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

Beyond the usual suspects: multi-factorial computational models in the search for neurodegenerative disease mechanisms

Khan, A. F., & Iturria‐Medina, Y. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03073-w · Cited by 31

Activating autophagy to eliminate toxic protein aggregates with small molecules in neurodegenerative diseases

Fu, Y., Zhang, J., Qin, R., Ren, Y., Zhou, T., Han, B., & Liu, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100053 · Cited by 29

Remodeling Alzheimer-amyloidosis models by seeding

Ulm, B. S., Borchelt, D., & Moore, B. D. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00429-4 · Cited by 26

A bifunctional probe that allows dual-channel fluorescence turn-on detection of protein aggregates and hydrogen peroxide in neurodegenerative diseases

Ma, J., Wang, X., Li, N., & Cheng, Y. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.130536 · Cited by 25

Prionoids in amyotrophic lateral sclerosis

Gosset, P., Camu, W., Raoul, C., & Mezghrani, A. (2022) · Brain Communications · doi:10.1093/braincomms/fcac145 · Cited by 31

Intercellular transmission of pathogenic proteins in ALS: Exploring the pathogenic wave

Arnold, F. J., Nguyen, A., Bedlack, R., Bennett, C. L., & Spada, A. R. L. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106218 · Cited by 29

Exosomes in Central Nervous System Diseases: A Comprehensive Review of Emerging Research and Clinical Frontiers

Li, J., Song, J., Jia, L., Wang, M., Ji, X., Meng, R., & Zhou, D. (2024) · Biomolecules · doi:10.3390/biom14121519 · Cited by 28

Pathogenic Extracellular Vesicle (EV) Signaling in Amyotrophic Lateral Sclerosis (ALS)

Kim, G., Chen, X., & Yang, Y. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01232-9 · Cited by 26

Post-COVID-19 Parkinsonism and Parkinson’s Disease Pathogenesis: The Exosomal Cargo Hypothesis

Mysiris, D. S., Vavougios, G. D., Karamichali, E., Papoutsopoulou, S., Stavrou, V. T., Papayianni, E., Boutlas, S., Mavridis, T., Foka, P., Zarogiannis, S. G., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179739 · Cited by 25

Senescent brain cell types in Alzheimer's disease: Pathological mechanisms and therapeutic opportunities

Hudson, H. R., Sun, X., & Orr, M. E. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00519 · Cited by 28

WWOX and Its Binding Proteins in Neurodegeneration

Hsu, C.-Y., Lee, K., Sun, T.-Y., Sze, C., Huang, S., Hsu, L., & Chang, N. (2021) · Cells · doi:10.3390/cells10071781 · Cited by 26

Unlocking the Epigenetic Symphony: Histone Acetylation’s Impact on Neurobehavioral Change in Neurodegenerative Disorders

Basavarajappa, B. S., & Subbanna, S. (2024) · Epigenomics · doi:10.2217/epi-2023-0428 · Cited by 24

Epilepsy and prion diseases: A narrative review

Mbizvo, G. K., Ziso, B., & Larner, A. J. (2020) · Epilepsy & Behavior · doi:10.1016/j.yebeh.2020.107630 · Cited by 24

Multi-Faceted Roles of DNAJB Protein in Cancer Metastasis and Clinical Implications

Kim, H.-Y., & Hong, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314970 · Cited by 27

The yeast prion protein Sup35 initiates α-synuclein pathology in mouse models of Parkinson’s disease

Meng, L., Liu, C., Li, Y., Chen, G., Xiong, M., Yu, T., Pan, L., Zhang, X., Zhou, L., Guo, T., et al. (2023) · Science Advances · doi:10.1126/sciadv.adj1092 · Cited by 24

The Role of Mitochondrial Copy Number in Neurodegenerative Diseases: Present Insights and Future Directions

Cerantonio, A., Citrigno, L., Greco, B. M., Benedittis, S. D., Passarino, G., Maletta, R., Qualtieri, A., Montesanto, A., Spadafora, P., & Cavalcanti, F. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116062 · Cited by 25

Co-Aggregation of TDP-43 with Other Pathogenic Proteins and Their Co-Pathologies in Neurodegenerative Diseases

Jiang, L., Zhang, X.-L., & Hu, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212380 · Cited by 25

Harnessing the Potential of Exosomes in Therapeutic Interventions for Brain Disorders

Bai, L., Yu, L., Ran, M., Zhong, X., Sun, M., Xu, M., Wang, Y., Yan, X., Lee, R. J., Tang, Y., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062491 · Cited by 26

Potential common pathogenesis of several neurodegenerative diseases

Fan, T., Peng, J., Liang, H., Chen, W., Wang, J., & Xu, R. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01054 · Cited by 29

Intestinal macrophages modulate synucleinopathy along the gut–brain axis

Schepper, S. D., Konstantellos, V., Conway, J. A., Sokolova, D., Zaccagnini, L., Cowley, M. V., Sierksma, A. S. R., Yudina, M. M., Edmonds, M. J., Gavriouchkina, D., et al. (2026) · Nature · doi:10.1038/s41586-025-09984-y · Cited by 29

Region-specific amyloid-β accumulation in the olfactory system influences olfactory sensory neuronal dysfunction in 5xFAD mice

Son, G., Yoo, S., Kang, S., Rasheed, A., Jung, D. H., Park, H., Cho, B., Steinbusch, H. W. M., Chang, K., Suh, Y., et al. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-00730-2 · Cited by 23

Alpha-Synuclein Handling by Microglia: Activating, Combating, and Worsening

Song, N., Chen, L., & Xie, J. (2021) · Neuroscience Bulletin · doi:10.1007/s12264-021-00651-6 · Cited by 25

The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils

Chien, H.-M., Lee, C.-C., & Huang, J. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158213 · Cited by 28

Novel chemical inhibitor against SOD1 misfolding and aggregation protects neuron-loss and ameliorates disease symptoms in ALS mouse model

Woo, T., Yoon, M.-H., Kang, S., Park, S., Cho, J.-H., Hwang, Y. J., Ahn, J., Jang, H., Shin, Y.-J., Jung, E., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02862-z · Cited by 24

18F-APN-1607 Tau Positron Emission Tomography Imaging for Evaluating Disease Progression in Alzheimer’s Disease

Xu, X., Ruan, W., Liu, F., Gai, Y., Liu, Q., Su, Y., Liang, Z., Sun, X., & Lan, X. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.789054 · Cited by 23

Exosomal Proteins and miRNAs as Mediators of Amyotrophic Lateral Sclerosis

Chen, Q. Y., Wen, T., Wu, P., Jia, R., Zhang, R., & Dang, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.718803 · Cited by 23

Tunneling nanotubes: A novel pharmacological target for neurodegenerative diseases?

Wang, X.-T., Sun, H., Chen, N.-H., & Yuan, Y.-H. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105541 · Cited by 22

Cell type-specific functions of Alzheimer's disease endocytic risk genes

Maninger, J.-K., Nowak, K., Goberdhan, S., O'Donoghue, R., & Connor-Robson, N. (2024) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2022.0378 · Cited by 22

C-reactive protein: the nexus between inflammation and protein misfolding diseases

Roy, A., Zeller, J., Nero, T. L., Klepetko, J., Eisenhardt, S. U., Parker, M. W., McFadyen, J. D., & Peter, K. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1612703 · Cited by 23

Structural basis for RNA recognition by the N-terminal tandem RRM domains of human RBM45

Chen, X., Yang, Z., Wang, W., Qian, K., Liu, M., Wang, J., & Wang, M. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab075 · Cited by 22

Praja1 RING ‐finger E3 ubiquitin ligase is a common suppressor of neurodegenerative disease‐associated protein aggregation

Watabe, K., Niida‐Kawaguchi, M., Tada, M., Kato, Y., Murata, M., Tanji, K., Wakabayashi, K., Yamada, M., Kakita, A., & Shibata, N. (2022) · Neuropathology · doi:10.1111/neup.12840 · Cited by 21

Bioengineering Human Pluripotent Stem Cell-Derived Retinal Organoids and Optic Vesicle-Containing Brain Organoids for Ocular Diseases

Arthur, P., Muok, L., Nathani, A., Zeng, E. Z., Sun, L. J., Li, Y., & Singh, M. S. (2022) · Cells · doi:10.3390/cells11213429 · Cited by 24

Predicting longitudinal brain atrophy in Parkinson’s disease using a Susceptible-Infected-Removed agent-based model

Abdelgawad, A., Rahayel, S., Zheng, Y., Tremblay, C., Vo, A., Mišić, B., & Dagher, A. (2022) · Network Neuroscience · doi:10.1162/netn_a_00296 · Cited by 22

Helicobacter hepaticus augmentation triggers Dopaminergic degeneration and motor disorders in mice with Parkinson’s disease

Ahn, E. H., Liu, X., Alam, A. M., Kang, S. S., & Ye, K. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01910-2 · Cited by 22

Age‐dependent NMDA receptor function is regulated by the amyloid precursor protein

Rajão‐Saraiva, J., Dunot, J., Ribera, A., Temido‐Ferreira, M., Coelho, J. E., König, S., Moréno, S., Enguita, F. J., Willem, M., Kins, S., et al. (2023) · Aging Cell · doi:10.1111/acel.13778 · Cited by 25

Therapeutic effects of saffron and its components on neurodegenerative diseases

Golpour-Hamedani, S., Pourmasoumi, M., Zarifi, S. H., Askari, G., Jamialahmadi, T., Bagherniya, M., & Sahebkar, A. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e24334 · Cited by 22

A crazy trio in Parkinson's disease: metabolism alteration, α-synuclein aggregation, and oxidative stress

Li, S., Liu, Y., Lu, S., Xu, J., Liu, X., Yang, D., Yang, Y., Hou, L., & Li, N. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-04985-3 · Cited by 22

Aggregation and phase separation of α-synuclein in Parkinson's disease

Han, W., Wei, M., Xu, F., & Niu, Z. (2024) · Chemical Communications · doi:10.1039/d4cc01591f · Cited by 22

Assembly of α-synuclein and neurodegeneration in the central nervous system of heterozygous M83 mice following the peripheral administration of α-synuclein seeds

Macdonald, J. A., Chen, J. L., Masuda‐Suzukake, M., Schweighauser, M., Jaunmuktane, Z., Warner, T. T., Holton, J. L., Grossman, A., Berks, R., Lavenir, I., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01291-7 · Cited by 22

Retinal Nerve Fiber Layer Thickness and Associations With Cognitive Impairment in Parkinson’s Disease

Chang, Z., Xie, F., Li, H., Yuan, F., Zeng, L., Shi, L., Zhu, S., Lu, X., Wei, X., & Wang, Q. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.832768 · Cited by 21

Pathogenic Role of RAGE in Tau Transmission and Memory Deficits

Kim, Y., Park, H., Kim, Y., Kim, S., Lee, J., Yang, H., Kim, S. J., Li, C. M., Lee, H., Na, D.-H., et al. (2022) · Biological Psychiatry · doi:10.1016/j.biopsych.2022.10.015 · Cited by 23

Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective

Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25

The beneficial pharmacological effects of Uncaria rhynchophylla in neurodegenerative diseases: focus on alkaloids

Chen, L., Liu, Y., & Xie, J. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1436481 · Cited by 20

Innate and adaptive immunity in neurodegenerative disease

Huang, Y., Zhang, G., Li, S., Feng, J., & Zhang, Z. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05533-4 · Cited by 22

Targeting amyloid proteins for clinical diagnosis of neurodegenerative diseases

Zhang, S., Dong, H., Bian, J., Li, D., & Liu, C. (2022) · Fundamental Research · doi:10.1016/j.fmre.2022.10.009 · Cited by 23

GABA signaling triggered by TMC-1/Tmc delays neuronal aging by inhibiting the PKC pathway in C. elegans

Wu, J., Wang, L., Ervin, J. F., Wang, S. J., Soderblom, E. J., Ko, D. C., & Yan, D. (2022) · Science Advances · doi:10.1126/sciadv.adc9236 · Cited by 17

Studies of Genetic and Proteomic Risk Factors of Amyotrophic Lateral Sclerosis Inspire Biomarker Development and Gene Therapy

Bagyinszky, E., Hulme, J., & An, S. S. A. (2023) · Cells · doi:10.3390/cells12151948 · Cited by 21

Defining and characterizing neuronal senescence, ‘neurescence’, as GX arrested cells

Hudson, H. R., Rießland, M., & Orr, M. E. (2024) · Trends in Neurosciences · doi:10.1016/j.tins.2024.09.006 · Cited by 21

Resveratrol in Neurodegeneration, in Neurodegenerative Diseases, and in the Redox Biology of the Mitochondria

Danışman, B., Kelek, S. E., & Aslan, M. (2023) · Psychiatry and Clinical Psychopharmacology · doi:10.5152/pcp.2023.23633 · Cited by 23

Alpha Synuclein Toxicity and Non-Motor Parkinson’s

Mazzotta, G. M., & Conte, C. (2024) · Cells · doi:10.3390/cells13151265 · Cited by 19

Identification of cis-acting determinants mediating the unconventional secretion of tau

Katsinelos, T., McEwan, W. A., Jahn, T. R., & Nickel, W. (2021) · Scientific Reports · doi:10.1038/s41598-021-92433-3 · Cited by 16

Neurodegenerative diseases and brain delivery of therapeutics: Bridging the gap using dendrimers

Kaur, A., Singh, N., Kaur, H., Kakoty, V., Sharma, D. S., Khursheed, R., Babu, M. R., Harish, V., Gupta, G., Gulati, M., et al. (2023) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2023.104868 · Cited by 19

Recent advances in understanding and treatment of Parkinson’s disease

Tarakad, A., & Jankovic, J. J. (2020) · Faculty Reviews · doi:10.12703/b/9-6 · Cited by 18

Overexpression-Induced α-Synuclein Brain Spreading

Pinto‐Costa, R., Harbachova, E. L., Vitola, P. L., & Monte, D. A. D. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01332-6 · Cited by 17

Emerging Roles of Extracelluar Vesicles Derived from Bacteria, Mammalian or Plant Cells in the Pathogenesis and Clinical Application of Neurodegenerative Diseases

Li, Y., Zhou, C., Liu, H., Cai, T., & Fan, H. (2024) · Biomolecules · doi:10.3390/biom14030312 · Cited by 20

Neurodegenerative disease-associated protein aggregates are poor inducers of the heat shock response in neuronal cells

Gil, R. S., Cox, D., McAlary, L., Berg, T., Walker, A. K., Yerbury, J. J., Ooi, L., & Ecroyd, H. W. (2020) · Journal of Cell Science · doi:10.1242/jcs.243709 · Cited by 18

A ROS-Responsive nanoparticle for nuclear gene delivery and autophagy restoration in Parkinson's disease therapy

Zhai, L., Gao, Y., Yang, H., Wang, H., Liao, B., Cheng, Y., Liu, C., Che, J., Xia, K., Zhang, L., et al. (2025) · Biomaterials · doi:10.1016/j.biomaterials.2025.123345 · Cited by 18

α-Synuclein aggregates inhibit ESCRT-III through sequestration and collateral degradation

Sitron, C. S., Trinkaus, V. A., Galesic, A., Garhammer, M., Yuste‐Checa, P., Dransfeld, U., Feigenbutz, D., Zhang, J., Ivashko, L., Dudanova, I., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.022 · Cited by 19

Distinct cutaneous α-synuclein signatures in body-first and brain-first Parkinson’s disease subtypes

Liu, M., Wen, T., Luo, H., Yang, T., Kong, Y., Jin, Y., Li, L., Yuan, Y., Liu, X., Yuan, J., et al. (2025) · Brain · doi:10.1093/brain/awaf395 · Cited by 18

Nanoparticle-based colorimetric sensors to detect neurodegenerative disease biomarkers

Fan, Q., Gao, Y., Mazur, F., & Chandrawati, R. (2021) · Biomaterials Science · doi:10.1039/d1bm01226f · Cited by 17

The paradigm of amyloid precursor protein in amyotrophic lateral sclerosis: The potential role of the 682 YENPTY 687 motif

Matrone, C. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.01.008 · Cited by 17

Applications of Artificial Intelligence to Diagnosis of Neurodegenerative Diseases

Feng, T. (2023) · Studies in health technology and informatics · doi:10.3233/shti230896 · Cited by 18

Neuronal exosomal miRNAs modulate mitochondrial functions and cell death in bystander neuronal cells under Parkinson’s disease stress conditions

Currim, F., Shukla, S., Singh, J., Gohel, D., Mane, M., Shinde, A., Roy, M., Goyani, S., Vasiyani, H., Chandran, A., et al. (2024) · NeuroToxicology · doi:10.1016/j.neuro.2024.02.005 · Cited by 17

White and gray matter alterations in de novo PD patients: which matter most?

Pietracupa, S., Belvisi, D., Piervincenzi, C., Tommasin, S., Pasqua, G., Petsas, N., Bartolo, M. I. D., Fabbrini, A., Costanzo, M., Manzo, N., et al. (2023) · Journal of Neurology · doi:10.1007/s00415-023-11607-3 · Cited by 16

Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR

Shenoy, J., Lends, A., Berbon, M., Abdul-Shukkoor, M. B., Mammeri, N. E., Bertoni, M., Saad, A., Morvan, E., Grélard, A., Lecomte, S., et al. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1148302 · Cited by 19

A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization

Azimi, F. C., Dean, T. T., Minari, K., Basso, L. G. M., Vance, T. D. R., & Serrão, V. H. B. (2023) · Biomolecules · doi:10.3390/biom13071130 · Cited by 16

Sustained CREB phosphorylation by lipid-peptide liquid crystalline nanoassemblies

Wu, Y., Angelov, B., Deng, Y., Fujino, T., Hossain, M. S., Drechsler, M., & Angelova, A. (2023) · Communications Chemistry · doi:10.1038/s42004-023-01043-9 · Cited by 19

Exosomes: The endogenous nanomaterials packed with potential for diagnosis and treatment of neurologic disorders

Tang, X., He, Y., Liu, J., Xu, J., & Peng, Q. (2024) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2024.113938 · Cited by 17

Chimeric brain models: Unlocking insights into human neural development, aging, diseases, and cell therapies

Papetti, A. V., Jin, M., Ma, Z., Stillitano, A. C., & Jiang, P. (2025) · Neuron · doi:10.1016/j.neuron.2025.03.036 · Cited by 15

The proSAAS Chaperone Provides Neuroprotection and Attenuates Transsynaptic α-Synuclein Spread in Rodent Models of Parkinson’s Disease

Lindberg, I., Shu, Z., Lam, H. A., Helwig, M., Yucer, N., Laperle, A., Svendsen, C. N., Monte, D. A. D., & Maidment, N. T. (2022) · Journal of Parkinson s Disease · doi:10.3233/jpd-213053 · Cited by 15

Multifunctional Anti-Alzheimer’s Disease Effects of Natural Xanthone Derivatives: A Primary Structure-Activity Evaluation

Hu, X., Liu, C., Wang, K., Zhao, L., Qiu, Y. L., Chen, H., Hu, J., & Xu, J. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.842208 · Cited by 15

Levodopa responsiveness and white matter alterations in Parkinson's disease: A DTI‐based study and brain network analysis: A cross‐sectional study

Du, J., Zhou, X., Liang, Y., Zhao, L., Dai, C., Zhong, Y., Liu, H., Liu, G., Mo, L., Tan, C., et al. (2022) · Brain and Behavior · doi:10.1002/brb3.2825 · Cited by 14

Neutrophil extracellular traps in central nervous system (CNS) diseases

Shao, B., Jiang, J., Zhao, Y.-C., Zheng, X.-R., Xi, N., Zhao, G.-R., Huang, X., & Wang, S. (2024) · PeerJ · doi:10.7717/peerj.16465 · Cited by 15

Actin-nucleation promoting factor N-WASP influences alpha-synuclein condensates and pathology

Jackson, J., Hoffmann, C., Scifo, E., Wang, H., Wischhof, L., Piazzesi, A., Mondal, M., Shields, H., Zhou, X., Mondin, M., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06686-7 · Cited by 14

Let food be your medicine – dietary fiber

Liu, M., Li, S., Cao, S., Liu, C., Han, Y., Cheng, J., Zhang, S., Zhao, J., & Shi, Y. (2024) · Food & Function · doi:10.1039/d3fo05641d · Cited by 17

Advancing alkaloid-based medicines: medical applications, scalable production and synthetic innovations

Hashim, S. E., Basar, N., Samad, A. A., Jamil, S., Bakar, M. B., Jamalis, J., Abd-Aziz, N., Wagiran, A., Razak, M. R. M. A., & Samad, A. F. A. (2024) · Phytochemistry Reviews · doi:10.1007/s11101-024-10050-0 · Cited by 15

Particulate matter 2.5 (PM 2.5 ) - associated cognitive impairment and morbidity in humans and animal models: a systematic review

Chauhan, R., Dande, S., Hood, D. B., Chirwa, S., Langston, M. A., Grady, S. K., Dojcsak, L., Tabatabai, M., Wilus, D. M., Valdez, R. B., et al. (2025) · Journal of Toxicology and Environmental Health Part B · doi:10.1080/10937404.2025.2450354 · Cited by 18

C. elegans Models to Study the Propagation of Prions and Prion-Like Proteins

Sandhof, C. A., Hoppe, S. O., Tittelmeier, J., & Nussbaum-Krammer, C. I. (2020) · Biomolecules · doi:10.3390/biom10081188 · Cited by 15

Role of VAPB and vesicular profiles in α‐synuclein aggregates in multiple system atrophy

Mori, F., Miki, Y., Tanji, K., Kon, T., Tomiyama, M., Kakita, A., & Wakabayashi, K. (2021) · Brain Pathology · doi:10.1111/bpa.13001 · Cited by 14

The tau oligomer antibody APNmAb005 detects early-stage pathological tau enriched at synapses and rescues neuronal loss in long-term treatmentsPreprint

Tai, H., Ma, H.-T., Huang, S.-C., Wu, M., Wu, C., Lai, Y., Li, Z., Margolin, R. A., Intorcia, A. J., Serrano, G. E., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.24.497452 · Cited by 15

Infections in the Etiology of Parkinson’s Disease and Synucleinopathies: A Renewed Perspective, Mechanistic Insights, and Therapeutic Implications

Mercado, G., Käufer, C., Richter, F., & Peelaerts, W. (2024) · Journal of Parkinson s Disease · doi:10.3233/jpd-240195 · Cited by 16

Immunity in Alzheimer’s disease: From mechanisms to therapies

Chen, X., Holtzman, D. M., & Colonna, M. (2026) · Immunity · doi:10.1016/j.immuni.2026.02.004 · Cited by 18

Vaccination with structurally adapted fungal protein fibrils induces immunity to Parkinson’s disease

Pesch, V., Flores-Fernández, J. M., Reithofer, S., Ma, L., Özdüzenciler, P., Busch, Y., Sriraman, A., Wang, Y., Amidian, S., Kroepel, C. V. M., et al. (2024) · Brain · doi:10.1093/brain/awae061 · Cited by 14

Non-covalent delivery of native proteins and peptides by phenylboronic cell-penetrating poly(disulfide)s

Guo, J., Wan, T. Y., Qi, Z., Zhang, Y., Yan, X., Zhang, B., Pan, Q., Li, B., Li, Z., & Ping, Y. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102283 · Cited by 14

Frontotemporal dementia-like disease progression elicited by seeded aggregation and spread of FUS

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