The DOI matches its Crossref record; 81 of the 81 references it cites were found in a registry or an index.
Apolipoprotein E aggregation in microglia initiates Alzheimer’s disease pathology by seeding β-amyloidosis
Open accessAbstract
The seeded growth of pathogenic protein aggregates underlies the pathogenesis of Alzheimer's disease (AD), but how this pathological cascade is initiated is not fully understood. Sporadic AD is linked genetically to apolipoprotein E (APOE) and other genes expressed in microglia related to immune, lipid, and endocytic functions. We generated a transgenic knockin mouse expressing HaloTag-tagged APOE and optimized experimental protocols for the biochemical purification of APOE, which enabled us to identify fibrillary aggregates of APOE in mice with amyloid-β (Aβ) amyloidosis and in human AD brain autopsies. These APOE aggregates that stained positive for β sheet-binding dyes triggered Aβ amyloidosis within the endo-lysosomal system of microglia, in a process influenced by microglial lipid metabolism and the JAK/STAT signaling pathway. Taking these observations together, we propose a model for the onset of Aβ amyloidosis in AD, suggesting that the endocytic uptake and aggregation of APOE by microglia can initiate Aβ plaque formation.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“However, Aβ can bind to lipoproteins such as clusterin (ApoJ) and ApoE in the brain82–84, which facilitates its clearance by microglia via TREM281.”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [81]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Although TREM2 has been shown to bind to Aβ and facilitate its uptake80,81, the surface expression changes of other receptors involved in Aβ recognition and uptake might have counteracted the effects of increased TREM2 signaling upon INPP5D haploinsufficiency83,84.”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [81]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Microglia may also play a direct role in the fibrillization of Aβ through the uptake of Aβ bound to ApoE”
From Lipidome and proteome of astrocyte and microglia ApoE lipoprotein reveal differences based on cell type and ApoE isoform (2026) · cites this paper as [12]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Microglia have also been implicated in the initial fibrillization of Aβ, where ApoE and Aβ aggregates colocalize in lysosomes (12).”
From Lipidome and proteome of astrocyte and microglia ApoE lipoprotein reveal differences based on cell type and ApoE isoform (2026) · cites this paper as [12]
The cited source says what the claim attributes to it.
In the citing paper
“where both molecules aggregate in the endolysosomal pathway (12).”
From Lipidome and proteome of astrocyte and microglia ApoE lipoprotein reveal differences based on cell type and ApoE isoform (2026) · cites this paper as [12]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Fiji: an open-source platform for biological-image analysis
Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2019 · Cited by 66,890
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
Neuroinflammation in Alzheimer's disease
Heneka, M. T., Carson, M. J., Khoury, J. E., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)70016-5 · Cited by 6,226
A Unique Microglia Type Associated with Restricting Development of Alzheimer’s Disease
Keren-Shaul, H., Spinrad, A., Weiner, A., Matcovitch-Natan, O., Dvir-Szternfeld, R., Ulland, T. K., David, E., Baruch, K., Lara-Astaiso, D., Toth, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.018 · Cited by 5,493
Scheltens, P., De Strooper, B., Kivipelto, M., Holstege, H., Chételat, G., Teunissen, C. E., Cummings, J., & van der Flier, W. M. (2021) · The Lancet · doi:10.1016/s0140-6736(20)32205-4 · Cited by 5,465
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Self-citationOakley, 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
Krasemann, S., Madore, C., Cialic, R., Baufeld, C., Calcagno, N., El Fatimy, R., Beckers, L., O’Loughlin, E., Xu, Y., Fanek, Z., et al. (2017) · Immunity · doi:10.1016/j.immuni.2017.08.008 · Cited by 2,979
Self-citationCRISPOR: intuitive guide selection for CRISPR/Cas9 genome editing experiments and screens
Concordet, J., & Haeussler, M. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky354 · Cited by 2,392
Jansen, I. E., Savage, J. E., Watanabe, K., Bryois, J., Williams, D. M., Steinberg, S., Sealock, J., Karlsson, I. K., Hägg, S., Athanasiu, L., et al. (2019) · Nature Genetics · doi:10.1038/s41588-018-0311-9 · Cited by 2,277
Hammond, T. R., Dufort, C., Dissing-Olesen, L., Giera, S., Young, A., Wysoker, A., Walker, A. J., Segel, M., Nemesh, J., Saunders, A., et al. (2018) · doi:10.1101/406140 · Cited by 2,225
The Cellular Phase of Alzheimer’s Disease
De Strooper, B., & Karran, E. (2016) · Cell · doi:10.1016/j.cell.2015.12.056 · Cited by 1,990
Microglia in Alzheimer’s disease
Hansen, D. V., Hanson, J. E., & Sheng, M. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709069 · Cited by 1,935
TREM2 Lipid Sensing Sustains the Microglial Response in an Alzheimer’s Disease Model
Wang, Y., Cella, M., Mallinson, K., Ulrich, J. D., Young, K. L., Robinette, M. L., Gilfillan, S., Krishnan, G. M., Sudhakar, S., Zinselmeyer, B. H., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.049 · Cited by 1,736
CNS synaptogenesis promoted by glia-derived cholesterol
Mauch, D. H., Nägler, K., Schumacher, S., Göritz, C., Müller, E.-C., Otto, A., & Pfrieger, F. W. (2001) · Science · doi:10.1126/science.294.5545.1354 · Cited by 1,711
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
Receptor-Mediated Endocytosis: Concepts Emerging from the LDL Receptor System
Goldstein, J. L., Brown, M. S., Anderson, R. G. W., Russell, D. W., & Schneider, W. J. (1985) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.01.110185.000245 · Cited by 1,600
Microglia Biology: One Century of Evolving Concepts
Prinz, M., Jung, S., & Priller, J. (2019) · Cell · doi:10.1016/j.cell.2019.08.053 · Cited by 1,525
Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies
Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425
Single App knock-in mouse models of Alzheimer’s disease
Saito, T., Matsuba, Y., Mihira, N., Takano, J., Nilsson, P., Itohara, S., Iwata, N., & Saido, T. C. (2014) · Nature Neuroscience · doi:10.1038/nn.3697 · Cited by 1,366
Namba, Y., Tomonaga, M., Kawasaki, H., Otomo, E., & Ikeda, K. (1991) · Brain Research · doi:10.1016/0006-8993(91)91092-f · Cited by 1,157
iPSC-derived human microglia-like cells to study neurological diseases
Abud, E. M., Ramirez, R. N., Martinez, E. S., Healy, L. M., Nguyen, C. H. H., Newman, S. A., Yeromin, A. V., Scarfone, V. M., Marsh, S. E., Fimbres, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.042 · Cited by 1,154
APOE and Alzheimer’s disease: Advances in genetics, pathophysiology, and therapeutic approaches
Serrano-Pozo, A., Das, S., & Hyman, B. T. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30412-9 · Cited by 1,037
Wightman, D. P., Jansen, I. E., Savage, J. E., Shadrin, A. A., Bahrami, S., Holland, D., Rongve, A., Børte, S., Winsvold, B. S., Drange, O. K., et al. (2021) · Nature Genetics · doi:10.1038/s41588-021-00921-z · Cited by 1,011
Disease-associated astrocytes in Alzheimer’s disease and aging
Habib, N., McCabe, C., Medina, S., Varshavsky, M., Kitsberg, D., Dvir-Szternfeld, R., Green, G., Dionne, D., Nguyen, L., Marshall, J. L., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0624-8 · Cited by 1,009
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971
Spatial Transcriptomics and In Situ Sequencing to Study Alzheimer’s Disease
Chen, W.-T., Lu, A., Craessaerts, K., Pavie, B., Sala Frigerio, C., Corthout, N., Qian, X., Laláková, J., Kühnemund, M., Voytyuk, I., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.038 · Cited by 949
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
Spangenberg, E., Severson, P. L., Hohsfield, L. A., Crapser, J., Zhang, J., Burton, E. A., Zhang, Y., Spevak, W., Lin, J., Phan, N. Y., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11674-z · Cited by 939
Sala Frigerio, C., Wolfs, L., Fattorelli, N., Thrupp, N., Voytyuk, I., Schmidt, I., Mancuso, R., Chen, W.-T., Woodbury, M. E., Srivastava, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.099 · Cited by 926
Parkinson's disease dementia: convergence of α-synuclein, tau and amyloid-β pathologies
Irwin, D. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2013) · Nature reviews. Neuroscience · doi:10.1038/nrn3549 · Cited by 914
Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition
Bales, K. R., Verina, T., Dodel, R. C., Du, Y., Altstiel, L., Bender, M., Hyslop, P., Johnstone, E. M., Little, S. P., Cummins, D. J., et al. (1997) · Nature Genetics · doi:10.1038/ng1197-263 · Cited by 830
High cholesterol level is essential for myelin membrane growth
Saher, G., Brügger, B., Lappe-Siefke, C., Möbius, W., Tozawa, R.-I., Wehr, M. C., Wieland, F., Ishibashi, S., & Nave, K.-A. (2005) · Nature Neuroscience · doi:10.1038/nn1426 · Cited by 799
Self-citationProtein aggregation diseases: pathogenicity and therapeutic perspectives
Aguzzi, A., & O’Connor, T. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3050 · Cited by 766
Neuron-Astrocyte Metabolic Coupling Protects against Activity-Induced Fatty Acid Toxicity
Ioannou, M. S., Jackson, J., Sheu, S.-H., Chang, C.-L., Weigel, A. V., Liu, H., Pasolli, H. A., Xu, C. S., Pang, S., Matthies, D., et al. (2019) · Cell · doi:10.1016/j.cell.2019.04.001 · Cited by 760
Temporal Tracking of Microglia Activation in Neurodegeneration at Single-Cell Resolution
Mathys, H., Adaikkan, C., Gao, F., Young, J. Z., Manet, E., Hemberg, M., De Jager, P. L., Ransohoff, R. M., Regev, A., & Tsai, L.-H. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.039 · Cited by 740
Spangenberg, E. E., Lee, R. J., Najafi, A. R., Rice, R. A., Elmore, M. R. P., Blurton-Jones, M., West, B. L., & Green, K. N. (2016) · Brain · doi:10.1093/brain/aww016 · Cited by 695
Type I interferon response drives neuroinflammation and synapse loss in Alzheimer disease
Roy, E. R., Wang, B., Wan, Y.-W., Chiu, G., Cole, A., Yin, Z., Propson, N. E., Xu, Y., Jankowsky, J. L., Liu, Z., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci133737 · Cited by 563
Late onset Alzheimer’s disease genetics implicates microglial pathways in disease risk
Efthymiou, A. G., & Goate, A. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0184-x · Cited by 562
Loss of TREM2 function increases amyloid seeding but reduces plaque-associated ApoE
Parhizkar, S., Arzberger, T., Brendel, M., Kleinberger, G., Deussing, M., Focke, C., Nuscher, B., Xiong, M., Ghasemigharagoz, A., Katzmarski, N., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0296-9 · Cited by 555
Self-citationCryo-EM structures of amyloid-β 42 filaments from human brains
Yang, Y., Arseni, D., Zhang, W., Huang, M., Lövestam, S., Schweighauser, M., Kotecha, A., Murzin, A. G., Peak-Chew, S. Y., Macdonald, J., et al. (2022) · Science · doi:10.1126/science.abm7285 · Cited by 546
Xu, Q., Bernardo, A., Walker, D., Kanegawa, T., Mahley, R. W., & Huang, Y. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5476-05.2006 · Cited by 524
APOE4 impairs myelination via cholesterol dysregulation in oligodendrocytes
Blanchard, J. W., Akay, L. A., Davila-Velderrain, J., von Maydell, D., Mathys, H., Davidson, S. M., Effenberger, A., Chen, C.-Y., Maner-Smith, K., Hajjar, I., et al. (2022) · Nature · doi:10.1038/s41586-022-05439-w · Cited by 496
Microglia use TAM receptors to detect and engulf amyloid β plaques
Huang, Y., Happonen, K. E., Burrola, P. G., O’Connor, C., Hah, N., Huang, L., Nimmerjahn, A., & Lemke, G. (2021) · Nature Immunology · doi:10.1038/s41590-021-00913-5 · Cited by 483
ApoE and Clusterin Cooperatively Suppress Aβ Levels and Deposition
DeMattos, R. B., Cirrito, J. R., Parsadanian, M., May, P. C., O'Dell, M. A., Taylor, J. W., Harmony, J. A. K., Aronow, B. J., Bales, K. R., Paul, S. M., et al. (2004) · Neuron · doi:10.1016/s0896-6273(03)00850-x · Cited by 459
ApoE4 Accelerates Early Seeding of Amyloid Pathology
Liu, C.-C., Zhao, N., Fu, Y., Wang, N., Linares, C., Tsai, C.-W., & Bu, G. (2017) · Neuron · doi:10.1016/j.neuron.2017.11.013 · Cited by 451
Sadick, J. S., O’Dea, M. R., Hasel, P., Dykstra, T., Faustin, A., & Liddelow, S. A. (2022) · Neuron · doi:10.1016/j.neuron.2022.03.008 · Cited by 415
Formation and maintenance of Alzheimer's disease β-amyloid plaques in the absence of microglia
Grathwohl, S. A., Kälin, R. E., Bolmont, T., Prokop, S., Winkelmann, G., Kaeser, S. A., Odenthal, J., Radde, R., Eldh, T., Gandy, S., et al. (2009) · Nature Neuroscience · doi:10.1038/nn.2432 · Cited by 401
Elucidating the Role of TREM2 in Alzheimer’s Disease
Ulrich, J. D., Ulland, T. K., Colonna, M., & Holtzman, D. M. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.042 · Cited by 325
Microglia facilitate repair of demyelinated lesions via post-squalene sterol synthesis
Berghoff, S. A., Spieth, L., Sun, T., Hosang, L., Schlaphoff, L., Depp, C., Düking, T., Winchenbach, J., Neuber, J., Ewers, D., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-020-00757-6 · Cited by 307
Self-citationApolipoprotein E: Structural Insights and Links to Alzheimer Disease Pathogenesis
Chen, Y., Strickland, M. R., Soranno, A., & Holtzman, D. M. (2021) · Neuron · doi:10.1016/j.neuron.2020.10.008 · Cited by 298
Oligodendroglial myelination requires astrocyte-derived lipids
Camargo, N., Goudriaan, A., van Deijk, A.-L. F., Otte, W. M., Brouwers, J. F., Lodder, H., Gutmann, D. H., Nave, K.-A., Dijkhuizen, R. M., Mansvelder, H. D., et al. (2017) · PLOS Biology · doi:10.1371/journal.pbio.1002605 · Cited by 296
Self-citationApolipoprotein E, Especially Apolipoprotein E4, Increases the Oligomerization of Amyloid β Peptide
Hashimoto, T., Serrano-Pozo, A., Hori, Y., Adams, K. W., Takeda, S., Banerji, A. O., Mitani, A., Joyner, D., Thyssen, D. H., Bacskai, B. J., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1542-12.2012 · Cited by 294
Matarin, M., Salih, D. A., Yasvoina, M., Cummings, D. M., Guelfi, S., Liu, W., Nahaboo Solim, M. A., Moens, T. G., Paublete, R. M., Ali, S. S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2014.12.041 · Cited by 290
Fibrillogenesis in Alzheimer's disease of amyloid β peptides and apolipoprotein E
Castano, E. M., Prelli, F., Wisniewski, T., Golabek, A., Kumar, R. A., Soto, C., & Frangione, B. (1995) · Biochemical Journal · doi:10.1042/bj3060599 · Cited by 267
Deczkowska, A., Matcovitch-Natan, O., Tsitsou-Kampeli, A., Ben-Hamo, S., Dvir-Szternfeld, R., Spinrad, A., Singer, O., David, E., Winter, D. R., Smith, L. K., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00769-0 · Cited by 260
Apolipoprotein E and Alzheimer’s disease: Findings, hypotheses, and potential mechanisms
Koutsodendris, N., Nelson, M. R., Rao, A., & Huang, Y. (2022) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-030421-112756 · Cited by 231
Emerging Microglia Biology Defines Novel Therapeutic Approaches for Alzheimer’s Disease
Lewcock, J. W., Schlepckow, K., Di Paolo, G., Tahirovic, S., Monroe, K. M., & Haass, C. (2020) · Neuron · doi:10.1016/j.neuron.2020.09.029 · Cited by 221
Self-citationMicroglia contribute to the propagation of Aβ into unaffected brain tissue
d’Errico, P., Ziegler-Waldkirch, S., Aires, V., Hoffmann, P., Mezö, C., Erny, D., Monasor, L. S., Liebscher, S., Ravi, V. M., Joseph, K., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-021-00951-0 · Cited by 214
Absence of microglia promotes diverse pathologies and early lethality in Alzheimer’s disease mice
Kiani Shabestari, S., Morabito, S., Danhash, E. P., McQuade, A., Sanchez, J. R., Miyoshi, E., Chadarevian, J. P., Claes, C., Coburn, M. A., Hasselmann, J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110961 · Cited by 167
Lipoproteins in the Central Nervous System
LADU, M. J., REARDON, C., VAN ELDIK, L., FAGAN, A. M., BU, G., HOLTZMAN, D., & GETZ, G. S. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06365.x · Cited by 167
The role of APOE on lipid homeostasis and inflammation in normal brains
Rebeck, G. W. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075408 · Cited by 160
Su, B., Bettcher, L., Hsieh, W.-Y., Hornburg, D., Pearson, M. J., Blomberg, N., Giera, M. A., Snyder, M. P., Raftery, D., Bensinger, S. J., et al. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00203 · Cited by 137
Self-citationAn exhausted-like microglial population accumulates in aged and APOE4 genotype Alzheimer’s brains
Millet, A., Ledo, J. H., & Tavazoie, S. F. (2024) · Immunity · doi:10.1016/j.immuni.2023.12.001 · Cited by 132
Ziegler‐Waldkirch, S., d’Errico, P., Sauer, J., Erny, D., Savanthrapadian, S., Loreth, D., Katzmarski, N., Blank, T., Bartos, M., Prinz, M., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201797021 · Cited by 123
Medin co-aggregates with vascular amyloid-β in Alzheimer’s disease
Wagner, J., Degenhardt, K., Veit, M., Louros, N., Konstantoulea, K., Skodras, A., Wild, K., Liu, P., Obermüller, U., Bansal, V., et al. (2022) · Nature · doi:10.1038/s41586-022-05440-3 · Cited by 110
Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils
Hatters, D. M., Zhong, N., Rutenber, E., & Weisgraber, K. H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.080 · Cited by 105
Potent prion-like behaviors of pathogenic α-synuclein and evaluation of inactivation methods
Tarutani, A., Arai, T., Murayama, S., Hisanaga, S., & Hasegawa, M. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0532-2 · Cited by 105
Kaji, S., Maki, T., Kinoshita, H., Uemura, N., Ayaki, T., Kawamoto, Y., Furuta, T., Urushitani, M., Hasegawa, M., Kinoshita, Y., et al. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.12.001 · Cited by 93
Self-citationFilipello, F., You, S.-F., Mirfakhar, F. S., Mahali, S., Bollman, B., Acquarone, M., Korvatska, O., Marsh, J. A., Sivaraman, A., Martinez, R., et al. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02568-y · Cited by 81
Hubin, E., Verghese, P. B., van Nuland, N., & Broersen, K. (2019) · FEBS Letters · doi:10.1002/1873-3468.13428 · Cited by 73
Shirotani, K., Tomioka, M., Kremmer, E., Haass, C., & Steiner, H. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.04.011 · Cited by 69
Self-citationPrion-like propagation of β-amyloid aggregates in the absence of APP overexpression
Ruiz‐Riquelme, A., Lau, H. H. C., Stuart, E., Goczi, A. N., Wang, Z., Schmitt‐Ulms, G., & Watts, J. C. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0529-x · Cited by 69
Native Complex Formation between Apolipoprotein E Isoforms and the Alzheimer's Disease Peptide Aβ
Chan, W., Fornwald, J. A., Brawner, M. E., & Wetzel, R. B. (1996) · Biochemistry · doi:10.1021/bi952852v · Cited by 57
Raulin, A.-C., Kraft, L., Al-Hilaly, Y. K., Xue, W.-F., McGeehan, J. E., Atack, J. R., & Serpell, L. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.04.019 · Cited by 47
Aβ Seeding as a Tool to Study Cerebral Amyloidosis and Associated Pathology
Friesen, M., & Meyer‐Luehmann, M. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00233 · Cited by 41
Type I interferon remodels lysosome function and modifies intestinal epithelial defense
Zhang, H., Zoued, A., Liu, X., Sit, B., & Waldor, M. K. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010723117 · Cited by 37
Multiscale ATUM-FIB Microscopy Enables Targeted Ultrastructural Analysis at Isotropic Resolution
Kislinger, G., Gnaegi, H., Kerschensteiner, M., Simons, M., Misgeld, T., & Schifferer, M. (2020) · iScience · doi:10.1016/j.isci.2020.101290 · Cited by 20
Self-citationTakacs, C. N., Andreo, U., Belote, R. L., Pulupa, J., Scull, M. A., Gleason, C. E., Rice, C. M., & Simon, S. M. (2017) · Traffic · doi:10.1111/tra.12467 · Cited by 10
Diagnostic criteria for primary progressive mutiple sclerosis: a position paper.
(2000) · Pure Amsterdam UMC · doi:10.1002/1531-8249(200006)47:6 · Cited by 2
Cited by
Sorted by citations
Baligács, N., Albertini, G., Borrie, S. C., Serneels, L., Pridans, C., Balusu, S., & De Strooper, B. (2024) · Nature Communications · doi:10.1038/s41467-024-54779-w · Cited by 123
Oligodendrocytes in Alzheimer’s disease pathophysiology
Kedia, S., & Simons, M. (2025) · Nature Neuroscience · doi:10.1038/s41593-025-01873-x · Cited by 86
Self-citationFerroptosis and Iron Homeostasis: Molecular Mechanisms and Neurodegenerative Disease Implications
Abdukarimov, N., Kokabi, K., & Kunz, J. (2025) · Antioxidants · doi:10.3390/antiox14050527 · Cited by 93
Liu, Y., Gu, X., Li, Y., Wang, F., Vyas, C. M., Peng, C., Dong, D., Li, Y., Zhang, Y., Zhang, Y., et al. (2025) · Nature Medicine · doi:10.1038/s41591-025-03891-5 · Cited by 55
Alzheimer’s disease pathogenesis: standing at the crossroad of lipid metabolism and immune response
Wang, Z., Zhang, L., & Qin, C. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00857-6 · Cited by 60
Metadata
- Authors
- Kaji, S., Berghoff, S. A., Spieth, L., Schlaphoff, L., Sasmita, A. O., Vitale, S., Büschgens, L., Kedia, S., Zirngibl, M., Nazarenko, T., Damkou, A., Hosang, L., Depp, C., Kamp, F., Scholz, P., Ewers, D., Giera, M., Ischebeck, T., Wurst, W., Wefers, B., Schifferer, M., Willem, M., Nave, K.-A., Haass, C., Arzberger, T., Jäkel, S., Wirths, O., Saher, G., & Simons, M.
- Affiliations
- German Center for Neurodegenerative Diseases (DE)
- Max Planck Institute for Multidisciplinary Sciences (DE)
- Universitätsmedizin Göttingen (DE)
- University of Göttingen (DE)
- Leiden University Medical Center (NL)
- University of Münster (DE)
- Munich Cluster for Systems Neurology (DE)
- Ludwig-Maximilians-Universität München (DE)
- LMU Klinikum (DE)
- Institut für Schlaganfall- und Demenzforschung (DE)
- Corresponding author
- Berghoff, Stefan A.
- Simons, Mikael
- ORCID
- Kaji, Seiji
- Berghoff, Stefan A.
- Spieth, Lena
- Schlaphoff, Lennart
- Sasmita, Andrew O.
- Büschgens, Luca
- Kedia, Shreeya
- Zirngibl, Martin
- Damkou, Alkmini
- Depp, Constanze
- Kamp, Frits
- Scholz, Patricia
- Ewers, David
- Giera, Martin
- Ischebeck, Till
- Wurst, Wolfgang
- Wefers, Benedikt
- Schifferer, Martina
- Willem, Michael
- Nave, Klaus-Armin
- Haass, Christian
- Jäkel, Sarah
- Wirths, Oliver
- Saher, Gesine
- Simons, Mikael
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2024-11
- Volume
- 57
- Issue
- 11
- Pages
- 2651-2668.e12
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W4403455151
- Cited by
- 104
- References
- 81
- Citations by year
- 2026: 38 · 2025: 58 · 2024: 8
- FWCI
- 29.60
- Type
- journal article
- Language
- en
- Update notices
- erratum (2025-01-14)
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Immunity (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion, cc-by)
- Leiden Repository (Leiden University) (submittedVersion, cc-by)
- Open access LMU (Ludwid Maxmilian's Universitat Munchen) (submittedVersion, cc-by)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion)
- DZNE Pub (submittedVersion, cc-by)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- Funders
- HORIZON EUROPE European Research Council
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- apolipoprotein E, protein aggregation, microglia, Alzheimer's disease, amyloid-beta, seeding, endolysosomal system, JAK/STAT signaling, endocytic uptake, amyloid plaques, HaloTag
- MeSH terms
- Alzheimer Disease, Amyloidosis, Animals, Apolipoproteins E, Brain, Disease Models, Animal, Humans, Mice, Transgenic, Signal Transduction, Amyloid beta-Peptides, Microglia, Lipid Metabolism, STAT Transcription Factors, Mice, Janus Kinases, Plaque, Amyloid, Protein Aggregation, Pathological
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
