Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System

Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease

Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240

AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease

Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836

α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868

Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain

DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., & Aronin, N. (1997) · Science · doi:10.1126/science.277.5334.1990 · Cited by 2,439

The synaptic vesicle cycle: a cascade of protein–protein interactions

Südhof, T. C. (1995) · Nature · doi:10.1038/375645a0 · Cited by 1,991

Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal

Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,646

Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes

Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,622

Modulation of memory fields by dopamine Dl receptors in prefrontal cortex

Williams, G. V., & Goldman-Rakic, P. S. (1995) · Nature · doi:10.1038/376572a0 · Cited by 1,593

NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded

Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., & Lansbury, P. T. (1996) · Biochemistry · doi:10.1021/bi961799n · Cited by 1,524

Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease

Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,520

Disentangling the Amyloid Pathways: A Mechanistic Approach to Etiology

Malmberg, M., Malm, T., Gustafsson, O., Sturchio, A., Graff, C., Espay, A. J., Wright, A. P. H., Andaloussi, S. E., Lindén, A., & Ezzat, K. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00256 · Cited by 30

Linking Alpha-Synuclein to the Actin Cytoskeleton: Consequences to Neuronal Function

da Silva, M. I. O., & Liz, M. A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00787 · Cited by 33

Pivotal Role of Fyn Kinase in Parkinson’s Disease and Levodopa-Induced Dyskinesia: a Novel Therapeutic Target?

Angelopoulou, E., Paudel, Y. N., Julian, T. H., Shaikh, M. F., & Piperi, C. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02201-z · Cited by 34

Autophagy in α-Synucleinopathies—An Overstrained System

Fellner, L., Gabassi, E., Haybaeck, J., & Edenhofer, F. (2021) · Cells · doi:10.3390/cells10113143 · Cited by 36

The clearance of misfolded proteins in neurodegenerative diseases by zinc metalloproteases: An inorganic perspective

Malgieri, G., & Grasso, G. (2013) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2013.10.008 · Cited by 33

Whole genome expression analyses of single- and double-knock-out mice implicate partially overlapping functions of alpha- and gamma-synuclein

Kuhn, M., Häbig, K., von Bonin, M., Ninkina, N. N., Buchman, V. L., Poths, S., & Rieß, O. (2007) · Neurogenetics · doi:10.1007/s10048-007-0079-z · Cited by 33

Glial inflammation and neurodegeneration induced by candoxin, a novel neurotoxin from Bungarus candidus venom: global gene expression analysis using microarray

Pachiappan, A., Thwin, M. M., Manikandan, J., & Gopalakrishnakone, P. (2005) · Toxicon · doi:10.1016/j.toxicon.2005.08.017 · Cited by 35

An updated review on animal models to study attention-deficit hyperactivity disorder

Kim, D., Yadav, D., & Song, M. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-02893-0 · Cited by 38

Oligomerization of Cysteine String Protein alpha mutants causing adult neuronal ceroid lipofuscinosis

Zhang, Y.-Q., & Chandra, S. S. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.07.009 · Cited by 34

Effects of LRRK2 Inhibitors on Nigrostriatal Dopaminergic Neurotransmission

Qin, Q., Zhi, L., Li, X., Yue, Z., Li, G., & Zhang, H. (2016) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12660 · Cited by 34

Crosstalk between presynaptic trafficking and autophagy in Parkinson's disease

Pan, P., Zhu, Y., Shen, Y., & Yue, Z. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.04.020 · Cited by 33

The Non-amyloidal Component Region of α-Synuclein Is Important for α-Synuclein Transport Within Axons

Anderson, E. N., Hirpa, D., Zheng, K. H., Banerjee, R., & Gunawardena, S. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00540 · Cited by 32

Therapeutic antisense oligonucleotides for movement disorders

Doxakis, E. (2020) · Medicinal Research Reviews · doi:10.1002/med.21706 · Cited by 34

Pre-clinical Studies Identifying Molecular Pathways of Neuroinflammation in Parkinson's Disease: A Systematic Review

Fathi, M., Vakili, K. G., Yaghoobpoor, S., Qadirifard, M. S., Kosari, M., Naghsh, N., Taei, A. A., Klegeris, A., Dehghani, M., Bahrami, A., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.855776 · Cited by 35

Novel AAV-Based Rat Model of Forebrain Synucleinopathy Shows Extensive Pathologies and Progressive Loss of Cholinergic Interneurons

Aldrin-Kirk, P., Davidsson, M., Holmqvist, S., Li, J., & Björklund, T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100869 · Cited by 32

Motor impairment and aberrant production of neurochemicals in human α-synuclein A30P+A53T transgenic mice with α-synuclein pathology

Ikeda, M., Kawarabayashi, T., Harigaya, Y., Sasaki, A., Yamada, S., Matsubara, E., Murakami, T., Tanaka, Y., Kurata, T., Wuhua, X., et al. (2008) · Brain Research · doi:10.1016/j.brainres.2008.10.011 · Cited by 34

Dopamine-related and caspase-independent apoptosis in dopaminergic neurons induced by overexpression of human wild type or mutant α-synuclein

Zhou, Z., Yap, B. J., Gung, Y.-T.-A., LEONG, S., ANG, S., & Lim, T. H. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.10.012 · Cited by 32

β‐Synuclein exhibits chaperone activity more efficiently than α‐synuclein

Lee, D., Paik, S. R., & Choi, K. Y. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.08.075 · Cited by 32

Alpha-Synuclein and Presynaptic Function: Implications for Parkinson's Disease

Lykkeboe, S., & Jensen, P. H. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:115 · Cited by 32

α-Synuclein: Experimental PathologyPreprint

Hasegawa, M., Nonaka, T., & Masuda‐Suzukake, M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024273 · Cited by 33

Emerging pathways in genetic Parkinson’s disease: tangles, Lewy bodies and LRRK2

Devine, M. J., & Lewis, P. A. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06707.x · Cited by 30

Lower nucleus accumbens α-synuclein load and D3 receptor levels in Parkinson's disease with impulsive compulsive behaviours

Barbosa, P., Hapuarachchi, B., Djamshidian, A., Strand, K. M., Lees, A. J., de Silva, R., Holton, J. L., & Warner, T. T. (2019) · Brain · doi:10.1093/brain/awz298 · Cited by 30

Alpha-Synuclein deficiency ameliorates chronic methamphetamine induced neurodegeneration in mice

Ding, J., Hu, S., Meng, Y., Li, C., Huang, J. A., He, Y., & Qiu, P. (2020) · Toxicology · doi:10.1016/j.tox.2020.152461 · Cited by 31

α-Synuclein-mediated neurodegeneration in Dementia with Lewy bodies: the pathobiology of a paradox

Simon, C. A., Soga, T., Okano, H. J., & Parhar, I. S. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00709-y · Cited by 35

Postnatal Expression of α-Synuclein Protein in the Rodent Substantia nigra and Striatum

Jakowec, M. W., Donaldson, D. M., Barba, J., & Petzinger, G. M. (2001) · Developmental Neuroscience · doi:10.1159/000048700 · Cited by 31

Strategic Selection of Neuroinflammatory Models in Parkinson's Disease: Evidence from Experimental Studies

More, S. V., Kumar, H., Kim, I., Koppula, S., Kim, B.-W., & Choi, D. (2013) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/18715273113129990059 · Cited by 31

Alpha-synuclein: between synaptic function and dysfunction.

Rosa, G. D., Puzzo, D., Sant'Angelo, A., Trinchese, F., & Arancio, O. (2003) · PubMed · doi:10.14670/hh-18.1257 · Cited by 31

Alpha-synuclein ferrireductase activity is detectible in vivo, is altered in Parkinson's disease and increases the neurotoxicity of DOPAL

McDowall, J., Ntai, I., Honeychurch, K. C., Hart, J. P., Colin, P., Schneider, B. L., & Brown, D. R. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.08.001 · Cited by 36

Neuronal to oligodendroglial alpha-synuclein redistribution in a double transgenic model of multiple system atrophy

Rockenstein, E. M., Ubhi, K. K., Inglis, C. A., Mante, M., Patrick, C., Adame, A., & Masliah, E. (2012) · Neuroreport · doi:10.1097/wnr.0b013e3283509842 · Cited by 31

Mutant genes responsible for Parkinson's disease

Le, W. (2003) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2003.09.005 · Cited by 31

Interaction of LRRK2 and α-Synuclein in Parkinson’s Disease

Daher, J. P. L. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-49969-7_11 · Cited by 30

Dopamine Transporter/α-Synuclein Complexes Are Altered in the Post Mortem Caudate Putamen of Parkinson’s Disease: An In Situ Proximity Ligation Assay Study

Longhena, F., Faustini, G., Missale, C., Pizzi, M., & Bellucci, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061611 · Cited by 30

Immunotherapy Targeting Neurodegenerative Proteinopathies: α-Synucleinopathies and Tauopathies

Shin, J. H., Kim, H., & Jeon, B. (2019) · Journal of Movement Disorders · doi:10.14802/jmd.19057 · Cited by 31

Phosphorylation of the aggregate-forming protein alpha-synuclein on serine-129 inhibits its DNA-bending properties

Dent, S. E., King, D. P., Osterberg, V. R., Adams, E. K., Mackiewicz, M. R., Weissman, T. A., & Unni, V. K. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101552 · Cited by 34

The Role of α-Synuclein in the Regulation of Serotonin System: Physiological and Pathological Features

Miquel-Rio, L., Sarriés-Serrano, U., Pavia-Collado, R., Meana, J. J., & Bortolozzi, A. A. (2023) · Biomedicines · doi:10.3390/biomedicines11020541 · Cited by 31

Mitochondrial dysfunction in Parkinson’s disease

Бунеева, О. А., & Medvedev, A. E. (2011) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750811040032 · Cited by 30

Localization of Synucleins in the Mammalian Cochlea

Akil, O., Weber, C. M., Park, S. N., Ninkina, N. N., Buchman, V. L., & Lustig, L. R. (2008) · Journal of the Association for Research in Otolaryngology · doi:10.1007/s10162-008-0134-y · Cited by 30

Blood-Based Protein Biomarkers for Diagnosis and Classification of Neurodegenerative Diseases

Noelker, C., Hampel, H. J., & Dodel, R. C. (2011) · Molecular Diagnosis & Therapy · doi:10.1007/bf03256398 · Cited by 29

Antiapoptotic property of human α‐synuclein in neuronal cell lines is associated with the inhibition of caspase‐3 but not caspase‐9 activity

Li, W., & Lee, M. K. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03146.x · Cited by 30

G209A mutant alpha synuclein expression specifically enhances dopamine induced oxidative damage

Orth, M. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2004.03.029 · Cited by 30

Brain reward in the absence of alpha-synuclein

Oksman, M., Tanila, H., & Yavich, L. (2006) · Neuroreport · doi:10.1097/01.wnr.0000230507.70843.51 · Cited by 30

Coumarin 6 and 1,6-diphenyl-1,3,5-hexatriene (DPH) as fluorescent probes to monitor protein aggregation

Makwana, P. K., Jethva, P. N., & Roy, I. (2011) · The Analyst · doi:10.1039/c0an00829j · Cited by 32

Recent Advances in Research on Parkinson Disease: Synuclein and Parkin

Burke, R. E. (2004) · The Neurologist · doi:10.1097/01.nrl.0000117822.90759.83 · Cited by 30

Lack of α‐synuclein does not alter apoptosis of neonatal catecholaminergic neurons

Stefanis, L., Wang, Q., Oo, T. F., Lang‐Rollin, I., Burke, R. E., & Dauer, W. T. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03638.x · Cited by 29

Alpha-synuclein deletion decreases motor impulsivity but does not affect risky decision making in a mouse Gambling Task

Peña‐Oliver, Y., Sanchez‐Roige, S., Stephens, D., & Ripley, T. L. (2014) · Psychopharmacology · doi:10.1007/s00213-013-3416-y · Cited by 29

Synaptic Protein Alterations in Parkinson’s Disease

Pienaar, I. S., Burn, D. J., Morris, C. M., & Dexter, D. T. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8226-9 · Cited by 28

Striatal Dopamine Transmission Is Subtly Modified in Human A53Tα-Synuclein Overexpressing Mice

Platt, N. J., Gispert, S., Auburger, G. W. J., & Cragg, S. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036397 · Cited by 28

A novel resource for studying function and dysfunction of α-synuclein: mouse lines for modulation of endogenous Snca gene expression

Ninkina, N. N., Connor‐Robson, N., Ustyugov, A. A., Tarasova, T. V., Shelkovnikova, T. A., & Buchman, V. L. (2015) · Scientific Reports · doi:10.1038/srep16615 · Cited by 29

Optogenetic Rescue of Locomotor Dysfunction and Dopaminergic Degeneration Caused by Alpha-Synuclein and EKO Genes

Cheng, Q., Varga, S. J., Oh, S., Lee, C. J., & Lee, D. (2017) · Experimental Neurobiology · doi:10.5607/en.2017.26.2.97 · Cited by 29

Endosomal sorting pathways in the pathogenesis of Parkinson's disease

(2020) · Progress in Brain Research · doi:10.1016/bs.pbr.2020.02.001 · Cited by 25

Ablating Tau Reduces Hyperexcitability and Moderates Electroencephalographic Slowing in Transgenic Mice Expressing A53T Human α-Synuclein

Peters, S. T., Fahrenkopf, A., Choquette, J. M., Vermilyea, S. C., Lee, M. K., & Vossel, K. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00563 · Cited by 29

Striatal Dopamine Transporter Function Is Facilitated by Converging Biology of α-Synuclein and Cholesterol

Threlfell, S., Mohammadi, A. S., Ryan, B. J., Connor‐Robson, N., Platt, N. J., Anand, R., Serres, F., Sharp, T., Bengoa‐Vergniory, N., Wade‐Martins, R., et al. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.658244 · Cited by 31

Genes Implicated in Familial Parkinson’s Disease Provide a Dual Picture of Nigral Dopaminergic Neurodegeneration with Mitochondria Taking Center Stage

Franco, R., Rivas‐Santisteban, R., Navarro, G., Pinna, A., & Reyes‐Resina, I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094643 · Cited by 31

Roles for α-Synuclein in Gene Expression

Somayaji, M., Lanseur, Z., Choi, S. J., Sulzer, D., & Mosharov, E. V. (2021) · Genes · doi:10.3390/genes12081166 · Cited by 32

Stress-inducible phosphoprotein 1 (HOP/STI1/STIP1) regulates the accumulation and toxicity of α-synuclein in vivo

Lackie, R. E., de Miranda, A. S., Lim, M. P., Novikov, V., Madrer, N., Karunatilleke, N. C., Rutledge, B. S., Tullo, S., Brickenden, A. M., Maitland, M. E. R., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02491-8 · Cited by 29

Review on the interactions between dopamine metabolites and α-Synuclein in causing Parkinson's disease

Sivakumar, P., Nagashanmugam, K. B., Priyatharshni, S., Lavanya, R., Prabhu, N., & Ponnusamy, S. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105461 · Cited by 29

DJ-1 is Essential for Long-Term Depression at Hippocampal CA1 Synapses

Wang, Y., Chandran, J. S., Cai, H., & Mattson, M. P. (2008) · NeuroMolecular Medicine · doi:10.1007/s12017-008-8023-4 · Cited by 29

The Clustering and Spatial Arrangement of β-Sheet Sequence, but Not Order, Govern α-Synuclein Fibrillogenesis

Suk, J.-E., Lokappa, S. B., & Ulmer, T. S. (2010) · Biochemistry · doi:10.1021/bi901753h · Cited by 29

Modulation of α-synuclein expression in transgenic animals for modelling synucleinopathies — is the juice worth the squeeze?

Buchman, V. L., & Ninkina, N. N. (2008) · Neurotoxicity Research · doi:10.1007/bf03033857 · Cited by 29

Effects of Exercise and Ferulic Acid on Alpha Synuclein and Neuroprotective Heat Shock Protein 70 in An Experimental Model of Parkinsonism Disease

Askar, M. H., Hussein, A. M., El-Basiony, S. F., Meseha, R. K., Metias, E. F., Salama, M., Antar, A., & Elsayed, A. (2018) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527317666180816095707 · Cited by 29

Perturbed Signal Transduction in Neurodegenerative Disorders Involving Aberrant Protein Aggregation

Mattson, M. P., & Sherman, M. Y. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:109 · Cited by 29

Synaptic sabotage: How Tau and α-Synuclein undermine synaptic health

Uytterhoeven, V., Verstreken, P., & Nachman, E. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202409104 · Cited by 29

Membrane Trafficking Illuminates a Path to Parkinson’s Disease

Hasegawa, T., Sugeno, N., Kikuchi, A., Baba, T., & Aoki, M. (2017) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.242.63 · Cited by 29

Methods for detecting toxic α-synuclein species as a biomarker for Parkinson’s disease

O’Hara, D. M., Kalia, S. K., & Kalia, L. V. (2020) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2019.1711359 · Cited by 29

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

Functions of Intracellular Alpha-Synuclein in Microglia: Implications for Parkinson’s Disease Risk

Booms, A., & Coetzee, G. A. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.759571 · Cited by 30

Ferritinophagy and α-Synuclein: Pharmacological Targeting of Autophagy to Restore Iron Regulation in Parkinson’s Disease

Boag, M. K., Roberts, A., Uversky, V. N., Ma, L., Richardson, D. R., & Pountney, D. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042378 · Cited by 31

Vascular and Nonvascular Mechanisms of Cognitive Impairment and Dementia

Kara, B., Gordon, M. N., Gifani, M., Dorrance, A. M., & Counts, S. (2022) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2022.07.006 · Cited by 29

Over‐expression of alpha‐synuclein in the nervous system enhances axonal degeneration after peripheral nerve lesion in a transgenic mouse strain

Siebert, H., Kahle, P. J., Kramer, M. L., Isik, T., Schlüter, O. M., Schulz‐Schaeffer, W., & Brück, W. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06832.x · Cited by 28

Olfactory neuron-specific expression of A30P alpha-synuclein exacerbates dopamine deficiency and hyperactivity in a novel conditional model of early Parkinson's disease stages

Nuber, S., Petrasch‐Parwez, E., Arias-Carrión, Ó., Koch, L., Kohl, Z., Schneider, J., Calaminus, C., Dermietzel, R., Samarina, A., Boy, J., et al. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.06.017 · Cited by 29

Rabs, SNAREs and α-synuclein — Membrane trafficking defects in synucleinopathies

Chua, C. E. L., & Tang, B. L. (2011) · Brain Research Reviews · doi:10.1016/j.brainresrev.2011.03.002 · Cited by 28

Pathological α-synuclein impairs adult-born granule cell development and functional integration in the olfactory bulb

Neuner, J., Ovsepian, S. V., Dorostkar, M. M., Filser, S., Gupta, A., Michalakis, S., Biel, M., & Herms, J. W. (2014) · Nature Communications · doi:10.1038/ncomms4915 · Cited by 28

NMR Structure of Calmodulin Complexed to an N-Terminally Acetylated α-Synuclein Peptide

Gruschus, J. M., Yap, T. L., Pistolesi, S., Maltsev, A. S., & Lee, J. C. (2013) · Biochemistry · doi:10.1021/bi400199p · Cited by 28

CSF from Parkinson disease Patients Differentially Affects Cultured Microglia and Astrocytes

Schiess, M. C., Barnes, J. L., Ellmore, T. M., Poindexter, B. J., Dinh, K., & Bick, R. J. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-151 · Cited by 30

Synucleinopathies: a pathological and molecular review

Murray, I. V. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2001) · Clinical Neuroscience Research · doi:10.1016/s1566-2772(01)00023-8 · Cited by 28

The effects of α-synuclein on phospholipid vesicle integrity: a study using31P NMR and electron microscopy

Madine, J., Hughes, E., Doig, A. J., & Middleton, D. A. (2008) · Molecular Membrane Biology · doi:10.1080/09687680802467977 · Cited by 28

α-Synuclein deficiency promotes neuroinflammation by increasing Th1 cell-mediated immune responses

Ettle, B., Kuhbandner, K., Haase, S., Hoffmann, A., Winkler, J., & Linker, R. A. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0694-4 · Cited by 28

From Synaptic Physiology to Synaptic Pathology: The Enigma of α-Synuclein

Nordengen, K., & Morland, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020986 · Cited by 30

Non-cell-autonomous actions of α-synuclein: Implications in glial synucleinopathies

Lim, S., Kim, H., Kim, D., & Lee, S. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.06.010 · Cited by 28

Current Evidence for a Bidirectional Loop Between the Lysosome and Alpha-Synuclein Proteoforms

Wildburger, N. C., Hartke, A.-S., Schidlitzki, A., & Richter, F. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.598446 · Cited by 28

Synphilin suppresses α‐synuclein neurotoxicity in a Parkinson's disease Drosophila model

Hernández-Vargas, R., Fonseca‐Ornelas, L., López‐González, I., Riesgo‐Escovar, J. R., Zurita, M., & Reynaud, E. (2011) · genesis · doi:10.1002/dvg.20740 · Cited by 29

Pale Body-Like Inclusion Formation and Neurodegeneration following Depletion of 26S Proteasomes in Mouse Brain Neurones are Independent of α-Synuclein

Paine, S., Anderson, G. W., Bedford, K., Lawler, K., Mayer, R. J., Lowe, J. S., & Bedford, L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054711 · Cited by 27

RNA Interference of Human α-Synuclein in Mouse

Kim, Y.-C., Miller, A., Lins, L. C. R. F., Han, S.-W., Keiser, M. S., Boudreau, R. L., Davidson, B. L., & Narayanan, N. S. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00013 · Cited by 28

Targets and Mechanisms in Prevention of Parkinson's Disease through Immunomodulatory Treatments

Chelpin, M. V. E., & Vorup‐Jensen, T. (2017) · Scandinavian Journal of Immunology · doi:10.1111/sji.12542 · Cited by 27

α - synuclein and Parkinson's disease: the first roadblock

Chua, C. E. L., & Tang, B. L. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00528.x · Cited by 27

Astrocytes and Alpha-Synuclein: Friend or Foe?

Ozoran, H., & Srinivasan, R. (2023) · Journal of Parkinson s Disease · doi:10.3233/jpd-230284 · Cited by 28

Revista Española de Geriatría y Gerontología

Santos, R. P., Torres, C. F., Martín‐Arranz, M. D., de Parga, J. M. S., & Martínez, M. A. (2016) · Cited by 26

Ultrastructural changes in peripheral blood leukocytes in α-synuclein knockout mice

Tashkandi, H., Shameli, A., Harding, C. V., & Maitta, R. W. (2018) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2018.09.001 · Cited by 26

Reduction of αSYN Pathology in a Mouse Model of PD Using a Brain-Penetrating Bispecific Antibody

Roshanbin, S., Julku, U. H., Xiong, M., Eriksson, J., Masliah, E., Hultqvist, G., Bergström, J. J. E., Ingelsson, M., Syvänen, S., & Sehlin, D. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14071412 · Cited by 30

Advances in modelling alpha-synuclein-induced Parkinson’s diseases in rodents: Virus-based models versus inoculation of exogenous preformed toxic species

Carta, A. R., Boi, L., Pisanu, A., Palmas, M. F., Carboni, E., & Simone, A. D. (2020) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2020.108685 · Cited by 27

Alpha‐ and beta‐synucleins are new diagnostic tools for acute erythroid leukemia and acute megakaryoblastic leukemia

Maitta, R. W., Wolgast, L. R., Wang, Q., Zhang, H., Bhattacharyya, P. K., Gong, J. Z., Sunkara, J. L., Albanese, J. M., Pizzolo, J. G., Cannizzaro, L. A., et al. (2010) · American Journal of Hematology · doi:10.1002/ajh.21932 · Cited by 28

Brain sites of movement disorder: Genetic and environmental agents in neurodevelopmental perturbations

Palomo, T., Beninger, R. J., Kostrzewa, R. M., & Archer, T. (2003) · Neurotoxicity Research · doi:10.1007/bf03033369 · Cited by 26

Biomolecular condensates and disease pathogenesis

Ruan, K., Bai, G., Fang, Y., Li, D., Li, T., Liu, X., Lu, B., Lü, Q., Songyang, Z., Sun, S., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-024-2661-3 · Cited by 28

Positron emission tomography tracers for synucleinopathies

Xiang, J., Zhang, Z., Wu, S., & Ye, K. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00787-9 · Cited by 27

G6PD deficiency triggers dopamine loss and the initiation of Parkinson’s disease pathogenesis

Stykel, M. G., Siripala, S. V., Soubeyrand, E., Coackley, C. L., Lu, P., Camargo, S., Thevasenan, S., Figueroa, G. B., So, R. W. L., Stuart, E., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2024.115178 · Cited by 25

Combined immunotherapy with “anti-insulin resistance” therapy as a novel therapeutic strategy against neurodegenerative diseases

Takamatsu, Y., Ho, G. J., Koike, W., Sugama, S., Takenouchi, T., Waragai, M., Wei, J., Sekiyama, K., & Hashimoto, M. (2017) · npj Parkinson s Disease · doi:10.1038/s41531-016-0001-1 · Cited by 26

Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules

Jiang, Z., Flynn, J. D., Teague, W. E., Gawrisch, K., & Lee, J. C. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.02.025 · Cited by 25

Intracerebral Administration of a Ligand-ASO Conjugate Selectively Reduces α-Synuclein Accumulation in Monoamine Neurons of Double Mutant Human A30P*A53T*α-Synuclein Transgenic Mice

Pavia-Collado, R., Cóppola-Segovia, V., Miquel-Rio, L., Alarcón-Arís, D., Rodríguez-Aller, R., Torres‐López, M., Paz, V., Ruiz‐Bronchal, E., Campa, L., Artigas, F., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22062939 · Cited by 26

Effects of Alpha-Synuclein Targeted Antisense Oligonucleotides on Lewy Body-Like Pathology and Behavioral Disturbances Induced by Injections of Pre-Formed Fibrils in the Mouse Motor Cortex

Boutros, S. W., Raber, J., & Unni, V. K. (2021) · Journal of Parkinson s Disease · doi:10.3233/jpd-212566 · Cited by 28

Aspects of innate immunity and Parkinson's disease

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Summary

Abeliovich, A., Schmitz, Y., Fariñas, I., Choi-lundberg, D., Ho, W.-H., Castillo, P. E., Shinsky, N., Manuel, J., Verdugo, G., Armanini, M. P., et al. (2013)

Increased striatal dopamine release and hyperdopaminergic‐like behaviour in mice lacking both alpha‐synuclein and gamma‐synuclein

Senior, S. L., Ninkina, N. N., Deacon, R. M. J., Bannerman, D. M., Buchman, V. L., Cragg, S. J., & Wade‐Martins, R. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06055.x · Cited by 160

Decreased reuptake of dopamine in the dorsal striatum in the absence of alpha-synuclein

Chadchankar, H., Ihalainen, J. A., Tanila, H., & Yavich, L. (2011) · Brain Research · doi:10.1016/j.brainres.2011.01.064 · Cited by 66

Alterations in the nigrostriatal system following conditional inactivation of α-synuclein in neurons of adult and aging mice

Ninkina, N. N., Tarasova, T. V., Chaprov, K., Roman, A. Y., Kukharsky, M. S., Колик, Л. Г., Ovchinnikov, R. K., Ustyugov, A. A., Дурнев, А. Д., & Buchman, V. L. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.02.026 · Cited by 35

Elevated tonic extracellular dopamine concentration and altered dopamine modulation of synaptic activity precede dopamine loss in the striatum of mice overexpressing human α‐synuclein

Lam, H. A., Wu, N., Cely, I., Kelly, R. L., Hean, S., Richter, F., Magen, I., Cepeda, C., Ackerson, L. C., Walwyn, W., et al. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22611 · Cited by 184