The DOI matches its Crossref record; 76 of the 76 references it cites were found in a registry or an index.
ApoE4 and Aβ Oligomers Reduce BDNF Expression via HDAC Nuclear Translocation
Open accessAbstract
Apolipoprotein E4 (ApoE4) is a major genetic risk factor for several neurodegenerative disorders, including Alzheimer's disease (AD). Epigenetic dysregulation, including aberrations in histone acetylation, is also associated with AD. We show here for the first time that ApoE4 increases nuclear translocation of histone deacetylases (HDACs) in human neurons, thereby reducing BDNF expression, whereas ApoE3 increases histone 3 acetylation and upregulates BDNF expression. Amyloid-β (Aβ) oligomers, which have been implicated in AD, caused effects similar to ApoE4. Blocking low-density lipoprotein receptor-related protein 1 (LRP-1) receptor with receptor-associated protein (RAP) or LRP-1 siRNA abolished the ApoE effects. ApoE3 also induced expression of protein kinase C ε (PKCε) and PKCε retained HDACs in the cytosol. PKCε activation and ApoE3 supplementation prevented ApoE4-mediated BDNF downregulation. PKCε activation also reversed Aβ oligomer- and ApoE4-induced nuclear import of HDACs, preventing the loss in BDNF. ApoE4 induced HDAC6-BDNF promoter IV binding, which reduced BDNF exon IV expression. Nuclear HDAC4 and HDAC6 were more abundant in the hippocampus of ApoE4 transgenic mice than in ApoE3 transgenic mice or wild-type controls. Nuclear translocation of HDA6 was also elevated in the hippocampus of AD patients compared with age-matched controls. These results provide new insight into the cause of synaptic loss that is the most important pathologic correlate of cognitive deficits in AD.
Overview
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
Cites
Statistics
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In another study, ApoE4 increased the nuclear translocation of histone deacetylases (HDACs) in human neuroblastomas, thereby reducing brain derived neurotrophic factor expression [54].”
From Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease (2017) · cites this paper as [54]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In contrast, ApoE3 retains HDACs in the cytosol via elevating the expression of protein kinase C ε.”
From Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease (2017) · cites this paper as [54]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Of note, sApoE has been found to influence the transcriptome by modulating histone acetylation (68, 69).”
From Secreted Apoe rewires melanoma cell state vulnerability to ferroptosis (2024) · cites this paper as [69]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“In the brains of Alzheimer's disease patients, nuclear translocation of HDA6 was increased as compared with controls.”
From Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease (2017) · cites this paper as [54]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Integrative genomics identifies APOE ε4 effectors in Alzheimer's disease
Rhinn, H., Fujita, R., Qiang, L., Cheng, R., Lee, J. H., & Abeliovich, A. (2013) · Nature · doi:10.1038/nature12415 · Cited by 151
RetractedAnalyzing real-time PCR data by the comparative CT method
Schmittgen, T. D., & Livak, K. J. (2008) · Nature Protocols · doi:10.1038/nprot.2008.73 · Cited by 26,190
Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268
Apolipoprotein E and Alzheimer disease: risk, mechanisms and therapy
Liu, C.-C., Kanekiyo, T., Xu, H., & Bu, G. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.263 · Cited by 3,459
Ca2+ Influx Regulates BDNF Transcription by a CREB Family Transcription Factor-Dependent Mechanism
Tao, X., Finkbeiner, S., Arnold, D. B., Shaywitz, A. J., & Greenberg, M. E. (1998) · Neuron · doi:10.1016/s0896-6273(00)81010-7 · Cited by 1,561
Strittmatter, W. J., Weisgraber, K. H., Huang, D. Y., Dong, L. M., Salvesen, G. S., Pericak-Vance, M., Schmechel, D., Saunders, A. M., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8098 · Cited by 1,363
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
Yang, X., & Seto, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2346 · Cited by 1,277
Recovery of learning and memory is associated with chromatin remodelling
Fischer, A., Sananbenesi, F., Wang, X., Dobbin, M., & Tsai, L.-H. (2007) · Nature · doi:10.1038/nature05772 · Cited by 1,227
Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy
Bu, G. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2620 · Cited by 1,168
Regulation of histone acetylation during memory formation in the hippocampus
Levenson, J. M., O'Riordan, K. J., Brown, K. D., Trinh, M. A., Molfese, D. L., & Sweatt, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402229200 · Cited by 1,131
Cited by
Sorted by citations
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870
Brain-Derived Neurotrophic Factor in Alzheimer’s Disease and Its Pharmaceutical Potential
Gao, L., Zhang, Y., Sterling, K., & Song, W. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00279-0 · Cited by 606
Numakawa, T., Odaka, H., & Adachi, N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113650 · Cited by 367
Shinohara, M., Tachibana, M., Kanekiyo, T., & Bu, G. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075796 · Cited by 297
Shen, S., & Kozikowski, A. P. (2016) · ChemMedChem · doi:10.1002/cmdc.201500486 · Cited by 288
Sexual dimorphism in predisposition to Alzheimer's disease
Fisher, D. W., Bennett, D. A., & Dong, H. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.04.004 · Cited by 270
Role of inflammatory molecules in the Alzheimer's disease progression and diagnosis
Bagyinszky, E., Giau, V. V., Shim, K., Suk, K., An, S. S. A., & Kim, S. (2017) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2017.03.031 · Cited by 276
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220
Amyloid clearance defect in ApoE4 astrocytes is reversed by epigenetic correction of endosomal pH
Prasad, H., & Rao, R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1801612115 · Cited by 207
Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease
Liao, F., Yoon, H., & Kim, J. (2017) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000383 · Cited by 191
Therapeutic potentials of plant iridoids in Alzheimer's and Parkinson's diseases: A review
Dinda, B., Dinda, M., Kulsi, G., Chakraborty, A., & Dinda, S. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.03.009 · Cited by 178
Astrocytic ApoE reprograms neuronal cholesterol metabolism and histone-acetylation-mediated memory
Li, X., Zhang, J., Li, D., He, C., He, K., Xue, T., Wan, L., Zhang, C., & Liu, Q. (2021) · Neuron · doi:10.1016/j.neuron.2021.01.005 · Cited by 165
Qin, X.-Y., Cao, C., Cawley, N. X., Liu, T.-T., Yuan, J., Loh, Y. P., & Cheng, Y. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.62 · Cited by 136
APOE4 drives inflammation in human astrocytes via TAGLN3 repression and NF-κB activation
Arnaud, L., Benech, P., Greetham, L., Stephan, D., Jimenez, A., Jullien, N., García‐González, L., Tsvetkov, P. O., Devred, F., Sancho-Martinez, I., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111200 · Cited by 130
Nelson, T. J., Sun, M., Lim, C. S., Sen, A., Khan, T. K., Chirila, F. V., & Alkon, D. L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170161 · Cited by 118
Self-citationHDAC6 in Diseases of Cognition and of Neurons
LoPresti, P. (2020) · Cells · doi:10.3390/cells10010012 · Cited by 105
Sex differences in Alzheimer’s disease: Understanding the molecular impact
Toro, C. A., Zhang, L., Cao, J., & Cai, D. (2019) · Brain Research · doi:10.1016/j.brainres.2019.05.031 · Cited by 105
Role of histone deacetylases and their inhibitors in neurological diseases
Zhang, L.-Y., Zhang, S.-Y., Wen, R., Zhang, T.-N., & Yang, N. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107410 · Cited by 84
Early Life Stress and Epigenetics in Late-onset Alzheimer’s Dementia: A Systematic Review
Lemche, E. (2018) · Current Genomics · doi:10.2174/1389202919666171229145156 · Cited by 84
PKR Inhibition Rescues Memory Deficit and ATF4 Overexpression in ApoE ε4 Human Replacement Mice
Segev, Y., Barrera, I., Ounallah-Saad, H., Wibrand, K., Sporild, I., Livne, A., Rosenberg, T., David, O., Mints, M., Bramham, C. R., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.5241-14.2015 · Cited by 81
Li, H., Tan, Y., Cheng, X. M., Zhang, Z., Huang, J., Hui, S., Zhu, L., Liu, Y., Zhao, D. S., Liu, Z., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.990307 · Cited by 77
Pharmacological intervention of histone deacetylase enzymes in the neurodegenerative disorders
Gupta, R. V., Ambasta, R. K., & Kumar, P. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117278 · Cited by 85
Epigenetic Regulation of BDNF Gene during Development and Diseases
Chen, K.-W., & Chen, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030571 · Cited by 75
Brain biometals and Alzheimer's disease – boon or bane?
Prakash, A. K., Dhaliwal, G. K., Kumar, P., & Majeed, A. B. A. (2016) · International Journal of Neuroscience · doi:10.3109/00207454.2016.1174118 · Cited by 71
Xia, Y., Wang, Z.-H., Zhang, J., Liu, X., Yu, S. P., Ye, K. X., Wang, J., Ye, K., & Wang, X. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-00956-4 · Cited by 66
Wu, Q., Yang, X., Zhang, L., Zhang, Y., & Feng, L. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0199-2 · Cited by 66
Allard, J. S., Ntekim, O. E., Johnson, S. P., Ngwa, J. S., Bond, V., Pinder, D., Gillum, R. F., Fungwe, T. V., Kwagyan, J., & Obisesan, T. O. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.11.001 · Cited by 69
Transcriptional Effects of ApoE4: Relevance to Alzheimer’s Disease
Theendakara, V., Peters-Libeu, C. A., Bredesen, D. E., & Rao, R. V. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0757-2 · Cited by 63
ApoE isoforms differentially regulates cleavage and secretion of BDNF
Sen, A., Nelson, T. J., & Alkon, D. L. (2017) · Molecular Brain · doi:10.1186/s13041-017-0301-3 · Cited by 60
Self-citationAutophagy regulation by acetylation—implications for neurodegenerative diseases
Son, S. M., Park, S. J., Fernandez-Estévez, M., & Rubinsztein, D. C. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00556-4 · Cited by 59
Xia, D., Huang, X., Bi, C., Mao, L., Peng, L., & Qian, H. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00065 · Cited by 57
Neurotrophins and Other Growth Factors in the Pathogenesis of Alzheimer’s Disease
Numakawa, T., & Kajihara, R. (2023) · Life · doi:10.3390/life13030647 · Cited by 57
Iannucci, J., Sen, A., & Grammas, P. (2021) · Current Issues in Molecular Biology · doi:10.3390/cimb43010018 · Cited by 57
Self-citationHistone acetylation in neuronal (dys)function
Bonnaud, E. M., Suberbielle, E., & Malnou, C. E. (2016) · BioMolecular Concepts · doi:10.1515/bmc-2016-0002 · Cited by 58
Yang, C., Liu, Y.-P., Dai, H.-Y., Shiue, Y., Tsai, C.-J., Huang, M., & Yeh, Y. (2015) · Oncotarget · doi:10.18632/oncotarget.4749 · Cited by 53
Wu, Y., Hou, F., Wang, X., Kong, Q., Han, X., & Bai, B. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00114 · Cited by 52
Development of a potential PET probe for HDAC6 imaging in Alzheimer's disease
Bai, P., Mondal, P., Bagdasarian, F. A., Rani, N., Liu, Y., Gomm, A., Tocci, D. R., Choi, S. H., Wey, H., Tanzi, R. E., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.05.017 · Cited by 50
Unlocking Alzheimer’s Disease: The Role of BDNF Signaling in Neuropathology and Treatment
Alqahtani, S. M., Al-Kuraishy, H. M., Al-Gareeb, A. I., Albuhadily, A. K., Alexiou, A. T., Papadakis, M., Hemeda, L. R., Faheem, S. A., & Batiha, G. E. (2025) · NeuroMolecular Medicine · doi:10.1007/s12017-025-08857-x · Cited by 57
Yang, A., Kantor, B., & Chiba‐Falek, O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031244 · Cited by 51
Wan, Q., Ma, X., Zhang, Z., Sun, T., Feng, X., Zhao, G., & Wu, Y. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9868-4 · Cited by 50
Jian, W., Zhang, Z., Zhan, J.-H., Chu, S., Ye, P., Zhao, M., Wang, Q., & Chen, N. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0334-5 · Cited by 51
Intranasal delivery of BDNF rescues memory deficits in AD11 mice and reduces brain microgliosis
Braschi, C., Capsoni, S., Narducci, R., Poli, A., Sansevero, G., Brandi, R., Maffei, L., Cattaneo, A., & Berardi, N. (2020) · Aging Clinical and Experimental Research · doi:10.1007/s40520-020-01646-5 · Cited by 53
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
Wang, Z.-H., Xia, Y., Liu, P., Liu, X., Edgington‐Mitchell, L. E., Lei, K., Yu, S. P., Wang, X., & Ye, K. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102032 · Cited by 48
Wang, Z.-H., Xia, Y., Wu, Z., Kang, S. S., Zhang, J.-C., Liu, P., Liu, X., Song, W., Huin, V., Dhaenens, C., et al. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102212 · Cited by 48
Guida, N., Laudati, G., Mascolo, L., Valsecchi, V., Sirabella, R., Selleri, C., Renzo, G. D., Canzoniero, L. M. T., & Formisano, L. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00008 · Cited by 47
Sen, A., Hongpaisan, J., Wang, D., Nelson, T. J., & Alkon, D. L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.730440 · Cited by 46
Self-citationInter-relationship of Histone Deacetylase-6 with Tau-cytoskeletal organization and remodeling
Balmik, A. A., & Chinnathambi, S. (2022) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2022.151202 · Cited by 44
PSD-95-nNOS Coupling Regulates Contextual Fear Extinction in the Dorsal CA3
Cai, C.-Y., Chen, C., Zhou, Y., Han, Z., Qin, C., Cao, B., Tao, Y., Bian, X.-L., Lin, Y., Chang, L., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-30899-4 · Cited by 41
Cao, K., Xiang, J., Dong, Y., Xu, Y., Li, Y., Song, H., Zeng, X.-X., Ran, L., Hong, W., & Guan, Z.-Z. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0490-3 · Cited by 40
Tokgöz, S., & Claassen, J. A. H. R. (2021) · Cardiology and Therapy · doi:10.1007/s40119-020-00209-z · Cited by 42
Sen, A., Nelson, T. J., Alkon, D. L., & Hongpaisan, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171008 · Cited by 40
Self-citationMitrović, M. M., Selaković, D., Jovicic, N. U., Ljujić, B., & Rosic, G. L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104926 · Cited by 42
Tian, X., Tao, F., Zhang, B., Dong, J., & Zhang, Z. (2018) · IUBMB Life · doi:10.1002/iub.1720 · Cited by 37
ADAMTS-4 promotes neurodegeneration in a mouse model of amyotrophic lateral sclerosis
Lemarchant, S., Pomeshchik, Y., Kidin, I., Kärkkäinen, V., Valonen, P. K., Lehtonen, Š., Goldsteins, G., Malm, T., Kanninen, K. M., & Koıstınaho, J. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0078-3 · Cited by 39
Numakawa, T., & Kajihara, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031596 · Cited by 35
Chen, Y., Lu, C.-H., Ke, C., Chiu, S.-J., Chang, C., Yang, B., Gelovani, J. G., & Liu, R.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168633 · Cited by 33
Late-onset dementia: a mosaic of prototypical pathologies modifiable by diet and lifestyle
Mattson, M. P. (2015) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2015.3 · Cited by 34
The X Files: “The Mystery of X Chromosome Instability in Alzheimer’s Disease”
Bajić, V., Essack, M., Živković, L., Stewart, A. J., Zafirovic, S. S., Bajić, V. B., Gojobori, T., Isenović, E. R., & Spremo‐Potparević, B. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2019.01368 · Cited by 33
Giarratana, A. O., Zheng, C., Reddi, S., Teng, S. L., Berger, D. S., Adler, D., Sullivan, P. M., Thakker‐Varia, S., & Alder, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-76849-x · Cited by 39
Status of precision medicine approaches to traumatic brain injury
Reddi, S., Thakker‐Varia, S., Alder, J., & Giarratana, A. O. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.335824 · Cited by 33
Synaptically Localized Transcriptional Regulators in Memory Formation
Uchida, S., & Shumyatsky, G. P. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.07.023 · Cited by 33
Kantor, B., O’Donovan, B., & Chiba‐Falek, O. (2025) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2025.102635 · Cited by 38
Schlüter, A., Aksan, B., Fioravanti, R., Valente, S., Mai, A., & Mauceri, D. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-01658-x · Cited by 31
Guida, N., Laudati, G., Mascolo, L., Cuomo, O., Anzilotti, S., Sirabella, R., Santopaolo, M., Galgani, M., Montuori, P., Renzo, G. D., et al. (2016) · Toxicological Sciences · doi:10.1093/toxsci/kfw157 · Cited by 30
Kakoty, V., Sarathlal, K. C., Kumari, S., Yang, C., Dubey, S. K., Sahebkar, A., Kesharwani, P., & Taliyan, R. (2023) · Inflammopharmacology · doi:10.1007/s10787-023-01187-z · Cited by 30
Wang, Y., Xia, Y., Hu, K., Zeng, M., Zhi, C., Lai, M., Wu, L., Liu, S., Zeng, S., Huang, Z., et al. (2019) · International Journal of Cancer · doi:10.1002/ijc.32321 · Cited by 29
Neuro-regeneration Therapeutic for Alzheimer’s Dementia: Perspectives on Neurotrophic Activity
Sun, M., & Alkon, D. L. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.07.008 · Cited by 31
Self-citationEpigenetic enzymes: A role in aging and prospects for pharmacological targeting
PASYUKOVA, E. G., Symonenko, A. V., Rybina, O. Y., & Vaiserman, A. M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101312 · Cited by 28
The Transcription Factor XBP1 in Memory and Cognition: implications in Alzheimer’s Disease
Cissé, M., Duplan, E., & Checler, F. (2016) · Molecular Medicine · doi:10.2119/molmed.2016.00229 · Cited by 28
Čechová, K., Andel, R., Angelucci, F., Chmátalová, Z., Marková, H., Laczó, J., Vyhnálek, M., Maťoška, V., Kaplan, V., Nedelská, Z., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190464 · Cited by 28
Into the Fourth Dimension: Dysregulation of Genome Architecture in Aging and Alzheimer’s Disease
Winick‐Ng, W., & Rylett, R. J. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00060 · Cited by 28
Secreted Apoe rewires melanoma cell state vulnerability to ferroptosis
More, S., Bonnereau, J., Wouters, D., Spotbeen, X., Karras, P., Rizzollo, F., Killian, T., Venken, T., Naulaerts, S., Vervoort, E., et al. (2024) · Science Advances · doi:10.1126/sciadv.adp6164 · Cited by 25
LRP1 receptor-mediated immunosuppression of α-MMC on monocytes
Deng, N., Li, M., Shen, D., He, Q., Sun, W., Liu, M., Liu, Y., Zhou, Y., Zheng, J., & Shen, F. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.01.036 · Cited by 25
Peptides Derived from Growth Factors to Treat Alzheimer’s Disease
Gascon, S., Jann, J., Langlois-Blais, C., Plourde, M., Lavoie, C. L., & Faucheux, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116071 · Cited by 24
Fang, Y., Chan, L., Liou, J., Tu, Y., Lai, M.-J., Chen, C. Y., Vidyanti, A. N., Lee, H., & Hu, C. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15358 · Cited by 22
Wang, L., Shen, F., Zhang, M., He, Q., Zhao, H., Yu, X., Yang, S., Liu, Y., Deng, N., Zheng, J., et al. (2016) · Toxicology · doi:10.1016/j.tox.2016.05.025 · Cited by 22
MohanaSundaram, A., Shanmugarajan, T. S., & Ravichandiran, V. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00532 · Cited by 22
Wang, Y., Jia, A., & Ma, W. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9694 · Cited by 22
Rey, R., Chauvet‐Gélinier, J., Suaud‐Chagny, M., Ragot, S., Bonin, B., d’Amato, T., & Teyssier, J. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1406-0 · Cited by 21
Lisek, M., Bochenska, N., Tomczak, J., Duraj, J., & Boczek, T. (2025) · Antioxidants · doi:10.3390/antiox14081015 · Cited by 19
Cytoplasmic HDAC4 recovers synaptic function in the 3×Tg mouse model of Alzheimer's disease
Colussi, C., Aceto, G., Ripoli, C., Bertozzi, A., Puma, D. D. L., Paccosi, E., D’Ascenzo, M., & Grassi, C. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12861 · Cited by 19
Turkman, N., Liu, D., & Pirola, I. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.114011 · Cited by 18
Takasu, K., Niidome, K., Hasegawa, M., & Ogawa, K. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.782206 · Cited by 18
APOE–NOTCH axis governs elastogenesis during human cardiac valve remodeling
Liu, Z., Liu, Y., Yu, Z., Tan, C., Pek, N. M. Q., O’Donnell, A., Wu, A., Glass, I. A., Winlaw, D. S., Guo, M., et al. (2024) · Nature Cardiovascular Research · doi:10.1038/s44161-024-00510-3 · Cited by 18
Huang, H., Yan, P., Sun, T., Mo, X., Yin, J., Li, P., Zhu, Y., Rong, S., Yang, W. Q., Chen, X., et al. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/4572893 · Cited by 17
Lee, Y. I., Kim, Y. G., Pyeon, H., Ahn, J., Logan, S., Orock, A. M., Joo, K. M., Lőrincz, A., & Deák, F. (2019) · GeroScience · doi:10.1007/s11357-019-00067-1 · Cited by 17
Jiao, F., Jiang, D., Li, Y., Mei, J., Wang, Q., & Li, X. (2022) · Cells · doi:10.3390/cells11203201 · Cited by 16
Charou, D., Rogdakis, T., Latorrata, A., Valcárcel, M., Papadogiannis, V., Athanasiou, C., Tsengenes, A., Papadopoulou, M. A., Lypitkas, D., Lavigne, M. D., et al. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-03818-w · Cited by 18
Banerjee, S., Mandal, S., Singh, S., Sen, A., & Das, P. (2025) · Nanoscale · doi:10.1039/d5nr00752f · Cited by 14
Self-citationA novel insight into neurological disorders through HDAC6 protein–protein interactions
Sangani, N. B., Koetsier, J., Mélius, J., Kutmon, M., Ehrhart, F., Evelo, C. T., Curfs, L., Reutelingsperger, C. P. M., & Eijssen, L. (2024) · Scientific Reports · doi:10.1038/s41598-024-65094-1 · Cited by 14
HIV Promotes Neurocognitive Impairment by Damaging the Hippocampal Microvessels
Sharma, A. L., Wang, H., Zhang, Z., Millien, G., Tyagi, M., & Hongpaisan, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02890-8 · Cited by 12
Dubey, H., Dubey, A., Gulati, K., & Ray, A. (2022) · International Journal of Neuroscience · doi:10.1080/00207454.2022.2150190 · Cited by 12
Li, J. Z., Ramalingam, N., & Li, S. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01827 · Cited by 11
Somatostatin: Linking Cognition and Alzheimer Disease to Therapeutic Targeting
Sandoval, K. E., & WITT, K. A. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.124.001117 · Cited by 14
Rodríguez‐Rojo, I. C., Cuesta, P., López, M. E., de Frutos‐Lucas, J., Bruña, R., Pereda, E., Barabash, A., Carrasco, P. M., Montenegro-Peña, M., Marcos, A., et al. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00684 · Cited by 11
Vilor‐Tejedor, N., Operto, G., Evans, T. E., Falcón, C., Crous‐Bou, M., Minguillón, C., Cacciaglia, R., Milà‐Alomà, M., Grau‐Rivera, O., Suárez‐Calvet, M., et al. (2020) · Brain Structure and Function · doi:10.1007/s00429-020-02125-3 · Cited by 9
Pin1 Is Involved in HDAC6-mediated Cancer Cell Motility
Chuang, H.-H., Huang, M., Wang, P., Liu, Y., Hsiao, M., & Yang, C. (2018) · International Journal of Medical Sciences · doi:10.7150/ijms.27426 · Cited by 9
Fowler, C. G., Tarantino, M. I., Gillett, A. E., Muñiz, V., Anderson, M. A., Bonner, R. L., & Vichaya, E. G. (2025) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2025.05.010 · Cited by 8
Elia, A., Parodi‐Rullán, R. M., Vázquez‐Torres, R., Carey, A. M., Zhao, H., Javadov, S. A., & Fossati, S. (2026) · Advanced Science · doi:10.1002/advs.202511924 · Cited by 9
Metadata
- Authors
- Sen, A., Nelson, T. J., & Alkon, D. L.
- Affiliations
- Blanchette Rockefeller Neurosciences Institute (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2015-05-13
- Volume
- 35
- Issue
- 19
- Pages
- 7538-7551
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6705431
- OpenAlex
- W1493503901
- Cited by
- 133
- References
- 76
- Citations by year
- 2026: 10 · 2025: 11 · 2024: 10 · 2023: 7 · 2022: 12 · 2021: 17 · 2020: 11 · 2019: 10 · 2018: 17 · 2017: 11 · 2016: 13 · 2015: 4
- FWCI
- 11.05
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- APOE ε4, amyloid-beta oligomers, BDNF expression, histone deacetylase, histone H3 acetylation, LRP1, receptor-associated protein, protein kinase C epsilon, HDAC6, HDAC4, hippocampus, synaptic loss, Alzheimer's disease, epigenetic regulation, APOE3
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Apolipoproteins E, Brain, Cell Nucleolus, Cells, Cultured, Cholesterol, Female, Gene Expression Regulation, Histone Deacetylases, Humans, Male, Mice, Transgenic, Middle Aged, Neuroblastoma, Neurons, Protein Kinase C, Case-Control Studies, Amyloid beta-Peptides, Brain-Derived Neurotrophic Factor, Protein Transport, Low Density Lipoprotein Receptor-Related Protein-1, RNA Interference, Cell Line, Tumor, Mice
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