang, H., Liang, Y., Qin, C., & Zhang, W. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.11.006 · Cited by 91 · see citing works
The role of APOE in transgenic mouse models of AD
Balu, D., Karstens, A. J., Loukenas, E., Maldonado Weng, J., York, J. M., Valencia-Olvera, A. C., & LaDu, M. J. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.134285 · Cited by 81 · see citing works
Hypercholesterolaemia-induced oxidative stress at the blood–brain barrier
Dias, I. H. K., Polidori, M. C., & Griffiths, H. R. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140164 · Cited by 78 · see citing works
Bezafibrate administration improves behavioral deficits and tau pathology in P301S mice
Dumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Gerges, M., Starkova, N. N., Calingasan, N. Y., Yang, L., Tampellini, D., Starkov, A. A., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds355 · Cited by 78 · 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
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
Self-citation
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
Self-citation
Pioglitazone ameliorates memory deficits in streptozotocin-induced diabetic mice by reducing brain β-amyloid through PPARγ activation
Liu, L., Yan, T., Jiang, L., Hu, W. M., Hu, M., Wang, C., Zhang, Q., Long, Y., Wang, J.-Q., Li, Y., et al. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2013.11 · Cited by 71 · see citing works
PPARγ Recruitment to Active ERK during Memory Consolidation Is Required for Alzheimer's Disease-Related Cognitive Enhancement
Jahrling, J. B., Hernandez, C. M., Denner, L. A., & Dineley, K. T. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.4024-13.2014 · 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
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
Transcriptional regulation and its misregulation in Alzheimer’s disease
Chen, X., Zhang, Y., Xu, H., & Bu, G. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-44 · Cited by 66 · 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
Influence of drug transporters and stereoselectivity on the brain penetration of pioglitazone as a potential medicine against Alzheimer's disease
Chang, K. L., Pee, H. N., Yang, S., & Ho, P. C. (2015) · Scientific Reports · doi:10.1038/srep09000 · Cited by 65 · 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
Liver X receptors: Emerging therapeutic targets for Alzheimer's disease
Sodhi, R. K., & Singh, N. (2013) · Pharmacological Research · doi:10.1016/j.phrs.2013.03.008 · Cited by 61 · see citing works
Boosting phagocytosis and anti‐inflammatory phenotype in microglia mediates neuroprotection by PPARγ agonist MDG548 in Parkinson's disease models
Lecca, D., Janda, E., Mulas, G., Diana, A., Martino, C., Angius, F., Spolitu, S., Casu, M. A., Simbula, G., Boi, L., et al. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14214 · Cited by 61 · see citing works
The neuroendocrine control of the innate immune system in health and brain diseases
Bellavance, M., & Rivest, S. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01129.x · Cited by 60 · 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
Long-term caloric restriction in ApoE-deficient mice results in neuroprotection via Fgf21-induced AMPK/mTOR pathway
Rühlmann, C., Wölk, T., Blümel, T., Stahn, L., Vollmar, B., & Kuhla, A. (2016) · Aging · doi:10.18632/aging.101086 · Cited by 55 · see citing works
Changes in the expression of genes related to neuroinflammation over the course of sporadic Alzheimer’s disease progression: CX3CL1, TREM2, and PPARγ
Strobel, S., Grünblatt, E., Riederer, P., Heinsen, H., Arzberger, T., Al‐Sarraj, S., Troakes, C., Ferrer, I., & Monoranu, C. M. (2015) · Journal of Neural Transmission · doi:10.1007/s00702-015-1369-5 · Cited by 54 · see citing works
Daidzein Augments Cholesterol Homeostasis via ApoE to Promote Functional Recovery in Chronic Stroke
Kim, E., Woo, M.-S., Qin, L., Ma, T. C., Beltran, C., Bao, Y., Bailey, J. A., Corbett, D., Ratan, R. R., Lahiri, D. K., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2890-15.2015 · Cited by 53 · see citing works
The Critical Role of Nurr1 as a Mediator and Therapeutic Target in Alzheimer’s Disease-related Pathogenesis
Jeon, S. G., Yoo, A., Chun, D. W., Hong, S. B., Chung, H., Kim, J.-I., & Moon, M. (2020) · Aging and Disease · doi:10.14336/ad.2019.0718 · Cited by 55 · see citing works
Insulin resistance and bioenergetic manifestations: Targets and approaches in Alzheimer's disease
Sharma, V., & Singh, T. G. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118401 · Cited by 53 · see citing works
Role of nuclear receptors in the regulation of drug transporters in the brain
Chan, G. N. Y., Hoque, M. T., & Bendayan, R. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.05.004 · Cited by 49 · see citing works
Defensive Effect of Lansoprazole in Dementia of AD Type in Mice Exposed to Streptozotocin and Cholesterol Enriched Diet
Sodhi, R. K., & Singh, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070487 · Cited by 49 · see citing works
MicroRNA-155 Promotes Heat Stress-Induced Inflammation via Targeting Liver X Receptor α in Microglia
Li, P., Wang, G., Zhang, X., He, G., Luo, X. G., Yang, J., Luo, Z., Shen, T., & Yang, X. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00012 · Cited by 47 · see citing works
PPARγ agonist pioglitazone improves scopolamine-induced memory impairment in mice
Xiang, G., Tang, S. S., Jiang, L. Y., Hong, H., Li, Q., Wang, C., Wang, X. Y., Zhang, T. T., & Yin, L. (2012) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.2011.01432.x · Cited by 45 · see citing works
PPAR‐γ – a possible drug target for complicated pregnancies
McCarthy, F. P., Delany, A. C., Kenny, L. C., & Walsh, S. K. (2012) · British Journal of Pharmacology · doi:10.1111/bph.12069 · Cited by 43 · see citing works
Peroxisome Proliferator-activated Receptors and Alzheimer's Disease: Hitting the Blood–Brain Barrier
Zolezzi, J. M., & Inestrosa, N. C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8435-5 · Cited by 44 · see citing works
Lentiviral-Mediated Overexpression of the 18 kDa Translocator Protein (TSPO) in the Hippocampal Dentate Gyrus Ameliorates LPS-Induced Cognitive Impairment in Mice
Wang, W., Zhang, L., Zhang, X., Xue, R., Li, L., Zhao, W., Fu, Q., Mi, W., & Li, Y.-F. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00384 · Cited by 36 · see citing works
Genome-wide analysis identifies novel loci influencing plasma apolipoprotein E concentration and Alzheimer’s disease risk
Aslam, M. M., Fan, K.-H., Lawrence, E., Bedison, M. A., Snitz, B. E., DeKosky, S. T., Lopez, O. L., Feingold, E., & Kamboh, M. I. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02170-4 · Cited by 39 · see citing works
Alzheimer's disease risk alleles in TREM2 illuminate innate immunity in Alzheimer's disease
Golde, T. E., Streit, W. J., & Chakrabarty, P. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt178 · Cited by 38 · see citing works
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
Neuropharmacological potential of honokiol and its derivatives from Chinese herb Magnolia species: understandings from therapeutic viewpoint
Faysal, M. F., Khan, J., Zehravi, M., Nath, N., Singh, L. P., Kakkar, S., Perusomula, R., Khan, P. A., Nainu, F., Asiri, M., et al. (2023) · Chinese Medicine · doi:10.1186/s13020-023-00846-1 · Cited by 36 · see citing works
Nr4a2 Transcription Factor in Hippocampal Synaptic Plasticity, Memory and Cognitive Dysfunction: A Perspective Review
Català-Solsona, J., Miñano-Molina, A. J., & Rodrı́guez-Álvarez, J. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.786226 · Cited by 35 · see citing works
Current and Emerging Pharmacological Targets for the Treatment of Alzheimer’s Disease
Morsy, A., & Trippier, P. C. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190744 · Cited by 34 · see citing works
Protocol for fast screening of multi-target drug candidates: Application to Alzheimer’s disease
Thai, N. Q., Nguyen, H. L., Linh, H. Q., & Li, M. S. (2017) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2017.08.002 · Cited by 33 · see citing works
Anti-Neuroinflammatory Agents for the Treatment of Alzheimer’s Disease
Zhou, W., & Hu, W. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.125 · Cited by 31 · see citing works
Development of Cerebral Microbleeds in the APP23-Transgenic Mouse Model of Cerebral Amyloid Angiopathy—A 9.4 Tesla MRI Study
Reuter, B., Venus, A., Heiler, P. M., Schad, L. R., Ebert, A., Hennerici, M. G., Grudzenski, S., & Fatar, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00170 · Cited by 27 · see citing works
Photoaffinity Labeling and Quantitative Chemical Proteomics Identify LXRβ as the Functional Target of Enhancers of Astrocytic apoE
Seneviratne, U. I., Huang, Z., Ende, C. W. A., Butler, T. W., Cleary, L., Dresselhaus, E. C., Evrard, E., Fisher, E. L., Green, M. E., Helal, C. J., et al. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.09.002 · Cited by 28 · see citing works
Anti-Alzheimer potential of a waste by-product (peel) of Omani pomegranate fruits: Quantification of phenolic compounds, in-vitro antioxidant, anti-cholinesterase and in-silico studies
Khokar, R., Hachani, K., Hasan, M., Othmani, F., Essam, M., Mamari, A. A., Dhanalekshmi, U. M., & Khan, S. A. (2021) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2021.102223 · Cited by 28 · see citing works
Malignant Brain Aging: The Formidable Link Between Dysregulated Signaling Through Mechanistic Target of Rapamycin Pathways and Alzheimer’s Disease (Type 3 Diabetes)
de la Monte, S. M. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230555 · Cited by 27 · 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
A manifesto for Alzheimer’s disease drug discovery in the era of disease-modifying therapies
Hering, H., Bussière, T., Liu, C., Glajch, K. E., Weihofen, A., Grogan, J. L., & Walsh, D. M. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00872-7 · Cited by 26 · see citing works
Mechanisms Involved in Microglial-Interceded Alzheimer’s Disease and Nanocarrier-Based Treatment Approaches
Md, S., Alhakamy, N. A., Alfaleh, M. A., Afzal, O., Altamimi, A. S. A., Iqubal, A., & Shaik, R. A. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11111116 · Cited by 24 · see citing works
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 · see citing works
Metabolic Profiling of CHO-AβPP695 Cells Revealed Mitochondrial Dysfunction Prior to Amyloid-β Pathology and Potential Therapeutic Effects of Both PPARγ and PPARα Agonisms for Alzheimer's Disease
Chang, K. L., Pee, H. N., TAN, W. P., Dawe, G. S., Holmes, E. C., Nicholson, J. K., Chan, E. C. Y., & Ho, P. C. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-140429 · Cited by 23 · see citing works
Regulation of behaviour by the nuclear receptor TLX
O'Leary, J. D., O'Leary, O., Cryan, J., & Nolan, Y. (2018) · Genes, Brain and Behavior · doi:10.1111/gbb.12357 · Cited by 22 · see citing works
Enhancement of cognitive functions by rice bran extract in a neuroinflammatory mouse model via regulation of PPARγ
Mostafa, A., Abdel-Kader, R. M., & Heikal, O. A. (2018) · Journal of Functional Foods · doi:10.1016/j.jff.2018.07.023 · Cited by 19 · see citing works
The Contribution of Hippocampal All-Trans Retinoic Acid (ATRA) Deficiency to Alzheimer’s Disease: A Narrative Overview of ATRA-Dependent Gene Expression in Post-Mortem Hippocampal Tissue
Almaguer, J., Hindle, A., & Lawrence, J. J. (2023) · Antioxidants · doi:10.3390/antiox12111921 · Cited by 19 · see citing works
TO901317 activation of LXR-dependent pathways mitigate amyloid-beta peptide-induced neurotoxicity in 3D human neural stem cell culture scaffolds and AD mice
Chiang, M., Nicol, C. J. B., Chen, S., & Huang, R. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.11.004 · Cited by 16 · see citing works
Effects of peroxisome proliferator-activated receptor-gamma agonists on cognitive function: a systematic review and meta-analysis
Zhong, H., Geng, R., Zhang, Y., Ding, J., Liu, M., Deng, S., & Tu, Q. (2023) · Biomedicines · doi:10.3390/biomedicines11020246 · Cited by 16 · see citing works
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 16 · see citing works
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 · see citing works
Liver X receptor agonist T0901317 reduces neuropathological changes and improves memory in mouse models of experimental dementia
Sodhi, R. K., & Singh, N. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.03.025 · Cited by 16 · see citing works
Rosiglitazone rescues human neural stem cells from amyloid-beta induced ER stress via PPARγ dependent signaling
Lin, C., Nicol, C. J. B., Cheng, Y., Chen, S., Yen, C., Huang, R., & Chiang, M. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.06.033 · Cited by 16 · see citing works
Small molecule TBTC as a new selective retinoid X receptor α agonist improves behavioral deficit in Alzheimer's disease model mice
Sun, Y., Fan, J. K., Zhu, Z., Guo, X., Zhou, T., Duan, W., & Shen, X. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.05.050 · Cited by 15 · see citing works
Novel disease-modifying therapeutics for the treatment of Alzheimer’s disease
Léger, G. C., & Massoud, F. (2013) · Expert Review of Clinical Pharmacology · doi:10.1586/17512433.2013.811237 · Cited by 10 · see citing works
Retinoic Acid Enhances Apolipoprotein E Synthesis in Human Macrophages
Clemens, V., Regen, F., Bret, N. L., Heuser, I., & Hellmann‐Regen, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170823 · Cited by 10 · see citing works
The Role of APOE and NF-κB in Alzheimer’s Disease
Davies, D. A. (2021) · Immuno · doi:10.3390/immuno1040027 · Cited by 10 · see citing works
Past, Present, and Future of Liver-Brain Axis in Alzheimer’s Disease: A Bibliometric Review
Liu, X. L., Yeerlan, J., Liu, Z., Bai, Y., Wang, Q., Yan, Y., Xu, L., Cui, J., & Zhang, L. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240688 · Cited by 9 · see citing works
Systematic analysis of diabetes- and glucose metabolism-related proteins and its application to Alzheimer’s disease
Yang, J., Li, S., & Liu, Y. (2013) · Journal of Biomedical Science and Engineering · doi:10.4236/jbise.2013.66078 · Cited by 9 · see citing works
Role of Liver X Receptor in Mastitis Therapy and Regulation of Milk Fat Synthesis
Hu, X., Zhang, N., & Fu, Y. (2018) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-018-9403-5 · Cited by 8 · see citing works
How Do Retinoids Affect Alzheimer’s Disease and Can They Be Novel Drug Candidates?
Alsharief, M. (2024) · Cureus · doi:10.7759/cureus.57548 · Cited by 8 · see citing works
Type II nuclear receptors with potential role in Alzheimer disease
Muñoz-Cabrera, J., Adrián, S.-H., & Arboleda, G. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100940 · Cited by 7 · see citing works
The Janus-like Association between Proton Pump Inhibitors and Dementia
Papazoglou, A., Arshaad, M. I., Henseler, C., Daubner, J., Broich, K., Haenisch, B., & Weiergräber, M. (2021) · Current Alzheimer Research · doi:10.2174/1567205018666210929144740 · Cited by 7 · see citing works
Isotschimgine promotes lifespan, healthspan and neuroprotection of Caenorhabditis elegans via the activation of nuclear hormone receptors
Shi, H., Gao, X., Yu, J., Zhang, L., Fan, B., Liu, Y. M., Wang, X., Fan, S., & Huang, C. (2024) · Biogerontology · doi:10.1007/s10522-024-10142-6 · Cited by 6 · see citing works
NRC-interacting factor directs neurite outgrowth in an activity-dependent manner
Zhao, X., Fu, W., Hung, K.-W., Chien, W. W. Y., Li, Z., Fu, A. K. Y., & Ip, N. Y. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2014.12.041 · Cited by 6 · see citing works
Seco-Prenylated Butylphloroglucinol Derivatives from Hypericum elodeoides and Their Anti-Alzheimer’s Disease Activities
Tian, W., He, S., Zhong, S., Wang, M., Yingting, L., Sun, J., Wang, G., Li, X., & Chen, H. (2025) · Organic Letters · doi:10.1021/acs.orglett.5c02367 · Cited by 5 · see citing works
Structure-based virtual screening for identification of potential non-steroidal LXR modulators against neurodegenerative conditions
Deshwal, S., Baidya, A. T. K., Kumar, R., & Sandhir, R. (2022) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2022.106150 · Cited by 5 · see citing works
Targeting Proteins in Nucleus through Dual-Regulatory Pathways Acting in Cytoplasm
Wu, X., Hu, J., Chen, L., Chen, Z., Wang, T., Wu, F., Dai, J., Xia, F., & Lou, X. (2023) · Nano Letters · doi:10.1021/acs.nanolett.3c01815 · Cited by 5 · see citing works
Investigation of Interactions between DNA and Nuclear Receptors: A Review of the Most Used Methods
Fattori, J., Indolfo, N. D. C., Campos, J. C. L. D. O., Videira, N. B., Bridi, A. V., Doratioto, T. R., de Assis, M. A., & Figueira, A. C. M. (2014) · Nuclear Receptor Research · doi:10.11131/2014/101090 · Cited by 5 · see citing works
The LXR/RXR Approaches in Alzheimer’s Disease: Is the Blood-Bra in Barrier the Forgotten Partner?
Fenart, P. C. L. (2013) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000e131 · Cited by 4 · see citing works
Ketogenic Diet and PPARgamma
Simeone, T. A. (2016) · doi:10.1093/med/9780190497996.003.0020 · Cited by 4 · see citing works
Synthetic receptors in medicine
Mishra, S., Raval, M., Singh, V., & Tiwari, A. K. (2022) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2022.09.011 · Cited by 3 · 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
Self-citation
P3–035: Investigating nuclear hormone receptors as a target for Alzheimer's disease
Iyer, S. V., Kushwaha, A., Crisp, A., & Pierce‐Shimomura, J. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.05.1104
Therapeutic Potential of PPARs in Alzheimer’s Disease
Upaganlawar, A. B., Upasani, C. D., & Ihim, S. A. (2022) · Springer eBooks · doi:10.1007/978-981-16-7606-2_14 · Cited by 2 · see citing works
Neuroprotective mechanisms of peroxisome proliferator-activated receptor agonists in Alzheimer’s disease
Sodhi, R. K., Singh, N., & Jaggi, A. S. (2011) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-011-0654-6 · Cited by 36 · see citing works
Recent Insights on the Role of Nuclear Receptors in Alzheimer’s Disease: Mechanisms and Therapeutic Application
Shan, X., Li, D., Yin, H., Tao, W., Zhou, L., Gao, Y. W., Xing, C., & Zhang, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031207 · Cited by 7 · see citing works

Authors: Mandrekar-Colucci, S., & Landreth, G. E.
Affiliations: Case Western Reserve University (US)
Corresponding author: Landreth, Gary E
ORCID: Landreth, Gary E
Venue: Expert Opinion on Therapeutic Targets
Publisher: Informa UK Limited
Published: 2011-07
Volume: 15
Issue: 9
Pages: 1085-1097
ISSN: 1472-8222 (ISSN-L)
1744-7631
DOI: 10.1517/14728222.2011.594043
PMC: PMC3156324
OpenAlex: W2151194854
Cited by: 126
References: 112
Citations by year: 2026: 9 · 2025: 4 · 2024: 8 · 2023: 8 · 2022: 5 · 2021: 9 · 2020: 4 · 2019: 8 · 2018: 8 · 2017: 5 · 2016: 9 · 2015: 9 · 2014: 10 · 2013: 20 · 2012: 10
FWCI: 1.39
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Expert Opinion on Therapeutic Targets (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute on Aging (1-R01-AG030482, R01AG030482)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: Alzheimer's disease, nuclear receptors, therapeutic target, amyloid-beta, PPARγ agonists, liver X receptor agonist, microglial activation, neuroinflammation, blood-brain barrier permeability, hepatic steatosis, drug development
MeSH terms: Alzheimer Disease, Animals, Brain, Energy Metabolism, Humans, Inflammation, Drug Design, Amyloid beta-Peptides, Drug Delivery Systems, Microglia, Receptors, Cytoplasmic and Nuclear

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Nuclear receptors as therapeutic targets for Alzheimer's disease

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks