The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Amyloid-β Pathology and APOE Genotype Modulate Retinoid X Receptor Agonist Activity in Vivo
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ApoE4 does not clear plaques or soluble Aβ as well as apoE3.
“studies have demonstrated that apoE4 does not clear plaques or soluble Aβ as well as apoE3 [45, 46].”
From Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation (2023) · cites this paper as [46]
The RXR Agonist Mechanism of Action section (page unavailable) explicitly says soluble Aβ clearance is lower with apoE4 than with apoE3. The Collective Data Analysis section (page unavailable) reports more insoluble Aβ in E4FAD than E3FAD mice, but does not establish that apoE4 clears existing plaques less effectively. (LLM, conf=0.88)
Experimental — accuracy not yet measuredCholesterol transport to apoE4-lipoproteins was not increased by AVAS.
“As measured by Western blot and normalized to β-actin (Fig. 7e), ABCA1 levels did not change with AVAS treatment, evidence that cholesterol transport to the apoE4-lipoproteins was not increased [52].”
From Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation (2023) · cites this paper as [52]
The RXR Agonist Treatment Protocols section describes treatment with bexarotene (Bex) or LG100268, not AVAS. The E4FAD hippocampus results report increased apoE4 lipoprotein association with those agonists, but they do not establish what happens with AVAS. Searches for AVAS treatment and AVAS-related cholesterol transport found no passage addressing the claim. (LLM, conf=0.76)
Experimental — accuracy not yet measuredSevere hepatomegaly is associated with RXR agonism due to induction of hepatic lipogenic pathways by SREBP1C.
“However, severe hepatomegaly is associated with RXR agonism due to an induction of hepatic lipogenic pathways by sterol-regulatory element-binding protein 1C (SREBP1C) [52, 53].”
From Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation (2023) · cites this paper as [52]
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“EFAD mice (31) were generated by crossing 5 FAD mice (48) and APOE-TR mice (49).”
MethodHuman ApoE isoforms differentially regulate brain amyloid-β peptide clearance
Castellano, J. M., Kim, J., Stewart, F. R., Jiang, H., DeMattos, R. B., Patterson, B. W., Fagan, A. M., Morris, J. C., Mawuenyega, K. G., Cruchaga, C., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002156 · Cited by 1,242
ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models
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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
Apolipoprotein E in Alzheimer’s disease and other neurological disorders
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“The levels of the soluble apoE/A complex are lower and oA higher with AD and APOE4 in EFAD mice and human tissue (32).”
BackgroundapoE isoform–specific disruption of amyloid β peptide clearance from mouse brain
Deane, R., Sagare, A., Hamm, K., Parisi, M., Lane, S., Finn, M. B., Holtzman, D. M., & Zlokovic, B. V. (2008) · Journal of Clinical Investigation · doi:10.1172/jci36663 · Cited by 771
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Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses
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Overexpression of ABCA1 reduces amyloid deposition in the PDAPP mouse model of Alzheimer disease
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Lack of ABCA1 Considerably Decreases Brain ApoE Level and Increases Amyloid Deposition in APP23 Mice
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Apolipoprotein E, Especially Apolipoprotein E4, Increases the Oligomerization of Amyloid β Peptide
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Human APOE Isoform-Dependent Effects on Brain β-Amyloid Levels in PDAPP Transgenic Mice
Bales, K. R., Liu, F., Wu, S., Lin, S., Koger, D., DeLong, C., Hansen, J. C., Sullivan, P. M., & Paul, S. M. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.0887-09.2009 · Cited by 274
APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease
Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407957 · Cited by 268 · cited 9×
“EFAD mice (31) were generated by crossing 5 FAD mice (48) and APOE-TR mice (49).”
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Self-citationFitz, N. F., Cronican, A. A., Lefterov, I., & Koldamova, R. (2013) · Science · doi:10.1126/science.1235809 · Cited by 151
Veeraraghavalu, K., Zhang, C., Miller, S., Hefendehl, J. K., Rajapaksha, T. W., Ulrich, J., Jucker, M., Holtzman, D. M., Tanzi, R. E., Vassar, R., et al. (2013) · Science · doi:10.1126/science.1235505 · Cited by 133
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Metadata
- Authors
- 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.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 289
- Issue
- 44
- Pages
- 30538-30555
- ISSN
- 0021-9258
- Cited by
- 89
- References
- 24
- Language
- en
- Licence
- Funders
- National Institutes of Health (P01AG030128)
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