The DOI matches its Crossref record; 159 of the 159 references it cites were found in a registry or an index.
Pathology of Neurodegenerative Diseases
Open accessAbstract
Neurodegenerative disorders are characterized by progressive loss of selectively vulnerable populations of neurons, which contrasts with select static neuronal loss because of metabolic or toxic disorders. Neurodegenerative diseases can be classified according to primary clinical features (e.g., dementia, parkinsonism, or motor neuron disease), anatomic distribution of neurodegeneration (e.g., frontotemporal degenerations, extrapyramidal disorders, or spinocerebellar degenerations), or principal molecular abnormality. The most common neurodegenerative disorders are amyloidoses, tauopathies, α-synucleinopathies, and TDP-43 proteinopathies. The protein abnormalities in these disorders have abnormal conformational properties. Growing experimental evidence suggests that abnormal protein conformers may spread from cell to cell along anatomically connected pathways, which may in part explain the specific anatomical patterns observed at autopsy. In this review, we detail the human pathology of select neurodegenerative disorders, focusing on their main protein aggregates.
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
“The presence of NFTs in the brain triggers a complex cascade of biochemical and cellular processes that result in neurodegeneration and neuronal loss [2].”
From Diffusion tensor imaging reveals whole-brain microstructural changes in the P301L mouse model of tauopathy. (2020) · cites this paper as [2]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“AD is the most prevalent of tauopathies and is considered a secondary tauopathy because tau aggregation is regarded as a response to other pathological proteins or events (Aβ), but it is not driven by tau mutations (19, 65).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [65]
The cited source says what the claim attributes to it.
In the citing paper
“Both 3R- and 4R-tau isoforms were detected with no noticeable difference in the 3R to 4R ratio between LOAD and HC 3D-CNs, consistent with the concept that AD is a mixed 3R/4R tauopathy (65, 66) (Fig. 3D).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [65]
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
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 3×
“Staging schemes have been developed for Alzheimer’s disease (AD) (Braak and Braak 1991; Thal et al. 2002), Parkinson’s disease (PD) (Braak et al.”
BackgroundStaging of brain pathology related to sporadic Parkinson’s disease
Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777
Hughes, A. J., Daniel, S. E., Kilford, L., & Lees, A. J. (1992) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.55.3.181 · Cited by 10,378
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
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
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,221
Diagnosis and management of dementia with Lewy bodies: Third report of the DLB consortium
McKeith, I. G., Dickson, D. W., Lowe, J., Emre, M., O'Brien, J. T., Feldman, H., Cummings, J., Duda, J. E., Lippa, C., Perry, E. K., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000187889.17253.b1 · Cited by 5,069
Self-citation
Cited by
Sorted by citations
Items 701–800 of 1,000
The Neuroprotective Potential of Endophytic Fungi and Proposed Molecular Mechanism: A Current Update
Semwal, P., Painuli, S., Anand, J., Martins, N. A., Machado, M., Sharma, R., Batiha, G. E., Yaro, C. A., Lorenzo, J. M., & Rahman, M. M. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/6214264 · Cited by 14
Linking Puberty and the Gut Microbiome to the Pathogenesis of Neurodegenerative Disorders
Esposito, P., & Ismail, N. (2022) · Microorganisms · doi:10.3390/microorganisms10112163 · Cited by 14
Lee, K. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00920-5 · Cited by 14
Onaolapo, A. Y., Ojo, F. O., Adeleye, O. O., Falade, J., & Onaolapo, O. J. (2023) · Current Diabetes Reviews · doi:10.2174/1573399819666230102141154 · Cited by 14
Nitta, Y., Kawai, H., Maki, R., Osaka, J., Hakeda‐Suzuki, S., Nagai, Y., Doubková, K., Uehara, T., Watanabe, K., Kosaki, K., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddac307 · Cited by 14
Załuski, M., Karcz, T. P., Drabczyńska, A., Vielmuth, C., Olejarz‐Maciej, A., Głuch‐Lutwin, M., Mordyl, B., Siwek, A., Satała, G., Müller, C. E., et al. (2023) · Biomolecules · doi:10.3390/biom13071079 · Cited by 14
Biomimetic IGA neuron growth modeling with neurite morphometric features and CNN-based prediction
Qian, K., Liao, A. S., Gu, S., Webster‐Wood, V. A., & Zhang, Y. J. (2023) · Computer Methods in Applied Mechanics and Engineering · doi:10.1016/j.cma.2023.116213 · Cited by 14
Yin, Z., Chen, J., Xia, M., Zhang, X., Li, Y., Chen, Z., Bao, Q.-N., Zhong, W., Yao, J., Wu, K., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-39520-9 · Cited by 15
Criado‐Marrero, M., Gebru, N. T., Gould, L. A., Blazier, D. M., Vidal-Aguiar, Y., Smith, T. M., Abdelmaboud, S. S., Shelton, L. B., Wang, X., Dahrendorff, J., et al. (2021) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-021-00062-x · Cited by 15
Neurodegenerative Disease Transmission and Transgenesis in MicePreprint
Dugger, B. N., Perl, D. P., & Carlson, G. A. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a023549 · Cited by 14
Self-citationLu, C., Xu, C., & Yang, J. (2024) · Medicina · doi:10.3390/medicina61010017 · Cited by 14
Histone demethylases in neurodevelopment and neurodegenerative diseases
Wang, H., Guo, B., & Guo, X. (2023) · International Journal of Neuroscience · doi:10.1080/00207454.2023.2276656 · Cited by 13
Reed, A. L., Mitchell, W., Alexandrescu, A. T., & Alder, N. N. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1263420 · Cited by 13
Protective role of serum albumin in dementia: a prospective study from United Kingdom biobank
Cui, Y., Li, C., Ke, B., Xiao, Y., Wang, S., Jiang, Q., Zheng, X., Lin, J., Huang, J., & Shang, H. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1458184 · Cited by 13
Parkinson’s disease models and death signaling: what do we know until now?
Pedrão, L. F. A. T., Medeiros, P., Leandro, E. C., & Falquetto, B. (2024) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2024.1419108 · Cited by 13
Neuroglia in Neurodegeneration: Exploring Glial Dynamics in Brain Disorders
Dar, N. J., Bhat, J. A., John, U., & Bhat, S. A. (2024) · Neuroglia · doi:10.3390/neuroglia5040031 · Cited by 14
Takhor, N. H., & Phan, C. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01746-6 · Cited by 13
Shafie, A. S. M., Kamarudin, S. N., Affandi, M. M. R. M. M., & Siran, R. (2025) · Nutritional Neuroscience · doi:10.1080/1028415x.2025.2499559 · Cited by 13
Htt is a repressor of Abl activity required for APP-induced axonal growth
Marquilly, C., Busto, G. U., Leger, B. S., Boulanger, A., Giniger, E., Walker, J. A., Fradkin, L. G., & Dura, J. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009287 · Cited by 13
TSPO Ligands Protect against Neuronal Damage Mediated by LPS‐Induced BV‐2 Microglia Activation
Ma, B., Liu, Y., Xiao, Z., Zhang, R., Zhang, Z., Zhang, Z., Liu, J., Juan, Z., Sun, X., Sun, L., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/5896699 · Cited by 15
Han, T., Zhang, S., Wei, R.-Y., Jia, G., Wang, B., Xu, Q., Su, J., Jiang, C., & Jin, C. (2022) · Fitoterapia · doi:10.1016/j.fitote.2022.105207 · Cited by 13
Neuroinflammation in early, late and recovery stages in a progressive parkinsonism model in rats
Cunha, D. M. G., Becegato, M. S., Meurer, Y. D. S. R., Lima, A. C., Gonçalves, N., Bioni, V. S., Engi, S. A., Bianchi, P., Cruz, F. C., dos Santos, J. R., et al. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.923957 · Cited by 14
Dar, G. H., Badierah, R., Nathan, E., Bhat, M. A., Dar, A. H., & Redwan, E. M. M. M. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.967231 · Cited by 13
Acero, N., Ortega, T., Villagrasa, V., Leon, G., Mingarro, D. M., Castillo, E., González‐Rosende, M. E., Borrás, S., Rı́os, J. L., Bosch‐Morell, F., et al. (2023) · Phytotherapy Research · doi:10.1002/ptr.7727 · Cited by 13
Singh, R. J., Hussain, J., Kaur, A., Jamdare, B. G., Pathak, D., Garg, K., Kaur, R., Shankar, S., & Sunkaria, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102002 · Cited by 14
Khan, Z., Hong, S., Lee, J.-W., Moon, E., Huh, J., Chang, K., & Kim, S. Y. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104432 · Cited by 13
Basic Microglial Functions and How They Go Awry in Neurodegenerative Disease
McKinney, J. E., Bennett, M. L., & Bennett, F. C. (2026) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-042624-114332 · Cited by 13
Potential Roles of Sestrin2 in Alzheimer’s Disease: Antioxidation, Autophagy Promotion, and Beyond
Chen, S., Yang, J., Hsieh, Y.-H., Lin, T., Lin, Y., Chao, A., & Yang, D. (2021) · Biomedicines · doi:10.3390/biomedicines9101308 · Cited by 13
Metabolomics as a Crucial Tool to Develop New Therapeutic Strategies for Neurodegenerative Diseases
Lanznaster, D., Dingeo, G., Samey, R. A., Emond, P., & Blasco, H. (2022) · Metabolites · doi:10.3390/metabo12090864 · Cited by 12
Das, S., & Ramanan, N. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1032504 · Cited by 13
Solid-to-liquid phase transition in the dissolution of cytosolic misfolded-protein aggregates
Tomaszewski, A., Wang, R., Sandoval, E., Zhu, J., Liu, J., & Li, R. (2023) · iScience · doi:10.1016/j.isci.2023.108334 · Cited by 12
Neuroprotective Effects of Bromelain on the Common Neurodegenerative Diseases: A Systematic Review
Rostamian, S., Raeisi, E., Heidari-Soureshjani, S., & Sherwin, C. M. T. (2023) · Neurochemical Journal · doi:10.1134/s1819712423040256 · Cited by 13
Tannic acid as a biphasic modulator of tau protein liquid–liquid phase separation
Xiang, J., Chen, J., Liu, Y., Ye, H., Han, Y., Li, P., Gao, M. Y., & Huang, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133578 · Cited by 12
Cheng, T., Afshan, N., Jiao, J., & Jiao, J. (2024) · Biosensors and Bioelectronics X · doi:10.1016/j.biosx.2024.100528 · Cited by 12
Liang, J., Zhu, Y., Liu, S., Kuang, B., Tian, Z., Zhang, L., Yang, S., Lin, M., Chen, N., Liu, X., et al. (2024) · Phytotherapy Research · doi:10.1002/ptr.8322 · Cited by 13
Chaubey, S., & Singh, L. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03515-8 · Cited by 12
Balakrishnan, P., Junaid, S., Ahmad, S., Wang, K., Hindalekar, Y. S., Shokr, H., Upadhya, M. A., Hopkins, S., Sacharczuk, J., Rana, K. S., et al. (2024) · Journal of Pharmaceutical Investigation · doi:10.1007/s40005-024-00711-9 · Cited by 12
Robust In Vitro Models for Studying Parkinson’s Disease? LUHMES Cells and SH-SH5Y Cells
Keighron, C. N., Avazzedeh, S., & Quinlan, L. R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252313122 · Cited by 13
Mravinacová, S., Bergström, S., Olofsson, J., José, N. G. D. S., Anderl‐Straub, S., Diehl‐Schmid, J., Fassbender, K. C., Fließbach, K., Jahn, H., Kornhuber, J., et al. (2025) · Scientific Reports · doi:10.1038/s41598-024-83281-y · Cited by 12
Reiriz, M., Beltrán-Velasco, A. I., Echeverry‐Alzate, V., Miguel, E. M., Gómez-Senent, S., Uceda, S., & Clemente‐Suárez, V. J. (2025) · Nutrients · doi:10.3390/nu17030391 · Cited by 12
Mechanistic insights into connexin-mediated neuroglia crosstalk in neurodegenerative diseases
Denaro, S., D’Aprile, S., Vicario, N., & Parenti, R. (2025) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2025.1532960 · Cited by 12
Piccirillo, S., Preziuso, A., Serfilippi, T., Cerqueni, G., Terenzi, V., Lariccia, V., & Magi, S. (2025) · Current Neuropharmacology · doi:10.2174/011570159x345397241210103538 · Cited by 12
Structural basis of a distinct α-synuclein strain that promotes tau inclusion in neurons
Sun, C., Zhou, K., DePaola, P., Li, C., Lee, V. M. ‐., Zhou, Z. H., Peng, C., & Jiang, L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108351 · Cited by 12
ABI-Net: Attention-Based Inception U-Net for Brain Tumor Segmentation From Multimodal MRI Images
Rutoh, E. K., Zhi-guang, Q., Bore, J. C., & Bahadar, N. (2025) · IEEE Access · doi:10.1109/access.2025.3585926 · Cited by 12
Onaolapo, O. J., Olofinnade, A. T., Ojo, F. O., & Onaolapo, A. Y. (2021) · Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry · doi:10.2174/1871523021666220815151559 · Cited by 12
Neuroprotective effects of betanin in mice with cerebral ischemia-reperfusion injury
Thong-asa, W., Puenpha, K., Lairaksa, T., & Saengjinda, S. (2023) · EXPERIMENTAL ANIMALS · doi:10.1538/expanim.22-0176 · Cited by 12
Chen, W., He, L., Pei, H., Li, J., Zhao, Y. D., Zong, Y., Kan, H., He, Z., & Du, R. (2023) · Aging · doi:10.18632/aging.204627 · Cited by 12
Effective Inhibition of TDP‐43 Aggregation by Native State Stabilization
Yang, L., Jasiqi, Y., Zettor, A., Vadas, O., Chiaravalli, J., Agou, F., & Lashuel, H. A. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202314587 · Cited by 12
Chronic Traumatic Encephalopathy: A Comparison with Alzheimer's Disease and Frontotemporal Dementia
Lesman‐Segev, O. H., Edwards, L., & Rabinovici, G. D. (2020) · Seminars in Neurology · doi:10.1055/s-0040-1715134 · Cited by 13
Dissolving the Complex Role Aggregation Plays in Neurodegenerative Disease
Croce, K. R., & Yamamoto, A. (2021) · Movement Disorders · doi:10.1002/mds.28522 · Cited by 12
Breast cancer type 1 and neurodegeneration: consequences of deficient DNA repair
Leung, E., & Hazrati, L. (2021) · Brain Communications · doi:10.1093/braincomms/fcab117 · Cited by 14
Benchoua, A., Lasbareilles, M., & Tournois, J. (2021) · Cells · doi:10.3390/cells10123290 · Cited by 14
Potential role of exosome in post-stroke reorganization and/or neurodegeneration
Azizi, F., Askari, S., Javadpour, P., Hadjighassem, M., & Ghasemi, R. (2020) · EXCLI journal · doi:10.17179/excli2020-3025 · Cited by 12
Huszar, I. N., Pallebage-Gamarallage, M., Foxley, S., Tendler, B. C., Leonte, A., Hiemstra, M., Mollink, J., Smart, A., Bangerter-Christensen, S., Brooks, H., et al. (2019) · doi:10.1101/849570 · Cited by 11
Athalye, C., Bahena, A., Khandelwal, P., Emrani, S., Trotman, W., Levorse, L. M., Khodakarami, Z., Ohm, D. T., Teunissen‐Bermeo, E., Capp, N., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02030-y · Cited by 11
Targeting lipid metabolism in neurodegenerative diseases: From experimental to clinical
Long, J., Liu, S., Shi, Y., Zhang, C., Li, Q., & Ai, Q. (2025) · Metabolism · doi:10.1016/j.metabol.2025.156436 · Cited by 12
Aetiology and pathophysiology of neurodegenerative disorders
Sahoo, R. K., Gupta, T., Smily, Kumar, V., Rani, S., & Gupta, U. D. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85544-0.00006-x · Cited by 13
Can Brain-derived Neurotrophic Factor (BDNF) Mimetics be a Way Out for Neurodegenerative Diseases?
Korkmaz, O. T. (2023) · Current Pharmaceutical Design · doi:10.2174/1381612829666230127142414 · Cited by 11
Tau expression and phosphorylation in enteroendocrine cells
Chapelet, G., Béguin, N., Castellano, B., Grit, I., de Coppet, P., Oullier, T., Neunlist, M., Blottière, H. M., Rolli‐Derkinderen, M., Dréan, G. L., et al. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1166848 · Cited by 13
Anti-Aging of the Nervous System and Related Neurodegenerative Diseases With Chinese Herbal Medicine
Du, X., Lou, N., Hu, S., Xiao, R., Chu, C., Huang, Q., Lü, L., Li, S., & Yang, J. (2023) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/15333175231205445 · Cited by 11
Beneficial Effects of Spirulina on Brain Health: A Systematic Review
Kumar, S., Saha, S., Singh, K., Singh, T., Miahra, A. K., Dubey, B. N., & Singh, S. (2024) · Current Functional Foods · doi:10.2174/0126668629269256231222092721 · Cited by 17
Beta-caryophyllene in psychiatric and neurological diseases: Role of blood-brain barrier
Mallmann, M. P., & Oliveira, M. S. (2024) · Vitamins and hormones · doi:10.1016/bs.vh.2024.02.004 · Cited by 11
The Neuromuscular Disorder Mediated by Extracellular Vesicles in Amyotrophic Lateral Sclerosis
Carata, E., Muci, M., Giulio, S. D., Giulio, T. D., Mariano, S., & Panzarini, E. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46060358 · Cited by 11
Sun, X., Badachhape, A., Bhandari, P., Chin, J., Annapragada, A., & Tanifum, E. A. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1428736 · Cited by 11
Coffee's protective mechanisms against neurodegeneration
Raeis-Abdollahi, E., Raise‐Abdullahi, P., Rashidy‐Pour, A., Meamar, M., & Askari, H. (2024) · Progress in brain research · doi:10.1016/bs.pbr.2024.06.017 · Cited by 11
Live-cell visualization of tau aggregation in human neurons
Hurtle, B. T., Donnelly, C. J., Zhang, X., & Thathiah, A. (2024) · Communications Biology · doi:10.1038/s42003-024-06840-z · Cited by 12
GHRH and its analogues in central nervous system diseases
Liu, Y., Fu, R., Jia, H. M., Yang, K., Ren, F., & Zhou, M.-S. (2024) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-024-09920-x · Cited by 11
Zhu, F., Yin, S., Wang, Y., Zhong, Y., Ji, Q., & Wu, J. (2024) · International Journal of General Medicine · doi:10.2147/ijgm.s499406 · Cited by 11
ts RNA s: A Prospective, Effective Therapeutic Intervention for Neurodegenerative Diseases
Li, T., Zhen, H., Wu, W., Yang, F., & Cao, Z. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70177 · Cited by 11
The role of mitochondrial remodeling in neurodegenerative diseases
Guan, D., Liang, C., Zheng, D., Liu, S., Luo, J., Cai, Z., Zhang, H., & Chen, J. (2025) · Neurochemistry International · doi:10.1016/j.neuint.2024.105927 · Cited by 11
Goudarzi, N., Taheri, Z., Salari, A. M. N., Kazemzadeh, K., & Tafakhori, A. (2025) · Reviews in the Neurosciences · doi:10.1515/revneuro-2024-0125 · Cited by 12
Li, X., Jin, S., Wang, D., Wu, Y., Tang, X., Liu, Y., Yao, T., Han, S., Sun, L., Wang, Y., et al. (2025) · Advanced Science · doi:10.1002/advs.202414260 · Cited by 11
Maazouzi, M., Rasheed, M., Mbarek, L., Wang, X., Liang, J., Ma, H., Chen, Z., & Deng, Y. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70031 · Cited by 11
Jeyabalan, J. B., Vignesh Pandi, A., Sankar, V., Sivasamy, R., Dhanasekaran, M., & Justin, A. (2025) · Neurological Sciences · doi:10.1007/s10072-025-08421-2 · Cited by 11
Pan-neurodegeneration proteomics reveals disease subtypes and molecular signatures
Shrestha, H. K., Sun, H., Yarbro, J. M., Lee, D., Liu, D., Wang, E., McReynolds, M. G., Zhang, N., Xie, B., Yang, S., et al. (2026) · Cell · doi:10.1016/j.cell.2026.02.026 · Cited by 11
Self-citationNanomedicines and Nanodrug Delivery Systems: Trends and Perspectives
Das, S., Das, M. K., Deka, T., Singha, L. R., & Das, P. (2020) · Springer eBooks · doi:10.1007/978-981-15-6255-6_6 · Cited by 11
Affective empathy in neurodegenerative disorders: The importance of measurement type
Wright, J. K. X., Grainger, S. A., Coundouris, S. P., & Henry, J. D. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.05.020 · Cited by 11
Exercise, Diet and Sleeping as Regenerative Medicine Adjuvants: Obesity and Ageing as Illustrations
Ghanemi, A., Yoshioka, M., & St‐Amand, J. (2022) · Medicines · doi:10.3390/medicines9010007 · Cited by 11
Yoon, H., Park, M., Yeom, S., Kirkcaldie, M., Summons, P., & Lee, S. (2021) · IEEE Access · doi:10.1109/access.2021.3132401 · Cited by 11
Teli, P., Kale, V. P., & Vaidya, A. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114107 · Cited by 11
Recent Advances Towards Diagnosis and Therapeutic Fingerprinting for Alzheimer’s Disease
Pradhan, L. K., Sahoo, P. K., Chauhan, S., & Das, S. K. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02009-7 · Cited by 11
Wang, Y., Liu, Z., Wei, J., Di, L., Wang, S., Wu, T., & Li, N. (2022) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2022.115430 · Cited by 12
Galectins—Potential Therapeutic Targets for Neurodegenerative Disorders
Chaudhary, S. S., Chaudhary, S. S., Rawat, S., Kulkarni, A., Bilgrami, A. L., Perveen, A., Alghamdi, B. S. A., Zughaibi, T. A., Ashraf, G. M., Alam, M. Z., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911012 · Cited by 12
Dendrimers-Based Drug Delivery System: A Novel Approach in Addressing Parkinson’s Disease
Ordonio, M. B., Zaki, R. M., & Elkordy, A. (2022) · Future Pharmacology · doi:10.3390/futurepharmacol2040027 · Cited by 11
Mechanisms of Protein Trafficking and Quality Control in the Kidney and Beyond
Shaw, J. L., Pablo, J. L., & Greka, A. (2023) · Annual Review of Physiology · doi:10.1146/annurev-physiol-031522-100639 · Cited by 15
D’Amico, G., Santonocito, R., Vitale, A. M., Scalia, F., Marino, A., Campanella, C., Bucchieri, F., Cappello, F., & Bavisotto, C. C. (2023) · Cells · doi:10.3390/cells12111498 · Cited by 11
The neuropathological landscape of Hispanic and non-Hispanic White decedents with Alzheimer disease
Scalco, R., Saito, N. H., Beckett, L. A., Nguyen, M.-L., Huie, E. Z., Wang, H.-P., Flaherty, D., Honig, L. S., DeCarli, C. S., Rissman, R. A., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01574-1 · Cited by 11
Self-citationErrico, S., Lucchesi, G., Odino, D., Osman, E. Y., Cascella, R., Neri, L., Capitini, C., Calamai, M., Bemporad, F., Cecchi, C., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00182 · Cited by 12
Qais, F. A., Parveen, N., Afzal, M. F., Furkan, M., & Khan, R. H. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128900 · Cited by 11
Advancements in the study of synaptic plasticity and mitochondrial autophagy relationship
Zhu, Y., Hui, Q., Zhang, Z., Fu, H., Qin, Y., Zhao, Q., Li, Q., Zhang, J., Guo, L., He, W., et al. (2024) · Journal of Neuroscience Research · doi:10.1002/jnr.25309 · Cited by 11
Bendstrup, N., Hejl, A., & Salvesen, L. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215616 · Cited by 11
Srinivasan, E., Chandrasekhar, G., & Rajasekaran, R. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109318 · Cited by 11
Editorial: The role of exosomes in neuroinflammation and neurodegeneration
Wang, Y., & Xia, X. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1109885 · Cited by 11
Sejda, A., Wierzba‐Bobrowicz, T., Adamek, D., Gulczyński, J., Michalak, S., Grajkowska, W., & Iżycka‐Świeszewska, E. (2021) · Neurologia i Neurochirurgia Polska · doi:10.5603/pjnns.a2021.0088 · Cited by 10
The role of ferroptosis in central nervous system damage diseases
Li, M., Jin, S., Zhu, X., Xu, J., Cao, Y., & Piao, H. (2024) · PeerJ · doi:10.7717/peerj.16741 · Cited by 10
The effect of epigenetic aging on neurodegenerative diseases: a Mendelian randomization study
Fan, J., Liu, Q., Liu, X., Gong, M., Leong, I. I., Tsang, Y., Xu, X., Lei, S., Duan, L., Zhang, Y., et al. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1372518 · Cited by 10
Exploring therapeutic potential: Targeting TRPM7 in neurodegenerative diseases
Soni, D., Khan, H., Chauhan, S., Kaur, A., Dhankhar, S., Garg, N., & Singh, T. G. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113142 · Cited by 10
Wang, Z., Yang, C., Wang, X., Liao, H., Liu, X., Liu, H., Zhang, M., Zhang, L., & Wang, H. (2024) · Aging Cell · doi:10.1111/acel.14418 · Cited by 10
Saiyisan, A., Zeng, S., Zhang, H., Wang, Z., Wang, J., Cai, P., & Huang, J. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01246 · Cited by 10
Furan Acids from Nutmeg and Their Neuroprotective and Anti-neuroinflammatory Activities
Le, T. T., Tran, S. H., Lee, S., Kang, S. W., Kim, J. H., Park, K., Kim, C. S., Kim, M., Kang, K., & Jung, S. H. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c02528 · Cited by 10
Metadata
- Authors
- Dugger, B. N., & Dickson, D. W.
- Affiliations
- University of California, San Francisco (US)
- Mayo Clinic in Florida (US)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2017-01-06
- Volume
- 9
- Issue
- 7
- Pages
- a028035
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC5495060
- OpenAlex
- W2570634615
- Cited by
- 1,665
- References
- 159
- Citations by year
- 2026: 161 · 2025: 265 · 2024: 319 · 2023: 334 · 2022: 233 · 2021: 210 · 2020: 98 · 2019: 21 · 2018: 14 · 2017: 7
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Henry M. Jackson Foundation
- CurePSP
- Daiichi-Sankyo
- National Institutes of Health (AG016574, NS084974, AG002132, NS072187, AG037491)
- National Institute on Aging (P01AG002132, R01AG037491, P50AG016574)
- National Institute of Neurological Disorders and Stroke (P01NS084974, P50NS072187)
- Daiichi Sankyo Europe
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- neurodegenerative diseases, proteinopathies, amyloidosis, tauopathy, synucleinopathies, TDP-43 proteinopathy, protein aggregation, protein conformation, prion-like spread, selective neuronal loss, dementia, parkinsonism, motor neuron disease, frontotemporal lobar degeneration, extrapyramidal disorders, spinocerebellar degeneration
- MeSH terms
- Humans, Protein Conformation, Neurodegenerative Diseases, Protein Aggregates
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
