Protein transmission in neurodegenerative disease

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

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

Staging 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

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

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484

Investigating key factors underlying neurodegeneration linked to alpha‐synuclein spread

Pang, C. C.-C., Sørensen, M. H., Lee, K., Luk, K. C., Trojanowski, J. Q., Lee, V. M. ‐., Noble, W. J., & Chang, R. C. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12829 · Cited by 4

Protein misfolding and its dual role in neurodegeneration and cancer progression

Jamwal, R. S., Sharma, B., Minerva, Gupta, A., Misri, S., Shankaryan, R., Shah, R., & Kumar, R. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.001 · Cited by 4

Seeding biosensor cell line that reproduces the Alzheimer tau fold

Katsinelos, T., Lövestam, S., Qi, C., Falcon, B., Macdonald, J. A., Stephenson, G., Ghetti, B. F., McKee, A. C., Scheres, S. H. W., & Goedert, M. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110952 · Cited by 4

From concept to application: Exploring the evolution and potential of DUBTAC technology

Wang, D., Min, W., Jiang, B., Sun, H., Sun, C., & Yang, P. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.11.022 · Cited by 6

Vaccines mimicking conformational epitopes on α-synuclein fibrils provide immunity to Parkinson’s disease

Ma, L., Reithofer, S., Pesch, V., Flores-Fernández, J. M., Sriraman, A., Duckering, C., Amidian, S., Özdüzenciler, P., Müller, L. D., Holger, W., et al. (2026) · Brain · doi:10.1093/brain/awag010 · Cited by 4

Multifaceted performances of α-synuclein in health and neurological diseases

Wang, M., Xu, Y., Wang, S., Liang, J., Cui, X., Zhang, C., Yang, J., Sun, L., & Jin, M. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.02.031 · Cited by 4

Dysregulation of the TFEB-ATP6V0C axis in microglia exacerbates α-synuclein pathology through impaired lysosomal acidification in Parkinson’s disease

Wang, Y., Ma, Z., Jin, Z., Kou, L., Xiong, N., Wang, T., & Xia, Y. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01800-y · Cited by 7

Tumor extrachromosomal DNA: Biogenesis and recent advances in the field

Wu, H., Liu, S., Wu, D., Zhou, H., & Wu, G. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116588 · Cited by 5

Endocytic Pathways Unveil the Role of Syndecans in the Seeding and Spreading of Pathological Protein Aggregates: Insights into Neurodegenerative Disorders

Hudák, A., & Letoha, T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094037 · Cited by 5

Driving Therapeutic Innovation in Neurodegenerative Disease With Hydrogen Deuterium eXchange Mass Spectrometry

Pierangelini, A., Kessler, B. M., & O'Brien, D. P. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101017 · Cited by 3

Therapeutic extracellular vesicles as a cornerstone of medicine in the next decade with gerontological focus

Pulver, A. Y., Tokmachev, R. E., Pulver, N. A., Антакова, Л. Н., & Emelianova, M. A. (2025) · Biogerontology · doi:10.1007/s10522-025-10332-w · Cited by 4

Research progress on the role and mechanism of action of exosomes in autoimmune thyroid disease

Chen, Y., Dong, B., Huang, L., Zhou, J., & Huang, H. (2022) · International Reviews of Immunology · doi:10.1080/08830185.2022.2057482 · Cited by 5

Casein Kinase 2 Mediates HIV- and Opioid-Induced Pathologic Phosphorylation of TAR DNA Binding Protein 43 in the Basal Ganglia

Ohene‐Nyako, M., Nass, S. R., Richard, H., Lukande, R. L., Nicol, M. R., McRae, M., Knapp, P. E., & Hauser, K. F. (2023) · ASN NEURO · doi:10.1177/17590914231158218 · Cited by 4

Repeat length of C9orf72-associated glycine–alanine polypeptides affects their toxicity

Morón-Oset, J., Fischer, L. K., Jauré, N., Zhang, P., Jahn, A. J., Supèr, T., Pahl, A., Isaacs, A. M., Grönke, S., & Partridge, L. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01634-6 · Cited by 5

Is Alzheimer's disease an individual-centered disease? Hypotheses from the atomic levels up to mathematical models for biological systems

Giorelli, M., Accavone, D., & Liso, A. D. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1352261 · Cited by 4

Low-density lipoprotein receptor–related protein 1 mediates α-synuclein transmission from the striatum to the substantia nigra in animal models of Parkinson’s disease

Luo, H., Peng, C., Wu, C.-S. C., Liu, C., Li, Q., Yu, S., Liu, J., & Chen, M. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01965 · Cited by 8

Coadministration of Monophosphoryl Lipid and Curcumin Modulates Neuroprotective Effects in LPS Stimulated Rat Primary Microglial Cells

Hooshmand, M., & Asoodeh, A. (2024) · Oxidative Medicine and Cellular Longevity · doi:10.1155/omcl/9422312 · Cited by 4

Blood-Derived α-Synuclein Aggregated in the Substantia Nigra of Parabiotic Mice

Ma, X., Chen, L., Song, N., Qu, L., Wang, J., & Xie, J. (2021) · Biomolecules · doi:10.3390/biom11091287 · Cited by 4

Predicting Mutational Effects on Ca2+-Activated Chloride Conduction of TMEM16A Based on a Simulation Study

Zhang, Y., Wu, K., Li, Y., Wu, S., Warshel, A., & Bai, C. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c11940 · Cited by 4

Mechanical force of uterine occupation enables large vesicle extrusion from proteostressed maternal neurons

Wang, G., Guasp, R. J., Salam, S., Chuang, E., Morera, A., Smart, A. J., Jimenez, D., Shekhar, S., Friedman, E., Melentijevic, I., et al. (2024) · eLife · doi:10.7554/elife.95443 · Cited by 9

Neurodegenerative Implications of Neuronal Cytoplasmic Protein Dysfunction in Response to Environmental Contaminants

Osemwegie, O., Ramkumar, S., & Smith, E. E. (2020) · Neurotoxicity Research · doi:10.1007/s12640-020-00308-8 · Cited by 4

Lysosomal Exocytosis Releases Pathogenic α-Synuclein Species from NeuronsPreprint

Xie, Y. X., Naseri, N. N., Fels, J. A., Kharel, P., Na, Y., Burré, J., & Sharma, M. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.10.439302 · Cited by 4

Exosomal transmission of α-synuclein initiates Parkinson’s disease-like pathologyPreprint

Howitt, J. A., Low, L. H., Bouman, M., Yang, J., Gordon, S. L., Hill, A. F., & Tan, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.10.443522 · Cited by 4

Global network structure and local transcriptomic vulnerability shape atrophy in sporadic and genetic behavioral variant frontotemporal dementiaPreprint

Shafiei, G., Bazinet, V., Dadar, M., Manera, A. L., Collins, D. L., Dagher, A., Borroni, B., Sánchez‐Valle, R., Moreno, F., Laforce, R. J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.24.457538 · Cited by 4

Network analysis identifies strain-dependent response to tau and tau seeding-associated genes

Acri, D. J., You, Y., Tate, M. D., Karahan, H., Martinez, P., McCord, B., Sharify, A. D., John, S., Kim, B., Dabin, L. C., et al. (2023) · Journal of Experimental Medicine · doi:10.1084/jem.20230180 · Cited by 3

Changes in white matter predict efficacy of repetitive transcranial magnetic stimulation in Parkinson's disease

Han, J., Lv, L., Chen, X., Wang, M., Hu, L., Xing, F., Liu, P., Yu, L., Zhao, Z., Sun, J., et al. (2025) · NeuroImage · doi:10.1016/j.neuroimage.2025.121354 · Cited by 3

Simultaneous detection of nitroreductase and adenosine triphosphate using a dual-emission fluorescent probe

Xu, Y., Nian, F., Wei, J., Li, L., Ma, R.-T., Ma, S., & Wang, W. (2025) · Chemical Communications · doi:10.1039/d5cc02820e · Cited by 3

Seed Amplification Assays as Powerful Tools for Detecting Peripheral Biomarkers in Prion-Like Diseases

Dellarole, I. L., Lombardo, A., Ciullini, A., Cazzaniga, F. A., Domina, R., Bacınoğlu, M. B., & Moda, F. (2025) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-97055-9_13 · Cited by 3

Integrating individualized connectome with amyloid pathology improves predictive modeling of future cognitive decline

He, H., Razlighi, Q. R., Gazes, Y., Habeck, C. G., Stern, Y., Initiative, A. D. N., Weiner, M. W., Aisen, P. S. S., Petersen, R. C., Jack, C. R., et al. (2025) · Communications Medicine · doi:10.1038/s43856-025-01170-5 · Cited by 5

Elucidation of Molecular Mechanisms of Lipid-Altered Cytotoxicity of TDP-43 Fibrils

Purvinsh, Y., Matveyenka, M., & Kurouski, D. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00934 · Cited by 3

Comparative Analysis of Protein Misfolding in Neurodegenerative Diseases Using Evaluation based on the Distance from Average Solution (EDAS) Method

Periyasamy, C. (2026) · Computer Science Engineering and Technology · doi:10.46632/cset/3/4/5 · Cited by 3

Lysophagy prevents neurotoxic aggregate transmission

Radulovic, M., & Stenmark, H. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2321181121 · Cited by 3

Differential accumulation of human β-amyloid and tau from enriched extracts in neuronal and endothelial cells

Rabanal‐Ruiz, Y., Pedrero-Prieto, C. M., Rodríguez, L. S., Flores‐Cuadrado, A., Saiz‐Sánchez, D., Frontiñán-Rubio, J., Úbeda‐Bañón, I., Durán‐Prado, M., Martínez-Marcos, A., & Peinado, J. R. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167204 · Cited by 3

PET-based brain molecular connectivity in neurodegenerative disease

Hanania, J. U., Reimers, E., Bevington, C. W. J., & Sossi, V. (2024) · Current Opinion in Neurology · doi:10.1097/wco.0000000000001283 · Cited by 3

Regulation of autophagy by ST3GAL2-mediated α2-3 sialylated glycosphingolipids in hepatic encephalopathy

Li, X., Xiao, Y., Zhu, Y., Li, P., Zhou, J., Yang, J., Chen, Z., Du, H., Yu, H., Guo, Y., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135196 · Cited by 3

Human induced pluripotent stem cell-derived dopaminergic neurons release alpha-synuclein through neuronal activity

Nuermaimaiti, M., Ishikawa, K., Oyama, G., Nonaka, R., Shiga, T., Jo, T., Tsunemi, T., Nakamura, R., Krüger, R., Akamatsu, W., et al. (2024) · Neuroscience Research · doi:10.1016/j.neures.2024.11.007 · Cited by 3

Fibrinogen-tau Aggregates Exacerbate Tau Pathology and Memory Deficits in Alzheimer’s Disease Model Mice

Wen, T., Meng, L., Liu, H., Zhang, Q., Dai, L., Huang, L., Liang, D., Zhu, K., Luo, J., & Zhang, Z. (2025) · Neuroscience Bulletin · doi:10.1007/s12264-025-01366-8 · Cited by 6

Paraquat exposure triggers amyloid-β and α-synuclein aggregation in the prefrontal cortex of mice: Suppression of microglial phagocytosis via IL-17A

Hu, R., Shi, G., Wu, C., Jiao, Y., Li, Y., Ai, Q., Li, Y., Zhang, Q., Liu, Q., Wang, K., et al. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114746 · Cited by 5

A High-Throughput ImmunoHistoFluorescence (IHF) Method for Sub-Nuclear Protein Analysis in Tissue

Oxe, K. C., Rohrberg, K. S., Lassen, U., & Larsen, D. H. (2025) · Cells · doi:10.3390/cells14141109 · Cited by 3

Bridging prion biology and Alzheimer’s disease: from pathogenic seeds to precision therapeutics

Wang, W., Feng, Z., Shu, L., Hu, Y., Chen, Y., Zhang, B., & Huang, H. (2025) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2025.1660151 · Cited by 3

Serum alpha-synuclein in restless legs syndrome

Tahanis, A., Hashem, V. I., & Ondo, W. G. (2024) · SLEEP · doi:10.1093/sleep/zsae217 · Cited by 3

Intraventricular Administration of Exosomes from Patients with Amyotrophic Lateral Sclerosis Provokes Motor Neuron Disease in Mice

Stavrovskaya, A. V., Воронков, Д. Н., Pavlova, A. K., Olshanskiy, A. S., Belugin, B. V., Mv, I., Zakharova, M. N., & Illarioshkin, S. N. (2024) · Acta Naturae · doi:10.32607/actanaturae.27499 · Cited by 3

Revisiting the advance of age-dependent α-synuclein propagation and aggregation

Song, D., & Li, J. (2025) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2024.44 · Cited by 4

Tau Protein in Drug-Resistant Epilepsy and Cognitive Decline

Thom, M., & Koepp, M. J. (2021) · Progress in inflammation research · doi:10.1007/978-3-030-67403-8_7 · Cited by 3

Demenz

Knell, S., Thal, D. R., & Lipp, V. (2022) · Verlag Karl Alber eBooks · doi:10.5771/9783495999370 · Cited by 2

The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular modelPreprint

Yuste‐Checa, P., Trinkaus, V. A., Riera-Tur, I., Imamoglu, R., Schaller, T., Wang, H., Dudanova, I., Hipp, M. S., Bracher, A., & Hartl, F. U. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.16.452659 · Cited by 4

Somatic mosaicism in amyotrophic lateral sclerosis and frontotemporal dementia identifies focal mutations associated with widespread degenerationPreprint

Zhou, Z., Kim, J., Huang, A. Y., Nolan, M., Park, J., Doan, R. N., Shin, T., Miller, M. B., Bae, M., Zhao, B., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.30.569436 · Cited by 3

Decoding Protein Aggregation through Computational Approach: Identification and Scoring of Aggregation-Prone Regions in Protein SequencesPreprint

Kaushik, R., & Launey, T. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.11.598423 · Cited by 3

Phosphoproteome modifications and cortical circuit dysfunction are linked to the early-stage progression of alpha-synuclein aggregationPreprint

Dutta, S., Hensel, J. A., Scott, A. N., Mohallem, R., Rossitto, L.-A. M., Khan, H. F., Diehl, L. A., Johnson, T., Colon, B. D., Gold, J. E., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.24.634820 · Cited by 3

The Effect of the Tau Protein on D. melanogaster Lifespan Depends on GSK3 Expression and Sex

Veselkina, E. R., Trostnikov, M. V., Roshina, N. V., & PASYUKOVA, E. G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032166 · Cited by 3

APOE contributes to longitudinal impulse control disorders progression in Parkinson’s disease

Chen, L., He, X., Mao, L., & Liu, P. (2024) · BMC Psychiatry · doi:10.1186/s12888-024-06084-5 · Cited by 2

Inspecting the Triazole Scaffold as Powerful Antifibril Agents against 2N4R Tau and α‑Synuclein Aggregates

Elbatrawy, A. A., Ademoye, T. A., Alnakhala, H., Tripathi, A., Zhu, X., Plascencia‐Villa, G., Perry, G. L., Dettmer, U., & Fortin, J. S. (2025) · ACS Omega · doi:10.1021/acsomega.4c08385 · Cited by 3

Unravelling the nexus of stroke and dementia: Deciphering the role of secondary neurodegeneration in orchestrating cognitive decline

Stuckey, S. M., Hood, R. J., Ong, L. K., Bilecki, I. M., Collins‐Praino, L. E., & Turner, R. J. (2025) · Neuroprotection/Neuroprotection (Chichester, England. Print) · doi:10.1002/nep3.74 · Cited by 2

Dual Role of Exosomes in Parkinson's Disease: Adenine Exerts a Beneficial Effect

Chen, L., Shao, Y., Geng, J., Liu, H., Liu, Q., Cheng, Y., & Sun, T. (2025) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70331 · Cited by 2

Cryptic Splicing of GAP43 mRNA is a Novel Hallmark of TDP‐43‐Associated ALS and AD

Yang, M., Wang, Q., Kang, D., Wang, S., Jiang, Y., Wang, J., Chen, M., Liu, R., Gu, J., & Wang, X. (2025) · Advanced Science · doi:10.1002/advs.202412054 · Cited by 3

Advancing nanotheranostics for neuro-immunological disorders: current status and future prospects

Rai, S., Nair, A., Saleem, Z., Ray, S. K., Kanwar, J. R., & Mukherjee, S. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.08.051 · Cited by 2

Formation of Condition‐Dependent Alpha‐Synuclein Fibril Strain in Artificial Cerebrospinal Fluid

Sniečkutė, R., Šulskis, D., Jocytė, A., Venclovaitė, U., Tamulytė, R., Žiaunys, M., Smirnovas, V., & Sakalauskas, A. (2025) · Advanced Science · doi:10.1002/advs.202505228 · Cited by 2

Anti-neuroinflammatory polyprenylated acylphloroglucinols from Hypericum patulum: LC-MS/MS-guided isolation, semi-synthesis, and TLR4 inhibition

Zhang, F., Chen, L., Jin, J., Ma, H., Li, Y., Xiao, T., Zeng, Y., Yang, J., Hao, X., & Yuan, C. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.109292 · Cited by 2

Differential microglial responses to structurally distinct alpha-synuclein polymorphs

Chang, K., Kim, J., Iba, M., Park, J. H., Beilina, A., Syed, Z. A., Baena, V., Horan-Portelance, L., Cookson, M., You, S., et al. (2025) · Molecular Brain · doi:10.1186/s13041-025-01256-0 · Cited by 2

Parkinson's disease in transition: Genetics, biomarkers, and emerging therapeutics

Fan, S., Okuzumi, A., Chen, P., Tai, Y., Kuo, Y.-C. J., Tai, C., Li, C., Chiang, H., Hatano, T., & Lin, C. (2025) · Journal of the Formosan Medical Association · doi:10.1016/j.jfma.2025.12.005 · Cited by 3

Identification of pesticides associated with an increased risk of Parkinson’s disease using a multi-screen approach

Arellano, M., Barnhill, L. M., Kim, A., Hasan, K. M. M., Li, S., Paul, K. C., Peng, C., Ritz, B. R., & Bronstein, J. M. (2026) · Environment International · doi:10.1016/j.envint.2026.110087 · Cited by 2

Label‐Free SERS Fingerprinting of Neuroprotein Conformational Dynamics in Human Saliva

Ja’farawy, M. S. A., Yang, J.-Y., Mun, C., Lee, S., Cho, C. S., Um, Y. H., Lee, M., Park, S., Kim, D., Yang, S. H., et al. (2026) · Advanced Materials · doi:10.1002/adma.202513500 · Cited by 3

Microscale dysfunction and mesoscale compensation in degenerating neuronal networks

Fiskum, V., Winter‐Hjelm, N., Christiansen, N., Sandvig, A., & Sandvig, I. (2026) · Network Neuroscience · doi:10.1162/netn.a.552 · Cited by 2

Structural evidence that RNA contributes to polymorphism of tau amyloid fibrils

Abskharon, R. N. N., Jiang, Y. X., Sawaya, M. R., Ge, P., Zhang, J., Boyer, D. R., Dolinsky, J. L., Pi, J., Cascio, D., Guo, F., et al. (2026) · iScience · doi:10.1016/j.isci.2026.115501 · Cited by 5

AI-driven insights into protein misfolding and innate immunity in neurodegenerative diseases

Deng, H. X., Cao, J. L., Yao, W., Jiang, S. J., Fang, Q. Q., Zhu, B. Y., & Jiang, Y. J. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1814357 · Cited by 2

Prion-like transmission of human tau strains in the mouse brain

Lövestam, S., Shimozawa, A., Tarutani, A., Ohtani, R., Masuda‐Suzukake, M., Hasegawa, K., Robinson, A., Saito, Y., Murayama, S., Yoshida, M., et al. (2026) · Nature · doi:10.1038/s41586-026-11061-x · Cited by 4

Biological aspects of nitrogen heterocycles for amyotrophic lateral sclerosis

Manjupriya, R., Pouthika, K., Madhumitha, G., & Roopan, S. M. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12317-y · Cited by 2

Inhibition of Self-Assembling Peptide Fibrils Formation Using Thioflavin T as a Photosensitizer

Tikhonova, T. N., Rubekina, A. A., Vorobev, V. A., Mefodeva, E. A., Maksimov, E. G., Efremov, Y. M., Darvin, M. E., Timashev, P. S., Gorelkin, P. V., Erofeev, A. S., et al. (2023) · Journal of Biomedical Photonics & Engineering · doi:10.18287/jbpe23.09.010304 · Cited by 2

Flavones in pomelo peel resist fibril formation of human islet amyloid polypeptide

Gao, C., Wan, Z., Liu, Y., Meng, Y., Chen, X., Tang, X., Hang, L., & Yuan, H. (2024) · Chinese Herbal Medicines · doi:10.1016/j.chmed.2024.02.002 · Cited by 2

Alcohol consumers with liver pathology rarely display α-synuclein pathology

Libard, S., Tamsen, F., & Alafuzoff, I. I. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02772-4 · Cited by 2

Biomarkers for Neurodegenerative Diseases

Abdelmoaty, M. M., Lu, E., & Foster, E. G. (2024) · Springer eBooks · doi:10.1007/978-3-031-68237-7_44 · Cited by 2

For Early Diagnosis of Neurodegenerative Diseases: Acting of Biomarkers

Yao, Y. (2020) · American Journal of Biomedical Science & Research · doi:10.34297/ajbsr.2020.11.001628 · Cited by 2

Nörodejeneratif Hastalık Araştırmalarında Drosophila melanogaster Modeli

HAZIR, C., Bora, G., & Erdem‐Yurter, H. (2020) · Uludağ Üniversitesi Tıp Fakültesi Dergisi · doi:10.32708/uutfd.732671 · Cited by 3

Tau in Health and Neurodegenerative Diseases

Chu, D., & Liu, F. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.101299 · Cited by 2

Altern und neurodegenerative Erkrankungen – warum gehen Nervenzellen verloren?

Klimaschewski, L. P. (2021) · Springer eBooks · doi:10.1007/978-3-662-63392-2_2 · Cited by 2

Frontotemporal lobar degeneration

Kim, B., Viera-Ortiz, A., Phan, J. M., Irwin, D. J., & Lee, E. B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85654-6.00041-1 · Cited by 3

Nanoformulations for neurodegenerative disorders

Sodhi, R. K., Madan, J., Babu, M. A., & Singh, Y. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85041-4.00006-8 · Cited by 2

The Potential of Curcumin and Its Applications in Neurodegenerative Diseases

da Silva, M. H., Moreira, R. D. A., Lima, E. C., & de Matos, J. M. E. (2023) · Springer eBooks · doi:10.1007/978-981-99-7731-4_12 · Cited by 2

Rhes protein transits from neuron to neuron and facilitates mutant huntingtin spreading in the brainPreprint

Ramírez-Jarquín, U. N., Sharma, M., Shahani, N., Li, Y., Boregowda, S., & Subramaniam, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.27.457956 · Cited by 2

LRP1 Regulates the Uptake and Propagation of α-SynucleinPreprint

Peng, C., Luo, H., Liu, J., Li, Q., Liu, C., & Chen, M. (2022) · Research Square · doi:10.21203/rs.3.rs-1411309/v1 · Cited by 2

Mechanical force of uterine occupation enables large vesicle extrusion from proteostressed maternal neuronsPreprint

Wang, G., Guasp, R. J., Salam, S., Chuang, E., Morera, A., Smart, A. J., Jimenez, D., Shekhar, S., Melentijevic, I., Nguyen, K. C. Q., et al. (2024) · eLife · doi:10.7554/elife.95443.1 · Cited by 2

Imbalanced mitochondrial dynamics in human and mouse PD brainsPreprint

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