Parkinsons Disease and other α-Synucleinopathies

α-Synuclein in Lewy bodies

Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382 · see citing works

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 · see citing works

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 · see citing works

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 3,151 · see citing works

A Drosophila model of Parkinson's disease

Feany, M., & Bender, W. (2000) · Nature · doi:10.1038/35006074 · Cited by 2,145 · see citing works

Dopaminergic Loss and Inclusion Body Formation in α-Synuclein Mice: Implications for Neurodegenerative Disorders

Masliah, E., Rockenstein, E. M., Veinbergs, I., Mallory, M. E., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., & Mucke, L. (2000) · Science · doi:10.1126/science.287.5456.1265 · Cited by 1,752 · see citing works

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

Abeliovich, A., Schmitz, Y., Fariñas, I., Choi-Lundberg, D., Ho, W.-H., Castillo, P. E., Shinsky, N., Verdugo, J. M. G., Armanini, M., Ryan, A., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)80886-7 · Cited by 1,722 · see citing works

Comparative Genomics of the Eukaryotes

Rubin, G. M., Yandell, M. D., Wortman, J. R., Gabor, G. L., Miklos, Nelson, C. R., Hariharan, I. K., Fortini, M. E., Li, P. W., Apweiler, R., et al. (2000) · Science · doi:10.1126/science.287.5461.2204 · Cited by 1,698 · see citing works

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 · see citing works

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 1,588 · see citing works

Neuropathology of Parkinson's Disease

Forno, L. (1996) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199603000-00001 · Cited by 1,556 · see citing works

Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,543 · see citing works

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 1,501 · see citing works

Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.

Uéda, K., Fukushima, H., Masliah, E., Xia, Y., Iwai, A., Yoshimoto, M., Otero, D. A., Kondo, J. D. M., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,469 · see citing works

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 · see citing works

The Lewy body variant of Alzheimer's disease: A clinical and pathologic entity

Hansen, L., Salmon, D., Galasko, D., Masliah, E., Katzman, R., DeTeresa, R., Thal, L., Pay, M. M., Hofstetter, R., Klauber, M., et al. (1990) · Neurology · doi:10.1212/wnl.40.1.1 · Cited by 1,068 · see citing works

Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies

Spillantini, M. G., Crowther, R. A., Jakes, R., Cairns, N. J., Lantos, P. L., & Goedert, M. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00504-7 · Cited by 1,026 · see citing works

Glial cytoplasmic inclusions in the CNS of patients with multiple system atrophy (striatonigral degeneration, olivopontocerebellar atrophy and Shy-Drager syndrome)

Papp, M. I., Kahn, J. E., & Lantos, P. L. (1989) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(89)90219-0 · Cited by 991 · see citing works

Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid

Conway, K. A., Harper, J. D., & Lansbury, P. T. (2000) · Biochemistry · doi:10.1021/bi991447r · Cited by 786 · see citing works

Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation

Serpell, L. C., Berriman, J. A., Jakes, R., Goedert, M., & Crowther, R. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.9.4897 · Cited by 748 · see citing works

α-Synuclein Fibrillogenesis Is Nucleation-dependent

Wood, S. J., Wypych, J., Steavenson, S., Louis, J., Citron, M., & Biere, A. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19509 · Cited by 719 · see citing works

Both Familial Parkinson's Disease Mutations Accelerate α-Synuclein Aggregation

Narhi, L. O., Wood, S. J., Steavenson, S., Jiang, Y., Wu, G. M., Anafi, D., Kaufman, S. A., Martin, F. H., Sitney, K. C., Denis, P., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9843 · Cited by 710 · see citing works

Glial cytoplasmic inclusions in white matter oligodendrocytes of multiple system atrophy brains contain insoluble α‐synuclein

Tu, P., Galvin, J. E., Baba, M., Giasson, B., Tomita, T., Leight, S., Nakajo, S., Iwatsubo, T., Trojanowski, J. Q., & Lee, V. M. ‐. (1998) · Annals of Neurology · doi:10.1002/ana.410440324 · Cited by 686 · see citing works

α-Synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy

Wakabayashi, K., Yoshimoto, M., Tsuji, S., & Takahashi, H. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00407-8 · Cited by 643 · see citing works

Subcellular Localization of Wild-Type and Parkinson's Disease-Associated Mutant α-Synuclein in Human and Transgenic Mouse Brain

Kahle, P. J., Neumann, M., Ozmen, L., Müller, V., Jacobsen, H., Schindzielorz, A., Okochi, M., Leimer, U., van der Putten, H., Probst, A., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-17-06365.2000 · Cited by 641 · see citing works

α-Synuclein Membrane Interactions and Lipid Specificity

Jo, E., McLaurin, J., Yip, C. M., George‐Hyslop, P. S., & Fraser, P. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004345200 · Cited by 602 · see citing works

Senile dementia of Lewy body type

Perry, R. H., Irving, D., Blessed, G., FAIRBAIRN, A. F., & Perry, E. K. (1990) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(90)90236-g · Cited by 573 · see citing works

Lewy Bodies Contain Altered α-Synuclein in Brains of Many Familial Alzheimer's Disease Patients with Mutations in Presenilin and Amyloid Precursor Protein Genes

Lippa, C. F., Fujiwara, H., Mann, D. M. A., Giasson, B., Baba, M., Schmidt, M. L., Nee, L. E., O'Connell, B., Pollen, D. A., St. George-Hyslop, P., et al. (1998) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65722-7 · Cited by 533 · see citing works

Binding of α-Synuclein to Brain Vesicles Is Abolished by Familial Parkinson's Disease Mutation

Jensen, P. H., Nielsen, M. S., Jakes, R., Dotti, C. G., & Goedert, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26292 · Cited by 512 · see citing works

Mutant and Wild Type Human α-Synucleins Assemble into Elongated Filaments with Distinct Morphologies in Vitro

Giasson, B. I., Uryu, K., Trojanowski, J. Q., & Lee, V. M. ‐. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7619 · Cited by 505 · see citing works

Neuropathology in mice expressing human alpha-synuclein

van der Putten, H., Wiederhold, K., Probst, A., Barbieri, S., Mistl, C., Danner, S., Kauffmann, S., Hofele, K., Spooren, W. P. J. M., Rüegg, M. A., et al. (2000) · PubMed Central · doi:10.5451/unibas-ep2767 · Cited by 505 · see citing works

Neuropathology in Mice Expressing Human α-Synuclein

van der Putten, H., Wiederhold, K., Probst, A., Barbieri, S., Mistl, C., Danner, S., Kauffmann, S., Hofele, K., Spooren, W. P. J. M., Rüegg, M. A., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-16-06021.2000 · Cited by 478 · see citing works

Interaction of Human α-Synuclein and Parkinson's Disease Variants with Phospholipids

Perrin, R. J., Woods, W. S., Clayton, D. F., & George, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004851200 · Cited by 432 · see citing works

Regulation of Phospholipase D2: Selective Inhibition of Mammalian Phospholipase D Isoenzymes by α- and β-Synucleins

Jenco, J. M., Rawlingson, A., Daniels, B., & Morris, A. J. (1998) · Biochemistry · doi:10.1021/bi972776r · Cited by 431 · see citing works

Synthetic filaments assembled from C‐terminally truncated α‐synuclein

Crowther, R. A., Jakes, R., Spillantini, M. G., & Goedert, M. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01146-6 · Cited by 417 · see citing works

PHASE AND ELECTRON MICROSCOPIC OBSERVATIONS OF LEWY BODIES AND MELANIN GRANULES IN THE SUBSTANTIA NIGRA AND LOCUS CAERULEUS IN PARKINSONʼS DISEASE

Duffy, P. E., & Tennyson, V. M. (1965) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196507000-00003 · Cited by 351 · see citing works

Identification of a breast cancer-specific gene, BCSG1, by direct differential cDNA sequencing.

Ji, H. W., Liu, Y. E., Jia, T., Wang, M., Liu, J., Xiao, G., Joseph, B. K., Rosen, C. A., & Shi, Y. (1997) · PubMed · Cited by 327 · see citing works

Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's disease

El‐Agnaf, O. M. A., Jakes, R., Curran, M. D., & Wallace, A. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01419-7 · Cited by 258 · see citing works

Membrane Association and Protein Conformation of α-Synuclein in Intact Neurons

McLean, P. J., Kawamata, H., Ribich, S. A., & Hyman, B. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8812 · Cited by 243 · see citing works

Lewy bodies in cerebral cortex. Report of three cases

Kosaka, K. (1978) · Acta Neuropathologica · doi:10.1007/bf00690978 · Cited by 235 · see citing works

Multiple-system atrophy: a new α-synuclein disease?

Gai, W., Power, J., Blumbergs, P. C., & Blessing, W. W. (1998) · The Lancet · doi:10.1016/s0140-6736(05)79256-4 · Cited by 229 · see citing works

Alpha synuclein in neurodegenerative disorders: Murderer or accomplice?

Mezey, É., Dehejia, A. M., Harta, G., Papp, M. I., Polymeropoulos, M. H., & Brownstein, M. (1998) · Nature Medicine · doi:10.1038/nm0798-755 · Cited by 185 · see citing works

Parkinson's Disease-associated α-Synuclein Is More Fibrillogenic than β- and γ-Synuclein and Cannot Cross-seed Its Homologs

Biere, A. L., Wood, S. J., Wypych, J., Steavenson, S., Jiang, Y., Anafi, D., Jacobsen, F. W., Jarosinski, M. A., Wu, G., Louis, J., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005514200 · Cited by 178 · see citing works

Lewy body in neurodegeneration with brain iron accumulation type 1 is immunoreactive for α-synuclein

Arawaka, S., Saito, Y., Murayama, S., & Mori, H. (1998) · Neurology · doi:10.1212/wnl.51.3.887 · Cited by 172 · see citing works

Persyn, a Member of the Synuclein Family, Has a Distinct Pattern of Expression in the Developing Nervous System

Buchman, V. L., Hunter, H. J. A., Piñón, L. G. P., Thompson, J., Privalova, E. M., Ninkina, N. N., & Davies, A. M. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-22-09335.1998 · Cited by 169 · see citing works

Characterisation of isolated α-synuclein filaments from substantia nigra of Parkinson's disease brain

Crowther, R. A., Daniel, S. E., & Goedert, M. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01440-3 · Cited by 154 · see citing works

CONCENTRIC HYALINE INCLUSION BODY FORMATION IN MENTAL DISEASE ANALYSIS OF TWENTY-SEVEN CASES

Woodard, J. S. (1962) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196207000-00012 · Cited by 128 · see citing works

Persyn, a member of the synuclein family, influences neurofilament network integrity

Buchman, V. L., Adu, J., Piñón, L. G. P., Ninkina, N. N., & Davies, A. M. (1998) · Nature Neuroscience · doi:10.1038/349 · Cited by 119 · see citing works

Microtubule-associated protein tau, heparan sulphate and α-synuclein in several neurodegenerative diseases with dementia

Spillantini, M. G., Tolnay, M., Love, S., & Goedert, M. (1999) · Acta Neuropathologica · doi:10.1007/s004010051034 · Cited by 78 · see citing works

Widespread occurrence of α‐synuclein/NACP‐immunoreactive neuronal inclusions in juvenileand adult‐onset Hallervorden–Spatz diseasewith Lewy bodies

Wakabayashi, Yoshimoto, Fukushima, Koide, R., Horikawa, Morita, & Takahashi, Y. (1999) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.1999.00193.x · Cited by 61 · see citing works

Untitled work

Mattson, M. (1999) · doi:10.1002/(sici)1097-4547(19991001)58:1

Untitled work

Price (1999) · doi:10.1002/1531-8249(199903)45:3

Untitled work

Goodrum (2000) · doi:10.1002/(sici)1097-4547(20000215)59:4

Conformational constraints for amyloid fibrillation: the importance of being unfolded

Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.12.008 · Cited by 1,012 · see citing works

Parkinson disease: from pathology to molecular disease mechanisms

Dexter, D. T., & Jenner, P. G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.018 · Cited by 716 · see citing works

α-Synuclein misfolding and Parkinson's disease

Breydo, L., Wu, J., & Uversky, V. N. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.002 · Cited by 656 · see citing works

What Macromolecular Crowding Can Do to a Protein

Kuznetsova, I. М., Константинович, Т. К., & Uversky, V. N. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151223090 · Cited by 560 · see citing works

Formation of Toxic Oligomeric α-Synuclein Species in Living Cells

Outeiro, T. F., Putcha, P., Tetzlaff, J. E., Spoelgen, R., Koker, M., Carvalho, F. L. F., Hyman, B. T., & McLean, P. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001867 · Cited by 400 · see citing works

The effect of macromolecular crowding on protein aggregation and amyloid fibril formation

Munishkina, L. A., Cooper, E. M., Uversky, V. N., & Fink, A. L. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.699 · Cited by 352 · see citing works

Biophysics of Parkinsons Disease: Structure and Aggregation of α- Synuclein

Uversky, V. N., & Eliezer, D. (2009) · Current Protein and Peptide Science · doi:10.2174/138920309789351921 · Cited by 320 · see citing works

Neurotoxicant-induced animal models of Parkinson?s disease: understanding the role of rotenone, maneb and paraquat in neurodegeneration

Uversky, V. N. (2004) · Cell and Tissue Research · doi:10.1007/s00441-004-0937-z · Cited by 312 · see citing works

Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo

Cullen, V., Lindfors, M., Ng, J., Paetau, A. E., Swinton, E., Kolodziej, P., Boston, H., Säftig, P., Woulfe, J., Feany, M. Β., et al. (2009) · Molecular Brain · doi:10.1186/1756-6606-2-5 · Cited by 277 · see citing works

The structural differences between patient-derived α-synuclein strains dictate characteristics of Parkinson’s disease, multiple system atrophy and dementia with Lewy bodies

Van der Perren, A., Gelders, G., Fenyi, A., Bousset, L., Brito, F., Peelaerts, W., Van den Haute, C., Gentleman, S., Melki, R., & Baekelandt, V. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02157-3 · Cited by 277 · see citing works

Dopamine and L‐dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease

Li, J., Zhu, M., Manning-Bog, A., Monte, D. A. D., & Fink, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0770fje · Cited by 257 · see citing works

Residual Structure and Dynamics in Parkinson's Disease-associated Mutants of α-Synuclein

Bussell, R., & Eliezer, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106777200 · Cited by 253 · see citing works

Intrinsic disorder in proteins associated with neurodegenerative diseases

Vladimir, N. (2009) · Frontiers in bioscience · doi:10.2741/3594 · Cited by 234 · see citing works

Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates

Rostami, J., Mothes, T., Kolahdouzan, M., Eriksson, O., Moslem, M., Bergström, J., Ingelsson, M., O’Callaghan, P., Healy, L. M., Falk, A., et al. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02158-3 · Cited by 224 · see citing works

Rifampicin Inhibits α-Synuclein Fibrillation and Disaggregates Fibrils

Li, J., Zhu, M., Rajamani, S., Uversky, V. N., & Fink, A. L. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.08.025 · Cited by 218 · see citing works

Glia and alpha-synuclein in neurodegeneration: A complex interaction

Brück, D., Wenning, G. K., Stefanova, N., & Fellner, L. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.003 · Cited by 202 · see citing works

Synergistic Effects of Pesticides and Metals on the Fibrillation of α-Synuclein: Implications for Parkinson’s Disease

Uversky, V. N., Li, J., Bower, K. S., & Fink, A. L. (2002) · NeuroToxicology · doi:10.1016/s0161-813x(02)00067-0 · Cited by 198 · see citing works

Neuropathology of sporadic Parkinson disease before the appearance of parkinsonism: preclinical Parkinson disease

Ferrer, I., Martinez, A., Blanco, R. E., Dalfó, E., & Carmona, M. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0482-8 · Cited by 190 · see citing works

Amyloidogenesis of Natively Unfolded Proteins

Uversky, V. N. (2008) · Current Alzheimer Research · doi:10.2174/156720508784533312 · Cited by 187 · see citing works

Methionine oxidation, α-synuclein and Parkinson's disease

Glaser, C. B., Yamin, G., Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.10.008 · Cited by 169 · see citing works

Proteome analysis of human substantia nigra in Parkinson's disease

Werner, C. J., Haußen, R. H., Mall, G., & Wolf, S. (2008) · Proteome Science · doi:10.1186/1477-5956-6-8 · Cited by 167 · see citing works

Multiple system atrophy: a clinical and neuropathological perspective

Ubhi, K. K., Low, P. A., & Masliah, E. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.08.003 · Cited by 159 · see citing works

Protein disorder in the human diseasome: unfoldomics of human genetic diseases

Midic, U., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-s1-s12 · Cited by 144 · see citing works

Vimentin Is the Specific Target in Skin Glycation

Kueper, T., Grune, T., Prahl, S., Lenz, H., Welge, V., Biernoth, T., Vogt, Y., Muhr, G., Gaemlich, A., Jung, T., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701586200 · Cited by 133 · see citing works

Altered Development of Synapse Structure and Function in Striatum Caused by Parkinson's Disease-Linked LRRK2-G2019S Mutation

Matikainen‐Ankney, B. A., Kezunovic, N., Mesias, R., Tian, Y., Williams, F. M. K., Huntley, G. W., & Benson, D. L. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3314-15.2016 · Cited by 131 · see citing works

Polycation‐induced oligomerization and accelerated fibrillation of human α‐synuclein in vitro

Goers, J. W. F., Uversky, V. N., & Fink, A. L. (2003) · Protein Science · doi:10.1110/ps.0230903 · Cited by 118 · see citing works

Early involvement of the cerebral cortex in Parkinson's disease: Convergence of multiple metabolic defects

Ferrer, I. (2009) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2009.02.004 · Cited by 105 · see citing works

Forcing Nonamyloidogenic β-Synuclein To Fibrillate

Yamin, G., Munishkina, L. A., Karymov, M. A., Lyubchenko, Y. L., Uversky, V. N., & Fink, A. L. (2005) · Biochemistry · doi:10.1021/bi048778a · Cited by 103 · see citing works

Protein folding diseases and neurodegeneration: Lessons learned from yeast

Winderickx, J., Delay, C., Vos, A. D., Klinger, H., Pellens, K., Vanhelmont, T., LEUVEN, F. V., & Zabrocki, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.020 · Cited by 102 · see citing works

Abnormal α-Synuclein Interactions with Rab Proteins in α-Synuclein A30P Transgenic Mice

Dalfó, E., Gómez‐Isla, T., Rosa, J. L., Bodelón, M. N., Tejedor, M. C., Barrachina, M., Ambrosio, S., & Ferrer, I. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.4.302 · Cited by 98 · see citing works

Non-enzymatic covalent modifications of proteins: mechanisms, physiological consequences and clinical applications

Cloos, P. A., & Christgau, S. (2002) · Matrix Biology · doi:10.1016/s0945-053x(01)00188-3 · Cited by 93 · see citing works

α-Synuclein Can Function as an Antioxidant Preventing Oxidation of Unsaturated Lipid in Vesicles

Zhu, M., Qin, Z., Hu, D., Munishkina, L. A., & Fink, A. L. (2006) · Biochemistry · doi:10.1021/bi052584t · Cited by 89 · see citing works

Neurochemistry and the non-motor aspects of PD

Ferrer, I., López‐González, I., Carmona, M., Dalfó, E., Pujol, A., & Martı́nez, A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.10.019 · Cited by 86 · see citing works

Neurogenesis in neurological and psychiatric diseases and brain injury: From bench to bedside

Ruan, L., Lau, B. W.-M., Wang, J., Huang, L., Zhuge, Q., Wang, B. Z., Jin, K., & So, K. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.12.006 · Cited by 85 · see citing works

Effect of melatonin on α-synuclein self-assembly and cytotoxicity

Ono, K., Mochizuki, H., Ikeda, T., Nihira, T., Takasaki, J., Teplow, D. B., & Yamada, M. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.10.015 · Cited by 84 · see citing works

Neuropathology and Neurochemistry of Nonmotor Symptoms in Parkinson's Disease

Ferrer, I. (2011) · Parkinson s Disease · doi:10.4061/2011/708404 · Cited by 73 · see citing works

Protein disulfide isomerase-immunopositive inclusions in patients with Alzheimer disease

Honjo, Y., Ito, H., Horibe, T., Takahashi, R., & Kawakami, K. (2010) · Brain Research · doi:10.1016/j.brainres.2010.06.016 · Cited by 73 · see citing works

Vitamin A potently destabilizes preformed α-synuclein fibrils in vitro: Implications for Lewy body diseases

Ono, K., & Yamada, M. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.10.010 · Cited by 67 · see citing works

Oligomeric alpha‐synuclein and its role in neuronal death

Brown, D. R. (2010) · IUBMB Life · doi:10.1002/iub.316 · Cited by 67 · see citing works

Multiple system atrophy of the cerebellar type: Clinical state of the art

Lin, D. J., Hermann, K. L., & Schmahmann, J. D. (2014) · Movement Disorders · doi:10.1002/mds.25847 · Cited by 66 · see citing works

Mechanism of cleavage of alpha-synuclein by the 20S proteasome and modulation of its degradation by the RedOx state of the N-terminal methionines

Alvarez‐Castelao, B., Goethals, M., Vandekerckhove, J. S., & Castaño, J. G. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.018 · Cited by 60 · see citing works

Cell-to-Cell Transmission of α-Synuclein Aggregates

Lee, S., Desplats, P., Lee, H.-J., Spencer, B. J., & Masliah, E. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-551-0_23 · Cited by 60 · see citing works

Identification of exosomal biomarkers and its optimal isolation and detection method for the diagnosis of Parkinson's disease: A systematic review and meta-analysis

Nila, I. S., Sumsuzzman, D. M., Khan, Z. A., Jung, J. H., Kazema, A. S., Kim, S. J., & Hong, Y. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101764 · Cited by 58 · see citing works

Characterization of the Non-Fibrillar α-Synuclein Oligomers

Hong, D.-P., Han, S., Fink, A. L., & Uversky, V. N. (2011) · Protein and Peptide Letters · doi:10.2174/092986611794578332 · Cited by 58 · see citing works

The Oligomer Hypothesis in α-Synucleinopathy

Ono, K. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2382-x · Cited by 58 · see citing works

Modulation of Alpha-Synuclein Aggregation by Dopamine Analogs

Latawiec, D., Herrera, F. E., Bek, A., Losasso, V., Candotti, M., Benetti, F., Carlino, E., Kranjc, A., Lazzarino, M., Gustincich, S., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009234 · Cited by 57 · see citing works

Spin‐Label EPR on α‐Synuclein Reveals Differences in the Membrane Binding Affinity of the Two Antiparallel Helices

Drescher, M., Godschalk, F., Veldhuis, G., van Rooijen, B. D., Subramaniam, V., & Huber, M. (2008) · ChemBioChem · doi:10.1002/cbic.200800238 · Cited by 56 · see citing works

Under‐folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis

Uversky, V. N. (2013) · Biopolymers · doi:10.1002/bip.22298 · Cited by 53 · see citing works

Time course and progression of wild type α-Synuclein accumulation in a transgenic mouse model

Amschl, D., Neddens, J., Havas, D., Flunkert, S., Rabl, R., Römer, H., Rockenstein, E. M., Masliah, E., Windisch, M., & Hutter‐Paier, B. (2013) · BMC Neuroscience · doi:10.1186/1471-2202-14-6 · Cited by 52 · see citing works

Melatonin, protocatechuic acid and hydroxytyrosol effects on vitagenes system against alpha-synuclein toxicity

Gallardo-Fernández, M., Ortega, R. H., Cerezo, A. B., Troncoso, A. M., & García-Parrilla, M. C. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2019.110817 · Cited by 47 · see citing works

Molecular Aspects of Dopaminergic Neurodegeneration: Gene-Environment Interaction in Parkin Dysfunction

Ali, S. F., BINIENDA, Z. K., & Imam, S. Z. (2011) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph8124702 · Cited by 46 · see citing works

α-Synuclein in Parkinson's Disease: Pathogenic Function and Translation into Animal Models

Eschbach, J., & Danzer, K. M. (2013) · Neurodegenerative Diseases · doi:10.1159/000354615 · Cited by 44 · see citing works

Structures and Free Energy Landscapes of the Wild-Type and A30P Mutant-Type α-Synuclein Proteins with Dynamics

Wise-Scira, O., Aloglu, A. K., Dunn, A., Sakallioglu, I. T., & Coskuner‐Weber, O. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn300198q · Cited by 43 · see citing works

Dissociation of Amyloid Fibrils of α‐Synuclein in Supercooled Water

Kim, H., Cho, M., Riedel, D., Fernández, C. O., & Zweckstetter, M. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200800342 · Cited by 40 · see citing works

microRNAs involved in Parkinson's disease: A systematic review

da Silva, F. C., Iop, R. D. R., Vietta, G. G., Kair, D. A., Filho, P. J. B. G., Alvarenga, J. G., & da Silva, R. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5759 · Cited by 39 · see citing works

Synphilin-1 inhibits alpha-synuclein degradation by the proteasome

Alvarez‐Castelao, B., & Castaño, J. G. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0592-3 · Cited by 36 · see citing works

Therapeutic Advances in Diabetes, Autoimmune, and Neurological Diseases

Liu, J., Ting, J. P., Al-Azzam, S., Ding, Y., & Afshar, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22062805 · Cited by 35 · see citing works

Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective

Daskalov, A., Mammeri, N. E., Lends, A., Shenoy, J., Lamon, G., Fichou, Y., Saad, A., Martinez, D., Morvan, E., Berbon, M., et al. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.670513 · Cited by 33 · see citing works

Biophysical Characterization of α-Synuclein and Rotenone Interaction

Silva, B., Einarsdóttir, Ó., Fink, A. L., & Uversky, V. N. (2013) · Biomolecules · doi:10.3390/biom3030703 · Cited by 30 · see citing works

Progress in Clinical Neurosciences: Parkinson's Disease with Dementia and Dementia with Lewy Bodies

Camicioli, R. M., & Fisher, N. (2004) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100002791 · Cited by 28 · see citing works

Protein-templated semiconductor nanoparticle chains

Padalkar, S., Hulleman, J. D., Kim, S. M., Rochet, J., Stach, E. A., & Stanciu, L. (2008) · Nanotechnology · doi:10.1088/0957-4484/19/27/275602 · Cited by 28 · see citing works

Targeting the Chameleon: a Focused Look at α-Synuclein and Its Roles in Neurodegeneration

Silva, B. A., Breydo, L., & Uversky, V. N. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8334-1 · Cited by 25 · see citing works

Steady-State Kinetics of α-Synuclein Ferrireductase Activity Identifies the Catalytically Competent Species

McDowall, J., Ntai, I., Hake, J., Whitley, P. R., Mason, J. M., Pudney, C. R., & Brown, D. R. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00257 · Cited by 24 · see citing works

Neuronal inclusions in degenerative disorders

Fornai, F., Soldani, P., Lazzeri, G., di Poggio, A. B., Biagioni, F., Fulceri, F., Batini, S., Ruggieri, S. A., & Paparelli, A. (2005) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2004.12.009 · Cited by 22 · see citing works

Hydroxytyrosol and dopamine metabolites: Anti-aggregative effect and neuroprotective activity against α-synuclein-induced toxicity

Gallardo-Fernández, M., Ortega, R. H., Cerezo, A. B., Troncoso, A. M., & García-Parrilla, M. C. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113542 · Cited by 20 · see citing works

Intrinsic Disorder in Proteins Associated with Neurodegenerative Diseases

Uversky, V. N. (2008) · Focus on structural biology · doi:10.1007/978-1-4020-9434-7_2 · Cited by 20 · see citing works

SF-6 attenuates 6-hydroxydopamine-induced neurotoxicity: An in vitro and in vivo investigation in experimental models of Parkinson's disease

Kopalli, S. R., Koppula, S., Shin, K. Y., Noh, S.-J., Jin, Q., Hwang, B. Y., & Suh, Y. (2012) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2012.07.032 · Cited by 17 · see citing works

Peripheral Sensory Neurons Survive in the Absence of α- and γ-Synucleins

Papachroni, K. K., Ninkina, N. N., Wanless, J., Kalofoutis, A., Gnuchev, N. V., & Buchman, V. L. (2005) · Journal of Molecular Neuroscience · doi:10.1385/jmn:25:2:157 · Cited by 17 · see citing works

The loss of inhibitory C‐terminal conformations in disease associated P123H β‐synuclein

Janowska, M. K., & Baum, J. (2015) · Protein Science · doi:10.1002/pro.2798 · Cited by 16 · see citing works

The interplay between α-synuclein aggregation and necroptosis in Parkinson’s disease: a spatiotemporal perspective

Xiang, H. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1567445 · Cited by 15 · see citing works

The unique neuropathological vulnerability of the human brain to aging

Ferrer, I. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101916 · Cited by 14 · see citing works

Anti-α-synuclein c-terminal antibodies block PFF uptake and accumulation of phospho-synuclein in preclinical models of Parkinson's disease

Brendza, R. P., Gao, X., Stark, K. L., Lin, H., Lee, S.-H., Hu, C., Cai, H., DiCara, D. M., Hsiao, Y.-C., Ngu, H., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105969 · Cited by 14 · see citing works

Mitochondria, monoamine oxidase B and Parkinson’s disease

Jenner, P. G. (2012) · Basal Ganglia · doi:10.1016/j.baga.2012.06.006 · Cited by 14 · see citing works

Epitope Mapping of Antibodies to Alpha-Synuclein in LRRK2 Mutation Carriers, Idiopathic Parkinson Disease Patients, and Healthy Controls

Alvarez‐Castelao, B., Gorostidi, A., Ruiz-Martínez, J., de Munaín, A. L., & Castaño, J. G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00169 · Cited by 14 · see citing works

Up and Down γ-Synuclein Transcription in Dopamine Neurons Translates into Changes in Dopamine Neurotransmission and Behavioral Performance in Mice

Pavia-Collado, R., Rodríguez-Aller, R., Alarcón-Arís, D., Miquel-Rio, L., Ruiz‐Bronchal, E., Paz, V., Campa, L., Galofré, M., Sgambato, V., & Bortolozzi, A. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031807 · Cited by 13 · see citing works

Diseases of movement and system degenerations

Ince, P. G., Clark, B., Holton, J. L., Révész, T., & Wharton, S. B. (2008) · CRC Press eBooks · doi:10.1201/b13319-14 · Cited by 13 · see citing works

Structural and Conformational Prerequisites of Amyloidogenesis

Uversky, V. N., Fernández, A., & Fink, A. L. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_1 · Cited by 12 · see citing works

α-Synuclein Aggregation and Parkinson’s Disease

Uversky, V. N. (2007) · Springer eBooks · doi:10.1007/978-0-387-36534-3_4 · Cited by 11 · see citing works

Dissociation of Amyloid Fibrils of α‐Synuclein in Supercooled Water

Kim, H., Cho, M., Riedel, D., Fernández, C. O., & Zweckstetter, M. (2008) · Angewandte Chemie · doi:10.1002/ange.200800342 · Cited by 10 · see citing works

Mapping of Surface-Exposed Epitopes of In Vitro and In Vivo Aggregated Species of Alpha-Synuclein

Almandoz-Gil, L., Lindström, V., Sigvardson, J., Kahle, P. J., Lannfelt, L., Ingelsson, M., & Bergström, J. J. E. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0454-0 · Cited by 8 · see citing works

Alpha-synuclein as a template for the synthesis of metallic nanowires

Padalkar, S., Hulleman, J. D., Deb, P., Cunzeman, K., Rochet, J., Stach, E. A., & Stanciu, L. (2007) · Nanotechnology · doi:10.1088/0957-4484/18/5/055609 · Cited by 7 · see citing works

Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins

Venati, S. R., & Uversky, V. N. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158399 · Cited by 6 · see citing works

Ligand Profiling as a Diagnostic Tool to Differentiate Patient-Derived α-Synuclein Polymorphs

Chisholm, T. S., Melki, R., & Hunter, C. A. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00178 · Cited by 6 · see citing works

Zur postmortalen Diagnose des idiopathischen Morbus Parkinson

Sandmann-Keil, D., & Braak, H. (2004) · Der Pathologe · doi:10.1007/s00292-004-0722-5 · Cited by 6 · see citing works

RIBONUCLEIC ACID INTERFERENCE FOR NEUROLOGICAL DISORDERS

Federici, T., & Boulis, N. M. (2007) · Neurosurgery · doi:10.1227/01.neu.0000249214.42461.a5 · Cited by 6 · see citing works

3, 4-Dihydroxyphenylacetic Acid (DOPAC) Impairs α-Synuclein Interaction with Lipids

Zhou, W., Long, C., Fink, A. L., & Uversky, V. N. (2010) · The Open Proteomics Journal · doi:10.2174/1875039701003010001 · Cited by 2 · see citing works

Neuro-pathological Implications of β-Amyloid Protein: An Update

Maurya, N., & Agarwal, N. R. (2018) · Proceedings of the Nature Research Society · doi:10.11605/j.pnrs.2018020061 · Cited by 2 · see citing works

Senile Dementia

Pedersen, W. A. (2007) · xPharm: The Comprehensive Pharmacology Reference · doi:10.1016/b978-008055232-3.60662-2 · Cited by 1 · see citing works

The interplay between Lewy body-like alpha-synuclein aggregates and protein degradation pathways in a cell-based model of Parkinson's disease

Tanik, S. A. (2013) · Scholarly Commons (University of Pennsylvania) · Cited by 1 · see citing works

Editorial: Glial Cell Biology and Neurological Disease

Lechleiter, J. D. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.11.013 · Cited by 1 · see citing works

BIOPHYSICAL STUDIES OF THE ALPHA-SYNUCLEIN PROTEIN ASSOCIATED WITH PARKINSON’S DISEASE AND OTHER SYNUCLEINOPATHIES

Apetri, M. M. (2006) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 1 · see citing works

Fundamentals of Protein Folding

Uversky, V. N. (2014) · Wiley eBooks · doi:10.1002/9781118845363.ch1

Simultaneous Occurrence of Bioactive Compounds (Melatonin, Protocatechuic Acid and Hydroxytyrosol) Increases Their Neuroprotective Effects Against Alpha-Synuclein-Induced ProteotoxicityPreprint

Gallardo-Fernández, M., Ortega, R. H., Cerezo, A. B., Troncoso, A. M., & García-Parrilla, M. C. (2018) · Preprints.org · doi:10.20944/preprints201811.0142.v1

Dementias☆

Anderson, H. S. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.05297-1

Alpha-Synuclein Dynamics in Cerebral Ischemia

Bordbar, S., Molavizade, S., Dehghani, F., Davoody, S., Bahadori, A. R., & Tafakhori, A. (2026) · ASN NEURO · doi:10.1080/17590914.2026.2615453

The α‐Synucleinopathies: Parkinson's Disease, Dementia with Lewy Bodies, and Multiple System Atrophy

Spillantini, M. G., & Goedert, M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06900.x · Cited by 520 · see citing works

Alpha-synuclein and neurodegenerative diseases

Goedert, M. (2001) · Nature reviews. Neuroscience · doi:10.1038/35081564 · Cited by 1,402 · see citing works

Parkinson’s Disease: Alpha-Synuclein and Neurodegeneration

Goedert, M. (2009) · Elsevier eBooks · doi:10.1016/b978-008045046-9.00512-x · Cited by 1 · see citing works

Parkinson's disease, dementia with Lewy bodies and multiple system atrophy are α-synucleinopathies

Spillantini, M. G. (1999) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(99)00031-0 · Cited by 80 · see citing works

α-Synuclein and Neurodegeneration

Goedert, M. (2004) · Elsevier eBooks · doi:10.1016/b978-012589762-4/50055-4 · Cited by 2 · see citing works