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

The expanding repertoire of ESCRT functions in cell biology and disease

Hurley, J. H., Coyne, A. N., Miączyńska, M., & Stenmark, H. (2025) · Nature · doi:10.1038/s41586-025-08950-y · Cited by 65

Stress Granule Dysregulation in Amyotrophic Lateral Sclerosis

Dudman, J., & Qi, X. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.598517 · Cited by 54

Bifunctional modalities for repurposing protein function

Modell, A. E., Lai, S., Nguyen, T. M., & Choudhary, A. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.06.005 · Cited by 52

Parkinson's Disease Derived Exosomes Aggravate Neuropathology in SNCA * A53T Mice

Huang, Y. X. R., Liu, Z., Li, N., Tian, C., Yang, H. K., Huo, Y., Li, Y., Zhang, J., & Yu, Z. (2022) · Annals of Neurology · doi:10.1002/ana.26421 · Cited by 53

Activated microglia facilitate the transmission of α-synuclein in Parkinson's disease

Zheng, T., & Zhang, Z. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105094 · Cited by 57

Proteomic analysis identifies HSP90AA1 , PTK2B, and ANXA2 in the human entorhinal cortex in Alzheimer's disease: Potential role in synaptic homeostasis and Aβ pathology through microglial and astroglial cells

Astillero‐Lopez, V., Villar‐Conde, S., González-Rodríguez, M., Flores‐Cuadrado, A., Úbeda‐Bañón, I., Saiz‐Sánchez, D., & Martínez-Marcos, A. (2024) · Brain Pathology · doi:10.1111/bpa.13235 · Cited by 54

Redox Homeostasis and Prospects for Therapeutic Targeting in Neurodegenerative Disorders

Akanji, M. A., Rotimi, D. E., Elebiyo, T. C., Awakan, O. J., & Adeyemı, O. S. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9971885 · Cited by 55

Neurodegeneration and astrogliosis in the entorhinal cortex in Alzheimer's disease: Stereological layer‐specific assessment and proteomic analysis

Astillero‐Lopez, V., González-Rodríguez, M., Villar‐Conde, S., Flores‐Cuadrado, A., Martı́nez-Marcos, A., Úbeda‐Bañón, I., & Saiz‐Sánchez, D. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12580 · Cited by 53

A review on traditional Chinese medicine natural products and acupuncture intervention for Alzheimer’s disease based on the neuroinflammatory

Chen, Z., Wang, X., Du, S., Liu, Q., Xu, Z., Guo, Y., & Lin, X. (2024) · Chinese Medicine · doi:10.1186/s13020-024-00900-6 · Cited by 59

Tau and Alpha Synuclein Synergistic Effect in Neurodegenerative Diseases: When the Periphery Is the Core

Vacchi, E., Kaelin‐Lang, A., & Melli, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145030 · Cited by 51

Tanshinone I: Pharmacological activities, molecular mechanisms against diseases and future perspectives

Ke, L., Zhong, C., Chen, Z., Zheng, Z., Li, S., Chen, B., Wu, Q., & Yao, H. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154632 · Cited by 53

Crosstalk between Oxidative Stress and Inflammation Caused by Noise and Air Pollution—Implications for Neurodegenerative Diseases

Kuntić, M., Hahad, O., Münzel, T. F., & Daiber, A. (2024) · Antioxidants · doi:10.3390/antiox13030266 · Cited by 53

The role of sphingosine 1-phosphate metabolism in brain health and disease

van Echten‐Deckert, G. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108381 · Cited by 50

Vesicular Transport of Encapsulated microRNA between Glial and Neuronal Cells

Lukiw, W. J., & Pogue, A. I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145078 · Cited by 48

Aggrephagy at a glance

Bauer, B., Martens, S., & Ferrari, L. (2023) · Journal of Cell Science · doi:10.1242/jcs.260888 · Cited by 50

α-Synuclein: A Promising Biomarker for Parkinson’s Disease and Related Disorders

Hatano, T., Okuzumi, A., Matsumoto, G., Tsunemi, T., & Hattori, N. (2024) · Journal of Movement Disorders · doi:10.14802/jmd.24075 · Cited by 49

Extracellular vesicles (exosomes and ectosomes) play key roles in the pathology of brain diseases

Meldolesi, J. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00040-5 · Cited by 47

Extracellular Vesicles from Mesenchymal Stem Cells: Towards Novel Therapeutic Strategies for Neurodegenerative Diseases

Turano, E., Scambi, I., Virla, F., Bonetti, B., & Mariotti, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032917 · Cited by 50

Review of Technological Challenges in Personalised Medicine and Early Diagnosis of Neurodegenerative Disorders

Domínguez-Fernández, C., Egiguren-Ortiz, J., Razquin, J., Gómez-Galán, M., Heras-García, L. D. L., Paredes-Rodriguez, E., Astigarraga, E., Miguélez, C., & Barreda‐Gómez, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043321 · Cited by 52

Single Molecule Protein Segments Sequencing by a Plasmonic Nanopore

Zhou, J., Lan, Q., Li, W., Ji, L., Wang, K., & Xia, X. (2023) · Nano Letters · doi:10.1021/acs.nanolett.3c00086 · Cited by 44

Tau immunotherapy is associated with glial responses in FTLD-tau

Kim, B., Mikytuck, B., Suh, E. R., Gibbons, G. S., Deerlin, V. M. V., Vaishnavi, S., Spindler, M., Massimo, L. M., Grossman, M., Trojanowski, J. Q., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02318-y · Cited by 44

Mechanistic roles for altered O-GlcNAcylation in neurodegenerative disorders

Balana, A. T., & Pratt, M. R. (2021) · Biochemical Journal · doi:10.1042/bcj20200609 · Cited by 46

Brain‐targeting drug delivery systems

Liu, P., & Jiang, C. (2022) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1818 · Cited by 47

Regulated cell death and its role in Alzheimer’s disease and amyotrophic lateral sclerosis

Thal, D. R., Gawor, K., & Moonen, S. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02722-0 · Cited by 50

Islet amyloid polypeptide cross-seeds tau and drives the neurofibrillary pathology in Alzheimer’s disease

Zhang, G., Meng, L., Wang, Z., Peng, Q., Chen, G., Xiong, J., & Zhang, Z. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00518-y · Cited by 44

Exosomes as Biomarkers and Therapeutic Agents in Neurodegenerative Diseases: Current Insights and Future Directions

Dehghani, S., Ocakcı, O., Hatipoglu, P. T., Özalp, V. C., & Tevlek, A. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04825-5 · Cited by 49

Brain Glymphatic/Lymphatic Imaging by MRI and PET

Lee, D. S., Suh, M., Sarker, A. K., & Choi, Y. (2020) · Nuclear Medicine and Molecular Imaging · doi:10.1007/s13139-020-00665-4 · Cited by 45

Astrogliosis and sexually dimorphic neurodegeneration and microgliosis in the olfactory bulb in Parkinson’s disease

Flores‐Cuadrado, A., Saiz‐Sánchez, D., Mohedano‐Moriano, A., Lamas-Cenjor, E., Leon-Olmo, V., Martı́nez-Marcos, A., & Úbeda‐Bañón, I. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-020-00154-7 · Cited by 42

The role of ferroptosis in neurodegenerative diseases

Xu, Y., Zhao, J., Zhao, Y., Zhou, L., Qiao, H., Xu, Q., & Liu, Y. (2022) · Molecular Biology Reports · doi:10.1007/s11033-022-08048-y · Cited by 43

Molecular structure of an amyloid fibril formed by FUS low-complexity domain

Sun, Y., Zhang, S., Hu, J., Tao, Y., Xia, W., Gu, J., Li, Y., Cao, Q., Li, D., & Liu, C. (2021) · iScience · doi:10.1016/j.isci.2021.103701 · Cited by 39

Recent Advances in the Application of Mesenchymal Stem Cell-Derived Exosomes for Cardiovascular and Neurodegenerative Disease Therapies

Yang, Z., Li, Y., & Wang, Z. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14030618 · Cited by 40

Unveiling the Complex Role of Exosomes in Alzheimer’s Disease

Sun, M., & Chen, Z. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s466821 · Cited by 39

Disrupting pathologic phase transitions in neurodegeneration

Hurtle, B. T., Xie, L., & Donnelly, C. J. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168549 · Cited by 40

Brain incoming call from glia during neuroinflammation: Roles of extracellular vesicles

D’Egidio, F., Castelli, V., d’Angelo, M., Ammannito, F., Quintiliani, M., & Cimini, A. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106663 · Cited by 41

The contribution of beta-amyloid to dementia in Lewy body diseases: a 1-year follow-up study

Biundo, R., Weis, L., Fiorenzato, E., Pistonesi, F., Cagnin, A., Bertoldo, A., Anglani, M., Cecchin, D., & Antonini, A. (2021) · Brain Communications · doi:10.1093/braincomms/fcab180 · Cited by 39

Phosphorylation of endogenous α-synuclein induced by extracellular seeds initiates at the pre-synaptic region and spreads to the cell body

Awa, S., Suzuki, G., Masuda‐Suzukake, M., Nonaka, T., Saito, M., & Hasegawa, M. (2022) · Scientific Reports · doi:10.1038/s41598-022-04780-4 · Cited by 39

The Emerging Roles of E3 Ligases and DUBs in Neurodegenerative Diseases

Liu, N., Lin, M., & Wang, Y. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03063-3 · Cited by 39

Alzheimer's disease brain‐derived extracellular vesicles reveal altered synapse‐related proteome and induce cognitive impairment in mice

Bodart‐Santos, V., Pinheiro, L. S., da Silva‐Junior, A. J., Frozza, R. L., Ahrens, R., Gonçalves, R. A., Andrade, M. M., Chen, Y., Alcantara, C. D. L., Grinberg, L. T., et al. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.13134 · Cited by 39

Molecular Mechanisms of Cellular Senescence in Neurodegenerative Diseases

Lee, H.-J., Yoon, Y.-S., & Lee, S.-J. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168114 · Cited by 36

Molecular rules governing the structural polymorphism of amyloid fibrils in neurodegenerative diseases

Li, D., & Liu, C. (2023) · Structure · doi:10.1016/j.str.2023.08.006 · Cited by 39

Protein aggregates containing wild-type and mutant NOTCH3 are major drivers of arterial pathology in CADASIL

Dupré, N., Gueniot, F., Domenga, V., Dubosclard, V., Nilles, C., Hill‐Eubanks, D. C., Morgenthaler-Roth, C., Nelson, M. T., Keime, C., Danglot, L., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci175789 · Cited by 41

Praja1 RING ‐finger E3 ubiquitin ligase suppresses neuronal cytoplasmic TDP ‐43 aggregate formation

Watabe, K., Kato, Y., Sakuma, M., Murata, M., Niida‐Kawaguchi, M., Takemura, T., Hanagata, N., Tada, M., Kakita, A., & Shibata, N. (2020) · Neuropathology · doi:10.1111/neup.12694 · Cited by 37

The Two Cysteines of Tau Protein Are Functionally Distinct and Contribute Differentially to Its Pathogenicityin Vivo

Prifti, E., Tsakiri, E. N., Vourkou, E., Stamatakis, G. M., Samiotaki, M. K., & Papanikolopoulou, K. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1920-20.2020 · Cited by 39

Syntenin-knock out reduces exosome turnover and viral transduction

Kashyap, R. S., Balzano, M., Lechat, B., Lambaerts, K., Egea-Jiménez, A. L., Lembo, F., Fares, J., Meeussen, S., Kügler, S., Roebroek, A., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-81697-4 · Cited by 38

Epigenetic Modulation of Microglia Function and Phenotypes in Neurodegenerative Diseases

Wang, L., Yu, C.-C., Liu, X., Deng, X., Tian, Q., & Du, Y. (2021) · Neural Plasticity · doi:10.1155/2021/9912686 · Cited by 41

The chaperone Clusterin in neurodegeneration−friend or foe?

Yuste‐Checa, P., Bracher, A., & Hartl, F. U. (2022) · BioEssays · doi:10.1002/bies.202100287 · Cited by 37

Network of hotspot interactions cluster tau amyloid folds

Mullapudi, V., Vaquer‐Alicea, J., Bommareddy, V., Vega, A. R., Ryder, B. D., White, C. L., Diamond, M. I., & Joachimiak, Ł. A. (2023) · Nature Communications · doi:10.1038/s41467-023-36572-3 · Cited by 36

Human amygdala involvement in Alzheimer's disease revealed by stereological and dia‐PASEF analysis

Gonzalez‐Rodriguez, M., Villar‐Conde, S., Astillero‐Lopez, V., Villanueva‐Anguita, P., Ubeda‐Banon, I., Flores‐Cuadrado, A., Martinez‐Marcos, A., & Saiz‐Sanchez, D. (2023) · Brain Pathology · doi:10.1111/bpa.13180 · Cited by 36

The involvement of α-synucleinopathy in the disruption of microglial homeostasis contributes to the pathogenesis of Parkinson’s disease

Miao, Y., & Meng, H. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-023-01402-y · Cited by 40

Recent advances of focused ultrasound induced blood-brain barrier opening for clinical applications of neurodegenerative diseases

Zhao, P., Wu, T., Tian, Y., You, J. E., & Cui, X. (2024) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2024.115323 · Cited by 44

Novel Therapeutic Strategies in Alzheimer’s Disease: Pitfalls and Challenges of Anti-Amyloid Therapies and Beyond

Tondo, G., Marchi, F. D., Bonardi, F., Menegon, F., Verrini, G., Aprile, D., Anselmi, M., Mazzini, L., & Comi, C. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13113098 · Cited by 45

Alpha-Synuclein: The Interplay of Pathology, Neuroinflammation, and Environmental Factors in Parkinson’s Disease

He, S., Zhong, S., Liu, G., & Yang, J. (2020) · Neurodegenerative Diseases · doi:10.1159/000511083 · Cited by 36

Gingko biloba abrogate lead-induced neurodegeneration in mice hippocampus: involvement of NF-κB expression, myeloperoxidase activity and pro-inflammatory mediators

Adebayo, O. G., Ben‐Azu, B., Ajayi, A. M., Wopara, I., Aduema, W., Kolawole, T. A., Umoren, E. B., Onyeleonu, I., Ebo, T. O., Ajibo, D. N., et al. (2021) · Biological Trace Element Research · doi:10.1007/s12011-021-02790-3 · Cited by 36

Microglial inclusions and neurofilament light chain release follow neuronal α-synuclein lesions in long-term brain slice cultures

Barth, M., Bacioglu, M., Schwarz, N., Novotny, R., Brandes, J., Welzer, M., Mazzitelli, S., Häsler, L. M., Schweighauser, M., Wuttke, T. V., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00471-2 · Cited by 35

FOXO and related transcription factors binding elements in the regulation of neurodegenerative disorders

Oli, V., Gupta, R. V., & Kumar, P. (2021) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2021.102012 · Cited by 36

Harnessing role of sesamol and its nanoformulations against neurodegenerative diseases

Singh, N., Vishwas, S., Kaur, A., Kaur, H., Kakoty, V., Khursheed, R., Chaitanya, M., Babu, M. R., Awasthi, A., Corrie, L., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115512 · Cited by 37

Neuroinflammation is associated with Alzheimer’s disease co-pathology in dementia with Lewy bodies

van Wetering, J., Geut, H., Bol, J. G. J. M., Galis, Y., Timmermans, E., Twisk, J. W. R., Hepp, D. H., Morella, M. L., Pihlstrøm, L., Lemstra, A. W., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01786-z · Cited by 41

Inhibitor Development for α-Synuclein Fibril’s Disordered Region to Alleviate Parkinson’s Disease Pathology

Zhang, S., Xiang, H., Tao, Y., Li, J., Zeng, S., Xu, Q., Xiao, H., Lv, S., Song, C., Yan, C., et al. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c08869 · Cited by 35

Role of Tumor-Derived Extracellular Vesicles in Glioblastoma

Chen, Y., Jin, Y., & Wu, N. (2021) · Cells · doi:10.3390/cells10030512 · Cited by 35

The Role of Extracellular Matrix Components in the Spreading of Pathological Protein Aggregates

Moretto, E., Stuart, S., Surana, S., Vargas, J. N. S., & Schiavo, G. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.844211 · Cited by 32

Multifunctional Metallothioneins as a Target for Neuroprotection in Parkinson’s Disease

Miyazaki, I., & Asanuma, M. (2023) · Antioxidants · doi:10.3390/antiox12040894 · Cited by 36

Spatial transcriptomic patterns underlying amyloid-β and tau pathology are associated with cognitive dysfunction in Alzheimer’s disease

Yu, M., Risacher, S. L., Nho, K. T., Wen, Q., Oblak, A. L., Unverzagt, F. W., Apostolova, L. G., Farlow, M. R., Brosch, J. R., Clark, D. G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113691 · Cited by 36

Current insights and assumptions on α-synuclein in Lewy body disease

Leak, R. K., Clark, R. N., Abbas, M., Xu, F., Brodsky, J. L., Chen, J., Hu, X., & Luk, K. C. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02781-3 · Cited by 41

Apolipoprotein E Genotype Contributes to Motor Progression in Parkinson's Disease

Pu, J., Jin, C., Wang, Z., Fang, Y., Li, Y., Xue, N., Zheng, R., Lin, Z., Yan, Y., Si, X., et al. (2021) · Movement Disorders · doi:10.1002/mds.28805 · Cited by 34

Mitochondrial function-associated genes underlie cortical atrophy in prodromal synucleinopathies

Rahayel, S., Tremblay, C., Vo, A., Mišić, B., Lehéricy, S., Arnulf, I., Vidailhet, M., Corvol, J.-C., the ICEBERG Study Group, Vidailhet, M., et al. (2023) · Brain · doi:10.1093/brain/awad044 · Cited by 35

Islet amyloid polypeptide triggers α-synuclein pathology in Parkinson’s disease

Meng, L., Li, Y., Liu, C., Zhang, G., Chen, J., Xiong, M., Pan, L., Zhang, X., Chen, G., Xiong, J., et al. (2023) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2023.102462 · Cited by 34

“Prion-like” seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders

Zampar, S., Gregorio, S. E. D., Grimmer, G., Watts, J. C., & Ingelsson, M. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1436262 · Cited by 39

Role of Glia-Derived Extracellular Vesicles in Neurodegenerative Diseases

Li, T., Tan, X., Li, S., Al-Nusaif, M., & Le, W. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.765395 · Cited by 33

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

Ramírez-Jarquín, U. N., Sharma, M., Shahani, N., Li, Y., Boregowda, S. V., & Subramaniam, S. (2022) · Science Advances · doi:10.1126/sciadv.abm3877 · Cited by 33

Tau protein quantification in skin biopsies differentiates tauopathies from alpha-synucleinopathies

Vacchi, E., Lazzarini, E., Pinton, S., Chiaro, G., Disanto, G., Marchi, F., Robert, T., Staedler, C., Galati, S., Gobbi, C., et al. (2022) · Brain · doi:10.1093/brain/awac161 · Cited by 35

α-Synuclein molecular behavior and nigral proteomic profiling distinguish subtypes of Lewy body disorders

Martínez-Valbuena, I., Swinkin, E., Santamaría, E., Fernández‐Irigoyen, J., Sackmann, V., Kim, A., Li, J., González-Latapí, P., Kuhlman, G. D., Bhowmick, S. S., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02453-0 · Cited by 32

Neuronal hyperactivity–induced oxidant stress promotes in vivo α-synuclein brain spreading

Helwig, M., Ulusoy, A., Rollar, A., O’Sullivan, S. A., Lee, S. S. L., Aboutalebi, H., Pinto‐Costa, R., Jevans, B., Klinkenberg, M., & Monte, D. A. D. (2022) · Science Advances · doi:10.1126/sciadv.abn0356 · Cited by 37

Magnetic transferrin nanoparticles (MTNs) assay as a novel isolation approach for exosomal biomarkers in neurological diseases

Jang, Y. O., Ahn, H., Dao, T. N. T., Hong, J., Shin, W., Lim, Y., Chung, S. J., Lee, J., Liu, H., Koo, B., et al. (2023) · Biomaterials Research · doi:10.1186/s40824-023-00353-2 · Cited by 32

Mitochondrial Complex I and β-Amyloid Peptide Interplay in Alzheimer’s Disease: A Critical Review of New and Old Little Regarded Findings

Atlante, A., & Valenti, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115951 · Cited by 33

Tau seeding activity in skin biopsy differentiates tauopathies from synucleinopathies

Dellarole, I. L., Vacchi, E., Ruíz‐Barrio, I., Pinton, S., Raimondi, A., Rossi, S., Morandi, S., Bianco, G., Bacınoğlu, M. B., Lombardo, A., et al. (2024) · npj Parkinson s Disease · doi:10.1038/s41531-024-00728-9 · Cited by 33

Framework Nucleic Acid Nanomaterials for Central Nervous System Therapies: Design for Barrier Penetration, Targeted Delivery, Cellular Uptake, and Endosomal Escape

Chen, X., Luo, X., Yin, W., Cui, W., He, Y., Tian, T., & Lin, Y. (2025) · ACS Nano · doi:10.1021/acsnano.5c03945 · Cited by 39

Neuroglial Senescence, α-Synucleinopathy, and the Therapeutic Potential of Senolytics in Parkinson’s Disease

Miller, S., Campbell, C. E., Jimenez-Corea, H. A., Wu, G., & Logan, R. A. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.824191 · Cited by 34

27‐Hydroxycholesterol Drives the Spread of α‐Synuclein Pathology in Parkinson's Disease

Dai, L., Wang, J., Zhang, X., Yan, M., Zhou, L., Zhang, G., Meng, L., Chen, L., Cao, X., Zhang, Z., et al. (2023) · Movement Disorders · doi:10.1002/mds.29577 · Cited by 32

Long way up: rethink diseases in light of phase separation and phase transition

Ding, M., Xu, W., Pei, G., & Li, P. (2023) · Protein & Cell · doi:10.1093/procel/pwad057 · Cited by 32

Pexophagy and Oxidative Stress: Focus on Peroxisomal Proteins and Reactive Oxygen Species (ROS) Signaling Pathways

Wei, X., Manandhar, L., Kim, H., Chhetri, A., Hwang, J., Jang, G., Park, C., & Park, R. (2025) · Antioxidants · doi:10.3390/antiox14020126 · Cited by 39

Biomimetic gene delivery system coupled with extracellular vesicle–encapsulated AAV for improving diabetic wound through promoting vascularization and remodeling of inflammatory microenvironment

He, S., Li, Z., Xie, L., Lin, R., Yan, B., Li, B., Luo, L., Xv, Y., Wen, H., Liang, Y., et al. (2025) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03261-w · Cited by 35

SETD7-mediated monomethylation is enriched on soluble Tau in Alzheimer’s disease

Bichmann, M., Oriol, N. P., Ercan-Herbst, E., Schöndorf, D. C., Ramos, B. G., Schwärzler, V., Neu, M., Schlüter, A., Wang, X., Jin, L., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00468-x · Cited by 31

Histone Deacetylases as Epigenetic Targets for Treating Parkinson’s Disease

Li, Y., Gu, Z., Lin, S., Chen, L., Dzreyan, V., Eid, M., Demyanenko, S. V., & He, B. (2022) · Brain Sciences · doi:10.3390/brainsci12050672 · Cited by 31

Upregulated astrocyte HDAC7 induces Alzheimer-like tau pathologies via deacetylating transcription factor-EB and inhibiting lysosome biogenesis

Ye, J., Zhong, S., Wan, H., Guo, X., Yao, X., Liu, Q., Chen, L., Wang, J., & Xiao, S. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00796-2 · Cited by 31

Seeding, maturation and propagation of amyloid β-peptide aggregates in Alzheimer’s disease

Li, X., Ospitalieri, S., Robberechts, T., Hofmann, L., Schmid, C., Upadhaya, A. R., Koper, M. J., Arnim, C. A. F. V., Kumar, S., Willem, M., et al. (2022) · Brain · doi:10.1093/brain/awac202 · Cited by 32

Mixed pathologies in pancreatic β cells from subjects with neurodegenerative diseases and their interaction with prion protein

Martínez-Valbuena, I., Valenti‐Azcarate, R., Amat, I., Marcilla, I., Martí‐Andrés, G., Caballero, M. C., Riverol, M., Tuñon, M.-T., Fraser, P. E., & Luquín, M. R. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01171-0 · Cited by 30

A Prospective Viewpoint on Neurological Diseases and Their Biomarkers

Zehravi, M., Kabir, J., Akter, R., Malik, S., Ashraf, G. M., Tagde, P., Ramproshad, S., Mondal, B., Rahman, M. H., Mohan, A. G., et al. (2022) · Molecules · doi:10.3390/molecules27113516 · Cited by 31

Reassessment of Neuronal Tau Distribution in Adult Human Brain and Implications for Tau Pathobiology

Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01394-9 · Cited by 30

Impact of the Renin-Angiotensin System on the Pathogeny and Pharmacotherapeutics of Neurodegenerative Diseases

Bild, W., Vasincu, A., Rusu, R.-N., Ababei, D. C., Stana, B. A., Stanciu, G. D., Savu, B., & Bild, V. (2022) · Biomolecules · doi:10.3390/biom12101429 · Cited by 32

Pathophysiological Association of Alzheimer’s Disease and Hypertension: A Clinical Concern for Elderly Population

Yao, Q., Jiang, K., Lin, F., Zhu, T., Khan, N. H., & Jiang, E. (2023) · Clinical Interventions in Aging · doi:10.2147/cia.s400527 · Cited by 31

Severe acute respiratory syndrome coronavirus 2 infection leads to Tau pathological signature in neurons

Primio, C. D., Quaranta, P., Mignanelli, M., Siano, G., Bimbati, M., Scarlatti, A., Piazza, C. R., Spezia, P. G., Perrera, P., Basolo, F., et al. (2023) · PNAS Nexus · doi:10.1093/pnasnexus/pgad282 · Cited by 29

Traumatic brain injury and the pathways to cerebral tau accumulation

Flavin, W. P., Hosseini, H. C., Ruberti, J. W., Kavehpour, H. P., Giza, C. C., & Prins, M. L. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1239653 · Cited by 33

Age-related macular degeneration and neurodegenerative disorders: Shared pathways in complex interactions

Jabbehdari, S., Oganov, A. C., Rezagholi, F., Mohammadi, S., Harandi, H., Yazdanpanah, G., & Arévalo, J. F. (2023) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2023.11.003 · Cited by 30

The Role of Exosomes in Thyroid Cancer and Their Potential Clinical Application

Feng, K., Ma, R., Zhang, L., Li, H., Tang, Y., Du, G., Niu, D., & Yin, D. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.596132 · Cited by 28

Parkinson's Disease and the Gut: Models of an Emerging Relationship

Bindas, A. J., Kulkarni, S., Koppes, R. A., & Koppes, A. N. (2020) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.03.071 · Cited by 27

Reactive oxygen species scavenging by hemin-based nanosheets reduces Parkinson’s disease symptoms in an animal model

Li, L., Tu, Q., Jiao, L., Song, X., Wang, L., Ran, X., Xiao, B., Feng, G., Feng, J. Y., & Zhang, C. (2021) · Chemical Engineering Journal · doi:10.1016/j.cej.2021.134356 · Cited by 28

Neurodegenerative Disease-Associated TDP-43 Fragments Are Extracellularly Secreted with CASA Complex Proteins

Casarotto, E., Sproviero, D., Corridori, E., Gagliani, M. C., Cozzi, M., Chierichetti, M., Cristofani, R., Ferrari, V., Galbiati, M., Mina, F., et al. (2022) · Cells · doi:10.3390/cells11030516 · Cited by 27

The role of LRRK2 in the periphery: link with Parkinson's disease and inflammatory diseases

Tsafaras, G., & Baekelandt, V. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105806 · Cited by 28

Therapeutic genetic variation revealed in diverse Hsp104 homologs

March, Z. M., Sweeney, K. M., Kim, H., Yan, X., Castellano, L. M., Jackrel, M. E., Lin, J., Chuang, E., Gomes, E., Willicott, C. W., et al. (2020) · eLife · doi:10.7554/elife.57457 · Cited by 28

Targeting α-synuclein aggregation with immunotherapy: a promising therapeutic approach for Parkinson’s disease

Henrı́quez, G., & Narayan, M. (2023) · Exploration of Neuroprotective Therapy · doi:10.37349/ent.2023.00048 · Cited by 27

Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases

Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641

Prion-like transmission of protein aggregates in neurodegenerative diseases

Brundin, P., Melki, R., & Kopito, R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2873 · Cited by 778

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

Prion-like Spreading of Protein Aggregation in Neurodegenerative Diseases

Vaquer‐Alicea, J., & Diamond, M. I. (2016) · Cited by 1

Protein aggregate spreading in neurodegenerative diseases: Problems and perspectives

Lee, S., Lim, H.-S., Masliah, E., & Lee, H.-J. (2011) · Neuroscience Research · doi:10.1016/j.neures.2011.05.008 · Cited by 190