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Epidermal growth factor receptor is a preferred target for treating Amyloid-β–induced memory loss
Open accessAbstract
Current understanding of amyloid-β (Aβ) metabolism and toxicity provides an extensive list of potential targets for developing drugs for treating Alzheimer’s disease. We took two independent approaches, including synaptic-plasticity–based analysis and behavioral screening of synthetic compounds, for identifying single compounds that are capable of rescuing the Aβ-induced memory loss in both transgenic fruit fly and transgenic mouse models. Two clinically available drugs and three synthetic compounds not only showed positive effects in behavioral tests but also antagonized the Aβ oligomers-induced activation of the epidermal growth factor receptor (EGFR). Such surprising converging outcomes from two parallel approaches lead us to conclude that EGFR is a preferred target for treating Aβ-induced memory loss.
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“as well as increased astrocyte expression of EGFR, which has been proposed as a potential receptor for Aβ37, and a regulator of astrocytes in multiple sclerosis38.”
From Human and mouse single-nucleus transcriptomics reveal TREM2-dependent and TREM2-independent cellular responses in Alzheimer’s disease (2020) · cites this paper as [37]
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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedSoluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Epidermal growth factor receptor mutations in lung cancer
Sharma, S. V., Bell, D. W., Settleman, J., & Haber, D. A. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2088 · Cited by 3,170
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452
The discovery of receptor tyrosine kinases: targets for cancer therapy
Gschwind, A., Fischer, O. M., & Ullrich, A. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1360 · Cited by 1,227
Alzheimer’s disease: Clinical trials and drug development
Mangialasche, F., Solomon, A., Winblad, B., Mecocci, P., & Kivipelto, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70119-8 · Cited by 1,217
Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease
Walsh, D. M., & Selkoe, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.010 · Cited by 1,207
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Zhou, Y., Song, W. M., Andhey, P. S., Swain, A., Levy, T., Miller, K. R., Poliani, P. L., Cominelli, M., Grover, S., Gilfillan, S., et al. (2020) · Nature Medicine · doi:10.1038/s41591-019-0695-9 · Cited by 1,150
Development of autophagy inducers in clinical medicine
Levine, B., Packer, M., & Codogno, P. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73938 · Cited by 351
Expression and Function of the Epidermal Growth Factor Receptor in Physiology and Disease
Chen, J., Zeng, F., Forrester, S. J., Eguchi, S., Zhang, M., & Harris, R. C. (2016) · Physiological Reviews · doi:10.1152/physrev.00030.2015 · Cited by 336
The amyloid precursor protein: A biochemical enigma in brain development, function and disease
Nalivaeva, N. N., & Turner, A. J. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.05.010 · Cited by 293
Drosophila melanogaster as a model organism for Alzheimer’s disease
Prüßing, K., Voigt, A., & Schulz, J. B. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-35 · Cited by 235
Mullane, K., & Williams, M. J. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.11.014 · Cited by 219
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Romanò, R., & Bucci, C. (2020) · Cells · doi:10.3390/cells9081887 · Cited by 214
EGF receptor in organ development, tissue homeostasis and regeneration
Tito, C., Masciarelli, S., Colotti, G., & Fazi, F. (2025) · Journal of Biomedical Science · doi:10.1186/s12929-025-01119-9 · Cited by 148
Zhou, Z.-Q., Fan, H., He, R., Xiao, J., Tsoi, B., Lan, K.-H., Kurihara, H., So, K., Yao, X., & Gao, H. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b05274 · Cited by 120
Self-citationBinding Sites for Amyloid-β Oligomers and Synaptic Toxicity
Smith, L. M., & Strittmatter, S. M. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024075 · Cited by 109
ErbB2 regulates autophagic flux to modulate the proteostasis of APP-CTFs in Alzheimer’s disease
Wang, B.-J., Her, G. M., Hu, M., Chen, Y.-W., Tung, Y.-T., Wu, P., Hsu, W., Lee, H., Jin, L., Hwang, S. L., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1618804114 · Cited by 94
Genomic convergence and network analysis approach to identify candidate genes in Alzheimer's disease
Talwar, P., Silla, Y., Grover, S., Gupta, M., Agarwal, R., Kushwaha, S. S., & Kukreti, R. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-199 · Cited by 86
Sung, Y. J., Yang, C., Norton, J., Johnson, M., Fagan, A., Bateman, R. J., Perrin, R. J., Morris, J. C., Farlow, M. R., Chhatwal, J. P., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abq5923 · Cited by 84
Bioinformatics methods in drug repurposing for Alzheimer’s disease
Siavelis, J. C., Bourdakou, M. M., Athanasiadis, E. I., Spyrou, G. M., & Nikita, K. S. (2015) · Briefings in Bioinformatics · doi:10.1093/bib/bbv048 · Cited by 85
Brody, A. H., & Strittmatter, S. M. (2017) · Advances in pharmacology · doi:10.1016/bs.apha.2017.09.007 · Cited by 89
Protein Phosphorylation is a Key Mechanism in Alzheimer’s Disease
Oliveira, J. M., Costa, M. G. C., Cachide, M., Silva, O. A. B. D. C. E., & Henriques, A. G. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170176 · Cited by 84
Genome-wide analysis of genetic predisposition to Alzheimer’s disease and related sex disparities
Nazarian, A., Yashin, A. I., & Kulminski, A. M. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0458-8 · Cited by 82
Yulug, B., Altay, O., Li, X., Hanoglu, L., Cankaya, S., Lam, S., Velioglu, H. A., Yang, H., Coskun, E., Idil, E., et al. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00336-2 · Cited by 79
Anti-inflammatory effect of afatinib (an EGFR-TKI) on OGD-induced neuroinflammation
Chen, Y., Hsu, C., Shiao, Y., Wang, H., Lo, Y., & Lin, A. M. Y. (2019) · Scientific Reports · doi:10.1038/s41598-019-38676-7 · Cited by 77
Tsuji, S., Hase, T., Yachie-Kinoshita, A., Nishino, T., Ghosh, S., Kikuchi, M., Shimokawa, K., Aburatani, H., Kitano, H., & Tanaka, H. (2021) · Alzheimer's Research & Therapy · doi:10.1186/s13195-021-00826-3 · Cited by 75
EGFR is a potential dual molecular target for cancer and Alzheimer’s disease
Choi, H.-J., Jeong, Y. J., Kim, J., & Hoe, H. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1238639 · Cited by 72
Thomas, R., Zuchowska, P., Morris, A. W. J., Marottoli, F. M., Sunny, S., Deaton, R., Gann, P. H., & Tai, L. M. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0387-3 · Cited by 72
Mansour, H. M., Fawzy, H. M., El-Khatib, A. S., & Khattab, M. M. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.06.013 · Cited by 69
Jayaswamy, P. K., Vijaykrishnaraj, M., Patil, P., Alexander, L. M., Kellarai, A., & Shetty, P. K. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101791 · Cited by 71
Puangmalai, N., Sengupta, U., Bhatt, N., Gaikwad, S., Montalbano, M., Bhuyan, A., Garcia, S., McAllen, S., Sonawane, M., Jerez, C., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101766 · Cited by 68
Tavassoly, O., Sato, T., & Tavassoly, I. (2020) · Molecular Pharmacology · doi:10.1124/mol.120.119909 · Cited by 68
Wu, W., Du, S., Shi, W., Liu, Y., Hu, Y., Xie, Z., Yao, X., Liu, Z., Ma, W., Xu, L., et al. (2019) · Protein & Cell · doi:10.1007/s13238-019-0641-0 · Cited by 68
Self-citationLee, H., Jeon, S. G., Kim, J., Kang, R. J., Kim, S., Han, K., Park, H., Kim, K., Sung, Y. M., Nam, H. Y., et al. (2021) · Aging Cell · doi:10.1111/acel.13332 · Cited by 62
Nodulisporiviridins A–H, Bioactive Viridins from Nodulisporium sp.
Zhao, Q., Chen, G., Feng, X., Yu, Y., He, R., Li, X., Huang, Y. Y., Zhou, W., Guo, L., Zheng, Y., et al. (2015) · Journal of Natural Products · doi:10.1021/np500912t · Cited by 61
Self-citationAndrews, J. L., & Fernandez, F. (2015) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2015.06.009 · Cited by 58
Liu, Q. F., Lee, J. H., Kim, Y., Lee, S., Hong, Y. K., Hwang, S., Oh, Y., Lee, K., Yun, H. S., Lee, I., et al. (2015) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-00459 · Cited by 58
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Chandrasekaran, S., & Bonchev, D. (2013) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201304004 · Cited by 58
Drosophila melanogaster: Deciphering Alzheimer's Disease
Tan, F. H. P., & Azzam, G. (2017) · Malaysian Journal of Medical Sciences · doi:10.21315/mjms2016.24.2.2 · Cited by 58
Khattab, M. N. M., Mansour, H. M., Fawzy, H. M., & El-Khatib, A. S. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.332132 · Cited by 53
Aging‐induced Akt activation involves in aging‐related pathologies and Aβ‐induced toxicity
Chen, Y., Li, Y., Hsieh, T., Wang, C., Cheng, K., Wang, L., Lin, T., Cheung, C. H. A., Wu, C., & Chiang, H. (2019) · Aging Cell · doi:10.1111/acel.12989 · Cited by 51
Self-citationDrosophila melanogaster as a model system in the study of pharmacological interventions in aging
Lee, S., & Min, K. (2019) · Translational Medicine of Aging · doi:10.1016/j.tma.2019.09.004 · Cited by 51
Mansour, H. M., Fawzy, H. M., El-Khatib, A. S., & Khattab, M. M. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113697 · Cited by 49
Marín, R., Rojo, J. A. P., Fabelo, N., Fernandez, C. E., & Díaz, M. L. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.04.025 · Cited by 51
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Tsuda, L., & Lim, Y. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-0529-0_3 · Cited by 48
Maurya, S. K., Mishra, J., Abbas, S., & Bandyopadhyay, S. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9061-6 · Cited by 46
Identification of Key Regulatory Genes and Pathways in Prefrontal Cortex of Alzheimer’s Disease
Yang, F., Diao, X., Wang, F., Wang, Q., Sun, J., Zhou, Y., & Xie, J. (2020) · Interdisciplinary Sciences Computational Life Sciences · doi:10.1007/s12539-019-00353-8 · Cited by 45
Genetic Dissection of Alzheimer’s Disease Using Drosophila Models
Jeon, Y., Lee, J., Choi, B., Won, S.-Y., & Cho, K. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030884 · Cited by 46
Russo, A. J. (2014) · Journal of Central Nervous System Disease · doi:10.4137/jcnsd.s13767 · Cited by 40
Lsh/HELLS regulates self-renewal/proliferation of neural stem/progenitor cells
Han, Y., Ren, J., Lee, E. Y., Xu, X., Yu, W., & Muegge, K. (2017) · Scientific Reports · doi:10.1038/s41598-017-00804-6 · Cited by 38
Ma, W., Tao, Y., Wang, Y., & Peng, I. (2017) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(18)30005-0 · Cited by 38
Self-citationFASTKD2 is associated with memory and hippocampal structure in older adults
Ramanan, V. K., Nho, K. T., Shen, L., Risacher, S. L., Kim, S., McDonald, B. C., Farlow, M. R., Foroud, T., Gao, S., Soininen, H. S., et al. (2014) · Molecular Psychiatry · doi:10.1038/mp.2014.142 · Cited by 37
Evaluation of Traditional Medicines for Neurodegenerative Diseases Using Drosophila Models
Lee, S., Bang, S. M., Lee, J. W., & Cho, K. S. (2014) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2014/967462 · Cited by 37
FDA-Approved Kinase Inhibitors in Preclinical and Clinical Trials for Neurological Disorders
Lui, A., Vanleuven, J., Perekopskiy, D., Liu, D., Xu, D., Alzayat, O., Elgokhy, T., Do, T., Gann, M., Martin, R. M., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15121546 · Cited by 36
Soelter, T. M., Howton, T. C., Clark, A. D., Oza, V. H., & Lasseigne, B. N. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01686-8 · Cited by 34
Matsuno, M., Horiuchi, J., Ofusa, K., Masuda, T., & Saitoe, M. (2019) · iScience · doi:10.1016/j.isci.2019.04.014 · Cited by 32
Corcino, Y. L., Gonzalez-Ferrer, S., Mantilla-Muriel, L. E., Trikeriotis, S., Yu, J., Kim, S., Hansen, S., Portillo, J. C., & Subauste, C. S. (2019) · Cellular Microbiology · doi:10.1111/cmi.13084 · Cited by 31
Talwar, P., Gupta, R., Kushwaha, S. S., Agarwal, R., Saso, L., Kukreti, S., & Kukreti, R. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180419124508 · Cited by 31
Xu, D. C., Sas‐Nowosielska, H., Donahue, G., Huang, H., Pourshafie, N., Good, C. R., & Berger, S. L. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01696-6 · Cited by 35
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Bisson, W. H. (2012) · Current Topics in Medicinal Chemistry · doi:10.2174/156802612804547344 · Cited by 30
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Zhang, A. Y., Matsushita, M. T., Zhang, L., Wang, H., Shi, X., Gu, H., Xia, Z., & Cui, J. Y. (2021) · Communications Biology · doi:10.1038/s42003-021-02898-1 · Cited by 29
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Fernandez, F., & Andrews, J. L. (2016) · Neural Regeneration Research · doi:10.4103/1673-5374.175048 · Cited by 28
Lee, S., Bang, S. M., Hong, Y. K., Lee, J. H., Jeong, H., Park, S. H., Liu, Q. F., Lee, I., & Cho, K. S. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.018069 · Cited by 28
Advani, D., & Kumar, P. (2021) · ACS Omega · doi:10.1021/acsomega.1c01526 · Cited by 27
Shen, Z. J., Fu, Y. B., Hou, J. L., Lin, L. N., Wang, X. Y., Li, C., & Yang, Y. (2022) · Chinese Medicine · doi:10.1186/s13020-022-00698-1 · Cited by 27
Wang, L., Liang, B., & Zhong, Y. (2013) · Protein & Cell · doi:10.1007/s13238-013-3043-8 · Cited by 27
Self-citationSong, Q., Feng, G., Huang, Z., Chen, X., Chen, Z., & Ping, Y. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0165-z · Cited by 26
Tavassoly, O., del Cid‐Pellitero, E., Larroquette, F., Cai, E., Thomas, R. A., Soubannier, V., Luo, W., Durcan, T. M., & Fon, E. A. (2021) · Neurotherapeutics · doi:10.1007/s13311-021-01017-6 · Cited by 26
Ferdousi, F., Kondo, S., Sasaki, K., Uchida, Y., Ohkohchi, N., Zheng, Y., & Isoda, H. (2020) · Aging · doi:10.18632/aging.102985 · Cited by 25
Machino, K., Link, C. D., Wang, S. S., Murakami, H., & Murakami, S. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00202 · Cited by 25
Mohaibes, R. J., Fiol-deRoque, M. A., Torres, M., Ordinas, M., López, D. J., Ja, C., Escribá, P. V., & Busquets, X. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.02.020 · Cited by 25
Lalwani, A. K., Krishnan, K., Bagabir, S. A., Alkhanani, M., Almalki, A. H., Haque, S., Sharma, S. K., Singh, R. K. B., & Malik, M. Z. (2022) · Biomolecules · doi:10.3390/biom12030451 · Cited by 25
Kim, J., Kim, S.-J., Jeong, H.-R., Park, J.-H., Moon, M., & Hoe, H.-S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.903309 · Cited by 23
Interactions between Autophagy and Bacterial Toxins: Targets for Therapy?
Mathieu, J. (2015) · Toxins · doi:10.3390/toxins7082918 · Cited by 24
Multifactorial Analysis of a Biomarker Pool for Alzheimer Disease Risk in a North Indian Population
Talwar, P., Grover, S., Sinha, J., Chandna, P., Agarwal, R., Kushwaha, S. S., & Kukreti, R. (2017) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000477206 · Cited by 23
Caporale, A., Tartaggia, S., Castellin, A., & Lucchi, O. D. (2014) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.10.36 · Cited by 21
A human-based multi-gene signature enables quantitative drug repurposing for metabolic disease
Timmons, J. A., Anighoro, A., Brogan, R. J., Stahl, J., Wahlestedt, C., Farquhar, D. G., Taylor‐King, J. P., Volmar, C., Kraus, W. E., & Phillips, S. M. (2021) · eLife · doi:10.7554/elife.68832 · Cited by 21
Wang, L., Li, M., Lin, Y., Du, S., Liu, Z., Ju, J., Suzuki, H., Sawada, M., & Umezawa, K. (2020) · The Journal of Antibiotics · doi:10.1038/s41429-020-0302-9 · Cited by 21
Self-citationScreening of sleep assisting drug candidates with a Drosophila model
Wang, Y., Ma, W., & Peng, I. (2020) · PLoS ONE · doi:10.1371/journal.pone.0236318 · Cited by 21
Self-citationBruban, J., Voloudakis, G., Huang, Q., Kajiwara, Y., Rahim, M. A., Yoon, Y., Shioi, J., Sosa, M. A. G., Shao, Z., Georgakopoulos, A., et al. (2015) · The FASEB Journal · doi:10.1096/fj.15-270645 · Cited by 21
Assessing Neuroprotective Agents for Aβ-Induced Neurotoxicity
Forest, K. H., & Nichols, R. A. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.05.013 · Cited by 19
Dhamodharan, J., Sekhar, G., & Muthuraman, A. (2022) · Molecules · doi:10.3390/molecules27165182 · Cited by 18
Salza, R., Lethias, C., & Ricard‐Blum, S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160751 · Cited by 18
Unraveling Alzheimer’s Disease Using Drosophila
Yeates, C. J., Sarkar, A., Kango‐Singh, M., & Singh, A. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_9 · Cited by 18
Martín‐Peña, A., Rincón-Limas, D. E., & Fernández-Fúnez, P. (2017) · Scientific Reports · doi:10.1038/s41598-017-11594-2 · Cited by 18
XBP1 and PERK Have Distinct Roles in Aβ-Induced Pathology
Cheng, K.-C., & Chiang, H.-C. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0942-y · Cited by 17
Self-citationJeon, Y., Lee, S., Shin, M., Lee, J. H., Suh, Y. S., Hwang, S., Yun, H. S., & Cho, K. S. (2017) · Animal Cells and Systems · doi:10.1080/19768354.2017.1313777 · Cited by 17
Harvey, H., & Durant, S. (2014) · Experimental Brain Research · doi:10.1007/s00221-014-4078-7 · Cited by 16
Vignon, A., Salvador-Prince, L., Lehmann, S., Perrier, V., & Torrent, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168769 · Cited by 17
Niu, M., Hu, J., Wu, S., Zhang, X., Xu, H., Zhang, Y., Zhang, J., & Yang, Y. (2013) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12200 · Cited by 16
Khanehzar, A., Fraire, J. C., Xi, M., Feizpour, A., Xu, F., Wu, L., Coronado, E. A., & Reinhard, B. M. (2018) · Nanoscale · doi:10.1039/c8nr01106k · Cited by 16
Ayikobua, E. T., Semuyaba, I., Eze, D. E., Kalange, M., Nansunga, M., Okpanachi, A. O., & Safiriyu, A. A. (2018) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2018/3717328 · Cited by 16
Ji, X., Cheng, K., Chen, Y., Lin, T., Cheung, C. H. A., Wu, C., & Chiang, H. (2017) · The FASEB Journal · doi:10.1096/fj.201700199rr · Cited by 18
Self-citationRusso, A. J. (2015) · Biomarker Insights · doi:10.4137/bmi.s21946 · Cited by 15
Yuen, S. C., Zhu, H., & Leung, S.-W. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00209 · Cited by 16
Ubiquilin proteins regulate EGFR levels and activity in lung adenocarcinoma cells
Kurlawala, Z., Saurabh, K., Dunaway, R., Shah, P. P., Siskind, L. J., & Beverly, L. J. (2020) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29830 · Cited by 14
Wendt, S., Lin, A. J., Ebert, S. N., Brennan, D. J., Cai, W., Bai, Y., Kong, D. Y., Sorrentino, S., Groten, C. J., Lee, C., et al. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03433-3 · Cited by 13
Khaire, A. S., Wimberly, C. E., Semmes, E. C., Hurst, J. H., & Walsh, K. M. (2022) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2022.05.011 · Cited by 13
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Ali, M., Wani, S. U. D., Dey, T., Sridhar, S. B., & QADRIE, Z. L. (2023) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2023.101625 · Cited by 14
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Metadata
- Authors
- Wang, L., Chiang, H.-C., Wu, W., Liang, B., Xie, Z., Yao, X., Ma, W., Du, S., & Zhong, Y.
- Affiliations
- Tsinghua University (CN)
- Cold Spring Harbor Laboratory (US)
- Tsinghua Shenzhen International Graduate School (CN)
- Hainan Normal University (CN)
- JoeKai Biotech, LLC, Beijing 100084, China; and
- Division of Life Science and Health, Graduate School at Shenzhen, Tsinghua University, Shenzhen 518055, China;
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2012-09-27
- Volume
- 109
- Issue
- 41
- Pages
- 16743-16748
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3478595
- OpenAlex
- W2091619946
- Cited by
- 190
- References
- 45
- Citations by year
- 2026: 9 · 2025: 16 · 2024: 21 · 2023: 25 · 2022: 14 · 2021: 18 · 2020: 13 · 2019: 11 · 2018: 8 · 2017: 14 · 2016: 8 · 2015: 11 · 2014: 14 · 2013: 6 · 2012: 2
- FWCI
- 7.07
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- epidermal growth factor receptor, amyloid-beta, Alzheimer's disease, memory loss, amyloid-beta oligomers, synaptic plasticity, behavioral screening, synthetic compounds, drug repurposing, transgenic mouse model
- MeSH terms
- Erlotinib Hydrochloride, Gefitinib, Animals, Chlorocebus aethiops, Drosophila, Drug Evaluation, Preclinical, Humans, Memantine, Memory, Memory Disorders, Mice, Transgenic, Peptide Fragments, Quinazolines, Blotting, Western, Molecular Structure, Amyloid beta-Peptides, Maze Learning, COS Cells, Drosophila Proteins, Animals, Genetically Modified, Protein Kinase Inhibitors, Mice, ErbB Receptors
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