The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Temporal Profile of Amyloid-β (Aβ) Oligomerization in an in Vivo Model of Alzheimer Disease
Open accessAbstract
Accumulation of amyloid-beta (Abeta) is one of the earliest molecular events in Alzheimer disease (AD), whereas tau pathology is thought to be a later downstream event. It is now well established that Abeta exists as monomers, oligomers, and fibrils. To study the temporal profile of Abeta oligomer formation in vivo and to determine their interaction with tau pathology, we used the 3xTg-AD mice, which develop a progressive accumulation of plaques and tangles and cognitive impairments. We show that SDS-resistant Abeta oligomers accumulate in an age-dependent fashion, and we present evidence to show that oligomerization of Abeta appears to first occur intraneuronally. Finally, we show that a single intrahippocampal injection of a specific oligomeric antibody is sufficient to clear Abeta pathology, and more importantly, tau pathology. Therefore, Abeta oligomers may play a role in the induction of tau pathology, making the interference of Abeta oligomerization a valid therapeutic target.
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
“Both Aβ and tau exhibit age- and region-dependent formation in these mice, with Aβ plaques appearing prior to tangles, which are extensive in older transgenic mice.”
From Brain microstructure abnormalities in the 3xTg-AD mouse – A diffusion MRI and morphology correlation study (2022) · cites this paper as [4]
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
“In our morphological analysis (Fig. 2 and 3), as previously described [3–6, 28], Aβ plaque and tau pathology are evident in 15-month-old TG mice, and significantly increased with age (online supplementary Fig.1 and 2).”
From Brain microstructure abnormalities in the 3xTg-AD mouse – A diffusion MRI and morphology correlation study (2022) · cites this paper as [4]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“It develops both amyloid-β (Aβ) and neurofibrillary tangles in a temporal and spatial pattern similar to human AD pathology [3–6].”
From Brain microstructure abnormalities in the 3xTg-AD mouse – A diffusion MRI and morphology correlation study (2022) · cites this paper as [4]
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Additionally, due to the variability of the degree of AD pathology described in this model [4, 6, 26], large ROIs, as used for the HD and HV, may have attenuated some effects.”
From Brain microstructure abnormalities in the 3xTg-AD mouse – A diffusion MRI and morphology correlation study (2022) · cites this paper as [4]
Experimental — accuracy not yet measuredIn the citing paper
“the ability of antibodies to reverse intracellular tau and synapse pathology (Chauhan et al., 2008; Oddo et al., 2006) and to provide cognitive benefits (Hillen et al., 2010; Takamura et al., 2011).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Oddo et al., 2006
In the citing paper
“Synapse deterioration in tg-mice is prevented by ICV injections of oligomer-specific antibodies (Chauhan, 2007; Oddo et al., 2006).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Oddo et al., 2006
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
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
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
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
Self-citationCommon structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Self-citationDiffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Self-citationAlzheimer Disease in the US Population: Prevalence Estimates Using the 2000 Census
Hebert, L. E., Scherr, P. A., Bienias, J. L., Bennett, D. A., & Evans, D. A. (2003) · Archives of Neurology · doi:10.1001/archneur.60.8.1119 · Cited by 2,168
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611
Research works printed but not linked: 1
- Oddo, 2006, Am. J. Pathol.
Cited by
Sorted by citations
Items 201–300 of 380
Advances on the Understanding of the Origins of Synaptic Pathology in AD
Lacor, P. N. (2007) · Current Genomics · doi:10.2174/138920207783769530 · Cited by 40
Weissmiller, A. M., Natera-Naranjo, O., Reyna, S. M., Pearn, M. L., Zhao, X., Nguyen, P. A. H., Cheng, S., Goldstein, L. S. B., Tanzi, R. E., Wagner, S. L., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118379 · Cited by 37
Pre‐amyloid stage of Alzheimer's disease in cognitively normal individuals
Tijms, B. M., Vermunt, L., Zwan, M. D., van Harten, A. C., van der Flier, W. M., Teunissen, C. E., Scheltens, P., Visser, P. J., & for, A. D. N. I. (2018) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.615 · Cited by 38
Immunotherapy for Alzheimer's Disease: Current Scenario and Future Perspectives
Usman, M. B., Bhardwaj, S., Roychoudhury, S., Kumar, D., Alexiou, A. T., Kumar, P., Ambasta, R. K., Prasher, P., Shukla, S. D., Upadhye, V. J., et al. (2021) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2021.52 · 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
Mitochondrial dysfunction induced by disease relevant AβPP and tau protein mutations
Keil, U., Hauptmann, S., Bonert, A., Scherping, I., Eckert, A., & Müller, W. E. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9206 · Cited by 36
The standardized Lycium chinense fruit extract protects against Alzheimer׳s disease in 3xTg-AD mice
Ye, M., Moon, J., Yang, J., Lim, H. H., Hong, S. B., Shim, I., & Bae, H. (2015) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2015.06.026 · Cited by 36
Caccamo, A., Magrì, A., & Oddo, S. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-51 · Cited by 35
Self-citationBellozi, P. M. Q., Gomes, G. F., da Silva, M. C. M., Lima, I. V. D. A., Batista, C. R. Á., Carneiro, W. D. O., Doria, J. G., Vieira, É. L. M., Vieira, R. P., de Freitas, R. P., et al. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107785 · Cited by 34
Xu, Y., Cui, C., Pang, C., Christen, Y., & Luo, Y. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05905.x · Cited by 33
Genetically Altering Aβ Distribution from the Brain to the Vasculature Ameliorates Tau Pathology
Oddo, S., Caccamo, A., Cheng, D., & LaFerla, F. M. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00194.x · Cited by 33
Self-citationSpecificity and sensitivity of the Abeta oligomer ELISA
Klaver, A. C., Patrias, L. M., Finke, J. M., & Loeffler, D. A. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.12.001 · Cited by 33
Extracellular quality control in the epididymis
Cornwall, G. A., von Horsten, H. H., Swartz, D. J., Johnson, S., Chau, K. M., & Whelly, S. (2007) · Asian Journal of Andrology · doi:10.1111/j.1745-7262.2007.00309.x · Cited by 32
Liu, Q., Jiang, H., Wang, Y., Wang, L., Zhang, J., He, C., Shao, S., Zhang, T., Xing, J., & Liu, R. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.10.041 · Cited by 32
Gwon, Y., Kam, T., Kim, S.-H., Song, S., Park, H., Lim, B., Lee, H., Lee, W., Jo, D., & Jung, Y. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1996-17.2018 · Cited by 33
Harte, N. P., Klyubin, I. V., McCarthy, E. K., Min, S., Garrahy, S. A., Xie, Y., Davey, G. P., Boland, J. J., Rowan, M. J., & Mok, K. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.676072 · Cited by 31
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
Seino, Y., Kawarabayashi, T., Wakasaya, Y., Watanabe, M., Takamura, A., Yamamoto‐Watanabe, Y., Kurata, T., Abe, K., Ikeda, M., Westaway, D. A., et al. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22516 · Cited by 31
Farizatto, K. L. G., Ikonne, U. S., de Almeida, M. F., Ferrari, M., & Bahr, B. A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182895 · Cited by 33
Choi, S.-I., Lee, B., Woo, J. H., Jeong, J. B., Jun, I., & Kim, E. K. (2019) · Experimental Eye Research · doi:10.1016/j.exer.2019.03.012 · Cited by 31
Dopamine release in prefrontal cortex in response to β-amyloid activation of α7∗ nicotinic receptors
Wu, J., Khan, G. M., & Nichols, R. A. (2007) · Brain Research · doi:10.1016/j.brainres.2007.08.079 · Cited by 30
IFN‐γ promotes τ phosphorylation without affecting mature tangles
Li, A., Ceballos‐Diaz, C., DiNunno, N., Levites, Y., Cruz, P. E., Lewis, J., Golde, T. E., & Chakrabarty, P. (2015) · The FASEB Journal · doi:10.1096/fj.15-275834 · Cited by 43
Body fluid biomarkers in Alzheimer's disease.
Lu, H., Zhu, X., Jiang, T., Yu, J., & Tan, L. (2015) · PubMed Central · doi:10.3978/j.issn.2305-5839.2015.02.13 · Cited by 29
New developments in mild cognitive impairment and Alzheimer's disease
Schott, J. M., Kennedy, J., & Fox, N. C. (2006) · Current Opinion in Neurology · doi:10.1097/01.wco.0000247611.44106.76 · Cited by 29
Ethanol Reduces Amyloid Aggregation In Vitro and Prevents Toxicity in Cell Lines
Ormeño, D., Romero, F., Fenner, J. L., Ávila, A. I., Martínez‐Torres, A., & Parodí, J. (2013) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.12.004 · Cited by 29
Alzheimer’s Disease and Neuronal Network Activity
Gleichmann, M., & Mattson, M. P. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8100-3 · Cited by 29
Of mice and men: more neurobiology in dementia
Codita, A., Winblad, B. G., & Mohammed, A. H. (2006) · Current Opinion in Psychiatry · doi:10.1097/01.yco.0000245757.06374.6a · Cited by 29
A model of amyloid's role in disease based on fibril fracture
Hall, D. R., & Edskes, H. K. (2009) · Biophysical Chemistry · doi:10.1016/j.bpc.2009.08.004 · Cited by 28
Legname, G., & Scialò, C. (2020) · Prion · doi:10.1080/19336896.2020.1854034 · Cited by 29
Algarzae, N. K., Hebron, M. L., Miessau, M., & Moussa, C. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.08.057 · Cited by 29
Aβ aggregation profiles and shifts in APP processing favor amyloidogenesis in canines
Pop, V., Head, E., Berchtold, N. C., Glabe, C. G., Studzinski, C. M., Weidner, A. M., Murphy, M. P., & Cotman, C. W. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.02.008 · Cited by 31
Self-citationAβPP Accumulation and/or Intraneuronal Amyloid-β Accumulation? The 3xTg-AD Mouse Model Revisited
Wirths, O., Dins, A., & Bayer, T. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111529 · Cited by 26
Shen, L., Chen, Y., Yang, A., Chen, C., Liao, L., Li, S., Ying, M., Tian, J., Liu, Q., & Ni, J. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17040469 · Cited by 26
The mechanism for heme to prevent Aβ1–40 aggregation and its cytotoxicity
Bao, Q., Luo, Y., Li, W., Sun, X., Zhu, C., Li, P., Huang, Z., & Tan, X. (2011) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-011-0783-x · Cited by 26
Isolation and characterization of antibody fragments selective for toxic oligomeric tau
Tian, H., Davidowitz, E. J., Lopez, P. L. D. C., He, P., Schulz, P., Moe, J. G., & Sierks, M. R. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.12.002 · Cited by 27
Han, F., Zhuang, T.-T., Chen, J., Zhu, X.-L., Cai, Y., & Lu, Y.-P. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185102 · Cited by 26
Falangola, M. F., Nie, X., Ward, R., Dhiman, S., Voltin, J., Nietert, P. J., & Jensen, J. H. (2021) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2021.06.022 · Cited by 25
Xu, H., Bhaskaran, S., Piekarz, K. M., Ranjit, R., Bian, J., Kneis, P., Ellis, A., Bhandari, S., Rice, H. C., & Remmen, H. V. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.876816 · Cited by 25
Jacquemont, T., Fallani, F. D. V., Bertrand, A., Epelbaum, S., Routier, A., Dubois, B., Hampel, H. J., Durrleman, S., & Olivier Colliot, A. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.03.023 · 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
Self-citationMotor impulsivity in APP-SWE mice: a model of Alzheimer??s disease
Adriani, W., Ognibene, E., Heuland, E., Ghirardi, O., Caprioli, A., & Laviola, G. (2006) · Behavioural Pharmacology · doi:10.1097/00008877-200609000-00019 · Cited by 26
Early diagnostics and therapeutics for Alzheimer’s disease – how early can we get there?
Monien, B. H., Apostolova, L. G., & Bitan, G. (2006) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.6.9.1293 · Cited by 27
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
Shen, L., Yang, A., Chen, X., Xiao, S., Liu, X., Lin, J., Zhao, Y., Zhang, K., Li, C., Ke, J., et al. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-021-01052-z · Cited by 24
Williams, S. M., Schulz, P., Rosenberry, T. L., Caselli, R. J., & Sierks, M. R. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161116 · Cited by 24
Solórzano-Vargas, R. S., Vasilevko, V., Acero, G., Ugen, K. E., Martinez, R., Govezensky, T., Vázquez‐Ramírez, R., Kubli‐Garfias, C., Cribbs, D. H., Manoutcharian, K., et al. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.08.008 · Cited by 24
Alexopoulos, P., Guo, L., Tsolakidou, A. F., Kratzer, M., Grimmer, T., Westerteicher, C., Jiang, M., Bujo, H., Diehl‐Schmid, J., Kurz, A., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110983 · Cited by 25
Amyloid imaging of alzheimer’s disease using pittsburgh compound B
Johnson, K. A. (2006) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-006-0052-5 · Cited by 25
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
Self-citationDiffusion MRI detects early brain microstructure abnormalities in 2-month-old 3×Tg-AD mice
Falangola, M. F., Nie, X., Ward, R., McKinnon, E. T., Dhiman, S., Nietert, P. J., Helpern, J. A., & Jensen, J. H. (2020) · NMR in Biomedicine · doi:10.1002/nbm.4346 · Cited by 22
Zott, B., Nästle, L., Grienberger, C., Unger, F., Knauer, M., Wolf, C., Keskin, A. D., Feuerbach, A., Busche, M. A., Skerra, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50153-y · Cited by 22
The concept of protein folding/unfolding and its impacts on human health
Alaei, L., Ashengroph, M., & Moosavi‐Movahedi, A. A. (2021) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2021.01.007 · Cited by 23
Ye, M., Chung, H., An, Y. H., Lim, S.-J., Choi, W., Yu, A., Kim, J. S., Kang, M., Cho, S., Shim, I., et al. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9458-x · Cited by 22
Nie, X., Falangola, M. F., Ward, R., McKinnon, E. T., Helpern, J. A., Nietert, P. J., & Jensen, J. H. (2019) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2018.12.003 · Cited by 22
Choi, J., Carreras, I., Aytan, N., Jenkins-Sahlin, E., Dedeoglu, A., & Jenkins, B. G. (2014) · Brain Research · doi:10.1016/j.brainres.2014.09.067 · Cited by 21
Irwin, J. A., Erişir, A., & Kwon, I. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666160208142456 · Cited by 21
BBB-Permeable, Neuroprotective, and Neurotrophic Polysaccharide, Midi-GAGR
Makani, V. S., Jang, Y.-G., Christopher, K., Judy, W., Eckstein, J. M., Hensley, K., Chiaia, N. L., Kim, D.-S., & Park, J. C. (2016) · PLoS ONE · doi:10.1371/journal.pone.0149715 · Cited by 21
Normal and Pathological Aging: From Animals to Humans
Berchtold, N. C., & Cotman, C. W. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-422-3_1 · Cited by 24
Republished: The role of amyloid β in the pathogenesis of Alzheimer’s disease
Gilbert, B. J. (2014) · Postgraduate Medical Journal · doi:10.1136/postgradmedj-2013-201515rep · Cited by 20
Goñi, F., Martá-Ariza, M., Herline, K., Peyser, D. K., Boutajangout, A., Mehta, P. D., Drummond, E., Prelli, F., & Wısnıewskı, T. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0337-3 · Cited by 20
Fu, L., Jiang, G., Weng, H., Dick, G. M., Chang, Y.-Z., & Kassab, G. S. (2019) · Brain Pathology · doi:10.1111/bpa.12759 · Cited by 20
Cao, Y., Wang, J.-C., Zhu, K., Zhang, H., Wang, G., & Liu, H. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.266061 · Cited by 20
Kitazawa, M., Vasilevko, V., Cribbs, D. H., & LaFerla, F. M. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1150-09.2009 · Cited by 20
Self-citationCassel, J., Mathis, C., Majchrzak, M. J., Moreau, P., & Dalrymple‐Alford, J. C. (2008) · Neurodegenerative Diseases · doi:10.1159/000135615 · Cited by 21
Parodí, J., Ormeño, D., & la Paz, L. D. O.-D. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.1.125 · Cited by 19
Tian, S. L., Ye, T., & Cheng, X. (2023) · Experimental Neurology · doi:10.1016/j.expneurol.2023.114505 · Cited by 21
Salman, M., Akram, M. V., Shahrukh, M., Ishrat, T., & Parvez, S. (2022) · NeuroToxicology · doi:10.1016/j.neuro.2022.07.006 · Cited by 19
Impairment of spatial memory consolidation in APP751SL mice results in cue-guided response
Blanchard, J., Martel, G., Guillou, J., Noguès, X., & Micheau, J. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.010 · Cited by 19
Kuo, Y., Lou, Y.-I., & Rajesh, R. (2020) · Journal of drug targeting · doi:10.1080/1061186x.2020.1761819 · Cited by 18
Interactions of Volatile Anesthetics with Neurodegenerative-Disease-Associated Proteins
Carnini, A., Eckenhoff, M. F., & Eckenhoff, R. G. (2006) · Anesthesiology Clinics of North America · doi:10.1016/j.atc.2006.02.002 · Cited by 18
Kobro‐Flatmoen, A., Hormann, T. M., & Gouras, G. K. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230349 · Cited by 17
He, Q., Huang, G. J., Chen, Y., Wang, X., Huang, Z., & Chen, Z. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2339-0 · Cited by 17
Alzheimer's amyloid story finds its star
Cole, G. M., & Frautschy, S. A. (2006) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.07.002 · Cited by 17
Dong, Z. H., Li, Y., Huang, G. J., Zhang, L., Mei, B., & Meng, B. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.03.048 · Cited by 18
Toward a Dynamic Biomarker Model in Alzheimer's Disease
Mouiha, A., Initiative, T. A. D. N., & Duchesne, S. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-111367 · Cited by 18
The Pathogenesis of Alzheimer's Disease and the Role of Aβ42
Golde, T. E. (2007) · CNS Spectrums · doi:10.1017/s1092852900025876 · Cited by 17
Yuksel, M., Biberoğlu, K., Önder, S., AKBULUT, K. G., & Tacal, Ö. (2017) · Biochimie · doi:10.1016/j.biochi.2017.12.004 · Cited by 17
Skaper, S. D., Facci, L., & Giusti, P. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1084-2 · Cited by 16
The Genetics of Frontotemporal Dementia
Haugarvoll, K., Wszołek, Z. K., & Hutton, M. L. (2007) · Neurologic Clinics · doi:10.1016/j.ncl.2007.03.002 · Cited by 16
Cerebrovascular Dysfunction in Alzheimer’s Disease and Transgenic Rodent Models
Fang, X., Fan, F., & Roman, R. J. (2024) · Journal of Experimental Neurology · doi:10.33696/neurol.5.087 · Cited by 17
Aβ and the dementia syndrome: Simple versus complex perspectives
Hunter, S., Smailagic, N., & Brayne, C. (2018) · European Journal of Clinical Investigation · doi:10.1111/eci.13025 · Cited by 15
Should development of Alzheimer¿s disease-specific intravenous immunoglobulin be considered?
Loeffler, D. A. (2014) · Journal of Neuroinflammation · doi:10.1186/s12974-014-0198-z · Cited by 15
Chiang, A. C. A., Fowler, S., Reddy, R., Pletniková, O., Troncoso, J. C., Sherman, M. A., Lesné, S., & Jankowsky, J. L. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.11.011 · Cited by 17
Blanchard, J., Decorte, L., Noguès, X., & Micheau, J. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2009.02.005 · Cited by 17
miR-128 as a Regulator of Synaptic Properties in 5xFAD Mice Hippocampal Neurons
Shvarts-Serebro, I., Sheinin, A., Gottfried, I., Adler, L., Schottlender, N., Ashery, U., & Barak, B. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-021-01862-2 · Cited by 15
Critical thinking of Alzheimer’s transgenic mouse model: current research and future perspective
Li, X., Quan, M., Wei, Y., Wang, W., Xu, L., Wang, Q., & Jia, J. (2023) · Science China Life Sciences · doi:10.1007/s11427-022-2357-x · Cited by 14
Bartley, S. C., Proctor, M. T., Xia, H., Ho, E., Kang, D. S., Schuster, K. H., Bicca, M. A., Seckler, H. S., Viola, K. L., Patrie, S. M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042208 · Cited by 14
Self-citationAβ Toxicity in Primary Cultured Neurons
Ferreira, A., Sinjoanu, R. C., Nicholson, A. M., & Kleinschmidt, S. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-744-0_11 · Cited by 14
Wang, H., Yu, Y., Liu, S., Zhao, M., & Xu, Q. (2016) · Vaccine · doi:10.1016/j.vaccine.2016.02.056 · Cited by 13
Tau kinase inhibitors protect hippocampal synapses despite of insoluble tau accumulation
Hinners, I., Hill, A., Otto, U., Michalsky, A., Mack, T. G. A., & Striggow, F. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.12.004 · Cited by 13
Sequence-dependent abnormal aggregation of human Tau fragment in an inducible cell model
Liu, X., Hu, J.-Y., Hu, M.-Y., Zhang, Y., Hong, Z., Cheng, X., Chen, J., Pang, D., & Liang, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.04.015 · Cited by 13
Treating the Lesions, Not the Disease
Zhu, X., Ávila, J., Perry, G. L., & Smith, M. A. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070193 · Cited by 13
Kapadia, M., Mian, M. F., Ma, D., Hutton, C. P., Azam, A., Narkaj, K., Cao, C., Brown, B., Michalski, B., Morgan, D., et al. (2021) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00745-9 · Cited by 14
Neuroinflammation and Alzheimer’s disease: lessons learned from 5-lipoxygenase
Joshi, Y. B., & Praticò, D. (2014) · Translational Neuroscience · doi:10.2478/s13380-014-0225-7 · Cited by 12
Scialò, C., & Legname, G. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.08.008 · Cited by 12
The 3xTg-AD Mouse Model: A Comprehensive Tool for Understanding Alzheimer’s Disease
Pattanayak, A., & Firdous, S. M. (2026) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01655-w · Cited by 13
Yu, Y., Liu, S., Wang, H., Shi, D., Xu, Q., Zhou, X., Sun, Z., & Huang, P. (2016) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-016-9678-5 · Cited by 11
Joseph, D. J., Liu, C., Peng, J., Liang, G., & Wei, H. (2019) · PLoS ONE · doi:10.1371/journal.pone.0223509 · Cited by 11
Acharya, N. K., Grossman, H. C., Clifford, P. M., Levin, E. C., Light, K., Choi, H.-N., Swanson, R. L., Kosciuk, M. C., Venkataraman, V., Libon, D. J., et al. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231028 · Cited by 13
From mild cognitive impairment to prodromal Alzheimer disease: A nosological evolution
Molinuevo, J. L., Valls‐Pedret, C., & Rami, L. (2010) · European Geriatric Medicine · doi:10.1016/j.eurger.2010.05.003 · Cited by 12
Metadata
- Authors
- Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L., & LaFerla, F. M.
- Affiliations
- University of California, Irvine (US)
- Northwestern University (US)
- Corresponding author
- LaFerla, Frank M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-01
- Volume
- 281
- Issue
- 3
- Pages
- 1599-1604
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2020497815
- Cited by
- 379
- References
- 41
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 8 · 2023: 5 · 2022: 9 · 2021: 8 · 2020: 12 · 2019: 13 · 2018: 14 · 2017: 16 · 2016: 17 · 2015: 15 · 2014: 21 · 2013: 21 · 2012: 22
- FWCI
- 18.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Larry L. Hillblom Foundation
- National Institutes of Health (AG00538)
- National Institute on Aging (AG-11385, AG18877, AG0212982, AG 00538, AG 22547, R01AG022547, R01AG018877)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta oligomers, Alzheimer's disease, 3xTg-AD mice, tau pathology, age-dependent accumulation, intrahippocampal injection, amyloid plaques, cognitive impairment, therapeutic target
- MeSH terms
- Aging, Alzheimer Disease, Animals, Disease Models, Animal, Hippocampus, Humans, Functional Laterality, Mice, Transgenic, Neurons, Recombinant Proteins, Amyloid beta-Peptides, tau Proteins, 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
