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Amyloid Precursor Protein Processing and Alzheimer's Disease
Open accessAbstract
Alzheimer's disease (AD), the leading cause of dementia worldwide, is characterized by the accumulation of the β-amyloid peptide (Aβ) within the brain along with hyperphosphorylated and cleaved forms of the microtubule-associated protein tau. Genetic, biochemical, and behavioral research suggest that physiologic generation of the neurotoxic Aβ peptide from sequential amyloid precursor protein (APP) proteolysis is the crucial step in the development of AD. APP is a single-pass transmembrane protein expressed at high levels in the brain and metabolized in a rapid and highly complex fashion by a series of sequential proteases, including the intramembranous γ-secretase complex, which also process other key regulatory molecules. Why Aβ accumulates in the brains of elderly individuals is unclear but could relate to changes in APP metabolism or Aβ elimination. Lessons learned from biochemical and genetic studies of APP processing will be crucial to the development of therapeutic targets to treat AD.
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“Mutations in APP are causal for Alzheimer's disease with abnormal processing of APP and the generation of toxic amyloid-β aggregates hallmarks of Alzheimer's pathology [89].”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [89]
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“Changes in APP processing and the formation of toxic amyloid-β aggregates are a key characteristic of Alzheimer's disease pathology [89].”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [89]
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“β-amyloid (Aβ) protein is the principal component of AD-associated amyloid plaques, and is produced by protease cleavage of the type I transmembrane amyloid precursor protein (APP) [16, 17].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [17]
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“In Alzheimer’s disease a series of cleavage events lead to several shorter soluble forms of amyloid precursor protein (sAPPα, sAPPβ), C-terminal fragments (AICD50, CTF 83, CTF 89, CTF 99, p3) and amyloid-beta peptides, which contribute to forming the characteristic plaques observed in the brains of diseased individuals.(10)”
From Putting humpty dumpty back together again: what does protein quantification mean in bottom-up proteomics? (2022) · cites this paper as [10]
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2 retracted
RETRACTED ARTICLE: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., & Tessier-Lavigne, M. (2009) · Nature · doi:10.1038/nature07767 · Cited by 992
RetractedRETRACTED: SIRT1 Suppresses β-Amyloid Production by Activating the α-Secretase Gene ADAM10
Dönmez, G., Wang, D., Cohen, D. E., & Guarente, L. (2010) · Cell · doi:10.1016/j.cell.2010.06.020 · Cited by 443
RetractedGlenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Blessed, G., Tomlinson, B. E., & Roth, M. (1968) · British Journal of Psychiatry · doi:10.1192/bjp.114.512.797 · Cited by 4,117
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
Forecasting the global burden of Alzheimer's disease
Brookmeyer, R., Johnson, E., Ziegler‐Graham, K., & Arrighi, H. M. (2007) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2007.04.381 · Cited by 3,370
Neurodegenerative Diseases Target Large-Scale Human Brain Networks
Seeley, W. W., Crawford, R. K., Zhou, J., Miller, B. L., & Greicius, M. D. (2009) · Neuron · doi:10.1016/j.neuron.2009.03.024 · Cited by 2,350
Chronic traumatic encephalopathy in athletes: Progressive tauopathy after repetitive head injury
McKee, A. C., Cantu, R. C., Nowinski, C. J., Hedley-Whyte, E. T., Gavett, B. E., Budson, A. E., Santini, V. E., Lee, H.-S., Kubilus, C. A., & Stern, R. A. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181a9d503 · Cited by 2,295
A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
De Strooper, B., Annaert, W., Cupers, P., Saftig, P., Craessaerts, K., Mumm, J. S., Schroeter, E. H., Schrijvers, V., Wolfe, M. S., Ray, W. J., et al. (1999) · Nature · doi:10.1038/19083 · Cited by 2,100
Research works printed but not linked: 4
- 10.1172/JCI20640 · DOI · Paper page
- Rohn TT, 2009, Int. J. Clin. Exp. Pathol., 2, 108
- Rohn TT, 2009, Int. J. Clin. Exp. Med., 2, 300
- 10.1042/0264-6021:3480359 · DOI · Paper page
Cited by
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DeTure, M. A., & Dickson, D. W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0333-5 · Cited by 3,329
“There are many reviews describing the generation of Aβ peptides [32], and these pathways remain viable therapeutic targets.”
BackgroundInflammation as a central mechanism in Alzheimer's disease
Kinney, J. W., Bemiller, S. M., Murtishaw, A. S., Leisgang, A. M., Salazar, A. M., & Lamb, B. T. (2018) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.06.014 · Cited by 2,253
“The function of APP is unknown but is believed to have a role in cell health and growth [5].”
BackgroundApolipoprotein E and Alzheimer disease: pathobiology and targeting strategies
Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425
Alzheimer’s disease: pathogenesis, diagnostics, and therapeutics
Tiwari, S., Atluri, V., Kaushik, A., Yndart, A., & Nair, M. (2019) · International Journal of Nanomedicine · doi:10.2147/ijn.s200490 · Cited by 1,308
Zhang, J., Zhang, Y., Wang, J., Xia, Y., Zhang, J., & Chen, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01911-3 · Cited by 1,138
“78,111,112 115 However, FAD mutations are not necessarily linked to an increase in A β 42 levels or an elevation of A β 42 /A β 40 ratio.”
BackgroundMolecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994
Essential versus accessory aspects of cell death: recommendations of the NCCD 2015
Galluzzi, L., Bravo-San Pedro, J. M., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Alnemri, E. S., Altucci, L., Andrews, D., Annicchiarico-Petruzzelli, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.137 · Cited by 1,002
At the interface of sensory and motor dysfunctions and Alzheimer’s disease.
Albers, M. W., Gilmore, G. C., Kaye, J., Murphy, C., Wingfield, A., Bennett, D. A., Boxer, A. L., Buchman, A. S., Cruickshanks, K. J., Devanand, D. P., et al. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2014.04.514 · Cited by 589
Role of gut-brain axis, gut microbial composition, and probiotic intervention in Alzheimer's disease
Kesika, P., Suganthy, N., Sivamaruthi, B. S., & Chaiyasut, C. (2021) · Life Sciences · doi:10.1016/j.lfs.2020.118627 · Cited by 479
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Olivares, D., K. Deshpande, V., Shi, Y., K. Lahiri, D., H. Greig, N., T. Rogers, J., & Huang, X. (2012) · Current Alzheimer Research · doi:10.2174/156720512801322564 · Cited by 407
Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331
GFAP as a Potential Biomarker for Alzheimer’s Disease: A Systematic Review and Meta-Analysis
Kim, K. Y., Shin, K. Y., & Chang, K.-A. (2023) · Cells · doi:10.3390/cells12091309 · Cited by 309
The Impact of Disease Comorbidities in Alzheimer’s Disease
Santiago, J. A., & Potashkin, J. A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.631770 · Cited by 259
Amyloidosis in Alzheimer’s Disease: Pathogeny, Etiology, and Related Therapeutic Directions
Ma, C., Hong, F., & Yang, S. (2022) · Molecules · doi:10.3390/molecules27041210 · Cited by 243
Drug repositioning: Progress and challenges in drug discovery for various diseases
Hua, Y., Dai, X., Xu, Y., Xing, G., Liu, H., Lu, T., Chen, Y., & Zhang, Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114239 · Cited by 232
Convergent genetic and expression data implicate immunity in Alzheimer's disease
International Genomics of Alzheimer's Disease Consortium (IGAP), Jones, L., Lambert, J., Wang, L., Choi, S., Harold, D., Vedernikov, A., Escott‐Price, V., Stone, T., Richards, A., et al. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2014.05.1757 · Cited by 199
MicroRNAs and neurodegeneration: role and impact
Abe, M., & Bonini, N. M. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.08.013 · Cited by 190
Deregulated Cdk5 activity is involved in inducing Alzheimer's disease
Shukla, V., Skuntz, S., & Pant, H. C. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.10.015 · Cited by 185
Alzheimer’s disease: Targeting the glutamatergic system
Conway, M. E. (2020) · Biogerontology · doi:10.1007/s10522-020-09860-4 · Cited by 180
Gene-environment interactions in Alzheimer's disease: A potential path to precision medicine
Eid, A., Mhatre, I., & Richardson, J. R. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.03.005 · Cited by 164
Hung, C. O. Y., & Livesey, F. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.095 · Cited by 159
Gourmaud, S., Shou, H., Irwin, D. J., Sansalone, K., Jacobs, L. M., Lucas, T. H., Marsh, E. D., Davis, K. A., Jensen, F. E., & Talos, D. M. (2020) · Brain · doi:10.1093/brain/awz381 · Cited by 155
Thambisetty, M., Metter, E. J., Yang, A., Dolan, H., Marano, C., Zonderman, A. B., Troncoso, J. C., Zhou, Y., Wong, D. F., Ferrucci, L., et al. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.284 · Cited by 155
Self-citationArber, C., Toombs, J., Lovejoy, C., Ryan, N. S., Paterson, R. W., Willumsen, N., Gkanatsiou, E., Portelius, E., Blennow, K., Heslegrave, A., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-019-0410-8 · Cited by 148
The aged rhesus macaque manifests Braak stage III/IV Alzheimer's‐like pathology
Paspalas, C. D., Carlyle, B. C., Leslie, S., Preuss, T. M., Crimins, J. L., Huttner, A. J., van Dyck, C. H., Rosene, D. L., Nairn, A. C., & Arnsten, A. F. T. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2017.11.005 · Cited by 140
Yuan, J., Venkatraman, S., Zheng, Y., McKeever, B. M., Dillard, L. W., & Singh, S. B. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301659n · Cited by 135
Pujadas, L., Rossi, D., Andrés, R., Teixeira, C. M., Serra-Vidal, B., Parcerisas, A., Maldonado, R., Giralt, E., Carulla, N., & Soriano, E. (2014) · Nature Communications · doi:10.1038/ncomms4443 · Cited by 129
Retinal amyloid peptides and complement factor H in transgenic models of Alzheimer's disease
Alexandrov, P. N., Pogue, A., Bhattacharjee, S., & Lukiw, W. J. (2011) · Neuroreport · doi:10.1097/wnr.0b013e3283497334 · Cited by 128
Alasmari, F., Alshammari, M. A., Alasmari, A. F., Alanazi, W. A., & Alhazzani, K. (2018) · BioMed Research International · doi:10.1155/2018/3087475 · Cited by 125
Alzheimer's disease failed clinical trials
Asher, S., & Priefer, R. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120861 · Cited by 124
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Blacher, E., Dadali, T., Bespalko, A., Haupenthal, V. J., Grimm, M. O. W., Hartmann, T., Lund, F. E., Stein, R., & Levy, A. (2015) · Annals of Neurology · doi:10.1002/ana.24425 · Cited by 117
Gasparotto, J., Girardi, C. S., Somensi, N., Ribeiro, C. T., Moreira, J. C. F., Michels, M., Sonai, B., Rocha, M., Steckert, A. V., Barichello, T., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.786756 · Cited by 120
Young, M. L., & Franklin, J. L. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103409 · Cited by 120
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Bulgart, H. R., Neczypor, E. W., Wold, L. E., & Mackos, A. R. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00378-4 · Cited by 116
Poudel, P., & Park, S. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14040835 · Cited by 124
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Monterey, M. D., Wei, H., Wu, X., & Wu, J. Q. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.619626 · Cited by 117
Polymicrobial Infections In Brain Tissue From Alzheimer’s Disease Patients
Pisa, D., Alonso, R., Fernández-Fernández, A. M., Rábano, A., & Carrasco, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-05903-y · Cited by 114
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Lionaki, E., Ploumi, C., & Tavernarakis, N. (2022) · Cells · doi:10.3390/cells11020214 · Cited by 110
Canonical and non-canonical Reelin signaling
Bock, H. H., & May, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00166 · Cited by 107
Fang, F., Yu, Q., Arancio, O., Chen, D., Gore, S. S., Yan, S. S., & Yan, S. F. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy017 · Cited by 103
Microglia and Astrocytes in Alzheimer’s Disease: Significance and Summary of Recent Advances
Deng, Q., Wu, C., Parker, E., Liu, T. C.-Y., Duan, R., & Yang, L. (2023) · Aging and disease · doi:10.14336/ad.2023.0907 · Cited by 102
Amyloid-β precursor protein promotes cell proliferation and motility of advanced breast cancer
Lim, S., Yoo, B. K., Kim, H.-S., Gilmore, H. L., Lee, Y., Lee, H.-P., Kim, S.-J., Letterio, J., & Lee, H.-G. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-928 · Cited by 100
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Ferrari, G., Avila, M., Medina, M., Perez-Palma, E., Bustos, B., & Alarcon, M. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527312666131223113900 · Cited by 95
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Zipfel, P., Rochais, C., Baranger, K., Rivera, S., & Dallemagne, P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00352 · Cited by 94
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Tüshaus, J., Müller, S. A., Kataka, E. S., Zaucha, J., Sebastian Monasor, L., Su, M., Güner, G., Jocher, G., Tahirovic, S., Frishman, D., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020105693 · Cited by 88
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Lao, K., Ji, N., Zhang, X., Qiao, W., Tang, Z., & Gou, X. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2018.1474361 · Cited by 86
Plubell, D. L., Käll, L., Webb-Robertson, B.-J., Bramer, L. M., Ives, A., Kelleher, N. L., Smith, L. M., Montine, T. J., Wu, C. C., & MacCoss, M. J. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00894 · Cited by 85
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Yang, C., Cai, C.-Z., Song, J.-X., Tan, J.-Q., Durairajan, S. S. K., Iyaswamy, A., Wu, M.-Y., Chen, L.-L., Yue, Z., Li, M., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1379633 · Cited by 83
Ullah, R., Park, T. J., Huang, X., & Kim, M. O. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101451 · Cited by 78
Shim, H. S., Horner, J. W., Wu, C.-J., Li, J., Lan, Z. D., Jiang, S., Xu, X., Hsu, W.-H., Zal, T., Flores, I. I., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00146-z · Cited by 73
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Aghaizu, N. D., Jin, H., & Whiting, P. J. (2020) · Brain Sciences · doi:10.3390/brainsci10120902 · Cited by 70
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Martiskainen, H., Herukka, S., Stančáková, A., Paananen, J., Soininen, H., Kuusisto, J., Laakso, M., & Hiltunen, M. (2017) · Annals of Neurology · doi:10.1002/ana.24969 · Cited by 64
Singh, A., Allen, D., Fracassi, A., Tumurbaatar, B., Natarajan, C., Scaduto, P., Woltjer, R., Kayed, R., Limon, A., Krishnan, B., et al. (2020) · Journal of Alzheimer's Disease · doi:10.3233/jad-200716 · Cited by 56
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Hoxha, E., Lippiello, P., Zurlo, F., Balbo, I., Santamaria, R., Tempia, F., & Miniaci, M. C. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00396 · Cited by 58
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Kelly, Á. M. (2018) · Brain Plasticity · doi:10.3233/bpl-180074 · Cited by 55
Wilson, E. N., Do Carmo, S., Iulita, M. F., Hall, H., Ducatenzeiler, A., Marks, A. R., Allard, S., Jia, D. T., Windheim, J., & Cuello, A. C. (2017) · Translational Psychiatry · doi:10.1038/tp.2017.169 · Cited by 56
Wu, Y., Chen, Q., Wen, B., Wu, N., He, B., & Chen, J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.640758 · Cited by 54
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Sosa, L. J., Bergman, J., Estrada-Bernal, A., Glorioso, T. J., Kittelson, J. M., & Pfenninger, K. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064521 · Cited by 53
Modulation of the Aβ peptide aggregation pathway by KP1019 limits Aβ-associated neurotoxicity
Jones, M. R., Mu, C., Wang, M. C. P., Webb, M. I., Walsby, C. J., & Storr, T. (2015) · Metallomics · doi:10.1039/c4mt00252k · Cited by 50
Kochman, U., Sitka, H., Kuźniar, J., Czaja, M., Kozubek, P., Beszłej, J. A., & Leszek, J. (2026) · Molecular Neurobiology · doi:10.1007/s12035-025-05417-z · Cited by 60
Beck, T. N., Nicolas, E., Kopp, M. C., & Golemis, E. A. (2014) · Oncoscience · doi:10.18632/oncoscience.64 · Cited by 50
Xu, L., Yao, S., Ding, Y. E., Xie, M., Feng, D., Sha, P., Tan, L., Bei, F., & Yao, Y. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05661-2 · Cited by 48
Nadiga, A. P. R., Suman, & Krishna, K. L. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176332 · Cited by 48
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Padhi, D., & Govindaraju, T. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00335 · Cited by 47
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Chu, Q., Diedrich, J. K., Vaughan, J. M., Donaldson, C. J., Nunn, M. F., Lee, K.-F., & Saghatelian, A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b03463 · Cited by 46
Monitoring phagocytic uptake of amyloid β into glial cell lysosomes in real time
Prakash, P., Jethava, K. P., Korte, N., Izquierdo, P., Favuzzi, E., Rose, I. V. L., Guttenplan, K. A., Manchanda, P., Dutta, S., Rochet, J.-C., et al. (2021) · Chemical Science · doi:10.1039/d1sc03486c · Cited by 45
The function of SUMOylation and its crucial roles in the development of neurological diseases
Chen, X., Zhang, Y., Wang, Q., Qin, Y., Yang, X., Xing, Z., Shen, Y., Wu, H., & Qi, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202002702r · Cited by 39
The dense-core plaques of Alzheimer’s disease are granulomas
Lemke, G., & Huang, Y. (2022) · Journal of Experimental Medicine · doi:10.1084/jem.20212477 · Cited by 37
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Kang, Y. J., Diep, Y. N., Tran, M., & Cho, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249591 · Cited by 36
Ma, G., Zhang, D.-F., Zou, Q.-C., Xie, X., Xu, L., Feng, X.-L., Li, X., Han, J.-B., Yu, D., Deng, Z.-H., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00458-3 · Cited by 30
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Mukhin, V. N., Pavlov, K. I., & Klimenko, V. M. (2017) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-017-0427-x · Cited by 27
Senescence in aging and disorders of the central nervous system
Swenson, B. L., Meyer, C. F., Bussian, T. J., & Baker, D. J. (2019) · Translational Medicine of Aging · doi:10.1016/j.tma.2019.01.002 · Cited by 24
Zhao, M., Ma, G., Yan, X., Li, X., Wang, E., Xu, X.-X., Zhao, J.-B., Ma, X., & Zeng, J. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02428-5 · Cited by 21
Li, X., Tang, X., Zeng, J., Duan, L., Hou, Z., Li, L., Guo, Y., Chai, C., Liu, J., Wang, Y., et al. (2026) · Cell · doi:10.1016/j.cell.2025.12.020 · Cited by 21
Ramos de Matos, M., Ferreira, C., Herukka, S.-K., Soininen, H., Janeiro, A., Santana, I., Baldeiras, I., Almeida, M. R., Lleó, A., Dols-Icardo, O., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-180512 · Cited by 18
Synaptic Organizers in Alzheimer’s Disease: A Classification Based on Amyloid-β Sensitivity
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Metadata
- Authors
- O'Brien, R. J., & Wong, P. C.
- Affiliations
- Department of Neurology, Johns Hopkins Bayview Medical Center
- Johns Hopkins University (US)
- ORCID
- Wong, Philip C.
- Venue
- Annual Review of Neuroscience
- Publisher
- Annual Reviews
- Published
- 2011-07-21
- Volume
- 34
- Issue
- 1
- Pages
- 185-204
- ISSN
- 0147-006X (ISSN-L)
- 1545-4126
- PMC
- PMC3174086
- OpenAlex
- W2129085204
- Cited by
- 2,061
- References
- 158
- Citations by year
- 2026: 118 · 2025: 182 · 2024: 227 · 2023: 194 · 2022: 197 · 2021: 225 · 2020: 185 · 2019: 143 · 2018: 144 · 2017: 105 · 2016: 91 · 2015: 76 · 2014: 70 · 2013: 63 · 2012: 33
- FWCI
- 5.83
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (P50AG005146)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid precursor protein, APP processing, amyloid-beta, gamma-secretase, intramembrane proteolysis, tau hyperphosphorylation, amyloid accumulation, APP metabolism, therapeutic target
- MeSH terms
- Alzheimer Disease, Animals, Brain, Humans, Models, Biological, Amyloid beta-Protein Precursor, Amyloidogenic Proteins
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