The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain
Open accessAbstract
Multiple lines of evidence implicate β-amyloid (Aβ) in the pathogenesis of Alzheimer's disease (AD), but the mechanisms whereby Aβ is involved remain unclear. Addition of Aβ to the extracellular space can be neurotoxic. Intraneuronal Aβ42 accumulation is also associated with neurodegeneration. We reported previously that in Tg2576 amyloid precursor protein mutant transgenic mice, brain Aβ42 localized by immunoelectron microscopy to, and accumulated with aging in, the outer membranes of multivesicular bodies, especially in neuronal processes and synaptic compartments. We now demonstrate that primary neurons from Tg2576 mice recapitulate the in vivo localization and accumulation of Aβ42 with time in culture. Furthermore, we demonstrate that Aβ42 aggregates into oligomers within endosomal vesicles and along microtubules of neuronal processes, both in Tg2576 neurons with time in culture and in Tg2576 and human AD brain. These Aβ42 oligomer accumulations are associated with pathological alterations within processes and synaptic compartments in Tg2576 mouse and human AD brains.
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
“Intraneuronal Ab is derived from Ab internalized by neurons from the extracellular space through ApoE-dependent and ApoE-independent uptakes and from intrinsic Ab that escapes exocytosis after APP cleavage that takes place in the endocytic compartment.34”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [34]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Intraneuronal accumulation of Ab is a potentially important aspect of AD pathogenesis.”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [34]
In the citing paper
“a subsequent immuno-EM study demonstrated that intraneuronal accumulation of higher molecular weight Aβ42 oligomers (antibody M16; [210]) was invariably associated with neuritic degeneration, even prior to plaques, in vulnerable distal neurites and synaptic compartments in brains of AD transgenic mice and human AD [187].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
In the citing paper
“C-terminal specific Aβ42 antibodies typically are best at detecting Aβ42 monomers, and have minimal reactivity against oligomers larger than trimers [187].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
In the citing paper
“Emerging data, such as FAD mutations noted above, and the direct association of intraneuronal Aβ42 with subcellular pathology [187, 188], cell death [23, 167], and behavioral and physiological abnormalities, even prior to plaques, in AD transgenic mouse models [140], are providing increasing evidence for the importance of intraneuronal Aβ.”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
In the citing paper
“Immuno-EM images of completely abnormal Aβ42 accumulating dystrophic neurites [187, 188], lacking the normal microtubule tracks required for organelle trafficking, secretion and exocytosis, argue against the active secretion of aggregating Aβ42 from neuritis prior to the dissolution of the plasma membrane [95].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
In the citing paper
“It needs to be stressed again that by immuno-EM high molecular weight Aβ42 oligomers are consistently associated with pathology within neurites even prior to plaques [187].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
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
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
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
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
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
Holcomb, L., Gordon, M. N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-097 · Cited by 1,386
Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268
Receptor downregulation and multivesicular-body sorting
Katzmann, D. J., Odorizzi, G., & Emr, S. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm973 · Cited by 1,201
Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 1×
“A 42 oligomerization in Tg2576 mouse brain with aging A previous report showed that microdeposits of A 42 appear as early as 7– 8 months in Tg2576 brain (Kawarabayashi et al., 2001).”
MethodIntraneuronal 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
Self-citation
Research works printed but not linked: 1
- Peters A, Palay SL, Webster Hd (1991) The fine structure of nervous system. Oxford: Oxford UP.
Cited by
Sorted by citations
Items 201–300 of 444
Impaired behavior of female tg-ArcSwe APP mice in the IntelliCage: A longitudinal study
Codita, A., Gumucio, A., Lannfelt, L., Gellerfors, P., Winblad, B. G., Mohammed, A. H. S., & Nilsson, L. N. G. (2010) · Behavioural Brain Research · doi:10.1016/j.bbr.2010.06.034 · Cited by 52
Evans, N. A., Facci, L., OWEN, D. E., Soden, P. E., Burbidge, S. A., Prinjha, R. K., Richardson, J. C., & Skaper, S. D. (2008) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2008.08.001 · Cited by 56
Mendoza‐Naranjo, A., Contreras-Vallejos, E., Henríquez, D. R., Carola Otth, L., Bamburg, J. R., Maccioni, R. B., & González-Billault, C. E. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-101575 · Cited by 51
Meli, G., Lecci, A., Manca, A., Jakovljevic, N. K., Albertini, V., Benussi, L., Ghidoni, R., & Cattaneo, A. (2014) · Nature Communications · doi:10.1038/ncomms4867 · Cited by 51
Zhang, L., Xia, R., Jia, J., Wang, L., Li, K., Li, Y., & Zhang, J. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.04.015 · Cited by 49
Neuronal spreading and plaque induction of intracellular Aβ and its disruption of Aβ homeostasis
Roos, T. T., Garcia, M. G., Martinsson, I., Mabrouk, R., Israelsson, B., Deierborg, T., Kobro‐Flatmoen, A., Tanila, H., & Gouras, G. K. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02345-9 · Cited by 48
Self-citationTitration of biologically active amyloid–β seeds in a transgenic mouse model of Alzheimer's disease
Morales, R., Bravo-Alegria, J. B., Duran-Aniotz, C. A., & Soto, C. A. (2015) · Scientific Reports · doi:10.1038/srep09349 · Cited by 49
Arendash, G. W., Cao, C., Abulaban, H., Baranowski, R., Wisniewski, G., Becerra, L. R., Andel, R., Lin, X., Zhang, X., Wittwer, D., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190367 · Cited by 52
Liu, F., Sun, J., Wang, X., Jin, S., Sun, F., Wang, T., Yuan, B., Qiu, W., & Ma, C. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00927-5 · Cited by 48
Duarte, A. I., Santos, M. S., Oliveira, C. R., & Moreira, P. I. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.01.044 · Cited by 49
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 53
Self-citationSirabella, R., Sisalli, M. J., Costa, G., Omura, K. M., Ianniello, G., Pinna, A., Morelli, M., Renzo, G. D., Annunziato, L., & Scorziello, A. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0775-7 · Cited by 48
Tate, B. A., & Mathews, P. M. (2006) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2006.10.re2 · Cited by 48
Lee, L. L., Ha, H., Chang, Y., & DeLisa, M. P. (2009) · Protein Science · doi:10.1002/pro.33 · Cited by 47
Lebois, E. P., Schroeder, J. P., Esparza, T. J., Bridges, T. M., Lindsley, C. W., Conn, P. J., Brody, D. L., Daniels, J. S., & Levey, A. I. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00278 · Cited by 45
Cellular Responses to Protein Accumulation Involve Autophagy and Lysosomal Enzyme Activation
Butler, D., Brown, Q. B., Chin, D. J., Batey, L., Karim, S. L., Mutneja, M. S., Karanian, D. A., & Bahr, B. A. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.227 · Cited by 46
Vrijsen, S., Vrancx, C., Vecchio, M. D., Swinnen, J. V., Agostinis, P., Winderickx, J., Vangheluwe, P., & Annaert, W. G. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.900338 · Cited by 53
β-amyloid and Oxidative Stress: Perspectives in Drug Development
Caruso, G., Spampinato, S. F., Cardaci, V., Caraci, F., Sortino, M. A., & Merlo, S. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666191209115431 · Cited by 45
Shah, P., Lal, N., Leung, E., Traul, D., Gonzalo‐Ruiz, A., & Geula, C. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090937 · Cited by 48
Yang, W., Ma, K., Chen, X. L., Shi, L., Bu, G., Hu, X. D., Han, H., Liu, Y., & Qian, Y. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.08.013 · Cited by 44
Aβ Influences Cytoskeletal Signaling Cascades with Consequences to Alzheimer’s Disease
Henriques, A. G., Oliveira, J. M., Carvalho, L., & Silva, O. A. B. D. C. E. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8913-4 · Cited by 45
Ling, D., Magallanes, M., & Salvaterra, P. M. (2014) · ASN NEURO · doi:10.1042/an20130044 · Cited by 43
The Bri2 and Bri3 BRICHOS Domains Interact Differently with Aβ 42 and Alzheimer Amyloid Plaques
Dolfe, L., Tambaro, S., Tigro, H., del Campo, M., Hoozemans, J. J. M., Wiehager, B., Graff, C., Winblad, B. G., Ankarcrona, M., Kaldmäe, M., et al. (2018) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-170051 · Cited by 44
Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease
Colom-Cadena, M., Toombs, J., Simzer, E., Holt, K., McGeachan, R., Tulloch, J., Jackson, R. J., Catterson, J. H., Spires-Jones, M. P., Rose, J., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02679-6 · Cited by 44
Astrocytic and neuronal apolipoprotein E isoforms differentially affect neuronal excitability
Konings, S. C., Torres-Garcia, L., Martinsson, I., & Gouras, G. K. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.734001 · Cited by 43
Self-citationRönnbäck, A., Sagelius, H., Bergstedt, K. D., Näslund, J., Westermark, G. T., Winblad, B., & Graff, C. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.07.012 · Cited by 43
Examination of potential mechanisms of amyloid-induced defects in neuronal transport
Shah, S. B., Nolan, R. L., Davis, E., Stokin, G. B., Niesman, I. R., Canto, I., Glabe, C. G., & Goldstein, L. S. B. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.016 · Cited by 45
Bretou, M., Sannerud, R., Escamilla‐Ayala, A., Leroy, T., Vrancx, C., Acker, Z. P. V., Perdok, A., Vermeire, W., Vorsters, I., Keymolen, S. V., et al. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.03.030 · Cited by 47
Autophagy-lysosomal pathway impairment and cathepsin dysregulation in Alzheimer’s disease
Mançano, A. S. F., Pina, J. G., Froes, B. R., & Sciani, J. M. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1490275 · Cited by 51
The Inside-Out Amyloid Hypothesis and Synapse Pathology in Alzheimer's Disease
Gouras, G. K., Willén, K. I., & Faideau, M. (2013) · Neurodegenerative Diseases · doi:10.1159/000354776 · Cited by 42
Self-citationFrameshift proteins in autosomal dominant forms of Alzheimer disease and other tauopathies
van Leeuwen, F. W., van Tijn, P., Sonnemans, M. A. F., Hobo, B., Mann, D. M. A., Broeckhoven, C. V., Kumar‐Singh, S., Cras, P. P., Leuba, G., Savioz, A., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000193882.46003.6d · Cited by 42
Impaired β-Amyloid Secretion in Alzheimer's Disease Pathogenesis
Tampellini, D., Rahman, N., Lin, M. T. S., Capetillo‐Zarate, E., & Gouras, G. K. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2986-11.2011 · Cited by 41
Self-citationAlzheimer’s Pathogenesis and Its Link to the Mitochondrion
Simoncini, C., Orsucci, D., Ienco, E. C., Siciliano, G., Bonuccelli, U., & Mancuso, M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/803942 · Cited by 45
Pérez, J. L. M., Carrero, I., Gonzalo, P., Arévalo‐Serrano, J., Anquela, J. M. S., Ortega, F. J., Rodríguez, M. J., & Gonzalo‐Ruiz, A. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.10.013 · Cited by 44
Mureşan, V., & Muresan, Z. L. (2009) · Future Neurology · doi:10.2217/fnl.09.54 · Cited by 41
Intraneuronal Aβ as a trigger for neuron loss: can this be translated into human pathology?
Bayer, T. A., & Wirths, O. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390857 · Cited by 41
Gouras, G. K., Willén, K., & Tampellini, D. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.06.004 · Cited by 39
Self-citationAlzheimer's Disease Modeling: Ups, Downs, and Perspectives for Human Induced Pluripotent Stem Cells
Wojda, U., & Kuźnicki, J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121984 · Cited by 40
Suppression of Amyloid β A11 Antibody Immunoreactivity by Vitamin C
Cheng, F., Cappai, R., Ciccotosto, G. D., Svensson, G., Multhaup, G., Fransson, L., & Mani, K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243345 · Cited by 39
Phospholipase A2 inhibitors protect against prion and Aβ mediated synapse degeneration
Bate, C., Tayebi, M., & Williams, A. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-13 · Cited by 39
Sanchez-Varo, R. M., Sánchez‐Mejías, E., Fernandez-Valenzuela, J. J., Castro, V. D., Mejias‐Ortega, M., Gómez-Arboledas, Á., Jiménez, S., Sanchez-Mico, M. V., Trujillo‐Estrada, L., Moreno‐González, I., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.752594 · Cited by 42
Wong, J., Higgins, M. J., Halliday, G. M., & Garner, B. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.02.037 · Cited by 38
Cerebral Arachidonate Cascade in Dementia: Alzheimers Disease and Vascular Dementia
Yagami, T. (2005) · Current Neuropharmacology · doi:10.2174/157015906775203011 · Cited by 39
Muresan, Z., & Muresan, V. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00371-06 · Cited by 35
Novel approaches for immunotherapeutic intervention in Alzheimer's disease
Vasilevko, V., & Cribbs, D. H. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.03.019 · Cited by 37
Absence of synaptophysin near cortical neurons containing oligomer Aβ in Alzheimer's disease brain
Ishibashi, K., Tomiyama, T., Nishitsuji, K., Hara, M., & Mori, H. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20952 · Cited by 37
Wu, Z., Zhu, Y., Cao, X., Sun, S., & Zhao, B. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8675-z · Cited by 36
Significant structural but not physiological changes in cortical neurons of 12-month-old Tg2576 mice
Rocher, A. B., Kinson, M. S., & Luebke, J. I. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.07.014 · Cited by 36
Yang, W., Zhang, J., Shi, L., Ji, S., Yang, X., Zhai, W., Zong, H.-F., & Qian, Y. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.12.011 · Cited by 35
Perdigão, C., Barata, M. A., Burrinha, T., & Almeida, C. G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101056 · Cited by 33
Self-citationMartinsson, I., Quintino, L., Garcia, M. G., Konings, S. C., Torres-Garcia, L., Svanbergsson, A., Stange, O., England, R., Deierborg, T., Li, J., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.946297 · Cited by 35
Self-citationSwanson, T. L., Knittel, L. M., Coate, T. M., Farley, S. M., Snyder, M. A., & Copenhaver, P. F. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.09.029 · Cited by 35
The Role of Extracellular Matrix Components in the Spreading of Pathological Protein Aggregates
Moretto, E., Stuart, S., Surana, S., Vargas, J. N. S., & Schiavo, G. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.844211 · Cited by 32
Excitatory synaptic transmission is depressed in cultured hippocampal neurons of APP/PS1 mice
Priller, C., Mitteregger, G., Paluch, S., Vassallo, N., Staufenbiel, M., Kretzschmar, H. A., Jucker, M., & Herms, J. W. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.10.016 · Cited by 33
Long non-coding RNAs in Alzheimer's disease
Zhang, Z. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150813142956 · Cited by 33
Retromers in Alzheimer’s Disease
Siegenthaler, B. M., & Rajendran, L. (2012) · Neurodegenerative Diseases · doi:10.1159/000335910 · Cited by 33
Ramakrishna, S., Jhaveri, V., Konings, S. C., Nawalpuri, B., Chakraborty, S., Holst, B., Schmid, B., Gouras, G. K., Freude, K., & Muddashetty, R. S. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.0435-21.2021 · Cited by 34
Self-citationPark, H., & Kim, J. (2022) · Journal of Pineal Research · doi:10.1111/jpi.12787 · Cited by 33
Karapetyan, G., Fereshetyan, K., Harutyunyan, H. A., & Yenkoyan, K. B. (2022) · Scientific Reports · doi:10.1038/s41598-022-22761-5 · Cited by 36
Linking molecular motors to Alzheimer’s disease
Stokin, G. B., & Goldstein, L. S. B. (2006) · Journal of Physiology-Paris · doi:10.1016/j.jphysparis.2005.12.085 · Cited by 32
Intracellular Localization of Amyloid-β Peptide in SH-SY5Y Neuroblastoma Cells
Zheng, L. P., Calvo‐Garrido, J., Hallbeck, M., Hultenby, K. R., Marcusson, J. O., Cedazo-Mı́nguez, Á., & Terman, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122455 · Cited by 33
Bengtsson, S. K. S., Johansson, M., Bäckström, T. C., & Wang, M. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120268 · Cited by 34
Purushothuman, S., Marotte, L. R., Stowe, S., Johnstone, D. M., & Stone, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059740 · Cited by 31
Vilasi, S., Carrotta, R., Ricci, C., Rappa, G. C., Librizzi, F., Martorana, V., Ortore, M. G., & Mangione, M. R. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00183 · Cited by 32
High-Resolution 3D Reconstruction Reveals Intra-Synaptic Amyloid Fibrils
Capetillo‐Zarate, E., Gracia, L., Yu, F., Banfelder, J. R., Lin, M. T. S., Tampellini, D., & Gouras, G. K. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.07.045 · Cited by 31
Self-citationAndersson, E., Lindblom, N., Janelidze, S., Salvadó, G., Gkanatsiou, E., Söderberg, L., Möller, C., Lannfelt, L., Ge, J., Hanrieder, J., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00810-8 · Cited by 38
Self-citationPseudoginsenoside‐F11 alleviates oligomeric β‐amyloid‐induced endosome‐lysosome defects in microglia
Yao, X., Xue, X., Zhang, H. T., Zhu, M., Yang, X. W., Wu, C. F., & Yang, J. (2018) · Traffic · doi:10.1111/tra.12620 · Cited by 30
Wang, P.-Y., Chen, J.-J., & Su, H. (2009) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2009.01.012 · Cited by 30
Muresan, Z. L., & Mureşan, V. (2008) · Neurodegenerative Diseases · doi:10.1159/000113716 · Cited by 30
APP depletion alters selective pre- and post-synaptic proteins
Martinsson, I., Capetillo-Zarate, E., Faideau, M., Willén, K., Esteras, N., Frykman, S., Tjernberg, L. O., & Gouras, G. K. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.02.003 · Cited by 29
Self-citationThe Role of Glial Cells and Synapse Loss in Mouse Models of Alzheimer’s Disease
Ziegler-Waldkirch, S., & Meyer-Luehmann, M. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00473 · Cited by 21
Richter, M., Vidovic, N., Biber, K. P. H., Dolga, A. M., Culmsee, C., & Dodel, R. C. (2019) · Brain Pathology · doi:10.1111/bpa.12807 · Cited by 31
Cyclooxygenase-Dependent Lipid-Modification of Brain Proteins
Boutaud, O. G., Andreasson, K. I., Zagol-Ikapitte, I. A., & Oates, J. A. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2005.tb00510.x · Cited by 29
Williamson, R., Laulagnier, K., Miranda, A. M., Fernandez, M. A., Wolfe, M. S., Sadoul, R., & Paolo, G. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.818138 · Cited by 28
Choi, S. W., Gerencser, A. A., Ng, R., Flynn, J. M., Melov, S., Danielson, S. R., Gibson, B. W., Nicholls, D. G., Bredesen, D. E., & Brand, M. D. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.2414-12.2012 · Cited by 28
Willén, K. I., Sroka-Oleksiak, A., Takahashi, R. H., & Gouras, G. K. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170262 · Cited by 28
Self-citationAccumulation of cellular prion protein within β‐amyloid oligomer plaques in aged human brains
Takahashi, R. H., Yokotsuka, M., Tobiume, M., Sato, Y., Hasegawa, H., Nagao, T., & Gouras, G. K. (2021) · Brain Pathology · doi:10.1111/bpa.12941 · Cited by 27
Self-citationMori, K., Asakawa, M., Hayashi, M., 井村実和子, Ohki, T., Hirao, E., Kim‐Kaneyama, J., Nose, K., & Shibanuma, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513111200 · Cited by 26
Caliban's heritance and the genetics of neuronal aging
Teter, B., & Finch, C. E. (2004) · Trends in Neurosciences · doi:10.1016/j.tins.2004.08.005 · Cited by 26
Nazere, K., Takahashi, T., Hara, N., Muguruma, K., Nakamori, M., Yamazaki, Y., Morino, H., & Maruyama, H. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.804702 · Cited by 26
DiChiara, T., DiNunno, N., Clark, J. R., Bu, R. L., Cline, E. N., Rollins, M. G., Gong, Y., Brody, D. L., Sligar, S. G., Velasco, P. T., et al. (2017) · PubMed · Cited by 25
Intraneuronal Aβ Accumulation, Amyloid Plaques, and Synapse Pathology in Alzheimer’s Disease
Capetillo‐Zarate, E., Gracia, L., Tampellini, D., & Gouras, G. K. (2012) · Neurodegenerative Diseases · doi:10.1159/000334762 · Cited by 25
Self-citationKokubo, H., Kayed, R., Glabe, C. G., Staufenbiel, M., Saido, T. C., Iwata, N., & Yamaguchi, H. (2009) · International Journal of Alzheimer s Disease · doi:10.4061/2009/689285 · Cited by 25
Candidate anti-Aβ fluorene compounds selected from analogs of amyloid imaging agents
Hong, H., Maezawa, I., Budamagunta, M. S., Rana, S., Shi, A., Vassar, R. J., Liu, R., Lam, K. S., Cheng, R. H., Hua, D. H., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.09.019 · Cited by 25
Bridging the age spectrum of neurodegenerative storage diseases
Boland, B., & Platt, F. M. (2014) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2014.08.009 · Cited by 24
Diabetes, Insulin and Alzheimer's Disease
Craft, S., & Christen, Y. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-04300-0 · Cited by 24
Frackowiak, J., Potempska, A., & Mazur‐Kolecka, B. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0497-0 · Cited by 24
Omi is a mammalian heat-shock protein that selectively binds and detoxifies oligomeric amyloid-β
Liu, M.-L., Liu, M.-J., Shen, Y.-F., Ryu, H., Kim, H., Klupsch, K., Downward, J., & Hong, S. (2009) · Journal of Cell Science · doi:10.1242/jcs.042226 · Cited by 23
Klein, W. L., Lacor, P. N., Felice, F. G. D., & Ferreira, S. T. (2007) · Research and perspectives in neurosciences · doi:10.1007/978-3-540-45702-2_11 · Cited by 23
Koinuma, S., Shimozawa, N., Yasutomi, Y., & Kimura, N. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.06.022 · Cited by 22
APP-BP1 inhibits Abeta42 levels by interacting with Presenilin-1.
Chen, Y., Bodles, A. M., McPhie, D. L., Neve, R. L., Mrak, R. E., & Griffin, W. S. T. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-3 · Cited by 23
Amyloid β production along the neuronal secretory pathway: Dangerous liaisons in the Golgi?
Fourrière, L., & Gleeson, P. A. (2021) · Traffic · doi:10.1111/tra.12808 · Cited by 24
Redox Imbalance in Neurological Disorders in Adults and Children
Rey, F., Berardo, C., Maghraby, E., Mauri, A., Messa, L., Esposito, L., Casili, G., Ottolenghi, S., Bonaventura, E., Cuzzocrea, S., et al. (2023) · Antioxidants · doi:10.3390/antiox12040965 · Cited by 23
Saul, A., Lashley, T., Révész, T., Holton, J. L., Ghiso, J. A., Coomaraswamy, J., & Wirths, O. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.014 · Cited by 23
Bengtsson, S. K. S., Bäckström, T. C., Brinton, R. D., Irwin, R. W., Johansson, M., Sjöstedt, J., & Wang, M. D. (2019) · Neurobiology of Stress · doi:10.1016/j.ynstr.2019.100206 · Cited by 22
Cholesterol Increases Ventricular Volume in a Rabbit Model of Alzheimer's Disease
Deci, S. E., Lemieux, S. K., Smith‐Bell, C. A., Sparks, D. L., & Schreurs, B. G. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111415 · Cited by 20
Norvin, D., Kım, G., Baker‐Nigh, A., & Geula, C. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.04.011 · Cited by 19
Arendash, G. W., Abulaban, H., Steen, S., Andel, R., Wang, Y., Bai, Y., Baranowski, R., McGarity, J., Scritsmier, L., Lin, X., et al. (2022) · Medicines · doi:10.3390/medicines9080042 · Cited by 21
Victoria, G. S., & Zurzolo, C. (2015) · Virus Research · doi:10.1016/j.virusres.2015.01.019 · Cited by 20
Morsy, A., Krishnaiah, M., Gao, J., Wang, H., Valdez, J., Dow, L. F., Wang, X., & Trippier, P. C. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00246 · Cited by 22
Metadata
- Authors
- Takahashi, R. H., Almeida, C. G., Kearney, P. F., Yu, F., Lin, M. T., Milner, T. A., & Gouras, G. K.
- Affiliations
- Cornell University (US)
- Corresponding author
- Gouras, Gunnar K.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2004-04-07
- Volume
- 24
- Issue
- 14
- Pages
- 3592-3599
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6729733
- OpenAlex
- W2128779293
- Cited by
- 445
- References
- 48
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 10 · 2023: 10 · 2022: 18 · 2021: 18 · 2020: 9 · 2019: 16 · 2018: 13 · 2017: 19 · 2016: 14 · 2015: 12 · 2014: 18 · 2013: 22 · 2012: 26
- FWCI
- 22.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- American Academy of Neurology
- National Institutes of Health (2k08ns002037-04, HL18974)
- National Heart, Lung, and Blood Institute (HL-18974, P01HL018974)
- National Institute of Neurological Disorders and Stroke (NS02037, R01NS045677, NS 045677)
- 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
- Alzheimer's disease, amyloid-beta, neural processes, synapses, multivesicular bodies, endosomal vesicles, microtubules, Tg2576 mice, amyloid precursor protein, neurodegeneration, primary neurons
- MeSH terms
- Adult, Aging, Alzheimer Disease, Animals, Brain, Cells, Cultured, Disease Models, Animal, Fluorescent Antibody Technique, Humans, Mice, Transgenic, Microtubules, Middle Aged, Neurons, Peptide Fragments, Endosomes, Synapses, Organelles, Amyloid beta-Peptides, Macromolecular Substances, Mice
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
