The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961

Basic local alignment search tool

Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

Physical basis of cognitive alterations in alzheimer's disease: Synapse loss is the major correlate of cognitive impairment

Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397

Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease.

Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268

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

Identification and localization of synaptophysin, an integral membrane glycoprotein of Mr 38,000 characteristic of presynaptic vesicles

Wiedenmann, B. J., & Franke, W. W. (1985) · Cell · doi:10.1016/s0092-8674(85)80082-9 · Cited by 1,432

Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation

Kagawa, Y., & Racker, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61930-1 · Cited by 1,361

Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases

Kennelly, P. J., & Krebs, E. G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98436-x · Cited by 1,331

Suppression of dynamin GTPase decreases α-synuclein uptake by neuronal and oligodendroglial cells: a potent therapeutic target for synucleinopathy

Konno, M., Hasegawa, T., Baba, T., Miura, E., Sugeno, N., Kikuchi, A., Fiesel, F. C., Sasaki, T., Aoki, M., Itoyama, Y., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-38 · Cited by 122

Structural Characteristics of α-Synuclein Oligomers

Cremades, N., Chen, S. W., & Dobson, C. M. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.08.010 · Cited by 123

Initiation and progression of α-synuclein pathology in Parkinson’s disease

Tofaris, G. K. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04240-2 · Cited by 126

Synphilin-1 Is Developmentally Localized to Synaptic Terminals, and Its Association with Synaptic Vesicles Is Modulated by α-Synuclein

Ribeiro, C. S., Carneiro, K., Ross, C. A., Menezes, J. R. L., & Engelender, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201115200 · Cited by 119

NACP, a Synaptic Protein Involved in Alzheimer's Disease, Is Differentially Regulated during Megakaryocyte Differentiation

Hashimoto, M., Yoshimoto, M., Sisk, A., Hsu, L. J., Sundsmo, M. P., Kittel, Á., Saitoh, T., Miller, A. L., & Masliah, E. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6978 · Cited by 120

Accumulation of phosphorylated a-synuclein in the brain and peripheral ganglia of patients with multiple system atrophy

Nishie, M., Mori, F., Fujiwara, H., Hasegawa, M., Yoshimoto, M., Iwatsubo, T., Takahashi, H., & Wakabayashi, K. (2004) · Acta Neuropathologica · doi:10.1007/s00401-003-0811-1 · Cited by 118

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

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

Genetic studies in Alzheimer's disease with an NACP/α‐synuclein polymorphism

Xia, Y., de Silva, H. A. R., Rosi, B. L., Yamaoka, L. H., Rimmler, J. B., Pericak‐Vance, M. A., Roses, A. D., Chen, X., Masliah, E., DeTeresa, R. M., et al. (1996) · Annals of Neurology · doi:10.1002/ana.410400212 · Cited by 120

Chapter 6 Molecular and Cellular Biology of Synucleins

Surguchov, A. P. (2008) · International review of cytology · doi:10.1016/s1937-6448(08)01406-8 · Cited by 123

Amyloidogenic α-synuclein seeds do not invariably induce rapid, widespread pathology in mice

Sacino, A. N., Brooks, M., Thomas, M. A., McKinney, A. B., McGarvey, N. H., Rutherford, N. J., Ceballos‐Diaz, C., Robertson, J., Golde, T. E., & Giasson, B. I. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1268-0 · Cited by 119

Alpha-Synuclein PET Tracer Development—An Overview about Current Efforts

Korat, Š., Bidesi, N., Bonanno, F., Nanni, A. D., Hoàng, A. N. N., Herfert, K., Maurer, A., Battisti, U. M., Bowden, G. D., Thonon, D., et al. (2021) · Pharmaceuticals · doi:10.3390/ph14090847 · Cited by 120

A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed α-synuclein

Zhou, C., Emadi, S., Sierks, M. R., & Messer, A. C. (2004) · Molecular Therapy · doi:10.1016/j.ymthe.2004.08.019 · Cited by 117

Dementia with Lewy Bodies. A Distinct Non‐Alzheimer Dementia Syndrome?

Ince, P. G., Perry, E. K., & Morris, C. M. (1998) · Brain Pathology · doi:10.1111/j.1750-3639.1998.tb00156.x · Cited by 116

Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved

Vasili, E., Dominguez‐Meijide, A., & Outeiro, T. F. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00107 · Cited by 121

Physiology and Pathophysiology of α‐Synuclein: Cell Culture and Transgenic Animal Models Based on a Parkinson's Disease‐associated Protein

Kahle, P. J., Neumann, M., Ozmen, L., & Haass, C. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06902.x · Cited by 115

Overexpression of the calpain-specific inhibitor calpastatin reduces human alpha-Synuclein processing, aggregation and synaptic impairment in [A30P]αSyn transgenic mice

Diepenbroek, M., Casadei, N., Esmer, H., Saido, T. C., Takano, J., Kahle, P. J., Nixon, R. A., Rao, M. V., Melki, R., Pieri, L., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu112 · Cited by 116

Multiple phosphorylation of α‐synuclein by protein tyrosine kinase Syk prevents eosin‐induced aggregation

Negro, A., Brunati, A. M., Donella‐Deana, A., Massimino, M. L., & Pinna, L. A. (2001) · The FASEB Journal · doi:10.1096/fj.01-0517fje · Cited by 112

Formation of dopamine-mediated α-synuclein-soluble oligomers requires methionine oxidation

Leong, S. L., Pham, C. L. L., Galatis, D., Fodero‐Tavoletti, M. T., Perez, K. A., Hill, A. F., Masters, C. L., Ali, F. E. A., Barnham, K. J., & Cappai, R. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.009 · Cited by 114

Oligomeropathies and pathogenesis of Alzheimer and Parkinson's diseases

Forloni, G., Artuso, V., Vitola, P. L., & Balducci, C. (2016) · Movement Disorders · doi:10.1002/mds.26624 · Cited by 116

Lovastatin ameliorates α-synuclein accumulation and oxidation in transgenic mouse models of α-synucleinopathies

Koob, A. O., Ubhi, K. K., Paulsson, J. F., Kelly, J. W., Rockenstein, E. M., Mante, M., Adame, A., & Masliah, E. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.11.015 · Cited by 113

Localization of the mouse α1A-adrenergic receptor (AR) in the brain: α1AAR is expressed in neurons, GABAergic interneurons, and NG2 oligodendrocyte progenitors

Papay, R. S., Gaivin, R. J., Jha, A., McCune, D. F., McGrath, J. C., Rodrigo, M. C., Simpson, P. C., Doze, V. A., & Perez, D. M. (2006) · The Journal of Comparative Neurology · doi:10.1002/cne.20992 · Cited by 118

Lipids at the Crossroad of α-Synuclein Function and Dysfunction: Biological and Pathological Implications

Alza, N. P., González, P. A. I., Conde, M. A., Uranga, R. M., & Salvador, G. A. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00175 · Cited by 116

Structural and Functional Insights into α-Synuclein Fibril Polymorphism

Mehra, S., Gadhe, L. G., Bera, R., Sawner, A. S., & Maji, S. K. (2021) · Biomolecules · doi:10.3390/biom11101419 · Cited by 111

β-Synuclein Regulates Akt Activity in Neuronal Cells

Hashimoto, M., Bar‐On, P., Ho, G. J., Takenouchi, T., Rockenstein, E. M., Crews, L. A., & Masliah, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313784200 · Cited by 111

The Role of α‐Synuclein in Both Neuroprotection and Neurodegeneration

Sidhu, A., Wersinger, C., Moussa, C., & Vernier, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1332.016 · Cited by 110

The Interplay between Alpha-Synuclein Clearance and Spreading

da Fonseca, T. L., Villar‐Piqué, A., & Outeiro, T. F. (2015) · Biomolecules · doi:10.3390/biom5020435 · Cited by 115

p53 mutation as a source of aberrant β-catenin accumulation in cancer cells

Cagatay, T., & Ozturk, M. (2002) · Oncogene · doi:10.1038/sj.onc.1205919 · Cited by 110

Remodeling of Lipid Vesicles into Cylindrical Micelles by α-Synuclein in an Extended α-Helical Conformation

Mizuno, N., Varkey, J., Kegulian, N. C., Hegde, B. G., Cheng, N., Langen, R., & Steven, A. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365817 · Cited by 112

Versatile Structures of α-Synuclein

Wang, C., Zhao, C., Li, D., Tian, Z., Lai, Y., Diao, J., & Liu, C. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00048 · Cited by 109

Copper- and iron-induced differential fibril formation in α-synuclein: TEM study

..., B., Indi, S. S., & Rao, K. S. J. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.06.052 · Cited by 109

Interactions of Amyloidogenic Proteins

Giasson, B. I., Lee, V. M. ‐., & Trojanowski, J. Q. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:49 · Cited by 106

Biochemical Staging of Synucleinopathy and Amyloid Deposition in Dementia With Lewy Bodies

Deramecourt, V., Bombois, S., Maurage, C., Ghestem, A., Drobecq, H., Vanmechelen, E., Lebert, F., Pasquier, F., & Delacourte, A. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000205145.54457.ea · Cited by 109

A Reductionist View of Alzheimer's Disease

Lansbury, P. T. (1996) · Accounts of Chemical Research · doi:10.1021/ar950159u · Cited by 109

Characterization of Hydrophobic Residue Requirements for α-Synuclein Fibrillization

Waxman, E. A., Mazzulli, J. R., & Giasson, B. I. (2009) · Biochemistry · doi:10.1021/bi900539p · Cited by 110

The microRNA miR-7a-5p ameliorates ischemic brain damage by repressing α-synuclein

Kim, T., Mehta, S. L., Morris-Blanco, K. C., Chokkalla, A. K., Chelluboina, B., Lopez, M. S., Sullivan, R., Kim, H. T., Cook, T. D., Kim, J. Y., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aat4285 · Cited by 107

Neurobiology of α-Synuclein

Vekrellis, K., Rideout, H. J., & Stefanis, L. (2004) · Molecular Neurobiology · doi:10.1385/mn:30:1:001 · Cited by 108

Organization, expression and polymorphism of the human persyn gene

Ninkina, N. N. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.9.1417 · Cited by 107

Metalloproteomics and metal toxicology of α-synuclein

Santner, A. A., & Uversky, V. N. (2010) · Metallomics · doi:10.1039/b926659c · Cited by 104

Degradative organelles containing mislocalized α- and β-synuclein proliferate in presenilin-1 null neurons

Wilson, C., Murphy, D. D., Giasson, B. I., Zhang, B., Trojanowski, J. Q., & Lee, V. M. ‐. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403061 · Cited by 108

Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators

Uversky, V. N. (2014) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2014.00006 · Cited by 108

Alpha-synuclein activates BV2 microglia dependent on its aggregation state

Hoffmann, A., Ettle, B., Bruno, A., Kulinich, A. O., Hoffmann, A.-C., von Wittgenstein, J., Winkler, J., Xiang, W., & Schlachetzki, J. C. M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.109 · Cited by 111

Controlling the mass action of α‐synuclein in Parkinson’s disease

Kim, C., & Lee, S. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05612.x · Cited by 108

Mechanistic aspects of Parkinson’s disease: α-synuclein and the biomembrane

Beyer, K. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0014-9 · Cited by 104

Chaperone-like activity of the AAA+ proteins Rvb1 and Rvb2 in the assembly of various complexes

Nano, N., & Houry, W. A. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0399 · Cited by 111

The usual suspects, dopamine and alpha‐synuclein, conspire to cause neurodegeneration

Mor, D. E., Daniels, M. J., & Ischiropoulos, H. (2019) · Movement Disorders · doi:10.1002/mds.27607 · Cited by 107

Transmission of α-synuclein seeds in neurodegenerative disease: recent developments

Karpowicz, R. J., Trojanowski, J. Q., & Lee, V. M. ‐. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0195-z · Cited by 105

Synucleinopathies: Where we are and where we need to go

Brás, I. C., Dominguez‐Meijide, A., Gerhardt, E., Koss, D. J., Lázaro, D. F., Santos, P. I., Vasili, E., Xylaki, M., & Outeiro, T. F. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14965 · Cited by 106

Mutant and Wild-Type α-Synuclein Interact with Mitochondrial Cytochrome C Oxidase

Elkon, H., Don, J., Melamed, E., Ziv, I., Shirvan, A., & Offen, D. (2002) · Journal of Molecular Neuroscience · doi:10.1385/jmn:18:3:229 · Cited by 103

Sorting out release, uptake and processing of alpha‐synuclein during prion‐like spread of pathology

Tyson, T., Steiner, J. A., & Brundin, P. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13449 · Cited by 110

Therapeutics in the Pipeline Targeting α-Synuclein for Parkinson's Disease

Jasutkar, H. G., Oh, S. E., & Mouradian, M. M. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000133 · Cited by 104

α-Synuclein Populates Both Elongated and Broken Helix States on Small Unilamellar Vesicles

Lokappa, S. B., & Ulmer, T. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.224055 · Cited by 102

γ‐Synuclein and the progression of cancer

Ahmad, M., Attoub, S., Singh, M. N., Martin, F. L., & El‐Agnaf, O. M. A. (2007) · The FASEB Journal · doi:10.1096/fj.07-8379rev · Cited by 103

Axonal transport of synucleins is mediated by all rate components

Jensen, P. H., Li, J., Dahlström, A. B., & Dotti, C. G. (1999) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1999.00754.x · Cited by 102

Functional Characterization of Novel Circular RNA Molecule, circzip-2 and Its Synthesizing Gene zip-2 in C. elegans Model of Parkinson’s Disease

Kumar, L., Shamsuzzama, S., Jadiya, P., Haque, R., Shukla, S., & Nazir, A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0903-5 · Cited by 101

Silencing Alpha Synuclein in Mature Nigral Neurons Results in Rapid Neuroinflammation and Subsequent Toxicity

Benskey, M. J., Sellnow, R. C., Sandoval, I. M., Sortwell, C. E., Lipton, J. W., & Manfredsson, F. P. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00036 · Cited by 102

C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH

van der Wateren, I. M., Knowles, T. P. J., Buell, A. K., Dobson, C. M., & Galvagnion, C. (2018) · Chemical Science · doi:10.1039/c8sc01109e · Cited by 98

Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson’s disease patients

Araki, K., Yagi, N., Ikemoto, Y., Yagi, H., Choong, C., Hayakawa, H., Beck, G., Sumi, H., Fujimura, H., Moriwaki, T., et al. (2015) · Scientific Reports · doi:10.1038/srep17625 · Cited by 101

Beyond the synucleinopathies: alpha synuclein as a driving force in neurodegenerative comorbidities

Visanji, N. P., Lang, A. E., & Kovács, G. G. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0172-x · Cited by 102

Axonopathy in an α-Synuclein Transgenic Model of Lewy Body Disease Is Associated with Extensive Accumulation of C-Terminal–Truncated α-Synuclein

Games, D., Seubert, P. A., Rockenstein, E. M., Patrick, C., Trejo, M., Ubhi, K. K., Ettle, B., Ghassemiam, M., Barbour, R., Schenk, D., et al. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.11.018 · Cited by 97

Parkinson's Disease-associated α-Synuclein Is a Calmodulin Substrate

Martinez, J., Moeller, I., Erdjument‐Bromage, H., Tempst, P., & Lauring, B. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209020200 · Cited by 100

Neurodegenerative diseases linked to misfolded proteins and their therapeutic approaches: A review

Khanam, H., Ali, A., Asif, M., & Shamsuzzaman (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.08.006 · Cited by 103

Structural Determinants of PLD2 Inhibition by α-Synuclein

Payton, J. E., Perrin, R. J., Woods, W. S., & George, J. M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.014 · Cited by 99

Distinct Region-Specific α-Synuclein Oligomers in A53T Transgenic Mice: Implications for Neurodegeneration

Tsika, E., Moysidou, M., Guo, J., Cushman-Nick, M., Gannon, P. J., Sandaltzopoulos, R., Giasson, B. I., Krainc, D., Ischiropoulos, H., & Mazzulli, J. R. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4977-09.2010 · Cited by 98

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

Proteinase K-resistant α-synuclein is deposited in presynapses in human Lewy body disease and A53T α-synuclein transgenic mice

Tanji, K., Mori, F., Mimura, J., Itoh, K., Kakita, A., Takahashi, H., & Wakabayashi, K. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0676-z · Cited by 102

Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau

Gracia, P., Polanco, D., Tarancón-Díez, J., Serra, I., Bracci, M. A., Oroz, J., Laurents, D. V., García‐Rubio, I., & Cremades, N. (2022) · Nature Communications · doi:10.1038/s41467-022-32350-9 · Cited by 95

Detecting Morphologically Distinct Oligomeric Forms of α-Synuclein

Emadi, S., Kasturirangan, S., Wang, M. S., Schulz, P., & Sierks, M. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806559200 · Cited by 100

Aggregation of αSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons

Taschenberger, G., Garrido, M., Tereshchenko, Y., Bähr, M., Zweckstetter, M., & Kügler, S. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0926-8 · Cited by 100

Animal models of cerebral β-amyloid angiopathy

Walker, L. C. (1997) · Brain Research Reviews · doi:10.1016/s0165-0173(97)00017-9 · Cited by 100

α-Synuclein Inclusions in Amygdala in the Brains of Patients with the Parkinsonism-Dementia Complex of Guam

Yamazaki, M., Arai, Y., Baba, M., Iwatsubo, T., Mori, O., Katayama, Y., & Oyanagi, K. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.7.585 · Cited by 98

The Cellular Environment Affects Monomeric α-Synuclein Structure

Stephens, A. D., Zacharopoulou, M., & Schierle, G. S. K. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.11.005 · Cited by 91

Expression Patterns of α-Synuclein in Human Hematopoietic Cells and in Drosophila at Different Developmental Stages

Shin, E., Cho, S. E., Lee, D.-K., Hur, M., Paik, S. R., Park, J. H., & Kim, J. (2000) · Molecules and Cells · doi:10.1007/s10059-000-0065-x · Cited by 97

The beneficial effect of a prolyl oligopeptidase inhibitor, KYP-2047, on alpha-synuclein clearance and autophagy in A30P transgenic mouse

Savolainen, M. H., Richie, C. T., Harvey, B. K., Männistö, P. T., Maguire‐Zeiss, K. A., & Myöhänen, T. T. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.04.003 · Cited by 96

Computational Studies Applied to Flavonoids against Alzheimer’s and Parkinson’s Diseases

Monteiro, A., Viana, J. D. O., Nayarisseri, A., Ernestine, N., Mendonça, F. J. B., Scotti, M. T., & Scotti, L. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7912765 · Cited by 101

Metal ions shape α-synuclein

Moons, R., Konijnenberg, A., Mensch, C., Elzen, R. V., Johannessen, C., Maudsley, S. R., Lambeir, A., & Sobott, F. (2020) · Scientific Reports · doi:10.1038/s41598-020-73207-9 · Cited by 96

Synoretin—A New Protein Belonging to the Synuclein Family

Surguchov, A. P., Surgucheva, I. G., Solessio, E. C., & Baehr, W. (1999) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0735 · Cited by 96

[11C]MODAG-001—towards a PET tracer targeting α-synuclein aggregates

Kuebler, L., Buss, S., Leonov, A., Ryazanov, S., Schmidt, F., Maurer, A., Weckbecker, D., Landau, A. M., Lillethorup, T. P., Bleher, D., et al. (2020) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-020-05133-x · Cited by 95

Number and Brightness analysis of alpha-synuclein oligomerization and the associated mitochondrial morphology alterations in live cells

Plotegher, N., Gratton, E., & Bubacco, L. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.02.013 · Cited by 95

Dopamine and the Dopamine Oxidation Product 5,6-Dihydroxylindole Promote Distinct On-Pathway and Off-Pathway Aggregation of α-Synuclein in a pH-Dependent Manner

Pham, C. L. L., Leong, S. L., Ali, F. E. A., Kenche, V. B., Hill, A. F., Gras, S. L., Barnham, K. J., & Cappai, R. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.02.007 · Cited by 99

Functional and Pathological Effects of α-Synuclein on Synaptic SNARE Complexes

Gao, V., Briano, J. A., Komer, L. E., & Burré, J. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167714 · Cited by 104

Synaptic vesicle trafficking and Parkinson's disease

Esposito, G., Clara, F. A., & Verstreken, P. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20916 · Cited by 101

Role of Individual Methionines in the Fibrillation of Methionine-Oxidized α-Synuclein

Hokenson, M. J., Uversky, V. N., Goers, J. W. F., Yamin, G., Munishkina, L. A., & Fink, A. L. (2004) · Biochemistry · doi:10.1021/bi049979h · Cited by 97

Inhibition of Vesicular Monoamine Transporter-2 Activity in α-Synuclein Stably Transfected SH-SY5Y Cells

Guo, J. T., Chen, A. Q., Kong, Q., Zhu, H., Ma, C. M., & Qin, C. (2007) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-007-9227-0 · Cited by 93

α-synuclein fibrils constitute the central core of oligodendroglial inclusion filaments in multiple system atrophy

Gai, W. P., Pountney, D. L., Power, J. H. T., Li, Q. X., Culvenor, J. G., McLean, C., Jensen, P. H., & Blumbergs, P. C. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00004-9 · Cited by 96

Increased α-synuclein aggregation following limited cleavage by certain matrix metalloproteinases

Levin, J., Giese, A., Boetzel, K., Israel, L., Högen, T., Nübling, G., Kretzschmar, H. A., & Lorenzl, S. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.10.010 · Cited by 92

Physiological and Pathological Role of Alpha-synuclein in Parkinson’s Disease Through Iron Mediated Oxidative Stress; The Role of a Putative Iron-responsive Element

Olivares, D., Huang, X., Branden, L., Greig, N. H., & Rogers, J. T. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10031226 · Cited by 93

Interaction of α-synuclein with biomembranes in Parkinson's disease —role of cardiolipin

Ghio, S., Kamp, F., Cauchi, R. J., Giese, A., & Vassallo, N. (2015) · Progress in Lipid Research · doi:10.1016/j.plipres.2015.10.005 · Cited by 95

Synucleins in ocular tissues

Surguchov, A. P., McMahan, B., Masliah, E., & Surgucheva, I. G. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1129 · Cited by 92

Disruptive membrane interactions of alpha-synuclein aggregates

Iyer, A., & Claessens, M. M. A. E. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.10.006 · Cited by 93

Pathophysiological Features of Nigral Dopaminergic Neurons in Animal Models of Parkinson’s Disease

Guatteo, E., Berretta, N., Monda, V., Ledonne, A., & Mercuri, N. B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094508 · Cited by 91

Genetic and environmental risk factors in Parkinson’s disease

Veldman, B. A. J., Wijn, A. M., Knoers, N. V. A. M., Praamstra, P., & Horstink, M. W. I. M. (1998) · Clinical Neurology and Neurosurgery · doi:10.1016/s0303-8467(98)00009-2 · Cited by 91

Review: Formation and Properties of Amyloid-like Fibrils Derived from α-Synuclein and Related Proteins

El‐Agnaf, O. M. A., & Irvine, G. B. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4262 · Cited by 91

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

Accumulation of phosphorylated α‐synuclein in dopaminergic neurons of transgenic mice that express human α‐synuclein

Wakamatsu, M., Ishii, A., Ukai, Y., Sakagami, J., Iwata, S., Ono, M., Matsumoto, K., Nakamura, A., Tada, N., Kobayashi, K., et al. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21310 · Cited by 90

Identification and characterization of a new alpha-synuclein isoform and its role in Lewy body diseases

Beyer, K., Domingo-Sàbat, M., Lao, J. I., Carrato, C., Ferrer, I., & Ariza, A. (2007) · Neurogenetics · doi:10.1007/s10048-007-0106-0 · Cited by 89

α-Synuclein accumulates in Lewy bodies in Parkinson's disease and dementia with Lewy bodies but not in Alzheimer's disease β-amyloid plaque cores

Bayer, T. A., Jäkälä, P., Hartmann, T., Havas, L., McLean, C., Culvenor, J. G., Li, Q.-X., Masters, C. L., Falkai, P., & Beyreuther, K. T. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00311-0 · Cited by 89

Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders

Carra, S., Rusmini, P., Crippa, V., Giorgetti, E., Boncoraglio, A., Cristofani, R., Naujock, M., Meister, M., Minoia, M., Kampinga, H. H., et al. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0409 · Cited by 90

Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease.

Masliah, E., Iwai, A., Mallory, M. E., Uéda, K., & Saitoh, T. (1996) · Europe PMC (PubMed Central) · Cited by 168

Characterization of the Precursor Protein of the Non-Aβ Component of Senile Plaques (NACP) in the Human Central Nervous System

Irizarry, M. C., Kim, T., McNamara, M. J., Tanzi, R. E., George, J. M., Clayton, D. F., & Hyman, B. T. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199608000-00004 · Cited by 205

The Non-Amyloid-β Component of Alzheimer’s Disease Plaque Amyloid: Comparative Analysis Suggests a Normal Function as a Synaptic Plasticizer

George, J. M., & Clayton, D. F. (1996) · Springer eBooks · doi:10.1007/978-1-4899-0209-2_16 · Cited by 3

Properties of NACP/α-synuclein and its role in Alzheimer’s disease

Iwai, A. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00036-3 · Cited by 78

The synaptic protein NACP is abnormally expressed during the progression of Alzheimer' s disease

Iwai, A., Masliah, E., Sundsmo, M. P., DeTeresa, R. M., Mallory, M. E., Salmon, D. P., & Saitoh, T. (1996) · Brain Research · doi:10.1016/0006-8993(96)00014-5 · Cited by 51