α-Synucleinopathy phenotypes

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

Diagnosis and management of dementia with Lewy bodies: Third report of the DLB consortium

McKeith, I. G., Dickson, D. W., Lowe, J., Emre, M., O'Brien, J. T., Feldman, H., Cummings, J., Duda, J. E., Lippa, C., Perry, E. K., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000187889.17253.b1 · Cited by 5,069

The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease

Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961

Second consensus statement on the diagnosis of multiple system atrophy

Gilman, S., Wenning, G. K., Low, P. A., Brooks, D. J., Mathias, C. J., Trojanowski, J. Q., Wood, N. W., Colosimo, C., Dürr, A., Fowler, C. J., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000324625.00404.15 · Cited by 3,140

Consortium to Establish a Registry for Alzheimer's Disease (CERAD)

Fillenbaum, G., & Heyman, A. (2002) · doi:10.1002/0470846410.ch42(iii · Cited by 2,859

Diagnostic Criteria for Parkinson Disease

Gelb, D. J., Oliver, E., & Gilman, S. (1999) · Archives of Neurology · doi:10.1001/archneur.56.1.33 · Cited by 2,822

The Sydney multicenter study of Parkinson's disease: The inevitability of dementia at 20 years

Hely, M. A., Reid, W. G. J., ADENA, M. A., Halliday, G. M., & Morris, J. G. (2008) · Movement Disorders · doi:10.1002/mds.21956 · Cited by 2,346

Identification of two distinct synucleins from human brain

Jakes, R., Spillantini, M. G., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00395-5 · Cited by 1,080

Lewy Bodies in Alzheimer's Disease: A Neuropathological Review of 145 Cases Using α‐Synuclein Immunohistochemistry

Hamilton, R. L. (2000) · Brain Pathology · doi:10.1111/j.1750-3639.2000.tb00269.x · Cited by 754

Identifying prodromal Parkinson's disease: Pre‐Motor disorders in Parkinson's disease

Postuma, R. B., Aarsland, D., Barone, P., Burn, D. J., Hawkes, C. H., Oertel, W. H., & Ziemssen, T. (2012) · Movement Disorders · doi:10.1002/mds.24996 · Cited by 615

HSP90 Co-Chaperone, CacyBP/SIP, Protects α-Synuclein from Aggregation

Bohush, A., & Filipek, A. (2020) · Cells · doi:10.3390/cells9102254 · Cited by 15

Parkinson’s Disease Associated with GBA Gene Mutations: Molecular Aspects and Potential Treatment Approaches

Senkevich, K. A., Kopytova, A. E., Usenko, T. S., Emelyanov, A., & Pchelina, S. (2021) · Acta Naturae · doi:10.32607/actanaturae.11031 · Cited by 17

Old age genetically confirmed frontotemporal lobar degeneration with TDP‐43 has limbic predominant TDP‐43 deposition

Buciuc, M., Whitwell, J. L., Baker, M., Rademakers, R., Dickson, D. W., & Josephs, K. A. (2021) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12727 · Cited by 16

Toward Automated Articulation Rate Analysis via Connected Speech in Dysarthrias

Illner, V., Tykalová, T., Novotný, M., Klempíř, J., Dušek, P., & Rusz, J. (2022) · Journal of Speech Language and Hearing Research · doi:10.1044/2021_jslhr-21-00549 · Cited by 17

Discovery and Evaluation of Imidazo[2,1-b][1,3,4]thiadiazole Derivatives as New Candidates for α-Synuclein PET Imaging

Zeng, Q., Zhang, X., Li, Y., Zhang, Q., Dai, J., Yan, X., Liu, Y., Zhang, J., Liu, S., & Cui, M. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00686 · Cited by 15

Editorial: Protein Misfolding and Spreading Pathology in Neurodegenerative Diseases

Lázaro, D. F., Bellucci, A., Brundin, P., & Outeiro, T. F. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00312 · Cited by 15

Sleep Medicine—What's in a Name?

Pevernagie, D., Arnardóttir, E. S., Bruni, O., Hartley, S., Lammers, G. J., Paunio, T., Riemann, D. W., & Riha, R. L. (2025) · Journal of Sleep Research · doi:10.1111/jsr.70150 · Cited by 17

Listening session with the US Food and Drug Administration, Lewy Body Dementia Association, and an expert panel

Sabbagh, M. N., Taylor, A., Galasko, D. R., Galvin, J. E., Goldman, J. G., Leverenz, J. B., Poston, K. L., Boeve, B. F., Irwin, D. J., & Quinn, J. F. (2023) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12375 · Cited by 14

Cholinergic Antagonists and Behavioral Disturbances in Neurodegenerative Diseases

Mahmoudi, R., Novella, J., Badr, S., Boulahrouz, S., Tran, D. D., Morrone, I., & Jaïdi, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24086921 · Cited by 16

SARS-CoV-2 Spike Protein 1 Causes Aggregation of α-Synuclein via Microglia-Induced Inflammation and Production of Mitochondrial ROS: Potential Therapeutic Applications of Metformin

Chang, M. H., Park, J. H., Lee, H., Choi, J. Y., & Koh, Y. H. (2024) · Biomedicines · doi:10.3390/biomedicines12061223 · Cited by 15

Emerging perspectives of copper-mediated transcriptional regulation in mammalian cell development

Fitisemanu, F. M., & Padilla‐Benavides, T. (2024) · Metallomics · doi:10.1093/mtomcs/mfae046 · Cited by 14

Fat and Protein Combat Triggers Immunological Weapons of Innate and Adaptive Immune Systems to Launch Neuroinflammation in Parkinson’s Disease

Hatton, S. L., & Pandey, M. K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031089 · Cited by 15

Structural and Biophysical Characterization of Stable Alpha-Synuclein Oligomers

Vaikath, N. N., Sudhakaran, I. P., Abdi, I. Y., Gupta, V. R., Majbour, N. K., Ghanem, S. S., Abdesselem, H., Vekrellis, K., & El‐Agnaf, O. M. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314630 · Cited by 14

Motor Dysfunction in REM Sleep Behavior Disorder: A Rehabilitation Framework for Prodromal Synucleinopathy

Summers, R. L. S., Rafferty, M. R., Howell, M. J., & MacKinnon, C. D. (2021) · Neurorehabilitation and neural repair · doi:10.1177/15459683211011238 · Cited by 13

A metabolomics study in aqueous humor discloses altered arginine metabolism in Parkinson’s disease

Serrano‐Marín, J., Marín, S., Bernal‐Casas, D., Lillo, A., González‐Subías, M., Navarro, G., Cascante, M., Sánchez-Navés, J., & Franco, R. (2023) · Fluids and Barriers of the CNS · doi:10.1186/s12987-023-00494-5 · Cited by 13

Strategies of positron emission tomography (PET) tracer development for imaging of tau and α-synuclein in neurodegenerative disorders

Mekala, S., Wu, Y., & Li, Y. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00576g · Cited by 13

Patient-specific pluripotent stem cell-based Parkinson’s disease models showing endogenous alpha-synuclein aggregation

Oh, Y. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.6.142 · Cited by 13

Aromaticity at position 39 in α‐synuclein: A modulator of amyloid fibril assembly and membrane‐bound conformations

Buratti, F. A., Böffinger, N. M., Garro, H. A., Flores, J. S., Hita, F. J., Gonçalves, P. D. C., Copello, F. D. R., Lizárraga, L., Rossetti, G., Carloni, P., et al. (2022) · Protein Science · doi:10.1002/pro.4360 · Cited by 12

Synthesis and Evaluation of 18 F-Labeled Chalcone Analogue for Detection of α-Synuclein Aggregates in the Brain Using the Mouse Model

Kaide, S., Watanabe, H., Iikuni, S., Hasegawa, M., & Ono, M. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00473 · Cited by 13

Chronic nigral neuromodulation aggravates behavioral deficits and synaptic changes in an α-synuclein based rat model for Parkinson’s disease

Torre-Muruzabal, T., Devoght, J., den Haute, C. V., Brône, B., der Perren, A. V., & Baekelandt, V. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0814-3 · Cited by 13

Orexin and Sleep Disturbances in Alpha-Synucleinopathies: a Systematic Review

Raheel, K., See, Q. R., Munday, V., Fakhroo, B., Ivanenko, O., Salvatelli, M. L., Mutti, C., Goadsby, P. J., Delogu, A., Naismith, S. L., et al. (2024) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-024-01359-6 · Cited by 12

Structural polymorphism of α-synuclein fibrils alters the pathway of Hsc70-mediated disaggregation

Jäger, S., Tittelmeier, J., Dang, T. L., Bellande, T., Redeker, V., Buell, A. K., Hennig, J., Melki, R., Nussbaum-Krammer, C. I., Bukau, B., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00573-3 · Cited by 13

Decreased plasma α-synuclein in idiopathic Parkinson’s disease patients after adjusting hemolysis factor

Shim, K. H., Kim, S. C., Youn, Y. C., Sung, Y. H., & An, S. S. A. (2020) · Molecular & Cellular Toxicology · doi:10.1007/s13273-020-00104-7 · Cited by 11

Lewy bodies in the olfactory system and the hypothalamus

Cersosimo, M. G., Benarroch, E. E., & Raina, G. B. (2021) · Handbook of clinical neurology · doi:10.1016/b978-0-12-819973-2.00016-2 · Cited by 14

Protective effect of thioredoxin reductase 1 in Parkinson’s disease

Liu, Z., ye, Q., Wang, F., Guo, Y., Cui, R., Wang, J., & Wang, D. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135457 · Cited by 11

Stabilization of 14-3-3 protein-protein interactions with Fusicoccin-A decreases alpha-synuclein dependent cell-autonomous death in neuronal and mouse models

Vinueza‐Gavilanes, R., Bravo-González, J. J., Basurco, L., Boncristiani, C., Fernández‐Irigoyen, J., Santamaría, E., Marcilla, I., Pérez‐Mediavilla, A., Luquín, M. R., Vales, Á., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106166 · Cited by 11

Modeling Parkinson’s Disease and Atypical Parkinsonian Syndromes Using Induced Pluripotent Stem Cells

Mishima, T., Fujioka, S., Fukae, J., Yuasa‐Kawada, J., & Tsuboi, Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123870 · Cited by 12

Assessment of the Retina of Plp-α-Syn Mice as a Model for Studying Synuclein-Dependent Diseases

Kaehler, K., Seitter, H., Sandbichler, A. M., Tschugg, B., Obermair, G. J., Stefanova, N., & Koschak, A. (2020) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.61.6.12 · Cited by 11

Gender-Related Vulnerability of Dopaminergic Neural Networks in Parkinson's Disease

Boccalini, C., Carli, G., Pilotto, A., Padovani, A., & Perani, D. (2020) · Brain Connectivity · doi:10.1089/brain.2020.0781 · Cited by 11

Plasma Homocysteine, Vitamin B12 and Folate Levels in Multiple System Atrophy: A Case-Control Study

Zhang, S., Shi, C., Mao, C., Song, B., Hou, H., Wu, J. W., Liu, X., Luo, H., Sun, S., & Xu, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136468 · Cited by 11

Influence of cognitive reserve on cognitive and motor function in α-synucleinopathies: A systematic review and multilevel meta-analysis

Saywell, I., Foreman, L. M., Child, B., Phillips‐Hughes, A. L., Collins‐Praino, L. E., & Baetu, I. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2024.105672 · Cited by 13

α-Synuclein aggregation decreases cortico-amygdala connectivity and impairs social behavior in mice

Zhou, W., Daniels, S. R., Singh, V., Menard, M. A., Galvis, M. L. E., & Chu, H. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106702 · Cited by 10

Alpha-Synuclein Pathology Coincides With Increased Number of Early Stage Neural Progenitors in the Adult Hippocampus

Bender, H., Fietz, S. A., Richter, F., & Stanojlović, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.691560 · Cited by 10

p27Kip1 regulates alpha-synuclein expression

Gallastegui, E., Domuro, C., Serratosa, J., Larrieux, A., Sin, L., Martinez, J., Besson, A., Morante‐Redolat, J. M., Orlando, S., Aligué, R., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.24687 · Cited by 10

Alpha-synuclein is highly prone to distribution in the hippocampus and midbrain in tree shrews, and its fibrils seed Lewy body-like pathology in primary neurons

Wu, Z., Gao, J., Du, T., Tang, D., Chen, N., Yuan, Y., & Ma, K. (2018) · Experimental Gerontology · doi:10.1016/j.exger.2018.12.008 · Cited by 8

Alpha-synuclein seeds of Parkinson's disease show high prion-exceeding resistance to steam sterilization

Pinder, P., Thomzig, A., Schulz‐Schaeffer, W., & Beekes, M. (2020) · Journal of Hospital Infection · doi:10.1016/j.jhin.2020.10.018 · Cited by 10

Galantamine suppresses α-synuclein aggregation by inducing autophagy via the activation of α7 nicotinic acetylcholine receptors.

Nozaki, S., Hijioka, M., Wen, X., Iwashita, N., Namba, J., Nomura, Y., Nakanishi, A., Kitazawa, S., Honda, R., Kamatari, Y. O., et al. (2024) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2024.07.008 · Cited by 9

The Imbalance of Homocysteine, Vitamin B12 and Folic Acid in Parkinson Plus Syndromes: A Review beyond Parkinson Disease

Poulidou, V., Liampas, I., Arnaoutoglou, M., Dardiotis, E., & Siokas, V. (2024) · Biomolecules · doi:10.3390/biom14101213 · Cited by 11

PET tracer development for imaging α-synucleinopathies

Alam, M. M., Lee, S. H., Wasim, S., & Lee, S. (2025) · Archives of Pharmacal Research · doi:10.1007/s12272-025-01538-0 · Cited by 9

Neurodegenerative diseases

Verkhratsky, A., & Butt, A. M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-821565-4.00012-2 · Cited by 10

Effect of Clemizole on Alpha-Synuclein-Preformed Fibrils-Induced Parkinson’s Disease Pathology: A Pharmacological Investigation

Vaidya, B., Gupta, P., Biswas, S., Laha, J. K., Roy, I., & Sharma, S. S. (2024) · NeuroMolecular Medicine · doi:10.1007/s12017-024-08785-2 · Cited by 9

Microwave fields have little effect on α‐synuclein aggregation in a Caenorhabditis elegans model of Parkinson's disease

de Pomerai, D. I., Iqbal, N., Lafayette, I., Nagarajan, A., Moghadam, M. K., Fineberg, A., Reader, T., Greedy, S., Smartt, C., & Thomas, D. W. P. (2016) · Bioelectromagnetics · doi:10.1002/bem.21959 · Cited by 9

Retinale Bildgebung von Makula und Papille bei neurodegenerativen Erkrankungen

Turski, G. N., Schmitz-Valckenberg, S., Holz, F. G., & Finger, R. P. (2016) · Der Ophthalmologe · doi:10.1007/s00347-016-0412-8 · Cited by 9

The diversity of SNCA transcripts in neurons, and its impact on antisense oligonucleotide therapeuticsPreprint

Evans, J. R., Gustavsson, E. K., Doykov, I., Murphy, D. P., Virdi, G. S., Lachica, J., Röntgen, A., Murtada, M. H., Pang, C. W., Macpherson, H. L., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.30.596437 · Cited by 9

Preserved proteinase K-resistant core after amplification of alpha-synuclein aggregates: Implication to disease-related structural study

Yoshinaga, S., Yamanaka, T., Miyazaki, H., Okuzumi, A., Hiyama, A., Murayama, S., & Nukina, N. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.11.142 · Cited by 8

Non-invasive systemic viral delivery of human alpha-synuclein mimics selective and progressive neuropathology of Parkinson’s disease in rodent brains

Bérard, M., Martínez-Drudis, L., Sheta, R., El‐Agnaf, O. M. A., & Oueslati, A. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00683-8 · Cited by 8

An immunoassay for the quantification of phosphorylated α-synuclein at serine 129 in human cerebrospinal fluid

Silva, A. M., Hickford, E. S., & Cutler, P. (2024) · Bioanalysis · doi:10.1080/17576180.2024.2407718 · Cited by 8

Hemoglobin-binding α-synuclein levels in erythrocytes are elevated in patients with multiple system atrophy

Zhang, X., Wang, S., Li, X., Li, X., Ran, W., Liu, C., Tian, W., Yu, X., Wu, C., Li, P., et al. (2022) · Neuroscience Letters · doi:10.1016/j.neulet.2022.136868 · Cited by 8

Chronic exposure to cerebrospinal fluid of multiple system atrophy in neuroblastoma and glioblastoma cells induces cytotoxicity via ER stress and autophagy activation

Wang, X., Ma, M., Teng, J., Zhang, J., Zhou, S. Y., Zhang, Y., Wu, E., & Ding, X. (2015) · Oncotarget · doi:10.18632/oncotarget.3748 · Cited by 7

Trauma Immediately Preceding REM-Behavior Disorder: A Valuable Prognostic Marker?

Williams, S., Henzler, N., Peřinová, P., Morrison, I., Ellis, J. G., & Riha, R. L. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.710584 · Cited by 7

Trophoblast glycoprotein is a new candidate gene for Parkinson’s disease

Park, S., Yoo, J., Yeon, G., Kim, J. H., Lee, J. S., Choi, S. K., Hwang, Y.-G., Park, C. W., Cho, M. S., Kim, J., et al. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-021-00252-0 · Cited by 7

Amyloid β,α-Synuclein and Amyloid β-α-Synuclein Combination Exert Significant but Different Alterations in Inflammatory Response Profile in Differentiated Human SH-SY5Y Cells

Keskin, E., Gezen‐Ak, D., & Dursun, E. (2023) · ACS Omega · doi:10.1021/acsomega.3c05585 · Cited by 7

C-terminal truncation is a prominent post-translational modification of human erythrocyte α-synuclein

Amagai, R., Otomo, R., Yoshioka, S., Nagano, H., Hashimoto, N., Sakakibara, R., Tanaka, T., & Okado‐Matsumoto, A. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae012 · Cited by 7

The potential of phosphorylated α‐synuclein as a biomarker for the diagnosis and monitoring of multiple system atrophy

Abdul‐Rahman, T., Herrera‐Calderón, R. E., Ahluwalia, A., Awuah, W. A., Ferreira, T., Tan, J. K., Wolfson, M., Ghosh, S., Horbas, V. A., Garg, V., et al. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14678 · Cited by 9

Propagated but Topologically Distributed Forebrain Neurons Expressing Alpha-Synuclein in Aged Macaques

Kimura, K., Inoue, K., Kuroiwa, Y., Tanaka, F., & Takada, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166861 · Cited by 8

Bradykinesia and postural instability in a model of prodromal synucleinopathy with α-synuclein aggregation initiated in the gigantocellular nuclei

Theologidis, V., Ferreira, S. A., Jensen, N. M., Moreira, D. G., Ahlgreen, O. A., Hansen, M. W., Rosenberg, E. D., Richner, M., Faress, I. M. G., Gram, H., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-01948-7 · Cited by 6

Autonomic nervous system dysregulation in neurodegenerative diseases: Bridging brain and heart

Singh, S., Singh, D., Ansari, A. H., & Singh, S. (2025) · Progress in brain research · doi:10.1016/bs.pbr.2025.04.010 · Cited by 6

α-synuclein pathogenesis in hiPSC models of Parkinson’s disease

Baena-Montes, J. M., Avazzadeh, S., & Quinlan, L. R. (2021) · Neuronal Signaling · doi:10.1042/ns20210021 · Cited by 6

Aptamer binding footprints discriminate α-synuclein fibrillar polymorphs from different synucleinopathies

Bouvier‐Müller, A., Fourmy, D., Fenyi, A., Bousset, L., Melki, R., & Ducongè, F. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae544 · Cited by 6

Different charged biopolymers induce α-synuclein to form fibrils with distinct structures

Yao, Y., Zhao, Q., Tao, Y., Liu, K., Cao, T., Chen, Z., Liu, C., Le, W., Zhao, J., Li, D., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107862 · Cited by 7

Comparison Study of Polysomnographic Features in Multiple System Atrophy-cerebellar Types Combined with and without Rapid Eye Movement Sleep Behavior Disorder

Ding, Y., Hu, Y., Zhan, S.-Q., Li, C., Wang, H., & Wang, Y. (2016) · Chinese Medical Journal · doi:10.4103/0366-6999.189903 · Cited by 6

Age-dependent aggregation of α-synuclein in the nervous system of gut-brain axis is associated with caspase-1 activation

Hu, Q. Z., Hong, M., Huang, M., Gong, Q., Zhang, X., Uversky, V. N., Pan-Montojo, F. J., Huang, T., Zhou, H., & Zhu, S. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-022-00917-6 · Cited by 7

Quantification of muscle activity during sleep for patients with neurodegenerative diseases

Hanif, U., Trap, L., Jennum, P., Zoetmulder, M., & Sørensen, H. B. D. (2015) · Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC) · doi:10.1109/embc.2015.7319759 · Cited by 6

Integrins—A missing link in synuclein's pathogenic mechanism

Surguchev, A. A., & Surguchov, A. P. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24384 · Cited by 6

Occurrence of Total and Proteinase K-Resistant Alpha-Synuclein in Glioblastoma Cells Depends on mTOR Activity

Ryskalin, L., Ferese, R., Morucci, G., Biagioni, F., Busceti, C. L., Michetti, F., Lenzi, P., Frati, A., & Fornai, F. (2022) · Cancers · doi:10.3390/cancers14061382 · Cited by 6

Clinicopathological Heterogeneity of Lewy Body Diseases: The Profound Influence of Comorbid Alzheimer’s DiseasePreprint

Beach, T. G., Serrano, G. E., Zhang, N., Driver‐Dunckley, E. D., Sue, L. I., Shill, H. A., Mehta, S. H., Belden, C. M., Tremblay, C., Choudhury, P., et al. (2024) · medRxiv · doi:10.1101/2024.08.30.24312864 · Cited by 6

Alpha-synuclein abundance and localization are regulated by the RNA-binding protein PUMILIO1

Cabaj, M., Mazzara, P. G., Gaertner, Z. A., Wang, R., Pauers, M. M., Randolph, L. K., Roque, C. G., Feeney, S., Raimo, S., de Prisco, N., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116145 · Cited by 6

Synucleinopathies in neurodegenerative diseases: Accomplices, an inside job and selective vulnerability

Azizi, S. A., & Azizi, S.-A. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.12.003 · Cited by 5

Astrocyte alterations in α-synucleinopathies

Rodríguez-Castañeda, M., Campos-Ríos, A., Lamas, J. A., & Covelo, A. (2025) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2025.1650326 · Cited by 5

Bringing natural killer cells to the clinic: Opportunities beyond cancer

Cayatte, M., Picant, V., Vétizou, M., & Vivier, É. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20250612 · Cited by 6

Quantitative Network Comparisons of REM Sleep Without Atonia Across the α-Synucleinopathy Spectrum: A Systematic Review

Byun, J., Yang, T., Sunwoo, J., Shin, W. C., Kwon, O., & Jung, K. (2023) · Nature and Science of Sleep · doi:10.2147/nss.s423878 · Cited by 4

A Forgotten Principle in Immunocytochemistry: Optimal Dilution

Dudás, B., Lane, M. V., Mupparaju, N., Kim, H. M., & Merchenthaler, I. J. (2022) · Journal of Histochemistry & Cytochemistry · doi:10.1369/00221554221146213 · Cited by 4

Influence of cognitive reserve on cognitive and motor function in α‐synucleinopathies: A systematic review protocol

Saywell, I., Child, B., Foreman, L. M., Collins‐Praino, L. E., & Baetu, I. (2023) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14967 · Cited by 4

Native-state proteomics of Parvalbumin interneurons identifies novel molecular signatures and metabolic vulnerabilities to early Alzheimer’s disease pathologyPreprint

Kumar, P., Goettemoeller, A. M., Espinosa‐García, C., Tobin, B. R., Tfaily, A., Nelson, R. S., Natu, A., Dammer, E. B., Santiago, J. V., Malepati, S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.17.541038 · Cited by 4

Effect of paraquat-induced toxicity and the therapeutic potentials of Moringa oleifera and Moringa stenopetala leaf alkaloid extracts

Adefegha, S. A., Ogunsuyi, O. B., Aro, O. P., & Oboh, G. (2025) · Pharmacological Research - Reports · doi:10.1016/j.prerep.2025.100049 · Cited by 4

Modeling Synucleinopathy Using hESC-Derived Cerebral Organoids

Kim, S. J., Jung, W. H., Choe, M. S., Jeon, Y., & Lee, M. Y. (2025) · Cells · doi:10.3390/cells14181436 · Cited by 3

Bereitschaftspotential in Multiple System Atrophy

Yang, Y.-C., Chang, F., Chen, J.-C., Tsai, C.-H., Lin, F.-Y., & Lu, M.-K. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.608322 · Cited by 3

Structure–Activity Relationships of Cyano-substituted Indole Derivatives as Ligands for α‑Synuclein Aggregates

Zeng, Q., Liu, S., & Cui, M. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00384 · Cited by 3

Obstructive Sleep Apnea and α-Synucleinopathies: Nationwide Analysis From South Korea’s Healthcare Database

Song, C., Oh, J., Kim, Y.-C., Um, Y. H., Kim, T., Seo, H., Jeong, J., & Hong, S. (2024) · Sleep Medicine Research · doi:10.17241/smr.2024.02201 · Cited by 3

Optical coherence tomography reveals retinal structural abnormalities in α-synucleinopathies: insights from the Padua-CESNE cohort

Campagnolo, M., Puthenparampil, M., Emmi, A., Weis, L., Basili, E., Mauceri, V. A., Miscioscia, A., Carecchio, M., Guerra, A., Misenti, V., et al. (2025) · Journal of Neural Transmission · doi:10.1007/s00702-025-02918-y · Cited by 3

Alpha-Synuclein Aggregation, Cholesterol Transport, and the 18-kDa Translocator Protein

Dimitrova‐Shumkovska, J., & Krstanoski, L. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.83459 · Cited by 3

Metabolic Role of Hyperhomocysteinemia in the Etiology of Chronic Diseases

Suresh, S., & Waly, M. I. (2021) · Springer eBooks · doi:10.1007/978-3-030-57839-8_4 · Cited by 3

The low dopamine hypothesis: A plausible mechanism underpinning residual urine, overactive bladder and nocturia (RON) syndrome in older patients

Haddad, R., Panicker, J. N., Verbakel, I., Dhondt, K., Ghijselings, L., Hervé, F., Petrović, M., Whishaw, M., Bliwise, D. L., & Everaert, K. (2023) · The French Journal of Urology · doi:10.1016/j.purol.2023.01.002 · Cited by 3

Cerebrospinal fluid/serum albumin ratio in patients with Lewy body disease: a systematic review and meta-analysis

Li, M., Gan, J., Yang, X., Liu, S., & Ji, Y. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1390036 · Cited by 3

Plasma level of alpha-synuclein oligomers as a biomarker for isolated rapid eye movement sleep behavior disorder diagnosis and progression: a prospective cohort study

Chao, Y., Zhang, H., Wang, T., Li, Y., Mao, W., Hu, S., Zhao, L., & Cai, Y. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1442173 · Cited by 3

Anti-TLR2 immunotherapy modulates neuron-to-oligodendrocyte propagation of α-synuclein in mouse and human models

Bae, E.-J., Ham, S., Jeong, Y. W., Yang, W. S., Shin, J., Lee, W.-J., Ahn, W. J., Yoon, Y.-S., Lee, H.-J., Lee, S. H., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-68870-x · Cited by 2

Les synucléinopathies sont-elles des maladies à prions ?

Arotçarena, M.-L., & Dehay, B. (2018) · Pratique Neurologique - FMC · doi:10.1016/j.praneu.2018.02.006 · Cited by 2

La disfunción autonómica en el paciente con enfermedad neurodegenerativa

Roa-Chamorro, R., Torres-Quintero, L., & González‐Bustos, P. (2020) · Hipertensión y Riesgo Vascular · doi:10.1016/j.hipert.2020.02.006 · Cited by 2

What Do We Know About the Validity and Reliability of Mindfulness Self-Report Measures in Persons with Dementia? A Critical Narrative Review

Keune, P. M., Meister, R., Keune, J., Springer, R., Oschmann, P., Hansen, S., Holmerová, I., & Auer, S. (2024) · Clinical Gerontologist · doi:10.1080/07317115.2024.2427268 · Cited by 2

Metal coordination and peripheral substitution modulate the activity of cyclic tetrapyrroles on αS aggregation: a structural and cell-based study

González, N., Gentile, I., Garro, H. A., Delgado‐Ocaña, S., Ramunno, C. F., Buratti, F. A., Griesinger, C., & Fernández, C. O. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01711-z · Cited by 2

Clinical and Epidemiological Aspects of Parkinson's Disease in the South of Western Siberia

Rozhdestvensky, A., Ra, D., Маркс, Е. А., Gaponenko, I. A., & Ханох, Е. В. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.538782 · Cited by 2

The Effects of Fibrillar Forms of α-Synuclein Protein on Neurogenesis in the Hippocampus, Dopaminergic Neurons of the Substantia Nigra, and the Behavior of Ageing Mice

Sherstnev, V. V., Соловьева, О. А., Алексеевна, Г. М., Kedrov, A. V., Коновалова, Е. В., & Ratmirov, A. M. (2018) · Neurochemical Journal · doi:10.1134/s1819712418040062 · Cited by 2

Proteostasis dysregulation in p.A53T-α-Synuclein iPSC-derived astrocytes exacerbates neurodegeneration in a Parkinson’s disease model with Lewy-like pathologyPreprint

Paschou, C., Apokotou, O., Κόλλιας, Α., Charmpi, K., Dede, S., Samiotaki, M. K., Palese, F., Dimoula, K., Emmanouilidou, E., Taoufik, E., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.06.621638 · Cited by 2

Development and In Vitro Characterization of [3H]GMC-058 as Radioligand for Imaging Parkinsonian-Related Proteinopathies

Varrone, A., Sousa, V. C., Mugnaini, M., Biesinger, S., Nordvall, G., Kingston, L. P., Guzzetti, I., Elmore, C. S., Sunnemark, D., Guarino, D. S., et al. (2025) · Cells · doi:10.3390/cells14120869 · Cited by 1

Cellular prion protein and calcium ions trigger the neurotoxicity of α-synuclein aggregates

Bigi, A., Conti, A. C., Napolitano, L., Fusco, G., Simone, A. D., Chiti, F., Cascella, R., & Cecchi, C. (2025) · Cell & Bioscience · doi:10.1186/s13578-025-01479-7 · Cited by 1

PAK1 expression protects cellular and behavioral defects in animal models of Parkinson’ s disease

Kim, J., Lee, K., Kim, H. J., Oh, W., & Kim, H. K. (2026) · Molecular Brain · doi:10.1186/s13041-026-01320-3 · Cited by 1

A Lewy-testes demencia klinikai és neuropatológiai jellemzői

Bencze, J., Simon, V., Bereczki, E., Majer, R. L., Varkoly, G., Murnyák, B., Kálmán, J., & Hortobágyi, T. (2017) · Orvosi Hetilap · doi:10.1556/650.2017.30735 · Cited by 2

Structural MRI in Neurodegenerative Non-Alzheimer’s Dementia

Paola, M. D., & Bourisly, A. K. (2018) · Neuromethods · doi:10.1007/978-1-4939-7647-8_15 · Cited by 2

Computational electroencephalography analysis for characterizing brain networks

Sunwoo, J., Cha, K. S., & Jung, K. (2020) · Annals of Clinical Neurophysiology · doi:10.14253/acn.2020.22.2.82 · Cited by 1

Methylation of MAPT Gene in Neurodegenerative Synucleinopathies

Iakovenko, E. V., Abramycheva, N. Y., Fedotova, E. Y., & Illarioshkin, S. N. (2022) · Russian Journal of Genetics · doi:10.1134/s1022795422050118 · Cited by 1

Neuropathology underlying clinical variability in patients with synucleinopathies

Halliday, G. M., Holton, J. L., Révész, T., & Dickson, D. W. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0852-9 · Cited by 447

Structural variations in αSyn fibrils of Parkinson’s disease and related disorders

Ikenaka, K., Aguirre, C., Araki, K., So, M., Kakuda, K., Nagano, S., & Hideki, M. (2017) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2017.08.995 · Cited by 1

Alpha-Synuclein and synuceinopathies as related to Parkinson's disease

Anyanwu, F. E. (2017) · BIBSYS Brage (BIBSYS (Norway))

Section II: Genetics

(2007) · CRC Press eBooks · doi:10.3109/9781420019223-8

α-Synuclein Strains and Their Relevance to Parkinson’s Disease, Multiple System Atrophy, and Dementia with Lewy Bodies

Graves, N. J., Gambin, Y., & Sierecki, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512134 · Cited by 36