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

Oxidation and nitration of α-synuclein and their implications in neurodegenerative diseases

Chavarría, C., & Souza, J. M. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.02.009 · Cited by 90

Alpha synuclein gene expression profile in the retina of vertebrates.

Martı́nez, G., Martín‐Nieto, J., Esteve-Rudd, J., Angulo, A., & Cuenca, N. (2007) · Europe PMC (PubMed Central) · Cited by 88

Oligomerization and fibril assembly of the amyloid-β protein

Roher, A. E., Baudry, J. Y., Chaney, M. O., Kuo, Y., Stine, W. B., & Emmerling, M. R. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00030-2 · Cited by 89

Limelight on Alpha-Synuclein: Pathological and Mechanistic Implications in Neurodegeneration

Wales, P., Pinho, R., Lázaro, D. F., & Outeiro, T. F. (2013) · Journal of Parkinson s Disease · doi:10.3233/jpd-130216 · Cited by 89

Alpha-synuclein dysfunction in Lewy body diseases

Tofaris, G. K., & Spillantini, M. G. (2005) · Movement Disorders · doi:10.1002/mds.20538 · Cited by 87

An antiaggregation gene therapy strategy for Lewy body disease utilizing β-synuclein lentivirus in a transgenic model

Hashimoto, M., Rockenstein, E. M., Mante, M., Crews, L. A., Bar‐On, P., Gage, F. H., Marr, R. A., & Masliah, E. (2004) · Gene Therapy · doi:10.1038/sj.gt.3302349 · Cited by 86

Sensitization of Neuronal Cells to Oxidative Stress with Mutated Human α‐Synuclein

Ko, L., Mehta, N. D., Farrer, M. J., Easson, C., Hussey, J., Yen, S. H., Hardy, J., & Yen, S.-H. C. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752546.x · Cited by 86

Rapid dissemination of alpha-synuclein seeds through neural circuits in an in-vivo prion-like seeding experiment

Okuzumi, A., Kurosawa, M., Hatano, T., Takanashi, M., Shuuko, N., Fukuhara, T., Yamanaka, T., Miyazaki, H., Yoshinaga, S., Furukawa, Y., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0587-0 · Cited by 91

Evidence of distinct α-synuclein strains underlying disease heterogeneity

Holec, S. A. M., & Woerman, A. L. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02163-5 · Cited by 91

A critical role for alpha-synuclein in development and function of T lymphocytes

Shameli, A., Xiao, W., Zheng, Y., Shyu, S., Sumodi, J., Meyerson, H. J., Harding, C. V., & Maitta, R. W. (2015) · Immunobiology · doi:10.1016/j.imbio.2015.10.002 · Cited by 86

Characterization of α-Synuclein Interactions with Selected Aggregation-Inhibiting Small Molecules

Rao, J. N., Dua, V., & Ulmer, T. S. (2008) · Biochemistry · doi:10.1021/bi8002378 · Cited by 85

Acyl-CoA Synthetase Activity Links Wild-Type but Not Mutant α-Synuclein to Brain Arachidonate Metabolism

Golovko, M. Y., Rosenberger, T. A., Færgeman, N. J., Feddersen, S., Cole, N. B., Pribill, I., Berger, J., Nussbaum, R. L., & Murphy, E. J. (2006) · Biochemistry · doi:10.1021/bi0600289 · Cited by 85

Dynamic structural flexibility of α-synuclein

Mor, D. E., Ugras, S. E., Daniels, M. J., & Ischiropoulos, H. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.12.018 · Cited by 85

Tau and Synuclein and Their Role in Neuropathology

Dickson, D. W. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00548.x · Cited by 83

α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner

Yin, G., da Fonseca, T. L., Eisbach, S. E., Anduaga, A. M., Breda, C., Orcellet, M. L., Szegő, É. M., Guerreiro, P. S., Lázaro, D. F., Braus, G. H., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.06.018 · Cited by 85

Immunohistochemical comparison of α- and β-synuclein in adult rat central nervous system

Mori, F., Tanji, K., Yoshimoto, M., Takahashi, H., & Wakabayashi, K. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02643-4 · Cited by 84

Site-Specific Interaction between α-Synuclein and Membranes Probed by NMR-Observed Methionine Oxidation Rates

Maltsev, A. S., Chen, J., Levine, R. L., & Bax, A. (2013) · Journal of the American Chemical Society · doi:10.1021/ja312415q · Cited by 84

Role of Synucleins in Alzheimer’s Disease

Crews, L. A., Tsigelny, I. F., Hashimoto, M., & Masliah, E. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9073-6 · Cited by 85

C-terminal α-synuclein immunoreactivity in structures other than Lewy bodies in neurodegenerative disorders

Takeda, A., Hashimoto, M., Mallory, M., Sundsumo, M., Hansen, L., & Masliah, E. (2000) · Acta Neuropathologica · doi:10.1007/pl00007441 · Cited by 83

The Convergence of Alpha-Synuclein, Mitochondrial, and Lysosomal Pathways in Vulnerability of Midbrain Dopaminergic Neurons in Parkinson’s Disease

Minakaki, G., Krainc, D., & Burbulla, L. F. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.580634 · Cited by 87

Subcellular localisation of recombinant α- and γ-synuclein

Specht, C. G., Tigaret, C. M., Rast, G. F., Thalhammer, A., Rudhard, Y., & Schoepfer, R. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2004.09.017 · Cited by 83

Fibrillogenic and Non-fibrillogenic Ensembles of SDS-bound Human α-Synuclein

Ahmad, M. F., Ramakrishna, T., Raman, B., & Rao, C. M. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.09.085 · Cited by 83

In vitro aggregation assays for the characterization of α-synuclein prion-like properties

Narkiewicz, J., Giachin, G., & Legname, G. (2014) · Prion · doi:10.4161/pri.28125 · Cited by 86

Pathogenic effects of α-synuclein aggregation

Lundvig, D. M. S., Lindersson, E., & Jensen, P. H. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.09.001 · Cited by 83

α‐Synuclein up‐regulates expression of caveolin‐1 and down‐regulates extracellular signal‐regulated kinase activity in B103 neuroblastoma cells: role in the pathogenesis of Parkinson's disease

Hashimoto, M., Takenouchi, T., Rockenstein, E. M., & Masliah, E. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01791.x · Cited by 83

Stimulatory effect of α‐synuclein on the tau‐phosphorylation by GSK‐3 β

Kawakami, F., Suzuki, M., Shimada, N., Kagiya, G., Ohta, E., Tamura, K., Maruyama, H., & Ichikawa, T. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08389.x · Cited by 82

α-Synuclein and Parkinsonism: Updates and Future Perspectives

Rosborough, K., Patel, N., & Kalia, L. V. (2017) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-017-0737-y · Cited by 83

Novel DNA Aptamers for Parkinson’s Disease Treatment Inhibit α-Synuclein Aggregation and Facilitate its Degradation

Yuan, Z., Qu, J. T., Xue, F., Zheng, Y., Yang, B., Chang, Y., Yang, H., & Zhang, J. (2018) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2018.02.011 · Cited by 82

Interactions between Calcium and Alpha-Synuclein in Neurodegeneration

Rcom-H'cheo-Gauthier, A. N., Goodwin, J., & Pountney, D. L. (2014) · Biomolecules · doi:10.3390/biom4030795 · Cited by 85

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

Influence of mutation type and X chromosome inactivation on Rett syndrome phenotypes

Amir, R. E., den Veyver, I. B. V., Schultz, R., Malicki, D. M., Tran, C. Q., Dahle, E. J., Philippi, A., Tímár, L., Percy, A. K., Motil, K. J., et al. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200005)47:5 · Cited by 351

α-Synuclein Stimulates a Dopamine Transporter-dependent Chloride Current and Modulates the Activity of the Transporter*

Swant, J., Goodwin, J., North, A., Ali, A. A., Gamble-George, J., Chirwa, S., & Khoshbouei, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.241232 · Cited by 85

The phosphorylation of α‐synuclein: development and implication for the mechanism and therapy of the Parkinson's disease

Xu, Y., Deng, Y., & Qing, H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13234 · Cited by 87

Expression of ??-synuclein in a human glioma cell line and its up-regulation by interleukin-1??

Tanji, K., Imaizumi, T., Yoshida, H., Mori, F., Yoshimoto, M., Satoh, K., & Wakabayashi, K. (2001) · Neuroreport · doi:10.1097/00001756-200107030-00028 · Cited by 81

α-Synuclein immunoreactivity in neuronal nuclear inclusions and neurites in multiple system atrophy

Lin, W.-L., DeLucia, M. W., & Dickson, D. W. (2003) · Neuroscience Letters · doi:10.1016/j.neulet.2003.09.075 · Cited by 80

Intrinsically disordered proteins in synaptic vesicle trafficking and release

Snead, D., & Eliezer, D. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.006493 · Cited by 79

Release and aggregation of cytochrome c and α-synuclein are inhibited by the antiparkinsonian drugs, talipexole and pramipexole

Kakimura, J., Kitamura, Y., Takata, K., Kohno, Y., Nomura, Y., & Taniguchi, T. (2001) · European Journal of Pharmacology · doi:10.1016/s0014-2999(01)00902-5 · Cited by 81

Alpha-Synuclein and Mitochondrial Dysfunction in Parkinson’s Disease: The Emerging Role of VDAC

Risiglione, P., Zinghirino, F., Rosa, M. C. D., Magrì, A., & Messina, A. A. (2021) · Biomolecules · doi:10.3390/biom11050718 · Cited by 84

Tyrosine-to-Cysteine Modification of Human α-Synuclein Enhances Protein Aggregation and Cellular Toxicity

Zhou, W., & Freed, C. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307563200 · Cited by 80

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

Role of C ‐terminal negative charges and tyrosine residues in fibril formation of α‐synuclein

Izawa, Y., Tateno, H., Kameda, H., HIRAKAWA, K., Hato, K., Yagi, H., Hongo, K., Mizobata, T., & Kawata, Y. (2012) · Brain and Behavior · doi:10.1002/brb3.86 · Cited by 80

β-Synuclein Displays an Antiapoptotic p53-dependent Phenotype and Protects Neurons from 6-Hydroxydopamine-induced Caspase 3 Activation

da Costa, C. A., Masliah, E., & Checler, F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306083200 · Cited by 81

Noninvasive delivery of an α‐synuclein gene silencing vector with magnetic resonance–guided focused ultrasound

Xhima, K., Nabbouh, F., Hynynen, K., Aubert, I., & Tandon, A. (2018) · Movement Disorders · doi:10.1002/mds.101 · Cited by 86

The N‐terminal region of non‐Aβ component of Alzheimer's Disease amyloid is responsible for its tendency to assume β‐sheet and aggregate to form fibrils

El‐Agnaf, O. M. A., Bodles, A. M., Guthrie, D. J. S., Harriott, P., & Irvine, G. B. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2580157.x · Cited by 80

Amyloid-Beta Peptides Trigger Aggregation of Alpha-Synuclein In Vitro

Köppen, J., Schulze, A., Machner, L., Wermann, M., Eichentopf, R., Guthardt, M., Hähnel, A., Klehm, J., Kriegeskorte, M.-C., Hartlage‐Rübsamen, M., et al. (2020) · Molecules · doi:10.3390/molecules25030580 · Cited by 79

Acetogenins from Annonaceae family. Their potential biological applications

Neske, A., Hidalgo, J. R., Cabedo, N., & Cortés, D. (2020) · Phytochemistry · doi:10.1016/j.phytochem.2020.112332 · Cited by 82

Cycles of Aberrant Synaptic Sprouting and Neurodegeneration in Alzheimer's and Dementia with Lewy Bodies

Hashimoto, M., & Masliah, E. (2003) · Neurochemical Research · doi:10.1023/a:1026073324672 · Cited by 78

Alpha-Synuclein as a Prominent Actor in the Inflammatory Synaptopathy of Parkinson’s Disease

Cardinale, A., Calabrese, V., de Iure, A., & Picconi, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126517 · Cited by 79

Nanoparticles in Combating Neuronal Dysregulated Signaling Pathways: Recent Approaches to the Nanoformulations of Phytochemicals and Synthetic Drugs Against Neurodegenerative Diseases

Fakhri, S., Abdian, S., Zarneshan, S. N., Moradi, S. Z., Farzaei, M. H., & Abdollahi, M. (2022) · International Journal of Nanomedicine · doi:10.2147/ijn.s347187 · Cited by 83

α‐Synuclein gene ablation increases docosahexaenoic acid incorporation and turnover in brain phospholipids

Golovko, M. Y., Rosenberger, T. A., Feddersen, S., Færgeman, N. J., & Murphy, E. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04357.x · Cited by 78

The role of α-synuclein in brain lipid metabolism: a downstream impact on brain inflammatory response

Golovko, M. Y., Barceló‐Coblijn, G., Castagnet, P. I., Austin, S. A., Combs, C. K., & Murphy, E. J. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-0008-y · Cited by 81

Release and uptake of pathologic alpha-synuclein

Grozdanov, V., & Danzer, K. M. (2018) · Cell and Tissue Research · doi:10.1007/s00441-017-2775-9 · Cited by 75

Co-localization of α-synuclein and phosphorylated tau in neuronal and glial cytoplasmic inclusions in a patient with multiple system atrophy of long duration

Piao, Y.-S., Hayashi, S., Hasegawa, M., Wakabayashi, K., Yamada, M., Yoshimoto, M., Ishikawa, A., Iwatsubo, T., & Takahashi, H. (2001) · Acta Neuropathologica · doi:10.1007/s004010000292 · Cited by 78

Dopamine agonists and neuroprotection in Parkinson's disease

Schapira, A. H. V. (2002) · European Journal of Neurology · doi:10.1046/j.1468-1331.9.s3.9.x · Cited by 77

Evidence of Native α-Synuclein Conformers in the Human Brain

Gould, N. S., Mor, D. E., Lightfoot, R. T., Malkus, K. A., Giasson, B. I., & Ischiropoulos, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.538249 · Cited by 80

Site-Specific Copper-Catalyzed Oxidation of α-Synuclein: Tightening the Link between Metal Binding and Protein Oxidative Damage in Parkinson’s Disease

Miotto, M., Rodríguez, E. E., Valiente‐Gabioud, A. A., Monserrat, V. T., Binolfi, A., Quintanar, L., Zweckstetter, M., Griesinger, C., & Fernández, C. O. (2014) · Inorganic Chemistry · doi:10.1021/ic4031377 · Cited by 77

α-Synuclein and Dopamine Metabolism

Yu, S., Uéda, K., & Chan, P. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:243 · Cited by 77

Reduced Neuritic Outgrowth and Cell Adhesion in Neuronal Cells Transfected with Human α-Synuclein

Takenouchi, T., Hashimoto, M., Hsu, L. J., Mackowski, B., Rockenstein, E. M., Mallory, M. E., & Masliah, E. (2001) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2000.0923 · Cited by 77

The link between the SNCA gene and parkinsonism

Xu, W., Tan, L., & Yu, J. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.10.042 · Cited by 84

Broken Helix in Vesicle and Micelle-Bound α-Synuclein: Insights from Site-Directed Spin Labeling-EPR Experiments and MD Simulations

Bortolus, M., Tombolato, F., Tessari, I., Bisaglia, M., Mammi, S., Bubacco, L., Ferrarini, A., & Maniero, A. L. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8010429 · Cited by 76

Cell cycle aberrations by α-synuclein over-expression and cyclin B immunoreactivity in Lewy bodies

Lee, S. S., Kim, Y. M., Junn, E., Lee, G., Park, K. H., Tanaka, M., Ronchetti, R., Quezado, M., & Mouradian, M. M. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00196-3 · Cited by 75

Mechanisms of alpha-synuclein toxicity: An update and outlook

Brás, I. C., Xylaki, M., & Outeiro, T. F. (2019) · Progress in brain research · doi:10.1016/bs.pbr.2019.10.005 · Cited by 78

Flexible Nets of Malleable Guardians: Intrinsically Disordered Chaperones in Neurodegenerative Diseases

Uversky, V. N. (2010) · Chemical Reviews · doi:10.1021/cr100186d · Cited by 75

Intracellular Dynamics of Synucleins

Surguchov, A. P. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.07.007 · Cited by 77

GABA transmission via ATP-dependent K + channels regulates α-synuclein secretion in mouse striatum

Emmanouilidou, E., Minakaki, G., Keramioti, M. V., Xylaki, M., Balafas, E., Chrysanthou‐Piterou, M., Kloukina, I., & Vekrellis, K. (2016) · Brain · doi:10.1093/brain/awv403 · Cited by 77

Differential expression of α‐synuclein isoforms in dementia with Lewy bodies

Beyer, K., Lao, J. I., Carrato, C., Mate, J. L., López, D., Ferrer, I., & Ariza, A. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00572.x · Cited by 75

Effects of the cholesterol‐lowering compound methyl‐β‐cyclodextrin in models of α‐synucleinopathy

Bar‐On, P., Rockenstein, E. M., Adame, A., Ho, G. J., Hashimoto, M., & Masliah, E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04017.x · Cited by 78

A simple, versatile and robust centrifugation‐based filtration protocol for the isolation and quantification of α‐synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in α‐synuclein research

Kumar, S. T., Donzelli, S., Chiki, A., Syed, M. M. K., & Lashuel, H. A. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14955 · Cited by 69

Interactome of the Amyloid Precursor Protein APP in Brain Reveals a Protein Network Involved in Synaptic Vesicle Turnover and a Close Association with Synaptotagmin-1

Kohli, B. M., Pflieger, D., Mueller, L. N., Carbonetti, G., Aebersold, R. H., Nitsch, R. M., & Konietzko, U. (2012) · Journal of Proteome Research · doi:10.1021/pr300123g · Cited by 77

Elevated Oxidative Stress in the Brain of Senescence-accelerated Mice at 5 Months of Age

Álvarez-García, Ó., Vega‐Naredo, I., Sierra, V., Caballero, B., Tomás‐Zapico, C., Camins, A., García, J. J., Pallàs, M., & Coto‐Montes, A. M. (2006) · Biogerontology · doi:10.1007/s10522-005-6041-2 · Cited by 78

Glial cytoplasmic inclusions and tissue injury in multiple system atrophy: A quantitative study in white matter (olivopontocerebellar system) and gray matter (nigrostriatal system)

Ishizawa, K., Komori, T., Arai, N., Mizutani, T., & Hirose, T. (2008) · Neuropathology · doi:10.1111/j.1440-1789.2007.00855.x · Cited by 74

Purification of α-Synuclein from Human Brain Reveals an Instability of Endogenous Multimers as the Protein Approaches Purity

Luth, E. S., Bartels, T., Dettmer, U., Kim, N. C., & Selkoe, D. J. (2014) · Biochemistry · doi:10.1021/bi501188a · Cited by 77

Interaction Between α-Synuclein and Metal Ions, Still Looking for a Role in the Pathogenesis of Parkinson’s Disease

Bisaglia, M., Tessari, I., Mammi, S., & Bubacco, L. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8082-1 · Cited by 74

Interplay between α-synuclein amyloid formation and membrane structure

O’Leary, E. I., & Lee, J. C. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.09.012 · Cited by 71

Aggregation of α-Synuclein in S. cerevisiae is Associated with Defects in Endosomal Trafficking and Phospholipid Biosynthesis

Soper, J. H., Kehm, V. M., Burd, C. G., Bankaitis, V. A., & Lee, V. M. ‐. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9455-5 · Cited by 77

Intercellular transfer of pathogenic α-synuclein by extracellular vesicles is induced by the lipid peroxidation product 4-hydroxynonenal

Zhang, S., Eitan, E., Wu, T.-Y., & Mattson, M. P. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.09.016 · Cited by 76

Beyond the Signal Sequence: Protein Routing in Health and Disease

Castro-Fernández, C., Maya‐Núñez, G., & Conn, P. M. (2004) · Endocrine Reviews · doi:10.1210/er.2004-0010 · Cited by 73

Unique insights to intrinsically disordered proteins provided by ion mobility mass spectrometry

Stuchfield, D., & Barran, P. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.01.007 · Cited by 72

Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein

Hannestad, J. K., Rocha, S., Agnarsson, B., Zhdanov, V. P., Wittung-Stafshede, P. E., & Höök, F. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914670117 · Cited by 72

Alpha‐synuclein overexpression in mice alters synaptic communication in the corticostriatal pathway

Wu, N., Joshi, P. R., Cepeda, C., Masliah, E., & Levine, M. S. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22327 · Cited by 74

Thermodynamics imprinting reveals differential binding of metals to α-synuclein: Relevance to parkinson’s disease

..., B., & Rao, K. S. J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.05.060 · Cited by 72

Expression of α-synuclein, the precursor of non-amyloid β component of Alzheimer's disease amyloid, in human cerebral blood vessels

Tamo, W., Imaizumi, T., Tanji, K., Yoshida, H., Mori, F., Yoshimoto, M., Takahashi, H., Fukuda, I., Wakabayashi, K., & Satoh, K. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00297-5 · Cited by 73

Genetic perspective on the synergistic connection between vesicular transport, lysosomal and mitochondrial pathways associated with Parkinson’s disease pathogenesis

Smolders, S., & Broeckhoven, C. V. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00935-4 · Cited by 72

DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synuclein

Meulener, M. C., Graves, C. L., Sampathu, D. M., Armstrong‐Gold, C. E., Bonini, N. M., & Giasson, B. I. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03145.x · Cited by 71

α-Synuclein aggregation and neurodegenerative diseases

Ma, Q., Chan, P., Yoshii, M., & Uéda, K. (2003) · Journal of Alzheimer s Disease · doi:10.3233/jad-2003-5208 · Cited by 72

Regional deficiencies in chaperone-mediated autophagy underlie α-synuclein aggregation and neurodegeneration

Malkus, K. A., & Ischiropoulos, H. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.03.017 · Cited by 71

The Parkinson disease‐associated A30P mutation stabilizes α‐synuclein against proteasomal degradation triggered by heme oxygenase‐1 over‐expression in human neuroblastoma cells

Song, W., Patel, A., Qureshi, H. Y., Han, D., Schipper, H. M., & Paudel, H. K. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06165.x · Cited by 72

A new role for α‐synuclein in Parkinson's disease: Alteration of ER–mitochondrial communication

Guardia‐Laguarta, C., Área-Gómez, E., Schon, E. A., & Przedborski, S. (2015) · Movement Disorders · doi:10.1002/mds.26239 · Cited by 70

Biophysical characterization of α-synuclein and its controversial structure

Alderson, T. R., & Markley, J. L. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.26255 · Cited by 75

Parkinson Disease Mutant E46K Enhances α-Synuclein Phosphorylation in Mammalian Cell Lines, in Yeast, and in Vivo

Mbefo, M. K., Fares, M.-B., Paleologou, K. E., Oueslati, A., Yin, G., Tenreiro, S., Pinto, M. M. M., Outeiro, T. F., Zweckstetter, M., Masliah, E., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.610774 · Cited by 69

α-Synuclein, Parkinson's disease, and Alzheimer's disease

Kim, S., Seo, J., & Suh, Y. (2004) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2003.11.005 · Cited by 70

Structure and topology of the non‐amyloid‐β component fragment of human α‐synuclein bound to micelles: Implications for the aggregation process

Bisaglia, M., Trolio, A., Bellanda, M., Bergantino, E., Bubacco, L., & Mammi, S. (2006) · Protein Science · doi:10.1110/ps.052048706 · Cited by 68

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Kiechle, M., Grozdanov, V., & Danzer, K. M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.562241 · Cited by 71

Involvement of molecular chaperone in protein-misfolding brain diseases

Wankhede, N. L., Kale, M. B., Upaganlawar, A. B., Taksande, B. G., Umekar, M. J., Behl, T., Abdellatif, A. A. H., Bhaskaran, P. M., Dachani, S. R., Sehgal, A., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112647 · Cited by 73

19F NMR studies of α‐synuclein‐membrane interactions

Wang, G., Li, C., & Pielak, G. J. (2010) · Protein Science · doi:10.1002/pro.449 · Cited by 69

Subcellular localization of α-synuclein in primary neuronal cultures: effect of missense mutations

McLean, P. J., Ribich, S. A., & Hyman, B. T. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6284-2_5 · Cited by 68

Caenorhabditis elegans: a model to investigate oxidative stress and metal dyshomeostasis in Parkinson's disease

Chege, P. M., & McColl, G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00089 · Cited by 68

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

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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