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Mechanisms of Hybrid Oligomer Formation in the Pathogenesis of Combined Alzheimer's and Parkinson's Diseases
Open accessAbstract
BACKGROUND: Misfolding and pathological aggregation of neuronal proteins has been proposed to play a critical role in the pathogenesis of neurodegenerative disorders. Alzheimer's disease (AD) and Parkinson's disease (PD) are frequent neurodegenerative diseases of the aging population. While progressive accumulation of amyloid beta protein (Abeta) oligomers has been identified as one of the central toxic events in AD, accumulation of alpha-synuclein (alpha-syn) resulting in the formation of oligomers and protofibrils has been linked to PD and Lewy body Disease (LBD). We have recently shown that Abeta promotes alpha-syn aggregation and toxic conversion in vivo, suggesting that abnormal interactions between misfolded proteins might contribute to disease pathogenesis. However the molecular characteristics and consequences of these interactions are not completely clear. METHODOLOGY/PRINCIPAL FINDINGS: In order to understand the molecular mechanisms involved in potential Abeta/alpha-syn interactions, immunoblot, molecular modeling, and in vitro studies with alpha-syn and Abeta were performed. We showed in vivo in the brains of patients with AD/PD and in transgenic mice, Abeta and alpha-synuclein co-immunoprecipitate and form complexes. Molecular modeling and simulations showed that Abeta binds alpha-syn monomers, homodimers, and trimers, forming hybrid ring-like pentamers. Interactions occurred between the N-terminus of Abeta and the N-terminus and C-terminus of alpha-syn. Interacting alpha-syn and Abeta dimers that dock on the membrane incorporated additional alpha-syn molecules, leading to the formation of more stable pentamers and hexamers that adopt a ring-like structure. Consistent with the simulations, under in vitro cell-free conditions, Abeta interacted with alpha-syn, forming hybrid pore-like oligomers. Moreover, cells expressing alpha-syn and treated with Abeta displayed increased current amplitudes and calcium influx consistent with the formation of cation channels. CONCLUSION/SIGNIFICANCE: These results support the contention that Abeta directly interacts with alpha-syn and stabilized the formation of hybrid nanopores that alter neuronal activity and might contribute to the mechanisms of neurodegeneration in AD and PD. The broader implications of such hybrid interactions might be important to the pathogenesis of other disorders of protein misfolding.
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“Co-immunoprecipitation experiments have shown that αSyn monomers, dimers, trimers and pentamers bind to monomeric Aβ in post-mortem samples from AD and DLB brains [67].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [67]
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Citations
Cites
A smooth particle mesh Ewald method
Essmann, U., Perera, L., Berkowitz, M., Darden, T., Lee, H.-C., & Pedersen, L. (1995) · The Journal of Chemical Physics · doi:10.1063/1.470117 · Cited by 21,378
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Lipid rafts and signal transduction
Simons, K., & Toomre, D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036052 · Cited by 5,371
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
Constant pressure molecular dynamics simulation: The Langevin piston method
Feller, S., Zhang, Y., Pastor, R., & Brooks, B. (1995) · The Journal of Chemical Physics · doi:10.1063/1.470648 · Cited by 4,271
McKeith, I. G., Galasko, D., Kosaka, K., Perry, E. K., Dickson, D. W., Hansen, L. A., Salmon, D. P., Lowe, J., Mirra, S. S., Byrne, E. J., et al. (1996) · Neurology · doi:10.1212/wnl.47.5.1113 · Cited by 3,960
Reversible multiple time scale molecular dynamics
Tuckerman, M. E., Berne, B. J., & Martyna, G. J. (1992) · The Journal of Chemical Physics · doi:10.1063/1.463137 · Cited by 3,623
NAMD2: Greater Scalability for Parallel Molecular Dynamics
Kalé, L. V., Skeel, R. D., Bhandarkar, M. A., Brunner, R., Gürsoy, A., Krawetz, N., Phillips, J., Shinozaki, A., Varadarajan, K., & Schulten, K. J. (1999) · Journal of Computational Physics · doi:10.1006/jcph.1999.6201 · Cited by 2,428
Masliah, E., Rockenstein, E. M., Veinbergs, I., Mallory, M. E., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., & Mucke, L. (2000) · Science · doi:10.1126/science.287.5456.1265 · Cited by 1,779
Self-citationCaughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Research works printed but not linked: 1
- IG McKeith, 1996, Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop., Neurology, 47, 1113, 10.1212/WNL.47.5.1113 · DOI · Paper page
Cited by
Sorted by citations
Items 201–281 of 281
Dementia in Germany: Past Trends and Future Developments
Ziegler, U. (2011) · DZNE Pub · doi:10.18453/rosdok_id00000815 · Cited by 11
Co‐pathologies modify hippocampal protein accumulation patterns in neurodegenerative diseases
Yoshida, K., Forrest, S. L., Ichimata, S., Tanaka, H., Kon, T., & Kovács, G. G. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14355 · Cited by 9
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Farmer, K. M., Gerson, J. E., & Kayed, R. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600103 · Cited by 10
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Tsiolaki, P. L., Nasi, G. I., Baltoumas, F. A., Louros, N. N., Magafa, V., Hamodrakas, S. J., & Iconomidou, V. A. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.02.008 · Cited by 10
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Liang, J., Li, R., Wong, G., & Huang, X. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00879-0 · Cited by 13
Ilyinsky, N. S., Nesterov, S. V., Shestoperova, E. I., Fonin, A. V., Uversky, V. N., & Gordeliy, V. (2021) · Biochemistry (Moscow) · doi:10.1134/s0006297921030056 · Cited by 9
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Horváth, I., Rocha, S., & Wittung-Stafshede, P. E. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7816-8_6 · Cited by 9
Bluhm, A., Schrempel, S., Schilling, S., von Hörsten, S., Schulze, A., Roßner, S., & Hartlage‐Rübsamen, M. (2022) · Biomolecules · doi:10.3390/biom12071006 · Cited by 8
Chen, L., Lu, H., Mao, L., Lin, J., & Liu, P. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e39194 · Cited by 9
Beyond amyloid plaque, targeting α-synuclein in Alzheimer disease: The battle continues
Al-Kuraishy, H. M., Sulaiman, G. M., Mohammed, H. A., Al-Gareeb, A. I., Albuhadily, A. K., Ali, A. A., & Abu-Alghayth, M. H. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102684 · Cited by 10
A diketoreductase exhibits unique renaturation profile from thermal-induced protein unfolding
Lü, M., Cao, X., Yang, X., Zheng, H., Liu, N., Jiang, Y., Lin, D., & Chen, Y. (2010) · Amino Acids · doi:10.1007/s00726-010-0491-9 · Cited by 8
What we can learn from animal models about cerebral multi-morbidity
Baker, S. L., & Götz, J. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0097-2 · Cited by 8
Electrophysiological and Imaging Calcium Biomarkers of Aging in Male and Female 5×FAD Mice
Ghoweri, A. O., Ouillette, L., Frazier, H. N., Anderson, K. L., Lin, R., Gant, J. C., Parent, R., Moore, S. J., Murphy, G. G., & Thibault, O. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200109 · Cited by 8
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Gasperini, R., & Small, D. H. (2011) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2011.05607.x · Cited by 8
Chan, D. K. Y., Braidy, N., Xu, Y. H., Chataway, T., Guo, F., Guillemin, G. J., Teo, C., & Gai, W. (2016) · Neurotoxicity Research · doi:10.1007/s12640-016-9644-2 · Cited by 8
α-Synuclein chaperone suppresses nucleation and amyloidogenesis of prion protein
Shirasaka, M., Kuwata, K., & Honda, R. P. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.10.120 · Cited by 8
Rad, F. R., Akbari, M. G., Zamani, M., Bayat, S., & Zamani, M. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02295-z · Cited by 7
Role of Prion Protein Oligomers in the Pathogenesis of Transmissible Spongiform Encephalopathies
Morales, R., Duran-Aniotz, C. A., & Soto, C. A. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_10 · Cited by 7
Yulianti, A. B., Sumarsono, S. H., Ridwan, A., & Yusuf, A. T. (2012) · Journal of Mathematical and Fundamental Sciences · doi:10.5614/itbj.sci.2012.44.4.3 · Cited by 7
Hartlage‐Rübsamen, M., Ratz, V., Zeitschel, U., Finzel, L., Machner, L., Köppen, J., Schulze, A., Demuth, H., von Hörsten, S., Höfling, C., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0726-2 · Cited by 7
A method of purifying alpha-synuclein in E. coli without chromatography
Kamboj, S., Harms, C., Kumar, L., Creamer, D., West, C., Klein‐Seetharaman, J., & Sarkar, S. K. (2021) · Heliyon · doi:10.1016/j.heliyon.2020.e05874 · Cited by 7
Shin, E. J., & Park, J. W. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c00058 · Cited by 7
Huin, C., Cronier, S., Guégan, P., Béringue, V., Rezaei, H., & Noinville, S. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108517 · Cited by 6
Muronets, V. I., Kudryavtseva, S. S., Kurochkina, L. P., Leisi, E. V., Stroylova, Y. Y., & Schmalhausen, E. V. (2025) · Biochemistry (Moscow) · doi:10.1134/s0006297924604003 · Cited by 5
Orr, A. A., Kuhlmann, S. K., & Tamamis, P. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106805 · Cited by 5
Jamerlan, A., Shim, K. H., Sharma, N., & An, S. S. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031199 · Cited by 5
Hao, Y.-N., Lu, Q., Zhai, Y.-H., Wang, H.-Y., Wu, M., Hu, M.-M., Yang, B., Wang, Z., Wu, Z., & Qi, J. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.10.003 · Cited by 5
Mechanistic Insight into the Suppression of Polyglutamine Aggregation by SRCP1
Haver, H. N., Wedemeyer, M. J., Butcher, E., Peterson, F. C., Volkman, B. F., & Scaglione, K. M. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00893 · Cited by 5
Friesen, M., Ziegler‐Waldkirch, S., Egenolf, M., d’Errico, P., Helm, C., Mezö, C., Dokalis, N., Erny, D., Katzmarski, N., Coelho, R., et al. (2021) · Brain Pathology · doi:10.1111/bpa.13032 · Cited by 4
Ahammad, R. U., Spencer, B. J., Quach, B., Salehi, S. N., & Rissman, R. A. (2025) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.70117 · Cited by 4
Self-citationVarenyk, Y., Theodorakis, P. E., Pham, D. Q. H., Li, M. S., & Krupa, P. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c00503 · Cited by 4
Exploring α-Syn’s Functions Through Ablation Models: Physiological and Pathological Implications
Praveen, A., Dougnon, G., & Matsui, H. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01560-2 · Cited by 4
Lim, M. J., Boschen, S. L., Kurti, A., Casey, M. C., Phillips, V. R., Fryer, J. D., Dickson, D. W., Jansen‐West, K. R., Petrucelli, L., Delenclos, M., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11102863 · Cited by 4
A New Interpretative Paradigm for Conformational Protein Diseases
Agnati, L. F., Guidolin, D., Woods, A. S., Ciruela, F., Carone, C., Vallelunga, A., Escuela, D. O. B., Genedani, S., & Fuxé, K. (2013) · Current Protein and Peptide Science · doi:10.2174/1389203711314020006 · Cited by 4
One or more β-amyloid(s)? New insights into the prion-like nature of Alzheimer's disease
Catania, M., & Fede, G. D. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.07.003 · Cited by 4
Aarsland, D., & Ravina, B. M. (2010) · Neurology · doi:10.1212/wnl.0b013e3181f6f272 · Cited by 4
Leitao, A. D. G., Spencer, B. J., Sarsoza, F. M., Ngolab, J., Amalraj, J., Masliah, E., Wu, C., & Rissman, R. A. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230232 · Cited by 3
Self-citationStylianopoulou, E., Daviti, A., Giourou, V., Gerasimidi, E., Nikolaou, A., Kourkoutas, Y., Grigoriou, M. E., Paleologou, K. E., & Skavdis, G. (2023) · Brain Sciences · doi:10.3390/brainsci14010035 · Cited by 5
Effect of APOE genotype on gray matter density in patients with Parkinson's disease
Chung, S. J., Lee, J. E., Hong, J. Y., Lim, S., Kim, M. H., Sohn, Y. H., & Lee, P. H. (2012) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2012.06.001 · Cited by 3
Li, R., Huang, X., Shen, L., Zhang, T., Liu, N., Hou, X., & Wong, G. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05383-0 · Cited by 3
Qiang, Q., Skudder‐Hill, L., Toyota, T., Huang, Z., Wei, W., & Adachi, H. (2025) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2025.02.008 · Cited by 3
Amyloid-Like Peptide Aggregates
Kokotidou, C., Tamamis, P., & Mitraki, A. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839161148-00217 · Cited by 3
Protein Misfolding and Toxicity in Dialysis-Related Amyloidosis
Hodkinson, J. P., Ashcroft, A. E., & Radford, S. E. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_12 · Cited by 3
Parkinson Dementia: PET Findings
Bohnen, N. I., & Frey, K. A. (2014) · Springer eBooks · doi:10.1007/978-3-642-54307-4_16 · Cited by 3
Parkinsonian Dementias: PET Findings
Kanel, P., Müller, M. L. T. M., & Bohnen, N. I. (2020) · Springer eBooks · doi:10.1007/978-3-030-53168-3_16 · Cited by 4
Nakamura, K., Tagai, K., Shinotoh, H., Hirano, S., Kitamura, S., Endo, H., Takahata, K., Takado, Y., Zhang, M., Kawamura, K., et al. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251351220 · Cited by 2
Ильинский, Н. С., Nesterov, S. V., Shestoperova, E. I., Fonin, A. V., Уверский, В. Н., & Gordeliy, V. (2021) · Biochemistry (Moscow) · doi:10.31857/s0320972521030040 · Cited by 2
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Pujari, G. R., Subramanian, V., & Rao, S. R. (2022) · Pharmaceutical Sciences Asia · doi:10.29090/psa.2022.03.21.254 · Cited by 1
Singh, S., Capacio, A., Braun, C. A., Carroll‐Portillo, A., Ryman, S. G., & Lin, H. C. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1672793 · Cited by 1
Yakubu, U. M., Catumbela, C. S. G., Morales, R., & Morano, K. A. (2020) · Open Biology · doi:10.1098/rsob.200282 · Cited by 1
Huntingtin aggregation at interfaces associated with membranes and organelles
Adegbuyiro, A. (2021) · doi:10.33915/etd.8315 · Cited by 1
Blanc, A. (2013) · Digital Commons - PCOM (Philadelphia College of Osteopathic Medicine)
CSF α-synuclein, tau, and amyloid β in Parkinson's disease
Sixel‐Döring, F. (2011)
An equilibrium model for the formation of apoC-II amyloid fibrils
Yang, S. (2012) · Minerva Access (University of Melbourne)
Alpha-synuclein expression influences the processing of the amyloid precursor protein
Hall‐Roberts, H. (2016) · The University of Bath Online Publications Store (The University of Bath)
Exploring the Role of Somatostatin in the Pathogenesis of Alzheimer’s disease
Solarski, M. (2018) · TSpace (University of Toronto)
Influences of the Global Deterioration Scale according to Routine Blood Chemistry Results
Kim, S.-G., & Park, C.-E. (2019) · Korean Journal of Clinical Laboratory Science · doi:10.15324/kjcls.2019.51.3.351
Divergence in Neuronal Calcium Dysregulation in Brain Aging and Animal Models of AD
Ghoweri, A. O. (2020) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2020.521
TAKAHASHI, J. C., & Morizane, A. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734318078.793555630
Faculty Opinions recommendation of SRCP1 conveys resistance to polyglutamine aggregation.
Gomer, R. H. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733671907.793549116
Daniele, S., Baldacci, F., Piccarducci, R., Palermo, G., Giampietri, L., Manca, M. L., Pietrobono, D., Frosini, D., Nicoletti, V., Tognoni, G., et al. (2020) · doi:10.21203/rs.3.rs-18776/v1
Role of the Gut Microbiome and Bacterial Amyloids in the Development of Synucleinopathies (Review)
Trubitsina, N. P., Matiiv, A. B., Rogoza, T. M., Zudilova, A. A., Bezgina, M. D., Zhouravleva, G. A., & Bondarev, S. A. (2024) · Biochemistry (Moscow) · doi:10.31857/s0320972524030089
Structural polymorphism in amyloids—states within proteins’ solid-state
Dhakal, S., & Rangachari, V. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21809-5.00024-7
Editors, T. P. O. (2025) · PLoS ONE · doi:10.1371/journal.pone.0321152
RetractedAge-related trends in amyloid positivity in Parkinson’s disease without dementia
Hatano, K., Kameyama, M., Kurihara, M., Ohse, K., Goto, R., Ihara, R., Higashihara, M., Sengoku, R., Nishina, Y., Kanemaru, K., et al. (2025) · Aging · doi:10.18632/aging.206297
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Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788590
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788593
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788602
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788596
Lloyd, G. M., Dhillon, J.-K. S., Gorion, K.-M. M., Riffe, C. J., Fromholt, S., Xia, Y., Giasson, B. I., & Borchelt, D. R. (2021) · Figshare · doi:10.6084/m9.figshare.16599506
Carvalho, F., Maximiano, P., Hashemi, M., & Simões, P. N. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.29.702600
Binding and internalization of exogenous protein assemblies by mammalian cells
Ruiz-Arlandis, G. (2015) · theses.fr (ABES) · doi:10.70675/437e0532ze4e1z4966z80e5z340b6fd3c49d
Romdhan, S. B. (2019) · theses.fr (ABES) · doi:10.70675/6735d8bdz3448z4836z8b6dzffcd8f2bd2da
Développement et caractérisation de nouveaux modèles murins de maladie à corps de Lewy
Schueller, E. (2020) · theses.fr (ABES) · doi:10.70675/4a313736z3f42z4d92zb1c1ze3cbd7bbe9f6
Xie, H., Zhu, M., Zhu, Z., Tang, J. W., Zhang, R., Ding, Z., Li, J., Wu, Z., Tam, P. K. H., Wang, Q., et al. (2026) · Advanced Science · doi:10.1002/advs.76054 · Cited by 1
Targeting protein aggregate co-pathologies in neurodegeneration: a viable therapeutic strategy?
Buck, S. A., Madhavan, S. S., & Sanders, L. H. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00047-8
Greimel, S. J. (2014) · University of Minnesota Digital Conservancy (University of Minnesota)
Metadata
- Authors
- Tsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., Yuan, J. X.-J., & Masliah, E.
- Affiliations
- San Diego Supercomputer Center (US)
- University of California San Diego (US)
- Corresponding author
- Masliah, Eliezer
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2008-09-04
- Volume
- 3
- Issue
- 9
- Pages
- e3135
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC2519786
- OpenAlex
- W2065878937
- Cited by
- 281
- References
- 115
- Citations by year
- 2026: 3 · 2025: 12 · 2024: 14 · 2023: 14 · 2022: 13 · 2021: 18 · 2020: 25 · 2019: 20 · 2018: 18 · 2017: 22 · 2016: 16 · 2015: 18 · 2014: 14 · 2013: 9 · 2012: 21
- FWCI
- 9.93
- Type
- journal article
- Language
- en
- Status
- Retracted
- Update notices
- retraction (2025-03-18)
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, public-domain)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- U.S. Department of Energy
- National Institutes of Health (AG‐18440)
- National Institute on Aging (R37AG018440, R01AG018440, AG 18440)
- National Heart, Lung, and Blood Institute (R01HL066012, HL066012)
- Argonne National Laboratory
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, Parkinson's disease, amyloid-beta, alpha-synuclein, protein-protein interaction, protein misfolding, Lewy body disease, nanopores, cation channels, calcium influx, protein aggregation, transgenic mice
- MeSH terms
- Alzheimer Disease, Animals, Brain, Calcium, Computer Simulation, Electrophysiology, Humans, Mice, Transgenic, Parkinson Disease, Protein Denaturation, Protein Structure, Tertiary, Protein Folding, Lewy Body Disease, Mice, alpha-Synuclein
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 ›
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