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

Quantitative analysis of related parameters of retinal nerve fiber layer and ganglion cell complex thickness in patients with different degrees of Parkinson's disease

Zhao, Y., Dai, W.-J., & Liu, D. (2022) · Aging Clinical and Experimental Research · doi:10.1007/s40520-022-02211-y · Cited by 12

Molecular Mechanisms Mediating the Transfer of Disease-Associated Proteins and Effects on Neuronal Activity

Brás, I. C., Khani, M. H., Vasili, E., Möbius, W., Riedel, D., Parfentev, I., Gerhardt, E., Fahlbusch, C., Urlaub, H., Zweckstetter, M., et al. (2022) · Journal of Parkinson s Disease · doi:10.3233/jpd-223516 · Cited by 18

Stalling the Course of Neurodegenerative Diseases: Could Cyanobacteria Constitute a New Approach toward Therapy?

Ramos, V., Reis, M. A., Ferreira, L., Silva, A. M., Ferraz, R., Vieira, M., Vasconcelos, V. M., & Martins, R. F. (2023) · Biomolecules · doi:10.3390/biom13101444 · Cited by 13

Preserving genome integrity: The vital role of SUMO-targeted ubiquitin ligases

Han, J., Mu, Y., & Huang, J. (2023) · Cell Insight · doi:10.1016/j.cellin.2023.100128 · Cited by 11

Synaptic Involvement of the Human Amygdala in Parkinson’s Disease

Villar‐Conde, S., Astillero‐Lopez, V., González-Rodríguez, M., Saiz‐Sánchez, D., Martı́nez-Marcos, A., Úbeda‐Bañón, I., & Flores‐Cuadrado, A. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100673 · Cited by 13

Invertebrate genetic models of amyotrophic lateral sclerosis

Zhou, L., & Xu, R. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1328578 · Cited by 12

Specific Binding of Alzheimer’s Aβ Peptides to Extracellular Vesicles

Coughlan, C. M., Lindenberger, J., Jacot, J. G., Johnson, N. R., Anton, P., Bevers, S., Welty, R., Graner, M., & Potter, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073703 · Cited by 12

Glycosaminoglycans in Neurodegenerative Diseases

Jin, W., Zhang, F., & Linhardt, R. J. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-70115-4_9 · Cited by 13

Oxidation of two cysteines within yeast Hsp70 impairs proteostasis while directly triggering an Hsf1-dependent cytoprotective response

Santiago, A., & Morano, K. A. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102424 · Cited by 13

RGMa collapses the neuronal actin barrier against disease-implicated protein and exacerbates ALS

Shimizu, M., Shiraishi, N., Tada, S., Sasaki, T., Beck, G., Nagano, S., Kinoshita, M., Sumi, H., Sugimoto, T., Ishida, Y., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg3193 · Cited by 12

The Multifaceted Role of Extracellular Vesicles in Alzheimer's Disease

Conceição, A. R., Marinatto, J., Pinheiro, L. S., Rody, T., & Felice, F. G. D. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70209 · Cited by 15

Visualizing liquid-liquid phase separation and protein aggregates

Xue, J., Cao, X.-W., Jia, X.-L., Chen, X., Guo, W., & Yin, D. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01756-z · Cited by 15

α-Synuclein-dependent increases in PIP5K1γ drive inositol signaling to promote neurotoxicity

Horvath, J. D., Casas, M., Kutchukian, C., Sánchez, S. C., Pergande, M. R., Cologna, S. M., Simó, S., Dixon, R. E., & Dickson, E. J. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113244 · Cited by 11

The role of DNA damage in neural stem cells ageing

Zhong, Y., Wang, G., Yang, S., Zhang, Y., & Wang, X. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.31187 · Cited by 12

Transcellular transmission and molecular heterogeneity of aggregation-prone proteins in neurodegenerative diseases

Lee, E., Park, H., & Kim, S. (2024) · Molecules and Cells · doi:10.1016/j.mocell.2024.100089 · Cited by 12

Biosensors for Parkinson’s Disease: Where Are We Now, and Where Do We Need to Go?

Maddocks, G. M., Eisenstein, M. S., & Soh, H. T. (2024) · ACS Sensors · doi:10.1021/acssensors.4c00790 · Cited by 12

Bifunctional Inhibitor Lentinan Inhibits Fibrillogenesis of Amyloid-β Protein and α-Synuclein and Alleviates Their Cytotoxicity: In Vitro and In Vivo Studies

Gao, W. H., Dong, Q., Wu, X., Wang, Y., Li, J., Zhang, Q., Lu, F., & Liu, F. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00164 · Cited by 11

Investigation into Alzheimer's-related amyloid-β conformational transformations and stability influenced by green iron oxide nanoparticles (GIONP)

Esawii, H. A., Маматкулов, К. З., Mahran, H. A., Arzumanyan, G., & Mohamed, N. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.140124 · Cited by 11

Advancements in extracellular vesicle therapy for neurodegenerative diseases

Hu, N., Chen, L., Hu, G., & Ma, R. (2025) · Exploration of Neuroprotective Therapy · doi:10.37349/ent.2025.1004104 · Cited by 12

Imbalanced mitochondrial dynamics in human PD and α-synuclein mouse brains

Brown, H. J., Fan, R. Z., Bell, R., Salehe, S. S., Gil, C. M., Lai, Y., & Tieu, K. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106976 · Cited by 16

Chemical probes for investigating protein liquid-liquid phase separation and aggregation

Sun, R., Zhang, S., Liu, Y., & Li, D. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102291 · Cited by 11

Comparative binding analysis of WGX50 and Alpha-M with APP family proteins APLP1 and APLP2 using structural-dynamics and free energy calculation approaches

Ali, A., Masood, A., Khan, A. A., Zhu, F.-Y., Cheema, M. A. R., Samad, A., Wadood, A., Khan, A., Yu, Q., Heng, W., et al. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp06083c · Cited by 11

Multi target-directed imidazole derivatives for neurodegenerative diseases

Eliewi, A. G., Al‐Garawi, Z. S., Alkazzaz, F. F., & Atia, A. J. K. (2021) · Journal of Physics Conference Series · doi:10.1088/1742-6596/1853/1/012066 · Cited by 11

4R-Tau seeding activity unravels molecular subtypes in patients with Progressive Supranuclear PalsyPreprint

Martínez-Valbuena, I., Lee, S., Santamaría, E., Fernández‐Irigoyen, J., Forrest, S. L., Li, J., Tanaka, H., Couto, B., Reyes, N. G. D., Qamar, S. H., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.28.559953 · Cited by 11

Insights into AlphaFold’s breakthrough in neurodegenerative diseases

Mubeen, H., Masood, A., Zafar, A., Khan, Z. Q., Khan, M. Q., & Nisa, A. U. (2024) · Irish Journal of Medical Science (1971 -) · doi:10.1007/s11845-024-03721-6 · Cited by 10

α-Synuclein fibrils enhance HIV-1 infection of human T cells, macrophages and microglia

Olari, L., Liu, S., Arnold, F., Kühlwein, J., Miró, M. G., Updahaya, A. R., Stürzel, C. M., Thal, D. R., Walther, P., Sparrer, K. M. J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56099-z · Cited by 10

Intercellular communication via exosomes: A new paradigm in the pathophysiology of neurodegenerative disorders

Satao, K. S., & Doshi, G. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123468 · Cited by 10

Raman spectroscopy and imaging of protein droplet formation and aggregation

Watson, M. D., & Lee, J. C. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103041 · Cited by 10

DNA-based nanostructures for cell membrane receptor regulation and disease treatment

Cheng, Z., Liu, Y., Chen, Q., Man, Y., Man, Y., Zhang, Z., Du, S., Lv, Z., Wang, Q., Shao, K., et al. (2025) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2025.115674 · Cited by 11

Peripheral administration of SOD1 aggregates does not transmit pathogenic aggregation to the CNS of SOD1 transgenic mice

Keskin, I., Bidhendi, E. E., Marklund, M., Andersen, P. M., Brännström, T., Marklund, S. L., & Nordström, U. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01211-9 · Cited by 10

Neuroanatomical Tract Tracers: Not Just for Neural Tracing Anymore

Wang, W., Clark, J., & Mao, G. (2023) · ACS Applied Bio Materials · doi:10.1021/acsabm.3c00063 · Cited by 10

Anti-alpha synuclein and anti-tau immunotherapies: Can a cocktail approach work?

del Giudice, K. P., Cosgaya, M., Zaro, I., Ravasi, V., Santacruz, P., Painous, C., Fernández, M., Cámara, A., & Compta, Y. (2024) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2024.106080 · Cited by 10

Reclassifying neurodegenerative diseases

Villoslada, P., Baeza-Yates, R. A., & Masdeu, J. C. (2020) · Nature Biomedical Engineering · doi:10.1038/s41551-020-0600-3 · Cited by 10

An early proinflammatory transcriptional response to tau pathology is age‐specific and foreshadows reduced tau burden

Rasmussen, J., Ewing, A. D., Bodea, L., Bodea, G. O., Gearing, M., & Faulkner, G. J. (2021) · Brain Pathology · doi:10.1111/bpa.13018 · Cited by 10

Aberrant interactions between amyloid-beta and alpha5 laminins as possible driver of neuronal disfunction in Alzheimer’s disease

Rodin, S., Kozin, S. A., Kechko, O. I., Mitkevich, V. A., & Makarov, A. А. (2020) · Biochimie · doi:10.1016/j.biochi.2020.04.011 · Cited by 11

TDP-43 Amyloid Fibril Formation via Phase Separation-Related and -Unrelated Pathways

Lin, P., Wu, G.-W., Lin, Y., Huang, J.-R., Jeng, U., Liu, W.-M., & Huang, J. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00503 · Cited by 9

Microglial Melatonin Receptor 1 Degrades Pathological Alpha‐Synuclein Through Activating LC3 ‐Associated Phagocytosis In Vitro

Yao, X., Cao, B., Liu, J., Lv, Q.-K., Zhang, J., Cheng, X., Mao, C., Ma, Q., Wang, F., & Liu, C. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70088 · Cited by 10

Proteopathic seed amplification assays in easily accessible specimens for human synucleinopathies, tauopathies, and prionopathies: A scoping review

Salciccia, C., Costanzo, M., Ruocco, G., Porreca, F., Vivacqua, G., Fabbrini, G., Belvisi, D., Ladogana, A., & Poleggi, A. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2024.105997 · Cited by 11

Drosophila aux orchestrates the phosphorylation-dependent assembly of the lysosomal V-ATPase in glia and contributes to SNCA/α-synuclein degradation

Zhang, S., Wang, L., Yi, S., Tsai, Y.-T., Cheng, Y.-H., Lin, Y.-T., Lin, C.-C., Lee, Y., Wang, H., Li, S., et al. (2025) · Autophagy · doi:10.1080/15548627.2024.2442858 · Cited by 10

Exploring exosome profiling via CytoFLEX Nano flow cytometer: Approaches and applications

Cao, L. K., Wang, H., Zhu, J., Li, W., Lin, H. L., Wang, Z., Wang, X., Guo, B., Ding, J., Tong, D., et al. (2025) · Open Research (University of Surrey) · doi:10.1002/viw.20250068 · Cited by 9

Hybrid Extracellular Vesicles With Combined Functional Properties From Mesenchymal Stem Cells and Astrocytes for Targeted Neurodegenerative Disease Applications

Wang, D., Clark, K. C., Rouen, K. C., Baird, G., Polackal, T. N., Kumar, P., Wyle, Y., Farmer, D. L., Carney, R. P., & Wang, A. (2025) · Journal of Extracellular Vesicles · doi:10.1002/jev2.70175 · Cited by 13

Hydrophobic tagging: A promising paradigm for targeted protein degradation

Xin, L., Wang, H., Yang, M., Guo, Z., Zhu, M., Moore, T. W., Dong, C., & Zhou, H. (2025) · Cell Insight · doi:10.1016/j.cellin.2025.100295 · Cited by 10

Could the Urease of the Gut Bacterium Proteus mirabilis Play a Role in the Altered Gut–Brain Talk Associated with Parkinson’s Disease?

Grahl, M. V. C., Andrade, B. D. S., Perin, A. P. A., Neves, G. A., Duarte, L. D. S., Uberti, A. F., Hohl, K. S., Follmer, C., & Carlini, C. R. (2023) · Microorganisms · doi:10.3390/microorganisms11082042 · Cited by 12

Potential of Microfluidics and Lab-on-Chip Platforms to Improve Understanding of “prion-like” Protein Assembly and Behavior

del Rı́o, J. A., & Ferrer, I. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.570692 · Cited by 8

Heparan sulfate proteoglycans: Mediators of cellular and molecular Alzheimer's disease pathogenic factors via tunnelling nanotubes?

Nguyen, D. L., Okolicsanyi, R. K., & Haupt, L. M. (2024) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2024.103936 · Cited by 9

pTau pathology in the retina of TAU58 mice: association with ganglion cell degeneration and implications on seeding and propagation of pTau from human brain lysates

Walkiewicz, G., Ronisz, A., Ospitalieri, S., Tsaka, G., Tomé, S. O., Vandenberghe, R. R., Arnim, C. A. F. V., Rousseau, F., Schymkowitz, J. W. H., Groef, L. D., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01907-8 · Cited by 8

α-Synuclein Degradation in Brain Pericytes Is Mediated via Akt, ERK, and p38 MAPK Signaling Pathways

Yokoya, M., Takata, F., Iwao, T., Matsumoto, J., Tanaka, Y., Aridome, H., Yasunaga, M., Mizoguchi, J., Sano, K., & Dohgu, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26041615 · Cited by 10

Recent Trends in Hydrogel-Based Biosensor Technology for the Diagnosis of Neurodegenerative Diseases

Ayçiçek, S., Cevher, Ş. C., & Acar, S. (2025) · ACS Applied Bio Materials · doi:10.1021/acsabm.5c00420 · Cited by 9

The role of autophagy in synucleinopathy: clearance versus spread of α-synuclein

Birnbaum, E., & Yue, Z. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2577406 · Cited by 10

Genetically encoded fluorescent reporters to visualize α-synuclein pathology in live brain

Zhang, L. I., Yu, M., Chen, G., Ge, S., Wang, M., Zhang, X., Zhao, M., Gu, H., Huang, M., Liu, A., et al. (2026) · Cell · doi:10.1016/j.cell.2026.01.035 · Cited by 10

Development of small molecules for disrupting pathological amyloid aggregation in neurodegenerative diseases

Cao, T., Li, X., Li, D., & Tao, Y. (2023) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2023.25 · Cited by 10

A Next-Generation Sequencing Study in a Cohort of Sicilian Patients with Parkinson’s Disease

Salemi, M., Lanza, G., Salluzzo, M. G., Schillaci, F. A., Blasi, F. D. D., Cordella, A., Caniglia, S., Lanuzza, B., Morreale, M., Marano, P., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11123118 · Cited by 10

Repurposing of the PET Probe Prototype PiB for Label and Radiation-Free CEST MRI Molecular Imaging of Amyloid

Zhuang, C., Chen, B., Wu, S., Xu, L., Zhang, X., Zheng, X., Chen, Y., Geng, Y., Guan, J., Lin, Y., et al. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00539 · Cited by 8

Extracellular Vesicles Physiological Role and the Particular Case of Disease-Spreading Mechanisms in Polyglutamine Diseases

Moreira, R., Mendonça, L. S., & de Almeida, L. P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212288 · Cited by 7

Characterizing the spatiotemporal variability of Alzheimer's disease pathologyPreprint

Vogel, J. W., Young, A., Oxtoby, N., Smith, R., Ossenkoppele, R., Strandberg, O., Joie, R. L., Aksman, L., Grothe, M., Iturria-Medina, Y., et al. (2020) · medRxiv · doi:10.1101/2020.08.20.20176883 · Cited by 10

Parkinson’s disease with hyposmia and dysautonomia: does it represent a distinct subtype?

Yoon, S. H., You, D. H., Na, H. K., Kang, S., Baik, K., Park, M., Lyoo, C. H., Sohn, Y. H., & Lee, P. H. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12332-1 · Cited by 7

Different Imaging Evaluating Performances Between Glymphatic System and Motor Symptoms and Levodopa Responsiveness of Parkinson Disease

Deng, J.-H., Zhang, H., Lan, X., Liu, Y., Liu, X.-L., Deng, H.-Z., Luo, S., Yao, G.-Z., Wu, H., Huang, B., et al. (2025) · Journal of Computer Assisted Tomography · doi:10.1097/rct.0000000000001720 · Cited by 7

Advances in clinical neurorestorative treatments of Parkinson's disease

Yin, Y., Su, D., Lam, J. S. T., & Feng, T. (2025) · Journal of Neurorestoratology · doi:10.1016/j.jnrt.2025.100204 · Cited by 8

PGRN as an emerging regulator of lipid metabolism in neurodegenerative diseases

Shi, Y., Hou, W., Li, B., & Zhu, C. (2025) · Communications Biology · doi:10.1038/s42003-025-08272-9 · Cited by 9

Design of Ig-like binders targeting α-synuclein fibril for mitigating its pathological activities

Zeng, S., Xiong, X., Long, H., Xu, Q., Yu, Y., Sun, B., Liu, C., Wang, Z., Xu, W., Zhang, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62755-1 · Cited by 7

Protein quality control systems in neurodegeneration – culprits, mitigators, and solutions?

Ciechanover, A. J., & Livneh, I. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1604076 · Cited by 8

Dual role of exosomes in neurodegenerative diseases: a molecular bridge between neuroinflammation and transmission of pathological proteins

An, W., Jin, Z., & Li, Y. (2026) · Frontiers in Neurology · doi:10.3389/fneur.2025.1708655 · Cited by 8

The α-Synuclein Monomer May Have Different Misfolding Mechanisms in the Induction of α-Synuclein Fibrils with Different Polymorphs

Zhao, N., Zhang, Q., Yu, F., Yao, X., & Liu, H. (2023) · Biomolecules · doi:10.3390/biom13040682 · Cited by 7

Clinical and histopathological features in horses with neuroaxonal degeneration: 100 cases (2017-2021)

Brown, K. A., Bender, S. J., & Johnson, A. L. (2023) · Journal of Veterinary Internal Medicine · doi:10.1111/jvim.16969 · Cited by 7

Transmission-selective muscle pathology induced by the active propagation of mutant huntingtin across the human neuromuscular synapse

Dinamarca, M. C., Colombo, L., Brykczynska, U., Grimm, A., Fruh, I., Hossain, I., Gabriel, D., Eckert, A., Müller, M. M., & Pecho‐Vrieseling, E. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1287510 · Cited by 7

Can dementia be predicted using olfactory identification test in the elderly? A Bayesian network analysis

Ding, D., Liang, X., Xiao, Z., Wu, W., Zhao, Q., & Cao, Y. (2020) · Brain and Behavior · doi:10.1002/brb3.1822 · Cited by 7

Therapeutic Potential of AAV1-Rheb(S16H) Transduction against Neurodegenerative Diseases

Nam, Y., Moon, G. J., & Kim, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063064 · Cited by 7

Clinical and Dopamine Depletion Patterns in Hyposmia- and Dysautonomia-Dominant Parkinson’s Disease

Yoo, H. S., Lee, S., Jeong, S. H., Ye, B. S., Sohn, Y. H., Yun, M., & Lee, P. H. (2021) · Journal of Parkinson s Disease · doi:10.3233/jpd-212747 · Cited by 7

A C-terminal ataxin-2 disordered region promotes Huntingtin protein aggregation and neurodegeneration in Drosophila models of Huntington’s disease

Huelsmeier, J., Walker, E., Bakthavachalu, B., & Ramaswami, M. (2021) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkab355 · Cited by 10

Multiple roles of neuronal extracellular vesicles in neurological disorders

Jiao, Z., He, Z., Liu, N., Lai, Y., & Zhong, T. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.979856 · Cited by 7

Experimental models of gut‐first Parkinson's disease: A systematic review

Videlock, E. J., Xing, T., Yehya, A. H. S., & Travagli, R. A. (2023) · Neurogastroenterology & Motility · doi:10.1111/nmo.14604 · Cited by 9

Common molecular mechanisms underlie the transfer of alpha-synuclein, Tau and huntingtin and modulate spontaneous activity in neuronal cellsPreprint

Brás, I. C., Khani, M., Vasili, E., Möbius, W., Riedel, D., Parfentev, I., Gerhardt, E., Fahlbusch, C., Urlaub, H., Zweckstetter, M., et al. (2021) · bioRxiv · doi:10.1101/2021.07.18.452825 · Cited by 3

Advances in Molecular Docking Techniques for Targeting Protein Misfolding in Neurodegenerative Diseases

Singh, K., Gupta, J. K., Narayan, S., Rani, K., Jain, D., Porwal, P., Sharma, M. C., & Kumar, S. (2025) · Current Pharmaceutical Biotechnology · doi:10.2174/0113892010298545241108062449 · Cited by 6

Multi-scale neural homeostasis mechanisms: Insights into neurodegenerative diseases and therapeutic approaches, including exercise

Wang, Y., Chen, X., Zhang, C., & Gao, S. (2025) · Advanced Exercise and Health Science · doi:10.1016/j.aehs.2025.02.002 · Cited by 8

Lysine-Targeting Inhibitors of Amyloidogenic Protein Aggregation: A Promise for Neurodegenerative Proteinopathies

Murakami, K., Nguyen, T. H. V., Nagao, C., Mizuguchi, K., & Bitan, G. (2025) · JACS Au · doi:10.1021/jacsau.5c00269 · Cited by 6

Brain and retina in Alzheimer's disease: Pathological intersections and estimates from imaging

Banihashemi, M. A., Krance, S. H., Ji, P. X., Koo, M., Ottoy, J., Swartz, R. H., Kertes, P. J., Hudson, C., Goubran, M., & Black, S. E. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70884 · Cited by 7

Recent Advances in Proximity Labeling-Based Subcellular Proteomic Mapping

Wang, G., Liu, J., Sun, X., Qin, W., Han, S., & Zou, P. (2026) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2026.101520 · Cited by 6

LRP1: a novel receptor for the transmission of pathological α-Synuclein

Pan, C., & Peng, C. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00582-4 · Cited by 6

Targeting Calpain-2 for Alzheimer’s Disease Treatment

Arnsten, A. F. T., & Baudry, M. (2023) · Medical Research Archives · doi:10.18103/mra.v11i2.3487 · Cited by 6

Revealing protein trafficking by proximity labeling-based proteomics

Wang, Y., & Qin, W. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.107041 · Cited by 6

A novel gene, TARDBP, and the protein it encodes can predict glioma patient prognosis and establish a prediction model

Fang, X., Wu, F., & Jiang, C. (2023) · BMC Neurology · doi:10.1186/s12883-023-03224-4 · Cited by 6

Interspecies chimerism with human embryonic stem cells generates functional human dopamine neurons at low efficiency

Wang, H., Yin, X., Xu, J., Chen, L., Karuppagounder, S. S., Xu, E., Mao, X., Dawson, V. L., & Dawson, T. M. (2023) · Stem Cell Reports · doi:10.1016/j.stemcr.2023.11.009 · Cited by 6

Brain network dynamics determine tau presence while regional vulnerability governs tau load in Alzheimer’s diseasePreprint

Xiao, Y., Spotorno, N., An, L., Bazinet, V., Hansen, J. Y., Strandberg, O. T., Shafiei, G., Behjat, H., Funck, T., Salvadó, G., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.17.648358 · Cited by 6

Factors responsible for alpha-Synuclein aggregation

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