Genetics of β-Amyloid Precursor Protein in Alzheimer's Disease
Open accessAbstract
Alzheimer's disease (AD) is characterized neuropathologically by neuronal cell loss, extracellular neuritic plaques composed of b-amyloid (Ab), and intracellular neurofibrillary tangles composed of hyperphosphorylated tau protein.Ab is generated by proteolytic processing of the b-amyloid precursor protein (APP).Most individuals with Down syndrome (DS) have three copies of APP, leading to elevated APP expression, increased Ab deposition, and characteristic AD neuropathology.Sequencing of APP in familial early-onset AD identified missense mutations that cause AD, while a recently discovered coding variant, APP A673T, reduces the risk for AD.Cellular and animal studies show that risk-associated mutations increase total Ab levels, Ab42 levels, or Ab fibrillogenesis, while protective alleles reduce Ab levels.Together, these studies provide compelling evidence for the Ab hypothesis and suggest that therapeutics that reduces Ab levels or Ab fibrillogenesis should lower the risk for or prevent AD.
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
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?
Mutations in the Aβ domain itself alter the hydrophobicity and downstream aggregation propensity of Aβ peptides, leading to an increase in plaque load.
“Mutations in the Aβ domain itself alter the hydrophobicity and downstream aggregation propensity of Aβ peptides, leading to an increase in plaque load [36].”
From Genetic architecture of Alzheimer's disease (2020) · cites this paper as [36]
Gene mutations that directly enhance Aβ aggregation underlie rare familial forms of Alzheimer's disease.
“In addition, gene mutations that directly enhance Aβ aggregation underlie rare familial forms of the disease [4, 5].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [4]
Aβ and tau play a pathogenic role in Alzheimer's disease.
“A wealth of evidence suggests these proteins play a pathogenic role in disease.”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [4]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659 · see citing works
Self-citationThe 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 · see citing works
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210 · see citing works
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516 · see citing works
A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline
Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., et al. (2012) · Nature · doi:10.1038/nature11283 · Cited by 1,738 · see citing works
Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus
Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611 · see citing works
Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513 · see citing works
The DNA sequence of human chromosome 21
Hattori, M., Fujiyama, A., Taylor, T. D., Watanabe, H., Yada, T., Park, H.-S., Toyoda, A., Ishii, K., Totoki, Y., Choi, D., et al. (2000) · Nature · doi:10.1038/35012518 · Cited by 1,475 · see citing works
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471 · see citing works
Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type
Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,380 · see citing works
Amyloid, the presenilins and Alzheimer’s disease
Hardy, J. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)01030-2 · Cited by 1,370 · see citing works
Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,333 · see citing works
Rovelet‐Lecrux, A., Hannequin, D., Raux, G., Meur, N. L., Laquerrière, A., Vital, A., Dumanchin‐Njock, C., Feuillette, S., Brice, A., Vercelletto, M., et al. (2005) · Nature Genetics · doi:10.1038/ng1718 · Cited by 1,249 · see citing works
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209 · see citing works
Occurrence of neuropathological changes and dementia of Alzheimer’s disease in Down’s syndrome
Wisniewski, K. E., Wisniewski, H. M., & Wen, G. Y. (1985) · Annals of Neurology · doi:10.1002/ana.410170310 · Cited by 1,159 · see citing works
A copy number variation map of the human genome
Zarrei, M., MacDonald, J. R., Merico, D., & Scherer, S. W. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3871 · Cited by 921 · see citing works
Hendriks, L., van Duijn, C. M., Cras, P. P., Cruts, M., Hul, W. V., van Harskamp, F., Warren, A., McInnis, M. G., Antonarakis, S. E., Martin, J., et al. (1992) · Nature Genetics · doi:10.1038/ng0692-218 · Cited by 735 · see citing works
The genetic epidemiology of neurodegenerative disease
Bertram, L. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24761 · Cited by 680 · see citing works
Amyloid A4 Protein and Its Precursor in Down's Syndrome and Alzheimer's Disease
Rumble, B. A., Retallack, R. W., Hilbich, C., Simms, G., Multhaup, G., Martins, R. N., Hockey, A., Montgomery, P., Beyreuther, K. T., & Masters, C. L. (1989) · New England Journal of Medicine · doi:10.1056/nejm198906013202203 · Cited by 652 · see citing works
Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells.
Busciglio, J., Gabuzda, D. H., Matsudaira, P., & Yankner, B. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.2092 · Cited by 569 · see citing works
Ellis, R. J., Olichney, J. M., Thal, L. J., Mirra, S. S., Morris, J. C., Beekly, D., & Heyman, A. (1996) · Neurology · doi:10.1212/wnl.46.6.1592 · Cited by 561 · see citing works
Ohno, M., Sametsky, E. A., Younkin, L. H., Oakley, H., Younkin, S. G., Citron, M., Vassar, R., & Disterhoft, J. F. (2004) · Neuron · doi:10.1016/s0896-6273(03)00810-9 · Cited by 549 · see citing works
Take five—BACE and the γ‐secretase quartet conduct Alzheimer's amyloid β‐peptide generation
Haass, C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600061 · Cited by 547 · see citing works
Salehi, A., Delcroix, J.-D., Belichenko, P. V., Zhan, K., Wu, C., Valletta, J. S., Takimoto-Kimura, R., Kleschevnikov, A. M., Sambamurti, K., Chung, P. P., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.05.022 · Cited by 543 · see citing works
Mann, D. M. A., & Esiri, M. M. (1989) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(89)90019-1 · Cited by 471 · see citing works
Copy number variants, diseases and gene expression
Henrichsen, C. N., Chaignat, E., & Reymond, A. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp011 · Cited by 432 · see citing works
Molecular mapping of alzheimer‐type dementia in Down's syndrome
Prasher, V. P., Farrer, M. J., Kessling, A. M., Fisher, E. M. C., West, R. J., Barber, P. C., & Butler, A. C. (1998) · Annals of Neurology · doi:10.1002/ana.410430316 · Cited by 414 · see citing works
Sleegers, K., Brouwers, N., Gijselinck, I., Theuns, J., Goossens, D., Wauters, J., Del‐Favero, J., Cruts, M., van Duijn, C. M., & Broeckhoven, C. V. (2006) · Brain · doi:10.1093/brain/awl203 · Cited by 406 · see citing works
Citron, M., Vigo-Pelfrey, C., Teplow, D. B., Miller, C., Schenk, D., Johnston, J., Winblad, B., Venizelos, N., Lannfelt, L., & Selkoe, D. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.11993 · Cited by 366 · see citing works
Burger, P. C., & Vogel, F. S. (1973) · PubMed · Cited by 342 · see citing works
Cerebral amyloid angiopathy and cognitive function: The HAAS autopsy study
Pfeifer, L. A., White, L. R., Ross, G. W., Petrovitch, H., & Launer, L. J. (2002) · Neurology · doi:10.1212/wnl.58.11.1629 · Cited by 338 · see citing works
Presence of soluble amyloid β–peptide precedes amyloid plaque formation in Down's syndrome
Teller, J. K., Russo, C., DeBusk, L. M., Angelini, G., Zaccheo, D., Dagna-Bricarelli, F., Scartezzini, P., Bertolini, S., Mann, D. M. A., Tabaton, M., et al. (1996) · Nature Medicine · doi:10.1038/nm0196-93 · Cited by 326 · see citing works
Causative and susceptibility genes for Alzheimer’s disease: a review
Rocchi, A., Pellegrini, S., Siciliano, G., & Murri, L. (2003) · Brain Research Bulletin · doi:10.1016/s0361-9230(03)00067-4 · Cited by 319 · see citing works
Haass, C., Hung, A. Y., Selkoe, D. J., & Teplow, D. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32503-6 · Cited by 315 · see citing works
van Duinen, S. G., Castaño, E. M., Prelli, F., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.16.5991 · Cited by 309 · see citing works
Molecular genetic analysis of Down syndrome
Patterson, D. (2009) · Human Genetics · doi:10.1007/s00439-009-0696-8 · Cited by 278 · see citing works
Wiltfang, J., Esselmann, H., Bibl, M., Av, S., Otto, M., Paul, S., Schmidt, B., Klafki, H., Maler, M., Dyrks, T., et al. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00818.x · Cited by 268 · see citing works
Atypical aging in down syndrome
Zigman, W. B. (2013) · Developmental Disabilities Research Reviews · doi:10.1002/ddrr.1128 · Cited by 262 · see citing works
Critical role of the D21S55 region on chromosome 21 in the pathogenesis of Down syndrome.
Rahmani, Z., Blouin, J., Créau, N., Watkins, P. C., Mattéi, J. F., Poissonnier, M., Prieur, M., Chettouh, Z., Nicole, A., & Aurias, A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5958 · Cited by 259 · see citing works
Genomic organization of the human amyloid beta-protein precursor gene
Yoshikai, S.-I., Sasaki, H., Doh‐ura, K., Furuya, H., & Sakaki, Y. (1990) · Gene · doi:10.1016/0378-1119(90)90310-n · Cited by 259 · see citing works
Wısnıewskı, T., Ghiso, J. A., & Frangione, B. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91706-i · Cited by 247 · see citing works
Hof, P. R. (1995) · Archives of Neurology · doi:10.1001/archneur.1995.00540280065020 · Cited by 234 · see citing works
Ling, Y., Morgan, K., & Kalsheker, N. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00133-x · Cited by 224 · see citing works
Maloney, J. A., Bainbridge, T. W., Gustafson, A. E., Zhang, S., Kyauk, R. V., Steiner, P., van der Brug, M., Liu, Y., Ernst, J. A., Watts, R. J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589069 · Cited by 199 · see citing works
Tamaoka, A., Odaka, A., Ishibashi, Y., Usami, M., Sahara, N., Suzuki, N., Nukina, N., Mizusawa, H., Shoji, S., & Kanazawa, I. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)30050-8 · Cited by 165 · see citing works
Kaminsky, Y. G., Marlatt, M. W., Smith, M. A., & Kosenko, E. A. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.09.005 · Cited by 165 · see citing works
Oyama, F., Cairns, N. J., Shimada, H., Oyama, R., Titani, K., & Ihara, Y. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62031062.x · Cited by 129 · see citing works
Hereditary Cerebral Hemorrhage With Amyloidosis Associated With the E693K Mutation of APP
Bugiani, O., Giaccone, G., Rossi, G., Mangieri, M., Capobianco, R., Morbin, M., Mazzoleni, G., Cupidi, C., Marcon, G., Gıovagnolı, A. R., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.178 · Cited by 115 · see citing works
Dense-Core Senile Plaques in the Flemish Variant of Alzheimer's Disease Are Vasocentric
Kumar-Singh, S., Cras, P., Wang, R., Kros, J. M., van Swieten, J., Lübke, U., Ceuterick, C., Serneels, S., Vennekens, K., Timmermans, J.-P., et al. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64207-1 · Cited by 114 · see citing works
APP Gene Family Alternative Splicing Generates Functionally Related Isoformsa
Sandbrink, R., Masters, C. L., & Beyreuther, K. T. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34433.x · Cited by 108 · see citing works
Genomic organization of the human-amyloid beta-protein precursor gene
Yoshikai, S.-I., Sasaki, H., Doh‐ura, K., Furuya, H., & Sakaki, Y. (1991) · Gene · doi:10.1016/0378-1119(91)90093-q · Cited by 105 · see citing works
A novel AβPP mutation exclusively associated with cerebral amyloid angiopathy
Obici, L. P., Demarchi, A., de Rosa, G., Bellotti, V., Marciano, S., Donadei, S., Arbustini, E., Palladini, G. O., Diegoli, M., Genovese, E., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20571 · Cited by 97 · see citing works
Kasuga, K., Shimohata, T., Nishimura, A., Shiga, A., Mizuguchi, T., Tokunaga, J., Ohno, T., Miyashita, A., Kuwano, R., Matsumoto, N., et al. (2009) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2008.161703 · Cited by 97 · see citing works
Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic ResonancePreprint
Tycko, R. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024083 · Cited by 86 · see citing works
β-Amyloid Prions and the Pathobiology of Alzheimer’s DiseasePreprint
Watts, J. C., & Prusiner, S. B. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a023507 · Cited by 83 · see citing works
Wolfe, M. S., & Guénette, S. Y. (2007) · Journal of Cell Science · doi:10.1242/jcs.03481 · Cited by 77 · see citing works
A family with Alzheimer disease and strokes associated with A713T mutation of the APP gene
Rossi, G., Giaccone, G., Maletta, R., Morbin, M., Capobianco, R., Mangieri, M., Gıovagnolı, A. R., Bizzi, A., Tomaino, C., Perri, M., et al. (2004) · Neurology · doi:10.1212/01.wnl.0000137048.80666.86 · Cited by 73 · see citing works
Neuropathology of the recessive A673V APP mutation: Alzheimer disease with distinctive features
Giaccone, G., Morbin, M., Moda, F., Botta, M., Mazzoleni, G., Uggetti, A., Catania, M., Moro, M. L., Redaelli, V., Spagnoli, A., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0747-1 · Cited by 73 · see citing works
Chen, H., Chang, C., Misra, R., Peters, H. A., Grijalva, N. S., Opitz, J. M., & Lowry, R. B. (1980) · American Journal of Medical Genetics · doi:10.1002/ajmg.1320070203 · Cited by 73 · see citing works
Amyloid precursor protein (APP) A673T mutation in the elderly Finnish population
Kero, M., Paetau, A., Polvikoski, T., Tanskanen, M., Sulkava, R., Jansson, L., Myllykangas, L., & Tienari, P. J. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.09.017 · Cited by 72 · see citing works
INTRAFAMILIAL DIVERSITY OF PHENOTYPE ASSOCIATED WITH APP DUPLICATION
Guyant-Marechal, I., Berger, É., Laquerrière, A., Rovelet‐Lecrux, A., Viennet, G., Frébourg, T., Rumbach, L., Campion, D., & Hannequin, D. (2008) · Neurology · doi:10.1212/01.wnl.0000339400.64213.56 · Cited by 64 · see citing works
Castellani, R. J., Smith, M. A., Perry, G., & Friedland, R. P. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.12.019 · Cited by 57 · see citing works
Down syndrome: Toward a molecular definition of the phenotype
Korenberg, J. R., Kawashima, H., Pulst, S. M., Allen, L., Magenis, E., & Epstein, C. J. (2005) · American Journal of Medical Genetics · doi:10.1002/ajmg.1320370719 · Cited by 40 · see citing works
Liu, Y.-W., He, Y.-H., Zhang, Y.-X., Cai, W.-W., Yang, L.-Q., Xu, L.-Y., & Kong, Q.-P. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.09.023 · Cited by 39 · see citing works
Good gene, bad gene: New APP variant may be both
Fede, G. D., Catania, M., Morbin, M., Giaccone, G., Moro, M. L., Ghidoni, R., Colombo, L., Messa, M., Cagnotto, A., Romeo, M., et al. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.06.004 · Cited by 39 · see citing works
Sadowski, M. J., Wı́sniewski, H. M., Tarnawski, M. J., Kozlowski, P. B., Lach, B., & Węgiel, J. (1999) · Acta Neuropathologica · doi:10.1007/s004010050968 · Cited by 38 · see citing works
Thonberg, H., Fallström, M., Björkström, J., Schoumans, J., Nennesmo, I., & Graff, C. (2011) · BMC Research Notes · doi:10.1186/1756-0500-4-476 · Cited by 33 · see citing works
Studies on the first described Alzheimer's disease amyloid β mutant, the Dutch variant
Levy, E., Prelli, F., & Frangione, B. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9s337 · Cited by 24 · see citing works
Younkin, S. G. (1994) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.174.217 · Cited by 20 · see citing works
Structural and Chemical Biology of Presenilin ComplexesPreprint
Johnson, D. S., Li, Y., Pettersson, M., & George‐Hyslop, P. S. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024067 · Cited by 18 · see citing works
Volume 179, Number 3, September 30, 1991
(1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81370-1 · Cited by 12 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Ã Prusiner SB. 2016. Ab prions and pathobiology of Alz- heimer's disease. Cold Spring Harb Perspect Med doi: 10.1101/cshperspect.a030676. · DOI
Cited by
Sorted by citations
Alzheimer Disease: An Update on Pathobiology and Treatment Strategies
Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204 · see citing works
Comprehensive Review on Alzheimer’s Disease: Causes and Treatment
Breijyeh, Z., & Karaman, R. (2020) · Molecules · doi:10.3390/molecules25245789 · Cited by 2,789 · see citing works
Pathology of Neurodegenerative Diseases
Dugger, B. N., & Dickson, D. W. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028035 · Cited by 1,665 · see citing works
Alzheimer’s disease: insights into pathology, molecular mechanisms, and therapy
Zheng, Q., & Wang, X. (2024) · Protein & Cell · doi:10.1093/procel/pwae026 · Cited by 454 · see citing works
Pathogenesis, diagnostics, and therapeutics for Alzheimer's disease: Breaking the memory barrier
Tryphena, K. P., Shukla, R., Khatri, D. K., & Vora, L. K. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102481 · Cited by 418 · see citing works
Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Scheres, S. H. W., Falcon, B., & Goedert, M. (2023) · Nature · doi:10.1038/s41586-023-06437-2 · Cited by 293 · see citing works
Relationship Between Amyloid-β Deposition and Blood–Brain Barrier Dysfunction in Alzheimer’s Disease
Wang, D., Chen, F., Han, Z., Yin, Z., Ge, X., & Lei, P. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.695479 · Cited by 201 · see citing works
Emerging role of gut microbiota dysbiosis in neuroinflammation and neurodegeneration
Solanki, R., Karande, A. A., & Ranganathan, P. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1149618 · Cited by 192 · see citing works
Alzheimer’s Disease: Exploring the Landscape of Cognitive Decline
Tenchov, R., Sasso, J. M., & Zhou, Q. A. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00339 · Cited by 170 · see citing works
Translating genetic risk of Alzheimer’s disease into mechanistic insight and drug targets
Sierksma, A. S. R., Escott‐Price, V., & Strooper, B. D. (2020) · Science · doi:10.1126/science.abb8575 · Cited by 149 · see citing works
The genetic landscape of Alzheimer disease
Carmona, S., Hardy, J., & Guerreiro, R. J. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-64076-5.00026-0 · Cited by 133 · see citing works
Genetic architecture of Alzheimer's disease
Neuner, S. M., TCW, J., & Goate, A. M. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104976 · Cited by 126 · see citing works
“Mutations in the Aβ domain itself alter the hydrophobicity and downstream aggregation propensity of Aβ peptides, leading to an increase in plaque load (TCW and Goate, 2017).”
BackgroundSelf-citationAlzheimer's disease failed clinical trials
Asher, S., & Priefer, R. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120861 · Cited by 124 · see citing works
Microglia in Alzheimer’s Disease in the Context of Tau Pathology
Perea, J. R., Bolós, M., & Ávila, J. (2020) · Biomolecules · doi:10.3390/biom10101439 · Cited by 127 · see citing works
NLRP3 inflammasome signalling in Alzheimer's disease
McManus, R. M., & Latz, E. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2024.109941 · Cited by 125 · see citing works
Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau
Rayaprolu, S., Higginbotham, L., Bagchi, P., Watson, C. M., Zhang, T., Levey, A. I., Rangaraju, S., & Seyfried, N. T. (2021) · Neuropsychopharmacology · doi:10.1038/s41386-020-00840-3 · Cited by 118 · see citing works
Habtemariam, S. (2019) · Molecules · doi:10.3390/molecules24081519 · Cited by 107 · see citing works
TREM2 in Alzheimer’s Disease: Microglial Survival and Energy Metabolism
Zheng, H., Cheng, B., Li, Y., Li, X., Chen, X., & Zhang, Y.-W. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00395 · Cited by 94 · see citing works
Brody, D. L., Jiang, H., Wildburger, N. C., & Esparza, T. J. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0293-3 · Cited by 84 · see citing works
Synaptic dysfunction in early phases of Alzheimer's Disease
Pelucchi, S., Gardoni, F., Luca, M. D., & Marcello, E. E. (2022) · Handbook of clinical neurology · doi:10.1016/b978-0-12-819410-2.00022-9 · Cited by 88 · see citing works
Genomics and Functional Genomics of Alzheimer's Disease
Kamboh, M. I. (2022) · Neurotherapeutics · doi:10.1007/s13311-021-01152-0 · Cited by 73 · see citing works
Exosomal miRNAs as Potential Diagnostic Biomarkers in Alzheimer’s Disease
Manna, I., Benedittis, S. D., Quattrone, A., Maisano, D., Iaccino, E., & Quattrone, A. (2020) · Pharmaceuticals · doi:10.3390/ph13090243 · Cited by 73 · see citing works
Essayan-Perez, S., & Südhof, T. C. (2023) · Neuron · doi:10.1016/j.neuron.2023.07.005 · Cited by 65 · see citing works
Carey, A. M., & Fossati, S. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12871 · Cited by 59 · see citing works
Zinc in Cognitive Impairment and Aging
Sun, R., Wang, J., Feng, J., & Cao, B. (2022) · Biomolecules · doi:10.3390/biom12071000 · Cited by 61 · see citing works
Lumsden, A. L., Rogers, J. T., Majd, S., Newman, M., Sutherland, G. T., Verdile, G., & Lardelli, M. T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00533 · Cited by 58 · see citing works
Zebrafish and Medaka: Important Animal Models for Human Neurodegenerative Diseases
Wang, J., & Cao, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910766 · Cited by 61 · see citing works
Azargoonjahromi, A., & Abutalebian, F. (2024) · Nutrition & Metabolism · doi:10.1186/s12986-024-00792-1 · Cited by 62 · see citing works
Mechanisms of neurodegeneration — Insights from familial Alzheimer’s disease
Chávez‐Gutiérrez, L., & Szaruga, M. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.03.005 · Cited by 54 · see citing works
The Role of Epigenetics in Neuroinflammatory-Driven Diseases
Giallongo, S., Longhitano, L., Denaro, S., D’Aprile, S., Torrisi, F., Spina, E. L., Giallongo, C., Mannino, G., Furno, D. L., Zappalà, A., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315218 · Cited by 60 · see citing works
Chang, J. L., Hinrich, A. J., Roman, B., Norrbom, M., Rigo, F., Marr, R. A., Norstrom, E. M., & Hastings, M. L. (2018) · Molecular Therapy · doi:10.1016/j.ymthe.2018.02.029 · Cited by 52 · see citing works
Anand, P., Zhang, Y., Patil, S., & Kaur, K. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02528 · Cited by 51 · see citing works
Hallmarks of neurodegenerative disease: A systems pharmacology perspective
Bloomingdale, P., Karelina, T., Ramakrishnan, V., Bakshi, S., Véronneau‐Veilleux, F., Moye, M., Sekiguchi, K., Meno‐Tetang, G. M. L., Mohan, A., Maithreye, R., et al. (2022) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.12852 · Cited by 50 · see citing works
Human iPSC-Based Modeling of Central Nerve System Disorders for Drug Discovery
Lu, Q., & Julia, T. C. W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031203 · Cited by 48 · see citing works
Self-citationGoto, T., Kuramoto, E., Dhar, A., Wang, R. P., Seki, H., Iwai, H., Yamanaka, A., Matsumoto, S., Hara, H., Michikawa, M., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200257 · Cited by 46 · see citing works
Current progress of cerebral organoids for modeling Alzheimer's disease origins and mechanisms
Sreenivasamurthy, S., Laul, M., Zhao, N., Kim, T., & Zhu, D. (2022) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10378 · Cited by 46 · see citing works
AMPK: Potential Therapeutic Target for Alzheimer's Disease
Yang, L., Jiang, Y., Shi, L., Zhong, D., Li, Y., Li, J., & Jin, R. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190819142746 · Cited by 46 · see citing works
Death-associated protein kinase 1 as a therapeutic target for Alzheimer's disease
Zhang, T., Kim, B. M., & Lee, T. H. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-023-00395-5 · Cited by 47 · see citing works
Mitochondrial dysfunction in neurodegenerative diseases: A focus on iPSC-derived neuronal models
Trombetta-Lima, M., Sabogal-Guáqueta, A. M., & Dolga, A. M. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102362 · Cited by 41 · see citing works
Phospholipid scramblase 1: a protein with multiple functions via multiple molecular interactors
Col, J. D., Lamberti, M. J., Nigro, A., Casolaro, V., Fratta, E., Steffan, A., & Montico, B. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00895-3 · Cited by 36 · see citing works
Intricate relationship between obstructive sleep apnea and dementia in older adults
Ercolano, E., Bencivenga, L., Palaia, M. E., Carbone, G., Scognamiglio, F., Rengo, G., & Femminella, G. D. (2023) · GeroScience · doi:10.1007/s11357-023-00958-4 · Cited by 39 · see citing works
Ding, X.-W., Li, R., Geetha, T., Tao, Y.-X., & Babu, J. R. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165858 · Cited by 36 · see citing works
Lim, J. L., Lin, C., Huang, C., & Chang, L. (2023) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2023.113676 · Cited by 34 · see citing works
Alzheimer’s in a dish – induced pluripotent stem cell-based disease modeling
de Leeuw, S., & Tackenberg, C. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0161-0 · Cited by 31 · see citing works
Amyloid Precursor Protein: A Regulatory Hub in Alzheimer's Disease
Chen, J., Chen, J.-S., Li, S., Zhang, F., Deng, J., Zeng, L., & Tan, J. (2023) · Aging and Disease · doi:10.14336/ad.2023.0308 · Cited by 30 · see citing works
Singh, A., Singh, K., Kaur, J., Kaur, R., Sharma, A., Kaur, J., Kaur, U., Chadha, R., & Bedi, P. M. S. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00393 · Cited by 29 · see citing works
Ali, F., Manzoor, U., Bhattacharya, R., Bansal, A. K., Chandrashekharaiah, K. S., Singh, L. R., Suma Mohan, S., Uversky, V. N., & Dar, T. A. (2022) · ACS Omega · doi:10.1021/acsomega.1c06990 · Cited by 28 · see citing works
The proteinopenia hypothesis: Loss of Aβ42 and the onset of Alzheimer’s Disease
Espay, A. J., Herrup, K., Kepp, K. P., & Daly, T. P. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102112 · Cited by 29 · see citing works
Alzheimer’s Disease: From Amyloid to Autoimmune Hypothesis
Arshavsky, Y. I. (2020) · The Neuroscientist · doi:10.1177/1073858420908189 · Cited by 28 · see citing works
Is It the Twilight of BACE1 Inhibitors?
Hrabinova, M., Pejchal, J., Kucera, T., Jun, D., Schmidt, M., & Soukup, O. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200503023323 · Cited by 28 · see citing works
Cholesterol and matrisome pathways dysregulated in human APOE ε4 gliaPreprint
Julia, T. C. W., Liang, S., Lü, Q., Pipalia, N. H., Chao, M. J., Shi, Y., Bertelsen, S. E., Kapoor, M., Marcora, E. M., Sikora, E., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/713362 · Cited by 28 · see citing works
Self-citationA short perspective on the long road to effective treatments for Alzheimer's disease
Reynolds, D. S. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14581 · Cited by 26 · see citing works
Chen, L.-Y., Wu, D.-S., & Shen, Y. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100660 · Cited by 27 · see citing works
Epigenetic biomarkers in Alzheimer's disease: Diagnostic and prognostic relevance
Behl, T., Kyada, A., Roopashree, R., Nathiya, D., Arya, R., Kumar, M., Khalid, M., Gulati, M., Sachdeva, M., Fareed, M., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102556 · Cited by 25 · see citing works
Lake, J., Storm, C. S., Makarious, M. B., & Bandrés‐Ciga, S. (2021) · Cells · doi:10.3390/cells10051030 · Cited by 24 · see citing works
Mural Cells: Potential Therapeutic Targets to Bridge Cardiovascular Disease and Neurodegeneration
Lin, A., Peiris, N. J., Dhaliwal, H., Hakim, M., Li, W., Ganesh, S., Ramaswamy, Y., Patel, S., & Misra, A. (2021) · Cells · doi:10.3390/cells10030593 · Cited by 23 · see citing works
Licochalcone A: A Potential Multitarget Drug for Alzheimer’s Disease Treatment
Olloquequi, J., Ettcheto, M., Cano, A. C., Fortuna, A. C., Bicker, J., Sánchez‐López, E., Paz, C., Ureña, J. M., Verdaguer, E., Auladell, C., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241814177 · Cited by 22 · see citing works
Serotonin Receptors as a Potential Target in the Treatment of Alzheimer’s Disease
Eremin, D. V., Kondaurova, E. M., Rodnyy, A. Y., Molobekova, C. A., Kudlay, D. A., & Naumenko, V. S. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923120064 · Cited by 22 · see citing works
Strynatka, K. A., Gurrola-Gal, M. C., Berman, J. N., & McMaster, C. R. (2018) · Genetics · doi:10.1534/genetics.117.300124 · Cited by 22 · see citing works
Genetic risk factors underlying white matter hyperintensities and cortical atrophy
Patel, Y., Shin, J., Sliz, E., Tang, A., Mishra, A., Xia, R., Hofer, E., Rajula, H., Wang, R.-Q., Beyer, F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53689-1 · Cited by 17 · see citing works
Amyloid β production along the neuronal secretory pathway: Dangerous liaisons in the Golgi?
Fourrière, L., & Gleeson, P. A. (2021) · Traffic · doi:10.1111/tra.12808 · Cited by 22 · see citing works
What have we learnt from past failures in Alzheimer’s disease drug discovery?
Cacabelos, R. (2022) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2022.2033724 · Cited by 22 · see citing works
Lin, J., Gao, S., Wang, T., Shen, Y., Yang, W., Li, Y., & Hu, H. (2019) · PubMed Central · Cited by 20 · see citing works
Membrane dynamics of γ‐secretase with the anterior pharynx‐defective 1B subunit
Dehury, B., & Kepp, K. P. (2020) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29832 · Cited by 20 · see citing works
Impact of New Drugs for Therapeutic Intervention in Alzheimer’s Disease
Olloquequi, J., Ettcheto, M., Cano, A. C., Sánchez‐López, E., Carrasco, M., Espinosa-Jiménez, T., Beas‐Zárate, C., Gudiño‐Cabrera, G., Ureña‐Guerrero, M. E., Verdaguer, E., et al. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2705146 · Cited by 21 · see citing works
Personalized Management and Treatment of Alzheimer’s Disease
Cacabelos, R., Naidoo, V., Martínez-Iglesias, O. A., Corzo, L., Cacabelos, N., Pego, R., & Carril, J. C. (2022) · Life · doi:10.3390/life12030460 · Cited by 19 · see citing works
Amyloidogenesis: What Do We Know So Far?
Alraawi, Z., Banerjee, N., Mohanty, S., & Kumar, T. K. S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213970 · Cited by 20 · see citing works
Gene delivery of a modified antibody to Aβ reduces progression of murine Alzheimer’s disease
Elmer, B. M., Swanson, K. A., Bangari, D. S., Piepenhagen, P. A., Roberts, E., Taksir, T. V., Guo, L. M., Obinu, M. C., Barnéoud, P., Ryan, S., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0226245 · Cited by 20 · see citing works
Nanomedicine against Alzheimer’s and Parkinson’s Disease
Tandon, A., Singh, S. J., & Chaturvedi, R. K. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666201021140904 · Cited by 19 · see citing works
Gotoh, N., Saito, Y., Hata, S., Saito, H., Ojima, D., Murayama, C., Shigeta, M., Abe, T., Konno, D., Matsuzaki, F., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012386 · Cited by 18 · see citing works
Shukla, R., Pahal, S., Gupta, A., Choudhary, P., Misra, K., & Singh, S. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2068072 · Cited by 18 · see citing works
Pharmacogenomics of Alzheimer’s Disease: Novel Strategies for Drug Utilization and Development
Cacabelos, R., Naidoo, V., Martínez-Iglesias, O. A., Corzo, L., Cacabelos, N., Pego, R., & Carril, J. C. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2573-6_13 · Cited by 19 · see citing works
Palanivelu, L., Chang, C.-W., Li, S., Liang, Y., Lo, Y., & Chen, Y. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00063 · Cited by 17 · see citing works
Abondio, P., Sarno, S., Giuliani, C., Laganà, V., Maletta, R., Bernardi, L., Bruno, F., Colao, R., Puccio, G., Frangipane, F., et al. (2021) · Biomedicines · doi:10.3390/biomedicines10010020 · Cited by 17 · see citing works
Khan, B., Iqbal, M. K., Khan, M. A., Khan, H. R., Kiyani, M. M., Bashir, S., & Li, S. (2025) · Journal of Molecular Neuroscience · doi:10.1007/s12031-025-02337-4 · Cited by 17 · see citing works
Rahimi, A., Sameei, P., Mousavi, S., Ghaderi, K., Hassani, A., Hassani, S., & Alipour, S. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04143-2 · Cited by 17 · see citing works
Expression of AHI1 Rescues Amyloidogenic Pathology in Alzheimer’s Disease Model Cells
Ting, L., Lu, H., Yen, S.-F., Ngo, T. H., Tu, F.-Y., Tsai, I.-S., Tsai, Y., Chang, F., Li, X., Li, S., et al. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1587-1 · Cited by 16 · see citing works
Lee, J., Lee, B., Lee, H. G., Kim, E. J. E., Kim, S. S., Kwon, H. C., Lee, H., Lee, G., Hong, W., Ham, S., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2505217122 · Cited by 15 · see citing works
Emerging Molecular Targets in Neurodegenerative Disorders: New Avenues for Therapeutic Intervention
Eroglu, E., & HARMANCI, N. (2025) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.70107 · Cited by 16 · see citing works
APP in the Neuromuscular Junction for the Development of Sarcopenia and Alzheimer’s Disease
Wu, M., Zou, W.-J., Lee, D., Mei, L., & Xiong, W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097809 · Cited by 15 · see citing works
Kumar, S., Kapadia, A., Theil, S., Joshi, P., Riffel, F., Heneka, M. T., & Walter, J. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.619639 · Cited by 15 · see citing works
Kung, W., & Lin, M.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073289 · Cited by 14 · see citing works
Kung, W., & Lin, M.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020934 · Cited by 14 · see citing works
Neurodegenerative Disease Transmission and Transgenesis in MicePreprint
Dugger, B. N., Perl, D. P., & Carlson, G. A. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a023549 · Cited by 14 · see citing works
Thussu, S., Naidu, A., Manivannan, S., & Grossberg, G. T. (2024) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2024.2402058 · Cited by 13 · see citing works
Novel techniques for early diagnosis and monitoring of Alzheimer’s disease
Parul, P., Singh, A. K., & Shukla, S. (2024) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2024.2415985 · Cited by 13 · see citing works
MacMullen, C., Sharma, N., & Davis, R. L. (2024) · Brain · doi:10.1093/brain/awae364 · Cited by 13 · see citing works
Susco, S. G., Ghosh, S. D., Mazzucato, P., Angelini, G., Beccard, A., Barrera, V., Berryer, M. H., Messana, A., Lam, D., Hazelbaker, D. Z., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111312 · Cited by 14 · see citing works
Özcan, G. G., Lim, S., Canning, T., Tirathdas, L., Donnelly, J., Kundu, T., & Rihel, J. (2024) · iScience · doi:10.1016/j.isci.2024.108870 · Cited by 12 · see citing works
Psychiatric Disease as a Potential Risk Factor for Dementia: A Narrative Review
Hedges, D. W., Chase, M., Farrer, T. J., & Gale, S. D. (2024) · Brain Sciences · doi:10.3390/brainsci14070722 · Cited by 12 · see citing works
Ma, W., Chen, A.-F., Xie, X., & Huang, Y. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108342 · Cited by 12 · see citing works
Recent advances in pre-clinical diagnosis of Alzheimer’s disease
Zhou, J., Benoit, M., & Sharoar, M. G. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00733-4 · Cited by 12 · see citing works
Conformational Models of APP Processing by Gamma Secretase Based on Analysis of Pathogenic Mutations
Kim, M., & Борисович, Б. И. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413600 · Cited by 12 · see citing works
Reed, A. L., Mitchell, W., Alexandrescu, A. T., & Alder, N. N. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1263420 · Cited by 13 · see citing works
Systems Biology Understanding of the Effects of Lithium on Affective and Neurodegenerative Disorders
Ge, W., & Jakobsson, E. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00933 · Cited by 12 · see citing works
Rathee, S., Sen, D., Pandey, V., & Jain, S. (2024) · Current Drug Targets · doi:10.2174/0113894501320096240627071400 · Cited by 13 · see citing works
Babaei, F. G., Saburi, E., Forouzanfar, F., Asgari, M., Keshavarzi, Z., & Hajali, V. (2025) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2025.101930 · Cited by 11 · see citing works
The Potential of cfDNA as Biomarker: Opportunities and Challenges for Neurodegenerative Diseases
Aydın, Ş., Özdemir, S., & Adıgüzel, A. (2025) · Journal of Molecular Neuroscience · doi:10.1007/s12031-025-02317-8 · Cited by 11 · see citing works
Fu, C.-X., Dai, L., Yuan, X.-Y., & Xu, Y. (2020) · Biological Trace Element Research · doi:10.1007/s12011-020-02280-y · Cited by 11 · see citing works
Borreca, A., Valeri, F., Luca, M. D., Ernst, L., Russo, A., Nobili, A., Cordella, A., Corsetti, V., Amadoro, G., Mercuri, N. B., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104787 · Cited by 11 · see citing works
- Authors
- TCW, J., & Goate, A. M.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Venue
- Cold Spring Harbor Perspectives in Medicine
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2016-12-21
- Volume
- 7
- Issue
- 6
- Pages
- a024539
- ISSN
- 2157-1422 (ISSN-L)
- PMC
- PMC5453386
- OpenAlex
- W2566006671
- Cited by
- 242
- References
- 73
- Citations by year
- 2026: 41 · 2025: 39 · 2024: 42 · 2023: 29 · 2022: 27 · 2021: 24 · 2020: 20 · 2019: 10 · 2018: 7 · 2017: 3
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- JPB Foundation
- National Institute on Aging
- Topics
- Health Sciences › Medicine › Physiology › 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 mutations, Down syndrome, amyloid-beta, amyloid-beta 42, amyloid fibril formation, early-onset familial Alzheimer's disease, genetic risk variants, neurofibrillary tangles, tau protein, amyloid hypothesis
- MeSH terms
- Alzheimer Disease, Animals, Brain, Down Syndrome, Humans, Amyloid beta-Protein Precursor, Neurofibrillary Tangles, tau Proteins, Mutation, Missense, Plaque, Amyloid
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