Clathrin mediated endocytosis in Alzheimer’s disease: cell type specific involvement in amyloid beta pathology
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This review provides a comprehensive examination of the role of clathrin-mediated endocytosis (CME) in Alzheimer’s disease (AD) pathogenesis, emphasizing its impact across various cellular contexts beyond neuronal dysfunction. In neurons, dysregulated CME contributes to synaptic dysfunction, amyloid beta (Aβ) processing, and Tau pathology, highlighting its involvement in early AD pathogenesis. Furthermore, CME alterations extend to non-neuronal cell types, including astrocytes and microglia, which play crucial roles in Aβ clearance and neuroinflammation. Dysregulated CME in these cells underscores its broader implications in AD pathophysiology. Despite significant progress, further research is needed to elucidate the precise mechanisms underlying CME dysregulation in AD and its therapeutic implications. Overall, understanding the complex interplay between CME and AD across diverse cell types holds promise for identifying novel therapeutic targets and interventions.
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These mechanisms (autophagy, phagocytosis, endocytosis) have been shown to be impaired in AD brains.
“These mechanisms has been shown to be impaired in AD brains [45, 55].”
From Enhanced microglial dynamics and a paucity of tau seeding in the amyloid plaque microenvironment contribute to cognitive resilience in Alzheimer’s disease (2024) · cites this paper as [45]
The Introduction identifies impaired autophagy in AD, and “AD and endolysosomal function” describes defects in that pathway. The Astrocytes section reports impaired phagocytosis of diseased synapses when astrocytes are overburdened with Aβ. But the paper does not establish that all three mechanisms are impaired in AD brains: it says how endocytosis itself is altered remains to be considered, and the phagocytosis passage does not establish a brain-wide finding. (LLM, conf=0.84)
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Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
Neurotoxic reactive astrocytes are induced by activated microglia
Liddelow, S. A., Guttenplan, K. A., Clarke, L. E., Bennett, F. C., Bohlen, C. J., Schirmer, L., Bennett, M. L., Münch, A. E., Chung, W.-S., Peterson, T. C., et al. (2017) · Nature · doi:10.1038/nature21029 · Cited by 7,971 · see citing works
Engineering precision nanoparticles for drug delivery
Mitchell, M. J., Billingsley, M. M., Haley, R. M., Wechsler, M. E., Peppas, N. A., & Langer, R. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0090-8 · Cited by 7,933 · see citing works
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works
The amyloid hypothesis of Alzheimer's disease at 25 years
Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164 · see citing works
Astrocytes: Biology and pathology
Sofroniew, M. V., & Vinters, H. V. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0619-8 · Cited by 5,196 · see citing works
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397 · 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
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · see citing works
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · see citing works
The neuropathological diagnosis of Alzheimer's disease
DeTure, M. A., & Dickson, D. W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0333-5 · Cited by 3,329 · cited 1× · see citing works
“These proteins cluster and bind to the plasma membrane to initiate membrane curvature and recruit other proteins, such as the changes that lead to it (Deture and Dickson, 2019) and the effort to identify early cellular changes before the onset of symptoms is of great importance.”
2023 Alzheimer's disease facts and figures
(2023) · Alzheimer's & Dementia · doi:10.1002/alz.13016 · Cited by 3,212 · see citing works
Doherty, G. J., & McMahon, H. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.110540 · Cited by 3,075 · see citing works
The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease
Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059 · see citing works
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538 · see citing works
Molecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223 · see citing works
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942 · see citing works
Donanemab in Early Alzheimer’s Disease
Mintun, M. A., Lo, A. C., Duggan Evans, C., Wessels, A. M., Ardayfio, P. A., Andersen, S. W., Shcherbinin, S., Sparks, J., Sims, J. R., Brys, M., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2100708 · Cited by 1,728 · cited 1× · see citing works
“A β burden can be decreased in some patients, but progression is not completely halted (Sevigny et al., 2016; Mintun et al., 2021; Swanson et al., 2021; Budd Haeberlein et al., 2022) suggesting that targeting A β is not sufficient to significantly alter other molecular pathways involved in later…”
Mechanisms of clathrin-mediated endocytosis
Kaksonen, M., & Roux, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.132 · Cited by 1,698 · see citing works
The role of apolipoprotein E in Alzheimer's disease
Kim, J., Basak, J. M., & Holtzman, D. M. (2009) · Neuron · doi:10.1016/j.neuron.2009.06.026 · Cited by 1,661 · see citing works
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · see citing works
Key principles and methods for studying the endocytosis of biological and nanoparticle therapeutics
Rennick, J. J., Johnston, A. P. R., & Parton, R. G. (2021) · Nature Nanotechnology · doi:10.1038/s41565-021-00858-8 · Cited by 1,500 · see citing works
Mechanisms of action of hydroxychloroquine and chloroquine:implications for rheumatology
Schrezenmeier, E., & Dörner, T. (2020) · Nature Reviews Rheumatology · doi:10.1038/s41584-020-0372-x · Cited by 1,468 · see citing works
The Rotterdam Study: objectives and design update
Albert Hofman, D., Breteler, M. M. B., van Duijn, C. M., Krestin, G. P., Pols, H. A. P., Stricker, B. H. C., Tiemeier, H. W., Uitterlinden, A. G., Vingerling, J. R., & Witteman, J. C. M. (2007) · European Journal of Epidemiology · doi:10.1007/s10654-007-9199-x · Cited by 1,404 · see citing works
Two Randomized Phase 3 Studies of Aducanumab in Early Alzheimer's Disease
Budd Haeberlein, S., Aisen, P. S., Barkhof, F., Chalkias, S., Chen, T., Cohen, S., Dent, G., Hansson, O., Harrison, K., von Hehn, C., et al. (2022) · The Journal of Prevention of Alzheimer's Disease · doi:10.14283/jpad.2022.30 · Cited by 1,367 · see citing works
Rajan, K. B., Weuve, J., Barnes, L. L., McAninch, E. A., Wilson, R. S., & Evans, D. A. (2021) · Alzheimer's & Dementia · doi:10.1002/alz.12362 · Cited by 1,268 · see citing works
Synaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo
Cirrito, J. R., Yamada, K. A., Finn, M. B., Sloviter, R. S., Bales, K. R., May, P. C., Schoepp, D. D., Paul, S. M., Mennerick, S., & Holtzman, D. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.10.028 · Cited by 1,265 · see citing works
Probing sporadic and familial Alzheimer’s disease using induced pluripotent stem cells
Israel, M. A., Yuan, S. H., Bardy, C., Reyna, S. M., Mu, Y., Herrera, C., Hefferan, M. P., Van Gorp, S., Nazor, K. L., Boscolo, F. S., et al. (2012) · Nature · doi:10.1038/nature10821 · Cited by 1,253 · see citing works
Lin, Y.-T., Seo, J., Gao, F., Feldman, H. M., Wen, H.-L., Penney, J., Cam, H. P., Gjoneska, E., Raja, W. K., Cheng, J., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.05.008 · Cited by 1,125 · see citing works
Targeting Strategies for Tissue-Specific Drug Delivery
Zhao, Z., Ukidve, A., Kim, J., & Mitragotri, S. (2020) · Cell · doi:10.1016/j.cell.2020.02.001 · Cited by 1,114 · see citing works
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991 · see citing works
Evidence that production and release of amyloid beta-protein involves the endocytic pathway
Koo, E. H., & Squazzo, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32449-3 · Cited by 989 · see citing works
APP processing in Alzheimer’s disease.
Zhang, Y.-W., Thompson, R., Zhang, H., & Xu, H. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-3 · Cited by 983 · see citing works
Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis.
Stenmark, H., Parton, R. G., Steele‐Mortimer, O., Lütcke, A., Gruenberg, J., & Zerial, M. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06381.x · Cited by 968 · see citing works
Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954 · see citing works
Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859 · see citing works
Swanson, C. J., Zhang, Y., Dhadda, S., Wang, J., Kaplow, J., Lai, R. Y. K., Lannfelt, L., Bradley, H., Rabe, M., Koyama, A., et al. (2021) · Alzheimer's Research & Therapy · doi:10.1186/s13195-021-00813-8 · Cited by 847 · see citing works
Regulation of synaptic connectivity by glia.
Eroglu, C., & Barres, B. A. (2010) · Nature · doi:10.1038/nature09612 · Cited by 813 · see citing works
Cataldo, A., Peterhoff, C., Troncoso, J., Gómez-Isla, T., Hyman, B., & Nixon, R. (2000) · American Journal of Pathology · doi:10.1016/s0002-9440(10)64538-5 · Cited by 789 · see citing works
Astrocyte Reactivity: Subtypes, States, and Functions in CNS Innate Immunity
Sofroniew, M. V. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.07.004 · Cited by 721 · see citing works
Man, H., Lin, J., Ju, W. H., Ahmadian, G., Liu, L., Becker, L. E., Sheng, M., & Wang, Y. T. (2000) · Neuron · doi:10.1016/s0896-6273(00)81067-3 · Cited by 698 · see citing works
Endocytosis Is Required for Synaptic Activity-Dependent Release of Amyloid-β In Vivo
Cirrito, J. R., Kang, J.-E., Lee, J., Stewart, F. R., Verges, D. K., Silverio, L. M., Bu, G., Mennerick, S., & Holtzman, D. M. (2008) · Neuron · doi:10.1016/j.neuron.2008.02.003 · Cited by 635 · see citing works
To degrade or not to degrade: Mechanisms and significance of endocytic recycling
Cullen, P. J., & Steinberg, F. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0053-7 · Cited by 590 · see citing works
Microglia, neuroinflammation, and beta-amyloid protein in Alzheimer’s disease
Cai, Z., Hussain, M. D., & Yan, L.-J. (2014) · International Journal of Neuroscience · doi:10.3109/00207454.2013.833510 · Cited by 583 · see citing works
Apolipoprotein E promotes astrocyte colocalization and degradation of deposited amyloid-β peptides
Koistinaho, M., Lin, S., Wu, X., Esterman, M., Koger, D., Hanson, J., Higgs, R., Liu, F., Malkani, S., Bales, K. R., et al. (2004) · Nature Medicine · doi:10.1038/nm1058 · Cited by 571 · see citing works
Actin dynamics counteract membrane tension during clathrin-mediated endocytosis
Boulant, S., Kural, C., Zeeh, J., Ubelmann, F., & Kirchhausen, T. L. (2011) · Nature Cell Biology · doi:10.1038/ncb2307 · Cited by 547 · see citing works
Wu, J. W., Herman, M., Liu, L., Simoes, S., Acker, C. M., Figueroa, H., Steinberg, J. I., Margittai, M., Kayed, R., Zurzolo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394528 · Cited by 537 · see citing works
Clathrin-independent pathways of endocytosis
Mayor, S., Parton, R. G., & Donaldson, J. G. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016758 · Cited by 525 · see citing works
Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation
Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516 · cited 1× · see citing works
“How microglia contribute to Tau pathology is reviewed in depth elsewhere (Das et al., 2020; Ayyubova, 2023; Chen and Yu, 2023; Ou-Yang et al., 2023”
Heckmann, B. L., Teubner, B. J. W., Tummers, B., Boada-Romero, E., Harris, L., Yang, M., Guy, C. S., Zakharenko, S. S., & Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.05.056 · Cited by 503 · see citing works
Astrocytes and microglia: In sickness and in health
Vainchtein, I. D., & Molofsky, A. V. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.01.003 · Cited by 450 · see citing works
Raj, T., Li, Y. I., Wong, G., Humphrey, J., Wang, M., Ramdhani, S., Wang, Y.-C., Ng, B., Gupta, I., Haroutunian, V., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0238-1 · Cited by 430 · see citing works
Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology
GERAD consortium, Chapuis, J., Hansmannel, F., Gistelinck, M., Mounier, A., Van Cauwenberghe, C., Kolen, K. V., Geller, F., Sottejeau, Y., Harold, D., et al. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.1 · Cited by 407 · see citing works
Nixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400 · cited 2× · see citing works
“These defects then result in various neuropathological outcomes such as A β 1-42 over production and clearance deficits, as well as dystrophic neurites (Nixon, 2017; Colacurcio et al., 2018; Szabo et al., 2022).”
The Rotterdam Study: 2016 objectives and design update
Albert Hofman, D., Brusselle, G., Murad, S. D., van Duijn, C. M., Franco, O. H., Goedegebure, A., Ikram, M. A., Klaver, C. C. W., Nijsten, T. E. C., Peeters, R. P., et al. (2015) · European Journal of Epidemiology · doi:10.1007/s10654-015-0082-x · Cited by 382 · see citing works
Cataldo, A. M., Petanceska, S., Terio, N. B., Peterhoff, C. M., Durham, R., Mercken, M., Mehta, P. D., Buxbaum, J., Haroutunian, V., & Nixon, R. A. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.027 · Cited by 363 · see citing works
Alzheimer's disease associated with Down syndrome: a genetic form of dementia
Fortea, J., Zaman, S. H., Hartley, S., Rafii, M. S., Head, E., & Carmona-Iragui, M. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(21)00245-3 · Cited by 357 · see citing works
Neuritic regeneration and synaptic reconstruction induced by withanolide A
Kuboyama, T., Tohda, C., & Komatsu, K. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706122 · Cited by 339 · see citing works
Alzheimer’s Disease: An Updated Overview of Its Genetics
Andrade-Guerrero, J., Santiago-Balmaseda, A., Jeronimo-Aguilar, P., Vargas-Rodríguez, I., Cadena-Suárez, A. R., Sánchez-Garibay, C., Pozo-Molina, G., Méndez-Catalá, C. F., Cardenas-Aguayo, M.-D.-C., Diaz-Cintra, S., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043754 · Cited by 336 · see citing works
Microglia Phenotypes in Aging and Neurodegenerative Diseases
Wendimu, M. Y., & Hooks, S. B. (2022) · Cells · doi:10.3390/cells11132091 · Cited by 336 · see citing works
The Endosomal-Lysosomal System of Neurons in Alzheimer's Disease Pathogenesis: A Review
Nixon, R., Cataldo, A., & Mathews, P. (2000) · Neurochemical Research · doi:10.1023/a:1007675508413 · Cited by 332 · see citing works
Kwart, D., Gregg, A., Scheckel, C., Murphy, E. A., Paquet, D., Duffield, M. D., Fak, J. J., Olsen, O., Darnell, R. B., & Tessier‐Lavigne, M. (2019) · Neuron · doi:10.1016/j.neuron.2019.07.010 · Cited by 317 · see citing works
ApoE Cascade Hypothesis in the pathogenesis of Alzheimer’s disease and related dementias
Martens, Y. A., Zhao, N., Liu, C.-C., Kanekiyo, T., Yang, A. J., Goate, A. M., Holtzman, D. M., & Bu, G. (2022) · Neuron · doi:10.1016/j.neuron.2022.03.004 · Cited by 316 · see citing works
A prospective 20‐year longitudinal follow‐up of dementia in persons with Down syndrome
McCarron, M., McCallion, P., Reilly, E., Dunne, P., Carroll, R., & Mulryan, N. (2017) · Journal of Intellectual Disability Research · doi:10.1111/jir.12390 · Cited by 295 · see citing works
Söllvander, S., Nikitidou, E., Brolin, R., Söderberg, L., Sehlin, D., Lannfelt, L., & Erlandsson, A. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0098-z · Cited by 267 · see citing works
Loss of Bin1 Promotes the Propagation of Tau Pathology
Calafate, S., Flavin, W., Verstreken, P., & Moechars, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.063 · Cited by 265 · see citing works
Ginsberg, S. D., Alldred, M. J., Counts, S., Cataldo, A. M., Neve, R. L., Jiang, Y., Wuu, J., Chao, M. V., Mufson, E. J., Nixon, R. A., et al. (2010) · Biological Psychiatry · doi:10.1016/j.biopsych.2010.05.030 · Cited by 257 · see citing works
TFEB enhances astroglial uptake of extracellular tau species and reduces tau spreading
Martini-Stoica, H., Cole, A. L., Swartzlander, D. B., Chen, F., Wan, Y.-W., Bajaj, L., Bader, D. A., Lee, V. M. Y., Trojanowski, J. Q., Liu, Z., et al. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20172158 · Cited by 253 · see citing works
Usenovic, M., Niroomand, S., Drolet, R. E., Yao, L., Gaspar, R. C., Hatcher, N. G., Schachter, J., Renger, J. J., & Parmentier-Batteur, S. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.1523-15.2015 · Cited by 245 · see citing works
NMDA Di-Heteromeric Receptor Populations and Associated Proteins in Rat Hippocampus
Al‐Hallaq, R. A., Conrads, T. P., Veenstra, T. D., & Wenthold, R. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2155-07.2007 · Cited by 244 · see citing works
Root, J. T., Merino, P., Nuckols, A., Johnson, M. A., & Kukar, T. L. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105360 · Cited by 230 · see citing works
van Gool, W. A., Weinstein, H. C., Scheltens, P., & Walstra, G. J. M. (2001) · The Lancet · doi:10.1016/s0140-6736(01)05623-9 · Cited by 210 · see citing works
Yao, P. J., Zhu, M., Pyun, E. I., Brooks, A. I., Therianos, S., Meyers, V. E., & Coleman, P. D. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(02)00009-8 · Cited by 205 · see citing works
Glial Cell-Mediated Neuroinflammation in Alzheimer’s Disease
Al-Ghraiybah, N. F., Wang, J., Alkhalifa, A. E., Roberts, A. B., Raj, R., Yang, E., & Kaddoumi, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810572 · Cited by 204 · see citing works
Congdon, E. E., Gu, J., Sait, H. B. R., & Sigurdsson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.491001 · Cited by 195 · see citing works
Evans, L., Wassmer, T., Fraser, G. M., Smith, J. C., Perkinton, M. S., Billinton, A., & Livesey, F. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.021 · Cited by 187 · see citing works
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 · see citing works
Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99)
Jiang, Y., Sato, Y., Im, E., Berg, M., Bordi, M., Darji, S., Kumar, A., Mohan, P. S., Bandyopadhyay, U., Diaz, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0578-19.2019 · Cited by 166 · see citing works
Endosomal Traffic Jams Represent a Pathogenic Hub and Therapeutic Target in Alzheimer’s Disease
Small, S. A., Simoes, S., Mayeux, R. P., & Petsko, G. A. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.08.003 · Cited by 163 · see citing works
Endocytic membrane trafficking and neurodegenerative disease
Schreij, A. M. A., Fon, E. A., & McPherson, P. S. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2105-x · Cited by 153 · see citing works
Alzheimer's disease first symptoms are age dependent: Evidence from the NACC dataset
Barnes, J., Dickerson, B. C., Frost, C. D., Jiskoot, L. C., Wolk, D. A., & van der Flier, W. M. (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2014.12.007 · Cited by 152 · see citing works
De Rossi, P., Buggia-Prévot, V., Clayton, B. L. L., Vasquez, J. B., van Sanford, C., Andrew, R. J., Lesnick, R., Botté, A., Deyts, C., Salem, S., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0124-1 · Cited by 151 · see citing works
The aging lysosome: An essential catalyst for late-onset neurodegenerative diseases
Nixon, R. A. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140443 · Cited by 149 · see citing works
NMDA and AMPA receptors dysregulation in Alzheimer's disease
Babaei, P. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174310 · Cited by 149 · see citing works
Clathrin Adaptor AP-2 Is Essential for Early Embryonal Development
Mitsunari, T., Nakatsu, F., Shioda, N., Love, P. E., Grinberg, A., Bonifacino, J. S., & Ohno, H. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9318-9323.2005 · Cited by 142 · see citing works
Ando, K., Brion, J.-P., Stygelbout, V., Suain, V., Authelet, M., Dedecker, R., Chanut, A., Lacor, P., Lavaur, J., Sazdovitch, V., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1111-z · Cited by 136 · see citing works
Phagocytosis of full-length Tau oligomers by Actin-remodeling of activated microglia
Das, R. R., Balmik, A. A., & Chinnathambi, S. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1694-y · Cited by 129 · see citing works
Revisiting the Role of Clathrin-Mediated Endoytosis in Synaptic Vesicle Recycling
Milosevic, I. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00027 · Cited by 122 · see citing works
Distribution and Expression of Picalm in Alzheimer Disease
Baig, S., Joseph, S. A., Tayler, H., Abraham, R., Owen, M. J., Williams, J., Kehoe, P. G., & Love, S. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181f52e01 · Cited by 115 · see citing works
Wesén, E. V., Jeffries, G. D. M., Dzebo, M. M., & Esbjörner, E. K. (2017) · Scientific Reports · doi:10.1038/s41598-017-02227-9 · Cited by 114 · see citing works
Puangmalai, N., Bhatt, N. N., Montalbano, M., Sengupta, U., Gaikwad, S., Ventura, F. L., McAllen, S., Ellsworth, A., García, S., & Kayed, R. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2503-3 · Cited by 110 · see citing works
Spreading of tau pathology in A lzheimer's disease by cell‐to‐cell transmission
Mohamed, N., Herrou, T., Plouffe, V., Piperno, N., & Leclerc, N. M. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12229 · Cited by 110 · see citing works
Oligomer-specific Aβ toxicity in cell models is mediated by selective uptake
Chafekar, S. M., Baas, F., & Scheper, W. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.06.003 · Cited by 110 · see citing works
Amyloid-β(1–42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity
Jin, S., Kedia, N., Illes‐Toth, E., Haralampiev, I., Prisner, S., Herrmann, A., Wanker, E. E., & Bieschke, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691840 · Cited by 109 · see citing works
New therapeutics beyond amyloid-β and tau for the treatment of Alzheimer’s disease
Zhang, F., Zhong, R.-J., Cheng, C., Li, S., & Le, W.-D. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-00565-5 · Cited by 105 · see citing works
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 · see citing works
Current Status of Clinical Trials on Tau Immunotherapies
Ji, C., & Sigurdsson, E. M. (2021) · Drugs · doi:10.1007/s40265-021-01546-6 · Cited by 96 · see citing works
Modes and mechanisms of synaptic vesicle recycling
Soykan, T., Maritzen, T., & Haucke, V. (2016) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2016.03.005 · Cited by 94 · see citing works
Amyloid‐β impairs the phagocytosis of dystrophic synapses by astrocytes in Alzheimer's disease
Sanchez‐Mico, M. V., Jimenez, S., Gomez‐Arboledas, A., Muñoz‐Castro, C., Romero‐Molina, C., Navarro, V., Sanchez‐Mejias, E., Nuñez‐Diaz, C., Sanchez‐Varo, R., Galea, E., et al. (2021) · Glia · doi:10.1002/glia.23943 · Cited by 93 · see citing works
Clathrin-mediated endocytosis and Alzheimer's disease: An update
Wu, F., & Yao, P. J. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.03.002 · Cited by 92 · see citing works
Ratan, Y., Rajput, A., Maleysm, S., Pareek, A., Jain, V. K., Pareek, A., Kaur, R., & Singh, G. (2023) · Biomedicines · doi:10.3390/biomedicines11051398 · Cited by 87 · see citing works
Thal, D. R., & Tomé, S. O. (2022) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2022.10.006 · Cited by 85 · see citing works
Pechstein, A., Bacetic, J., Vahedi‐Faridi, A., Gromova, K. V., Sundborger, A., Tomlin, N., Krainer, G., Vorontsova, O. V., Schäfer, J. G., Owe, S. G., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911073107 · Cited by 85 · see citing works
The Role of Microglia in Sporadic Alzheimer’s Disease
Streit, W. J., Khoshbouei, H., & Bechmann, I. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201248 · Cited by 84 · see citing works
The role of Alzheimer's disease risk genes in endolysosomal pathways
Szabo, M. P., Mishra, S., Knupp, A., & Young, J. E. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105576 · Cited by 81 · see citing works
Amyloid-Targeting Monoclonal Antibodies for Alzheimer Disease
Rabinovici, G. D., & La Joie, R. (2023) · JAMA · doi:10.1001/jama.2023.11703 · Cited by 80 · see citing works
Ceja, B. T., & Olsen, M. L. (2022) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2022.102550 · Cited by 80 · see citing works
PICALM Rescues Endocytic Defects Caused by the Alzheimer’s Disease Risk Factor APOE4
Narayan, P., Sienski, G., Bonner, J. M., Lin, Y.-T., Seo, J., Baru, V., Haque, A., Milo, B., Akay, L. A., Graziosi, A., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108224 · Cited by 75 · see citing works
Guntupalli, S., Jang, S. E., Zhu, T., Huganir, R. L., Widagdo, J., & Anggono, V. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.774554 · Cited by 70 · see citing works
The Chemical Inhibitors of Endocytosis: From Mechanisms to Potential Clinical Applications
Szewczyk-Roszczenko, O. K., Roszczenko, P., Shmakova, A., Finiuk, N. S., Holota, S. M., Lesyk, R., Bielawska, A., Vassetzky, Y. S., & Bielawski, K. (2023) · Cells · doi:10.3390/cells12182312 · Cited by 70 · see citing works
Omtri, R. S., Davidson, M. W., Arumugam, B., Poduslo, J. F., & Kandimalla, K. K. (2012) · Molecular Pharmaceutics · doi:10.1021/mp200530q · Cited by 68 · see citing works
Tesi, N., van der Lee, S. J., Hulsman, M., Jansen, I. E., Stringa, N., van Schoor, N. M., Scheltens, P., van der Flier, W. M., Huisman, M., Reinders, M. J. T., et al. (2020) · Translational Psychiatry · doi:10.1038/s41398-020-01018-7 · Cited by 67 · see citing works
Kim, S., Cho, Y.-S., Kim, Y., Park, J., Yoo, S., Gwak, J., Kim, Y., Gwon, Y., Kam, T., & Jung, Y. (2023) · Autophagy · doi:10.1080/15548627.2023.2181614 · Cited by 65 · see citing works
Imaging and Modeling the Dynamics of Clathrin-Mediated EndocytosisPreprint
Mettlen, M., & Danuser, G. M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a017038 · Cited by 61 · see citing works
Misfolded amyloid-β-42 impairs the endosomal–lysosomal pathway
Marshall, K. E., Vadukul, D. M., Staras, K., & Serpell, L. C. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03464-4 · Cited by 59 · see citing works
Upregulation of APP endocytosis by neuronal aging drives amyloid-dependent synapse loss
Burrinha, T., Martinsson, I., Gomes, R. A., Terrasso, A. P., Gouras, G. K., & Almeida, C. G. (2021) · Journal of Cell Science · doi:10.1242/jcs.255752 · Cited by 56 · see citing works
Synaptic frailty and clathrin-mediated synaptic vesicle trafficking in Alzheimer's disease
Yao, P. J. (2003) · Trends in Neurosciences · doi:10.1016/j.tins.2003.10.012 · Cited by 55 · see citing works
Thomas, R. S., Henson, A., Gerrish, A., Jones, L., Williams, J., & Kidd, E. J. (2016) · BMC Neuroscience · doi:10.1186/s12868-016-0288-1 · Cited by 55 · see citing works
Lacour, M., Quenez, O., Rovelet‐Lecrux, A., Salomon, B., Rousseau, S., Richard, A., Quillard‐Muraine, M., Pasquier, F., Rollin‐Sillaire, A., Martinaud, O., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190193 · Cited by 53 · see citing works
Brain clearance of protein aggregates: a close-up on astrocytes
Giusti, V., Kaur, G., Giusto, E., & Civiero, L. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00703-1 · Cited by 52 · see citing works
Varma, V. R., Desai, R. J., Navakkode, S., Wong, L., Anerillas, C., Loeffler, T., Schilcher, I., Mahesri, M., Chin, K., Horton, D. B., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01912-0 · Cited by 51 · see citing works
Impact of late-onset Alzheimer’s genetic risk factors on beta-amyloid endocytic production
Almeida, C. G., Mirfakhar, F. S., Perdigão, C., & Burrinha, T. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2825-9 · Cited by 48 · see citing works
Yao, P. J., Morsch, R., Callahan, L. M., & Coleman, P. D. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00360-7 · Cited by 48 · see citing works
Aβ and Tau Regulate Microglia Metabolism via Exosomes in Alzheimer’s Disease
Zhao, Y., Liu, B., Wang, J., Xu, L., Yu, S., Fu, J., Yan, X., & Su, J. (2022) · Biomedicines · doi:10.3390/biomedicines10081800 · Cited by 47 · see citing works
Tau internalization: A complex step in tau propagation
Zhao, J., Wu, H., & Tang, X. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101272 · Cited by 46 · see citing works
Endocytic Adaptor Proteins in Health and Disease: Lessons from Model Organisms and Human Mutations
Azarnia Tehran, D., López-Hernández, T., & Maritzen, T. (2019) · Cells · doi:10.3390/cells8111345 · Cited by 44 · see citing works
Eltom, K., Mothes, T., Libard, S., Ingelsson, M., & Erlandsson, A. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01745-8 · Cited by 44 · see citing works
Ahmad, S., Bannister, C. A., van der Lee, S. J., Vojinović, D., Adams, H. H. H., Ramı́rez, A., Escott‐Price, V., Sims, R., Baker, E. A., Williams, J. H., et al. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.01.005 · Cited by 44 · see citing works
Alsaqati, M., Thomas, R. S., & Kidd, E. J. (2018) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glx135 · Cited by 43 · see citing works
Changed Clathrin Regulatory Proteins in the Brains of Alzheimer's Disease Patients and Animal Models
Cao, Y., Xiao, Y. C., Ravid, R., & Guan, Z. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100162 · Cited by 43 · see citing works
Knockin’ on heaven’s door: Molecular mechanisms of neuronal tau uptake
La‐Rocque, S. D., Moretto, E., Butnaru, I., & Schiavo, G. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15144 · Cited by 42 · see citing works
Domínguez-Prieto, M., Velasco, A. L., Tabernero, A., & Medina, J. M. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180332 · Cited by 42 · see citing works
Thomas, R. S., Lelos, M. J., Good, M. A., & Kidd, E. J. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.10.131 · Cited by 41 · see citing works
Alzheimer's Disease: Tau Pathology and Dysfunction of Endocytosis
Ando, K., Houben, S., Homa, M., de Fisenne, M.-A., Potier, M., Erneux, C., Brion, J., & Leroy, K. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.583755 · Cited by 39 · see citing works
The Shaping of AMPA Receptor Surface Distribution by Neuronal Activity
Chater, T. E., & Goda, Y. (2022) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2022.833782 · Cited by 37 · see citing works
Traffic jam hypothesis: Relationship between endocytic dysfunction and Alzheimer's disease
Kimura, N., & Yanagisawa, K. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.07.002 · Cited by 37 · see citing works
Piras, I. S., Krate, J., Delvaux, E., Nolz, J., Both, M. D. D., Mastroeni, D., Serrano, G. E., Sue, L. I., Beach, T. G., Coleman, P. D., et al. (2019) · Brain Research · doi:10.1016/j.brainres.2019.06.004 · Cited by 36 · see citing works
Fujikura, M., Iwahara, N., Hisahara, S., Kawamata, J., Matsumura, A., Yokokawa, K., Saito, T., Manabe, T., Matsushita, T., Suzuki, S., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180904 · Cited by 35 · see citing works
Translational gene mapping of cognitive decline
Wilmot, B., McWeeney, S. K., Nixon, R. R., Montine, T. J., Laut, J., Harrington, C. A., Kaye, J. A., & Kramer, P. L. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.11.008 · Cited by 35 · see citing works
Dysfunctional microglia and tau pathology in Alzheimer’s disease
Ayyubova, G. (2022) · Reviews in the Neurosciences · doi:10.1515/revneuro-2022-0087 · Cited by 35 · see citing works
Song, M.-S., Baker, G. B., Todd, K. G., & Kar, S. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2010.12.055 · Cited by 34 · see citing works
Hori, T., Eguchi, K., Wang, H.-Y., Miyasaka, T., Guillaud, L., Taoufiq, Z., Mahapatra, S., Yamada, H., Takei, K., & Takahashi, T. (2022) · eLife · doi:10.7554/elife.73542 · Cited by 34 · see citing works
Ni, J., Xie, Z., Quan, Z., Meng, J., & Qing, H. (2023) · Glia · doi:10.1002/glia.24465 · Cited by 33 · see citing works
Amphiphysin-1 protein level changes associated with tau-mediated neurodegeneration
Jesús‐Cortés, H. D., Nogueras‐Ortiz, C. J., Gearing, M., Arnold, S. E., & Vega, I. E. (2012) · Neuroreport · doi:10.1097/wnr.0b013e32835982ce · Cited by 31 · see citing works
Nuripa, A., Kamino, K., Kimura, R., Yamamoto, M. L., Morihara, T., Kazui, H., Hashimoto, R., Tanaka, T., Kudo, T., Kida, T., et al. (2008) · Journal of Human Genetics · doi:10.1007/s10038-008-0251-9 · Cited by 30 · see citing works
Involvement of clathrin light chains in the pathology of Alzheimer's disease
Nakamura, Y., Takeda, M., Yoshimi, K., Hattori, H., Hariguchi, S., Kitajima, S., Hashimoto, S., & Nishimura, T. (1994) · Acta Neuropathologica · doi:10.1007/bf00386251 · Cited by 30 · see citing works
Tehran, D. A., Kochlamazashvili, G., Pampaloni, N. P., Sposini, S., Shergill, J. K., Lehmann, M., Pashkova, N., Schmidt, C., Löwe, D., Napieczyńska, H., et al. (2022) · Science Advances · doi:10.1126/sciadv.abl5032 · Cited by 29 · see citing works
Endosomal‐lysosomal dysfunctions in Alzheimer’s disease: Pathogenesis and therapeutic interventions
Lai, S. S. M., Ng, K. Y., Koh, R. Y., Chok, K. C., & Chye, S. M. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00737-0 · Cited by 28 · see citing works
The Role of Synaptic Dysfunction in Alzheimer’s Disease
Pei, Y. A., Davies, J., Zhang, M., & Zhang, H. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191334 · Cited by 28 · see citing works
Tau Oligomers in Sera of Patients with Alzheimer’s Disease and Aged Controls
Kolarova, M., Sengupta, U., Bartos, A., Ricny, J., & Kayed, R. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170048 · Cited by 27 · see citing works
Xie, A., Hou, T., Xiong, W., Huang, H., Zheng, J., Li, K., Man, H., Hu, Y., Han, Z., Zhang, H., et al. (2019) · Aging Cell · doi:10.1111/acel.12929 · Cited by 27 · see citing works
Decrease of dynamin 2 levels in late-onset Alzheimer’s disease alters Aβ metabolism
Kamagata, E., Kudo, T., Kimura, R., Tanimukai, H., Morihara, T., Sadik, M. G., Kamino, K., & Takeda, M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.147 · Cited by 27 · see citing works
Inhibition of clathrin-mediated endocytosis prevents amyloid β-induced axonal damage
Kuboyama, T., Lee, Y., Nishiko, H., & Tohda, C. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.02.005 · Cited by 26 · see citing works
Jang, S. K., Yu, J. M., Kim, S. T., Kim, G. H., Park, D. W., Lee, D. I., & Joo, S. S. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.03.071 · Cited by 26 · see citing works
Implication of tau propagation on neurodegeneration in Alzheimer’s disease
Lamontagne-Kam, D., Ulfat, A. K., Hervé, V., Vu, T.-M., & Brouillette, J. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1219299 · Cited by 25 · see citing works
The function of astrocytes and their role in neurological diseases
Yuan, W., Huang, W., Jiang, Y., Xu, H., Duan, C., Chen, N., Liu, Y., & Fu, X. (2023) · European Journal of Neuroscience · doi:10.1111/ejn.16160 · Cited by 24 · see citing works
The Amyloid Cascade Hypothesis 2.0: Generalization of the Concept
Volloch, V., & Rits‐Volloch, S. (2022) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-220079 · Cited by 21 · see citing works
Molecular Regulation Mechanism of Microglial Autophagy in the Pathology of Alzheimer's Disease
Ou-Yang, P., Cai, Z., & Zhang, Z.-H. (2023) · Aging and Disease · doi:10.14336/ad.2023.0106 · Cited by 21 · see citing works
Cell type-specific functions of Alzheimer's disease endocytic risk genes
Maninger, J., Nowak, K., Goberdhan, S., O’Donoghue, R., & Connor‐Robson, N. (2024) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2022.0378 · Cited by 21 · see citing works
Exploring the potential role of rab5 protein in endo-lysosomal impairment in Alzheimer’s disease
Behl, T., Kaur, D., Sehgal, A., Singh, S., Makeen, H. A., Albratty, M., Abdellatif, A. A. H., Dachani, S. R., & BUNGAU, S. G. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112773 · Cited by 20 · see citing works
Endosome Dysregulation in Down Syndrome: A Potential Contributor to Alzheimer Disease Pathology
Filippone, A., & Praticò, D. (2021) · Annals of Neurology · doi:10.1002/ana.26042 · Cited by 20 · see citing works
Focusing on cellular biomarkers: The endo-lysosomal pathway in Down syndrome.
Botté, A., & Potier, M. (2020) · Progress in Brain Research · doi:10.1016/bs.pbr.2019.10.002 · Cited by 20 · see citing works
Schork, N. J., Elman, J. A., & Initiative, A. D. N. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230548 · Cited by 20 · see citing works
Endocytosis Is a Key Mode of Interaction between Extracellular β-Amyloid and the Cell Membrane
Shi, J., Zhu, L., Lan, X., Zhao, D.-W., He, Y., Sun, Z.-Q., Wu, D., & Li, H. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.07.035 · Cited by 19 · see citing works
Zhang, X., Zou, L., Tang, L., Xiong, M., Yan, X., Meng, L., Chen, G., Xiong, J., Nie, S., Zhang, Z., et al. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002470 · Cited by 19 · see citing works
Brezováková, V., Syková, E., & Jadhav, S. (2022) · Cells · doi:10.3390/cells11091429 · Cited by 18 · see citing works
Cuddy, L. K., Alia, A. O., Salvo, M. A., Chandra, S., Grammatopoulos, T. N., Justman, C. J., Lansbury, P. T., Mazzulli, J. R., & Vassar, R. J. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00561-9 · Cited by 17 · see citing works
Yao, P. J. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00228-1 · Cited by 17 · see citing works
Endosomal trafficking and related genetic underpinnings as a hub in Alzheimer's disease
Limone, A., Veneruso, I., D’Argenio, V., & Sarnataro, D. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30864 · Cited by 16 · see citing works
Recent Trends in Active and Passive Immunotherapies of Alzheimer’s Disease
Alshamrani, M. (2023) · Antibodies · doi:10.3390/antib12020041 · Cited by 16 · see citing works
Alpha adaptins show isoform‐specific association with neurofibrillary tangles in Alzheimer's disease
Srinivasan, S., Gál, J., Bachstetter, A. D., & Nelson, P. T. (2021) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12776 · Cited by 15 · see citing works
Volloch, V., & Rits‐Volloch, S. (2022) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-220031 · Cited by 14 · see citing works
Theerasri, A., Janpaijit, S., Tencomnao, T., & Prasansuklab, A. (2022) · WIREs Mechanisms of Disease · doi:10.1002/wsbm.1591 · Cited by 13 · see citing works
Dynein dysfunction disrupts β-amyloid clearance in astrocytes through endocytic disturbances
Kimura, N., Okabayashi, S., & Ono, F. (2014) · Neuroreport · doi:10.1097/wnr.0000000000000124 · Cited by 13 · see citing works
Upregulation of endocytic protein expression in the Alzheimer’s disease male human brain
Alsaqati, M., Thomas, R. S., & Kidd, E. J. (2023) · Aging Brain · doi:10.1016/j.nbas.2023.100084 · Cited by 10 · see citing works
Wesén, E. V., Lundmark, R., & Esbjörner, E. K. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00053 · Cited by 9 · see citing works
Malakooti, N., Fowler, C., Volitakis, I., Ca, M., Rc, K., Ai, B., Rembach, A., Ma, P., Finkelstein, D. I., & Pa, A. (2019) · PubMed · doi:10.4172/2161-0460.1000462 · Cited by 9 · see citing works
The Oligomeric Form of Amyloid Beta Triggers Astrocyte Activation, Independent of Neurons
Mun, B.-R., Park, S.-B., & Choi, W. (2024) · Chonnam Medical Journal · doi:10.4068/cmj.2024.60.1.27 · Cited by 5 · see citing works
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Ullah, M., Akbar, S., Raza, A., Khan, K. A., & Zou, Q. (2024) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf026 · Cited by 48 · see citing works
Amyloid-β oligomers increase the binding and internalization of tau oligomers in human synapses
Kadamangudi, S., Marcatti, M., Zhang, W.-R., Fracassi, A., Kayed, R., Limon, A., & Taglialatela, G. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02839-2 · Cited by 25 · see citing works
Jury-Garfe, N., Redding-Ochoa, J., You, Y., Martínez, P., Karahan, H., Chimal-Juárez, E., Johnson, T. S., Zhang, J., Resnick, S., Kim, J., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02775-1 · Cited by 22 · see citing works
“These mechanisms has been shown to be impaired in AD brains [45, 55].”
BackgroundNjoku, G. C., & Kanmogne, G. D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26189069 · Cited by 15 · see citing works
Fei, J., Zheng, Y., LaLonde, C., Tao, Y., & Zhou, R. (2026) · Science Advances · doi:10.1126/sciadv.aeb0803 · Cited by 8 · see citing works
Barr, H. J., Caldwell, S. K., Reimertz, J. M., Depp, C., Walker, A. J., Marsh, S. E., Gupte, A. S., Hingerl, M., Patel, J., Park, S.-O., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.08.693074 · Cited by 8 · see citing works
Jaye, S., Sandau, U. S., McFarland, T. J., Woltjer, R. L., & Saugstad, J. A. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1426180 · Cited by 5 · see citing works
Self-citationHerbert, A. G. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1445540 · Cited by 5 · see citing works
Hudák, A., & Letoha, T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094037 · Cited by 5 · see citing works
KGiA: Drug repurposing through disease-aware knowledge graph augmentation
Oğuztüzün, Ç., Gao, Z., Li, H., & Xu, R. (2025) · Journal of Biomedical Informatics · doi:10.1016/j.jbi.2025.104857 · Cited by 4 · see citing works
Is the Voltage-Dependent Anion Channel a Major Player in Neurodegenerative Diseases?
Neumann, S., & Heumann, R. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136138 · Cited by 4 · see citing works
Clathrin-mediated endocytosis in budding yeast at a glance: animated
Owen, L. M., Riggi, M., Drubin, D. G., Iwasa, J., & Sun, Y. (2025) · Journal of Cell Science · doi:10.1242/jcs.264222 · Cited by 2 · see citing works
Guo, H., Peng, X., Zhang, X. C., Ruganzu, J. B., Wu, X., Zhao, M., Pengbo, Y., Ji, S., & Yang, W. (2026) · Experimental Cell Research · doi:10.1016/j.yexcr.2026.114920 · Cited by 1 · see citing works
Svirsky, S. E., Roberts, A., Parry, M., Henchir, J. J., Dixon, C. E., Jackson, T. C., Chang, Y., Conley, Y., Puccio, A. M., & Carlson, S. W. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05709-y · Cited by 1 · see citing works
Single-cell, multi-region profiling of the macaque brain across the lifespanPreprint
Yang, W., Watkins, K., DeCasien, A. R., O’Neill, M. B., Bohlen, M. O., O’Day, D. R., Duran, M., Qiu, C., Meleshko, A. N., Vo, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.31.685880 · Cited by 1 · see citing works
The Flipons, Infections, and Amyloids that Foreshadow the Fading Memories of Alzheimer’s Disease
Herbert, A. G. (2025) · Neuroscience Insights · doi:10.1177/26331055251338815
Ando, K., Lopez‐Gutierrez, L., Mansour, S., Yilmaz, Z., Dauphinot, L., Verheijen, J., Fontaine, G., Quintanilla‐Sánchez, C., Aydin, E., Doeraene, E., et al. (2026) · Cells · doi:10.3390/cells15030235
Gao, J., Zhu, B. J., Wang, B., Singh, B., Eisa-Beygi, S., Wu, H., Cui, K., Kulandaisamy, A., Huang, W., Wei, W., et al. (2026) · Cardiology Discovery · doi:10.1097/cd9.0000000000000188
BAG3 modulates clathrin-mediated endocytosis and tau uptake in astrocytes
Rodwell‐Bullock, J., Blau, E., Ganguly, A., Deaton, C. A., & Johnson, G. V. W. (2026) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00947.2025
Self-Assembling Short Peptide Carriers for Gene Delivery
An, L., Xu, Z., & Zhang, X. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27083464
Alia, A. O., Urquhart, K., Carson, H., Killinger, B. A., Janson, C., & Romanova, L. Y. (2026) · Acta Neuropathologica Communications · doi:10.64898/2026.05.13.724866
Chinnathambi, S., Baisya, U., & Ananthanarayana, V. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.07.004
3D nanoscale imaging of amyloid-β oligomer interactions with extracellular vesicles by cryo-ET
Khursheed, A., Shang, Q., Zhang, H., Tian, Y., Szwedziak, P., Volkov, V. A., & Viles, J. H. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2610068123
Fan, J.-D., Fu, Y., Li, Q., Zhang, Z.-Q., Zhao, Y., Hao, Q., Tan, L., Tan, M., & Initiative, T. A. D. N. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1875646
Benoist, M., & Vassilopoulos, S. (2026) · Traffic · doi:10.1111/tra.70053
Stage-specific proteomic signatures of synaptopathy in Alzheimer’s diseasePreprint
Georgiades, T., Griffiths, J., Gibbs, F., Chandra, E. A., Papageorgopoulou, M., Liang, D., Whitwell, H. J., Matthews, P. M., Barnes, S. J., Grant, S. G. N., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.02.755976
Zhang, Y., Su, Y., Huang, L., Guan, H., Qiu, Z., & Zou, C. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.117575
- Authors
- Jaye, S., Sandau, U. S., & Saugstad, J. A.
- Affiliations
- Oregon Health & Science University (US)
- Corresponding author
- Saugstad, Julie A.
- Venue
- Frontiers in Aging Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2024-04-17
- Volume
- 16
- Pages
- 1378576-1378576
- ISSN
- 1663-4365 (ISSN-L)
- PMC
- PMC11061891
- OpenAlex
- W4394904573
- Cited by
- 26
- References
- 178
- Citations by year
- 2026: 13 · 2025: 8 · 2024: 5
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Aging Neuroscience (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (RF1AG059392, T32AG055378)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- clathrin-mediated endocytosis, Alzheimer's disease, amyloid-beta, synaptic dysfunction, tau pathology, astrocytes, microglia, neuroinflammation, amyloid-beta clearance
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