The Genetics of Alzheimer's Disease

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

Finding the missing heritability of complex diseases

Manolio, T. A., Collins, F. S., Cox, N. J., Goldstein, D. B., Hindorff, L. A., Hunter, D. J., McCarthy, M. I., Ramos, E. M., Cardon, L. R., Chakravarti, A., et al. (2009) · Nature · doi:10.1038/nature08494 · Cited by 8,336

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

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

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

Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease.

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

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051

Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease

Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326

Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599

Candidate gene for the chromosome 1 familial Alzheimer’s disease locus

Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577

Super-enhancers in the control of cell identity and disease

Hnisz, D., Abraham, B. J., Lee, T. I., Lau, A., Saint-André, V., Sigova, A. A., Hoke, H. A., & Young, R. A. (2013) · Cell · doi:10.1016/j.cell.2013.09.053 · Cited by 3,662

Microglia Function in the Central Nervous System During Health and Neurodegeneration

Colonna, M., & Butovsky, O. (2017) · Annual Review of Immunology · doi:10.1146/annurev-immunol-051116-052358 · Cited by 2,894

Blood-Brain Barrier: From Physiology to Disease and Back

Sweeney, M. D., Zhao, Z., Montagne, A., Nelson, A. R., & Zlokovic, B. V. (2019) · Physiological Reviews · doi:10.1152/physrev.00050.2017 · Cited by 2,312

The Amyloid-β Pathway in Alzheimer’s Disease

Hampel, H., Hardy, J., Blennow, K., Chen, C., Perry, G., Kim, S. H., Villemagne, V. L., Aisen, P., Vendruscolo, M., Iwatsubo, T., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01249-0 · Cited by 1,952

Preclinical Alzheimer’s Disease: Definition, Natural History, and Diagnostic Criteria

Dubois, B., Hampel, H., Feldman, H. H., Scheltens, P., Aisen, P., Andrieu, S., Bakardjian, H., Benali, H., Bertram, L., Blennow, K., et al. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.02.002 · Cited by 1,925

Clearance systems in the brain—implications for Alzheimer disease

Tarasoff-Conway, J. M., Carare, R. O., Osorio, R. S., Glodzik, L., Butler, T., Fieremans, E., Axel, L., Rusinek, H., Nicholson, C., Zlokovic, B. V., et al. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.119 · Cited by 1,678

TREM2 Maintains Microglial Metabolic Fitness in Alzheimer’s Disease

Ulland, T. K., Song, W. M., Huang, S. C.-C., Ulrich, J. D., Sergushichev, A., Beatty, W. L., Loboda, A. A., Zhou, Y., Cairns, N. J., Kambal, A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.023 · Cited by 1,263

The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease

Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201

Molecular 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

TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ, and Thereby Facilitates Uptake of Amyloid-Beta by Microglia

Yeh, F. L., Wang, Y., Tom, I., Gonzalez, L. C., & Sheng, M. (2016) · Neuron · doi:10.1016/j.neuron.2016.06.015 · Cited by 943

TREM2-mediated early microglial response limits diffusion and toxicity of amyloid plaques

Wang, Y., Ulland, T. K., Ulrich, J. D., Song, W., Tzaferis, J. A., Hole, J. T., Yuan, P., Mahan, T. E., Shi, Y., Gilfillan, S., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151948 · Cited by 840

Alzheimer's disease: experimental models and reality

Drummond, E., & Wisniewski, T. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1662-x · Cited by 810

The case for rejecting the amyloid cascade hypothesis

Herrup, K. (2015) · Nature Neuroscience · doi:10.1038/nn.4017 · Cited by 768

Plasma Proteome Profiling to Assess Human Health and Disease

Geyer, P. E., Kulak, N. A., Pichler, G., Holdt, L. M., Teupser, D., & Mann, M. (2016) · Cell Systems · doi:10.1016/j.cels.2016.02.015 · Cited by 734

Alzheimer’s disease: A matter of blood–brain barrier dysfunction?

Montagne, A., Zhao, Z., & Zlokovic, B. V. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20171406 · Cited by 672

Neurovascular dysfunction and neurodegeneration in dementia and Alzheimer's disease

Nelson, A. R., Sweeney, M. D., Sagare, A. P., & Zlokovic, B. V. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.016 · Cited by 559

Inconsistencies and Controversies Surrounding the Amyloid Hypothesis of Alzheimer's Disease

Morris, G. P., Clark, I. A., & Vissel, B. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0135-5 · Cited by 522

Alteration of the microRNA network during the progression of Alzheimer's disease

Lau, P., Bossers, K., Janky, R., Salta, E., Frigerio, C. S., Barbash, S., Rothman, R., Sierksma, A. S. R., Thathiah, A., Greenberg, D., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201201974 · Cited by 474

TREM2, microglia, and neurodegenerative diseases

Yeh, F. L., Hansen, D. V., & Sheng, M. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.008 · Cited by 440

Neuron loss in the 5XFAD mouse model of Alzheimer’s disease correlates with intraneuronal Aβ42 accumulation and Caspase-3 activation

Eimer, W. A., & Vassar, R. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-2 · Cited by 425

TREM2 variants: new keys to decipher Alzheimer disease pathogenesis

Colonna, M., & Wang, Y. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.7 · Cited by 418

Central role for PICALM in amyloid-β blood-brain barrier transcytosis and clearance

Zhao, Z., Sagare, A. P., Ma, Q., Halliday, M. R., Kong, P., Kisler, K., Winkler, E. A., Ramanathan, A., Kanekiyo, T., Bu, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4025 · Cited by 410

TREM2 Acts Downstream of CD33 in Modulating Microglial Pathology in Alzheimer's Disease

Griciuc, A., Patel, S., Federico, A. N., Choi, S. H., Innes, B. J., Oram, M. K., Cereghetti, G., McGinty, D., Anselmo, A., Sadreyev, R. I., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.06.010 · Cited by 378

The epigenetics of aging and neurodegeneration

Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381

The familial Alzheimer's disease APPV717I mutation alters APP processing and Tau expression in iPSC-derived neurons

Muratore, C. R., Rice, H. C., Srikanth, P., Callahan, D. G., Shin, T., Benjamin, L. N. P., Walsh, D. M., Selkoe, D. J., & Young-Pearse, T. L. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu064 · Cited by 379

IL-33 ameliorates Alzheimer's disease-like pathology and cognitive decline

Fu, A. K. Y., Hung, K.-W., Yuen, M. Y. F., Zhou, X., Mak, D. S. Y., Chan, I. C. W., Cheung, T. H., Zhang, B., Fu, W.-Y., Liew, F. Y., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604032113 · Cited by 369

mTOR regulates tau phosphorylation and degradation: implications for Alzheimer's disease and other tauopathies

Caccamo, A., Magrì, A., Medina, D. X., Wisely, E. V., López‐Aranda, M. F., Silva, A. J., & Oddo, S. (2013) · Aging Cell · doi:10.1111/acel.12057 · Cited by 362

Microglia-Mediated Synapse Loss in Alzheimer's Disease

Rajendran, L., & Paolicelli, R. C. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.1136-17.2017 · Cited by 355

Immune Signaling in Neurodegeneration

Hammond, T. R., Marsh, S. E., & Stevens, B. (2019) · Immunity · doi:10.1016/j.immuni.2019.03.016 · Cited by 336

Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer’s disease

Thal, D. R., Walter, J., Saido, T. C., & Fändrich, M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1375-y · Cited by 319

Function, therapeutic potential and cell biology of BACE proteases: current status and future prospects

Vassar, R., Kuhn, P., Haass, C., Kennedy, M. E., Rajendran, L., Wong, P. C., & Lichtenthaler, S. F. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12715 · Cited by 311

Presynaptic dystrophic neurites surrounding amyloid plaques are sites of microtubule disruption, BACE1 elevation, and increased Aβ generation in Alzheimer’s disease

Sadleir, K. R., Kandalepas, P. C., Buggia-Prévot, V., Nicholson, D. A., Thinakaran, G., & Vassar, R. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1558-9 · Cited by 294

Altered microglial response to Aβ plaques in APPPS1-21 mice heterozygous for TREM2

Ulrich, J. D., Finn, M. B., Wang, Y., Shen, A., Mahan, T. E., Jiang, H., Stewart, F. R., Piccio, L., Colonna, M., & Holtzman, D. M. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-20 · Cited by 302

Emerging roles of innate and adaptive immunity in Alzheimer’s disease

Chen, X., & Holtzman, D. M. (2022) · Immunity · doi:10.1016/j.immuni.2022.10.016 · Cited by 297

Immunotherapeutic Approaches for Alzheimer’s Disease

Wisniewski, T., & Goñi, F. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.064 · Cited by 284

Aberrant Lipid Metabolism in the Forebrain Niche Suppresses Adult Neural Stem Cell Proliferation in an Animal Model of Alzheimer’s Disease

Hamilton, L. K., Dufresne, M., Joppé, S. E., Petryszyn, S., Aumont, A., Calon, F., Barnabé-Heider, F., Furtos, A., Parent, M., Chaurand, P., et al. (2015) · Cell Stem Cell · doi:10.1016/j.stem.2015.08.001 · Cited by 284

Cardiolipin, Mitochondria, and Neurological Disease

Falabella, M., Vernon, H. J., Hanna, M. G., Claypool, S. M., & Pitceathly, R. D. S. (2021) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2021.01.006 · Cited by 282

Cerebrovascular Effects of Apolipoprotein E: Implications for Alzheimer Disease

Zlokovic, B. V. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.2152 · Cited by 263

Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism

Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256

Apolipoprotein E, gender, and Alzheimer’s disease: an overlooked, but potent and promising interaction

Ungar, L., Altmann, A., & Greicius, M. D. (2014) · Brain Imaging and Behavior · doi:10.1007/s11682-013-9272-x · Cited by 246

Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease

Overk, C. R., & Masliah, E. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.015 · Cited by 242

Alzheimer’s disease as an inflammatory disease

Bolós, M., Perea, J. R., & Avila, J. (2017) · BioMolecular Concepts · doi:10.1515/bmc-2016-0029 · Cited by 216

Aβ reduction in BACE1 heterozygous null 5XFAD mice is associated with transgenic APP level

Sadleir, K. R., Eimer, W. A., Cole, S. L., & Vassar, R. (2015) · Molecular Neurodegeneration · doi:10.1186/1750-1326-10-1 · Cited by 213

Impaired vascular-mediated clearance of brain amyloid beta in Alzheimer’s disease: the role, regulation and restoration of LRP1

Ramanathan, A., Nelson, A. R., Sagare, A. P., & Zlokovic, B. V. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00136 · Cited by 205

Impact of Cytokines and Chemokines on Alzheimer’s Disease Neuropathological Hallmarks

Domingues, C., da Cruz e Silva, O. A. B., & Henriques, A. G. (2017) · Current Alzheimer Research · doi:10.2174/1567205014666170317113606 · Cited by 203

Multi-Target-Directed Ligands and other Therapeutic Strategies in the Search of a Real Solution for Alzheimer’s Disease

Agis-Torres, A., Sollhuber, M., Fernandez, M., & Sanchez-Montero, J. M. (2014) · Current Neuropharmacology · doi:10.2174/1570159x113116660047 · Cited by 202

Plaque-associated human microglia accumulate lipid droplets in a chimeric model of Alzheimer’s disease

Claes, C., Danhash, E. P., Hasselmann, J., Chadarevian, J. P., Shabestari, S. K., England, W. E., Lim, T. E., Hidalgo, J. L. S., Spitale, R. C., Davtyan, H., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00473-0 · Cited by 197

Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo

Vasconcelos, B., Stancu, I.-C., Buist, A., Bird, M., Wang, P., Vanoosthuyse, A., Van Kolen, K., Verheyen, A., Kienlen-Campard, P., Octave, J.-N., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1525-x · Cited by 192

Neuronal dark matter: the emerging role of microRNAs in neurodegeneration

Goodall, E. F., Heath, P. R., Bandmann, O., Kirby, J., & Shaw, P. J. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00178 · Cited by 187

Alzheimer's Disease Puzzle: Delving into Pathogenesis Hypotheses

(2024) · aging and disease · doi:10.14336/ad.2023.0608 · Cited by 183

Actin dynamics and cofilin‐actin rods in alzheimer disease

Bamburg, J. R., & Bernstein, B. W. (2016) · Cytoskeleton · doi:10.1002/cm.21282 · Cited by 181

What psychiatric genetics has taught us about the nature of psychiatric illness and what is left to learn

Kendler, K. S. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.50 · Cited by 178

Defining Alzheimer as a common age-related neurodegenerative process not inevitably leading to dementia

Ferrer, I. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.005 · Cited by 174

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

Aging and Neurodegenerative Disease: Is the Adaptive Immune System a Friend or Foe?

Mayne, K., White, J. A., McMurran, C. E., Rivera, F. J., & de la Fuente, A. G. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.572090 · Cited by 167

Dysfunction of autophagy and endosomal-lysosomal pathways: Roles in pathogenesis of Down syndrome and Alzheimer’s Disease

Colacurcio, D. J., Pensalfini, A., Jiang, Y., & Nixon, R. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.001 · Cited by 167

ApoE4 upregulates the activity of mitochondria‐associated ER membranes

Tambini, M. D., Pera, M., Kanter, E., Yang, H., Guardia‐Laguarta, C., Holtzman, D., Sulzer, D., Area‐Gomez, E., & Schon, E. A. (2016) · The EMBO Reports · doi:10.15252/embr.201540614 · Cited by 166

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

Multifunctional Liposomes Reduce Brain β-Amyloid Burden and Ameliorate Memory Impairment in Alzheimer's Disease Mouse Models

Balducci, C., Mancini, S., Minniti, S., La Vitola, P., Zotti, M., Sancini, G., Mauri, M., Cagnotto, A., Colombo, L., Fiordaliso, F., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.0284-14.2014 · Cited by 162

Activated iron-containing microglia in the human hippocampus identified by magnetic resonance imaging in Alzheimer disease

Zeineh, M. M., Chen, Y., Kitzler, H. H., Hammond, R., Vogel, H., & Rutt, B. K. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.05.022 · Cited by 151

Cellular cholesterol homeostasis and Alzheimer’s disease

Chang, T.-Y., Yamauchi, Y., Hasan, M. T., & Chang, C. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075630 · Cited by 155

APOE-amyloid interaction: Therapeutic targets

Wisniewski, T., & Drummond, E. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104784 · Cited by 131

Developing Effective Alzheimer’s Disease Therapies: Clinical Experience and Future Directions

Elmaleh, D. R., Farlow, M. R., Conti, P. S., Tompkins, R. G., Kundakovic, L., & Tanzi, R. E. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-190507 · Cited by 129

Extending the small-molecule similarity principle to all levels of biology with the Chemical Checker

Duran-Frigola, M., Pauls, E., Guitart-Pla, O., Bertoni, M., Alcalde, V., Amat, D., Juan-Blanco, T., & Aloy, P. (2020) · Nature Biotechnology · doi:10.1038/s41587-020-0502-7 · Cited by 126

Cerebrospinal Fluid Biomarkers of Neurovascular Dysfunction in Mild Dementia and Alzheimer'S Disease

Sweeney, M. D., Sagare, A. P., & Zlokovic, B. V. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.76 · Cited by 122

Structure-based inhibitors of amyloid beta core suggest a common interface with tau

Griner, S. L., Seidler, P., Bowler, J., Murray, K. A., Yang, T. P., Sahay, S., Sawaya, M. R., Cascio, D., Rodriguez, J. A., Philipp, S., et al. (2019) · eLife · doi:10.7554/elife.46924 · Cited by 121

Different effects of constitutive and induced microbiota modulation on microglia in a mouse model of Alzheimer’s disease

Mezö, C., Dokalis, N., Mossad, O., Staszewski, O., Neuber, J., Yilmaz, B., Schnepf, D., de Agüero, M. G., Ganal-Vonarburg, S. C., Macpherson, A. J., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00988-5 · Cited by 120

Mitochondrial Regulation of Microglial Immunometabolism in Alzheimer’s Disease

Fairley, L. H., Wong, J. H., & Barron, A. M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.624538 · Cited by 120

Gut microbiota–driven brain Aβ amyloidosis in mice requires microglia

Dodiya, H. B., Lutz, H. L., Weigle, I. Q., Patel, P., Michalkiewicz, J., Roman-Santiago, C. J., Zhang, C. M., Liang, Y., Srinath, A., Zhang, X., et al. (2022) · Journal of Experimental Medicine · doi:10.1084/jem.20200895 · Cited by 120

Characterization of biometal profiles in neurological disorders

Pfaender, S., & Grabrucker, A. M. (2014) · Metallomics · doi:10.1039/c4mt00008k · Cited by 117

‘Sealing off the CNS’: cellular and molecular regulation of blood–brain barriergenesis

Siegenthaler, J. A., Sohet, F., & Daneman, R. (2013) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2013.06.006 · Cited by 115

Biomarkers in Sporadic and Familial Alzheimer’s Disease

Lista, S., O’Bryant, S. E., Blennow, K., Dubois, B., Hugon, J., Zetterberg, H., & Hampel, H. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-143006 · Cited by 106

The association of antidepressant drug usage with cognitive impairment or dementia, including Alzheimer disease: A systematic review and meta-analysis: M oraros et al.

Moraros, J., Nwankwo, C., Patten, S. B., & Mousseau, D. D. (2017) · Depression and Anxiety · doi:10.1002/da.22584 · Cited by 105

APP Function and Lipids: A Bidirectional Link

Grimm, M. O. W., Mett, J., Grimm, H. S., & Hartmann, T. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00063 · Cited by 104

PICALM and Alzheimer’s Disease: An Update and Perspectives

Ando, K., Nagaraj, S., Küçükali, F., de Fisenne, M.-A., Kosa, A.-C., Doeraene, E., Lopez Gutierrez, L., Brion, J.-P., & Leroy, K. (2022) · Cells · doi:10.3390/cells11243994 · Cited by 104

Rare autosomal copy number variations in early-onset familial Alzheimer’s disease

Hooli, B. V., Kovacs-Vajna, Z. M., Mullin, K., Blumenthal, M. A., Mattheisen, M., Zhang, C., Lange, C., Mohapatra, G., Bertram, L., & Tanzi, R. E. (2014) · Molecular Psychiatry · doi:10.1038/mp.2013.77 · Cited by 100

Axonal organization defects in the hippocampus of adult conditional BACE1 knockout mice

Ou-Yang, M.-H., Kurz, J. E., Nomura, T., Popovic, J., Rajapaksha, T. W., Dong, H., Contractor, A., Chetkovich, D. M., Tourtellotte, W. G., & Vassar, R. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aao5620 · Cited by 94

Reduced mitochondria cytochrome oxidase activity in adult children of mothers with Alzheimer's disease

Mosconi, L., de Leon, M., Murray, J., E, L., Lu, J., Javier, E., McHugh, P., & Swerdlow, R. H. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110866 · Cited by 97

Secretome from SH-SY5Y APPSwe cells trigger time-dependent CHME3 microglia activation phenotypes, ultimately leading to miR-21 exosome shuttling

Fernandes, A., Ribeiro, A. R., Monteiro, M., Garcia, G., Vaz, A. R., & Brites, D. (2018) · Biochimie · doi:10.1016/j.biochi.2018.05.015 · Cited by 93

Amyloid precursor protein (APP) May act as a substrate and a recognition unit for CRL4CRBN and Stub1 E3 ligases facilitating ubiquitination of proteins involved in presynaptic functions and neurodegeneration

Del Prete, D., Rice, R. C., Rajadhyaksha, A. M., & D'Adamio, L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.733626 · Cited by 86

Shared genetic etiology underlying Alzheimer’s disease and type 2 diabetes

Hao, K., Di Narzo, A. F., Ho, L., Luo, W., Li, S., Chen, R., Li, T., Dubner, L., & Pasinetti, G. M. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2015.06.006 · Cited by 84

Integrated multi-omics analysis of Alzheimer’s disease shows molecular signatures associated with disease progression and potential therapeutic targets

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The Triggering Receptor Expressed on Myeloid Cells 2: A Molecular Link of Neuroinflammation and Neurodegenerative Diseases

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Chlamydia pneumoniae: An Etiologic Agent for Late-Onset Dementia

Balin, B. J., Hammond, C. J., Little, C. S., Hingley, S. T., Al-Atrache, Z., Appelt, D. M., Whittum-Hudson, J. A., & Hudson, A. P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00302 · Cited by 77

Dysfunction of the mTOR pathway is a risk factor for Alzheimer's disease

Yates, S. C., Zafar, A., Hubbard, P., Nagy, S., Durant, S., Bicknell, R., Wilcock, G., Christie, S., Esiri, M. M., Smith, A. D., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-3 · Cited by 76

On the identification of low allele frequency mosaic mutations in the brains of Alzheimer’s disease patients

Sala Frigerio, C., Lau, P., Troakes, C., Deramecourt, V., Gele, P., Van Loo, P., Voet, T., & De Strooper, B. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2015.02.007 · Cited by 71

The innate immune system in Alzheimer's disease

Boutajangout, A., & Wisniewski, T. (2013) · International Journal of Cell Biology · doi:10.1155/2013/576383 · Cited by 69

Dedifferentiation and neuronal repression define familial Alzheimer’s disease

Caldwell, A. B., Liu, Q., Schroth, G. P., Galasko, D. R., Yuan, S. H., Wagner, S. L., & Subramaniam, S. (2020) · Science Advances · doi:10.1126/sciadv.aba5933 · Cited by 69

Clustering of transcriptional profiles identifies changes to insulin signaling as an early event in a mouse model of Alzheimer’s disease

Jackson, H. M., Soto, I., Graham, L. C., Carter, G. W., & Howell, G. R. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-831 · Cited by 66

ER stress is not elevated in the 5XFAD mouse model of Alzheimer's disease

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Turning the tide on Alzheimer’s disease: modulation of γ-secretase

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Neuritic Plaques — Gateways to Understanding Alzheimer’s Disease

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Imaging-wide association study: integrating imaging endophenotypes in GWAS

Xu, Z., Wu, C., & Pan, W. (2017) · NeuroImage · doi:10.1016/j.neuroimage.2017.07.036 · Cited by 56

The P522R protective variant of PLCG2 promotes the expression of antigen presentation genes by human microglia in an Alzheimer's disease mouse model

Claes, C., England, W. E., Danhash, E. P., Kiani Shabestari, S., Jairaman, A., Chadarevian, J. P., Hasselmann, J., Tsai, A. P., Coburn, M. A., Sanchez, J., et al. (2022) · Alzheimer's & Dementia · doi:10.1002/alz.12577 · Cited by 52

Early and sustained altered expression of aging-related genes in young 3xTg-AD mice

Gatta, V, D'Aurora, M., Granzotto, A., Stuppia, L., & Sensi, S. L. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.11 · Cited by 44

From the Entorhinal Region via the Prosubiculum to the Dentate Fascia: Alzheimer Disease-Related Neurofibrillary Changes in the Temporal Allocortex

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Genetic perturbations of disease risk genes in mice capture transcriptomic signatures of late-onset Alzheimer’s disease

Pandey, R. S., Graham, L., Uyar, A., Preuss, C., Howell, G. R., & Carter, G. W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0351-3 · Cited by 37

AZP2006, a new promising treatment for Alzheimer’s and related diseases

Callizot, N., Estrella, C., Burlet, S., Henriques, A., Brantis, C., Barrier, M., Campanari, M. L., & Verwaerde, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-94708-1 · Cited by 35

Extracellular Proteolysis of Apolipoprotein E (apoE) by Secreted Serine Neuronal Protease

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ADAM10 Prodomain Mutations Cause Late-Onset Alzheimer’s Disease: Not Just the Latest FAD

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