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The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
Open accessAbstract
Non-A beta component of Alzheimer's disease amyloid (NAC) is the second component in the amyloid from brain tissue of patients affected with Alzheimer's disease. Its precursor protein (NACP) was shown to be a brain-specific protein. In rat brain, NACP was more abundant in the neocortex, hippocampus, olfactory bulb, striatum, thalamus, and cerebellum and less abundant in the brain stem. Confocal laser microscopy analysis revealed that anti-NACP immunostaining was colocalized with synaptophysin-immunoreactive presynaptic terminals. Ultrastructural analysis showed that NACP immunoreactivity was associated with synaptic vesicles. NACP sequence showed 95% identity with that of rat synuclein 1, a synaptic/nuclear protein previously identified in rat brain, and good homology with Torpedo synuclein from the electric organ synapse and bovine phosphoneuroprotein 14 (PNP-14), a brain-specific protein present in synapses. Therefore, NACP is a synaptic protein, suggesting that synaptic aberration observed in senile plaques might be involved in amyloidogenesis in Alzheimer's disease.
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“αSyn is predominantly expressed within the presynaptic terminals of neurons [141–143]”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [141]
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Cites
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
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
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
Self-citationStrittmatter, 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
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
Kennelly, P. J., & Krebs, E. G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98436-x · Cited by 1,331
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Metal ions as modulators of protein conformation and misfolding in neurodegeneration
Leal, S. S., Botelho, H. M., & Gomes, C. M. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.04.004 · Cited by 187
α-synuclein implicated in Parkinson’s disease catalyses the formation of hydrogen peroxide in vitro
Turnbull, S., Tabner, B. J., El‐Agnaf, O. M. A., Moore, S., Davies, Y., & Allsop, D. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00513-5 · Cited by 183
Genes, proteins, and neurotoxins involved in Parkinson’s disease
Halbach, O. V. B. U., Schober, A., & KRIEGLSTEIN, K. G. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.05.002 · Cited by 180
Norris, E. H., Giasson, B. I., Ischiropoulos, H., & Lee, V. M. ‐. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212436200 · Cited by 182
Non-Aβ Component of Alzheimer's Disease Amyloid (NAC) Revisited
Culvenor, J. G., McLean, C., Cutt, S., Campbell, B. C. V., Maher, F., Jäkälä, P., Hartmann, T., Beyreuther, K. T., Masters, C. L., & Li, Q. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65220-0 · Cited by 180
Metal-Catalyzed Oxidation of α-Synuclein in the Presence of Copper(II) and Hydrogen Peroxide
Paik, S. R., Shin, H.-J., & Lee, J. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1822 · Cited by 181
Burré, J., Sharma, M., & Südhof, T. C. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3545-12.2012 · Cited by 188
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Devoto, V. M. P., & Falzone, T. L. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.026294 · Cited by 184
Certain Metals Trigger Fibrillation of Methionine-oxidized α-Synuclein
Yamin, G., Glaser, C. B., Uversky, V. N., & Fink, A. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303302200 · Cited by 181
Gómez‐Isla, T., Irizarry, M. C., Mariash, A., Cheung, B. S., Soto, O., Schrump, S. E., Sondel, J., Kotilinek, L., Day, J., Schwarzschild, M. A., et al. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00091-x · Cited by 181
Structural Characteristics of α-Synuclein Oligomers Stabilized by the Flavonoid Baicalein
Hong, D.-P., Fink, A. L., & Uversky, V. N. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.039 · Cited by 181
Malek, N., Swallow, D. M. A., Grosset, K. A., Anichtchik, O. V., Spillantini, M. G., & Grosset, D. G. (2014) · Acta Neurologica Scandinavica · doi:10.1111/ane.12247 · Cited by 183
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Ganjam, G. K., Bolte, K., Matschke, L. A., Neitemeier, S., Dolga, A. M., Höllerhage, M., Höglinger, G. U., Adamczyk, A., Decher, N., Oertel, W. H., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2091-2 · Cited by 187
Ca2+ Binding to α-Synuclein Regulates Ligand Binding and Oligomerization
Nielsen, M. S., Vorum, H., Lindersson, E., & Jensen, P. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101181200 · Cited by 185
α-synuclein aggregation and its modulation
Ghosh, D., Mehra, S., Sahay, S., Singh, P. K., & Maji, S. K. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.10.021 · Cited by 193
Arai, Y., Yamazaki, M., Mori, O., Muramatsu, H., Asano, G., & Katayama, Y. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03082-1 · Cited by 173
Microglial Activation Parallels System Degeneration in Multiple System Atrophy
Ishizawa, K., Komori, T., Sasaki, S., Arai, N., Mizutani, T., & Hirose, T. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.1.43 · Cited by 172
Silencing of human α-synuclein in vitro and in rat brain using lentiviral-mediated RNAi
Sapru, M. K., Yates, J. W., Hogan, S., Jiang, L., Halter, J., & Bohn, M. C. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2005.12.024 · Cited by 173
Mandel, S. A., Maor, G., & Youdim, M. B. H. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:24:3:401 · Cited by 171
Kovács, G. G., Wagner, U., Dumont, B., Pikkarainen, M., Osman, A. A., Streichenberger, N., Leisser, I., Verchère, J., Baron, T., Alafuzoff, I. I., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0964-x · Cited by 174
Synaptic failure and α‐synuclein
Calò, L., Węgrzynowicz, M., Santivañez‐Perez, J., & Spillantini, M. G. (2016) · Movement Disorders · doi:10.1002/mds.26479 · Cited by 179
Polyphosphate: A Conserved Modifier of Amyloidogenic Processes
Cremers, C. M., Knoefler, D., Gates, S. N., Martin, N. R., Dahl, J., Lempart, J., Xie, L., Chapman, M. R., Galván, V., Southworth, D. R., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.07.016 · Cited by 170
Salivary biomarkers for the diagnosis and monitoring of neurological diseases
Farah, R., Haraty, H., Salame, Z., Fares, Y., Ojcius, D. M., & Sadier, N. S. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.03.004 · Cited by 175
Ben Gedalya, T., Loeb, V., Israeli, E., Altschuler, Y., Selkoe, D. J., & Sharon, R. (2009) · Traffic · doi:10.1111/j.1600-0854.2008.00853.x · Cited by 169
Alzheimer's disease as a disorder of mechanisms underlying structural brain self-organization
Arendt, T. (2001) · Neuroscience · doi:10.1016/s0306-4522(00)00516-9 · Cited by 172
Alpha-synuclein research: defining strategic moves in the battle against Parkinson’s disease
Oliveira, L. M. A., Gasser, T., Edwards, R. H., Zweckstetter, M., Melki, R., Stefanis, L., Lashuel, H. A., Sulzer, D., Vekrellis, K., Halliday, G. M., et al. (2021) · npj Parkinson s Disease · doi:10.1038/s41531-021-00203-9 · Cited by 174
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
Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers
Yamin, G., Uversky, V. N., & Fink, A. L. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00367-3 · Cited by 171
Statins reduce neuronal α‐synuclein aggregation in in vitro models of Parkinson’s disease
Bar‐On, P., Crews, L. A., Koob, A. O., Mizuno, H., Adame, A., Spencer, B. J., & Masliah, E. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05254.x · Cited by 169
Self-citationMasliah, E., Iwai, A., Mallory, M. E., Uéda, K., & Saitoh, T. (1996) · Europe PMC (PubMed Central) · Cited by 168
Self-citationMeier, J. J., Kayed, R., Lin, C., Gurlo, T., Haataja, L., Jayasinghe, S. A., Langen, R., Glabe, C. G., & Butler, P. C. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00082.2006 · Cited by 166
Jin, H., Kanthasamy, A., Ghosh, A., Yang, Y., Anantharam, V., & Kanthasamy, A. G. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5634-10.2011 · Cited by 164
Lowe, R. D., Pountney, D. L., Jensen, P. H., Gai, W., & Voelcker, N. H. (2004) · Protein Science · doi:10.1110/ps.04879704 · Cited by 166
Altered expression of the synuclein family mRNA in Lewy body and Alzheimer’s disease
Rockenstein, E. M., Hansen, L. A., Mallory, M. E., Trojanowski, J. Q., Galasko, D. R., & Masliah, E. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02772-x · Cited by 162
Self-citationα-Synuclein and the Lewy body disorders
Dickson, D. W. (2001) · Current Opinion in Neurology · doi:10.1097/00019052-200108000-00001 · Cited by 163
Dynamics of α‐synuclein aggregation and inhibition of pore‐like oligomer development by β‐synuclein
Tsigelny, I. F., Bar‐On, P., Sharikov, Y., Crews, L. A., Hashimoto, M., Miller, M. A., Keller, S. H., Platoshyn, O., Yuan, J. X. ‐., & Masliah, E. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05733.x · Cited by 164
Self-citationDoes α‐synuclein modulate dopaminergic synaptic content and tone at the synapse?
Sidhu, A., Wersinger, C., & Vernier, P. (2004) · The FASEB Journal · doi:10.1096/fj.03-1112rev · Cited by 167
Glial dysfunction in the pathogenesis of α-synucleinopathies: emerging concepts
Fellner, L., Jellinger, K. A., Wenning, G. K., & Stefanova, N. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0833-z · Cited by 162
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 162
Self-citationIncreased Immune Activation by Pathologic α‐Synuclein in Parkinson's Disease
Grozdanov, V., Bousset, L., Hoffmeister, M., Bliederhaeuser, C., Meier, C., Madiona, K., Pieri, L., Kiechle, M., McLean, P. J., Kassubek, J., et al. (2019) · Annals of Neurology · doi:10.1002/ana.25557 · Cited by 161
α-Synuclein Is Phosphorylated by Members of the Src Family of Protein-tyrosine Kinases
Ellis, C. E., Schwartzberg, P. L., Grider, T. L., Fink, D. W., & Nussbaum, R. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010316200 · Cited by 163
Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson’s disease
Horváth, I., & Wittung-Stafshede, P. E. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610371113 · Cited by 165
Mikolaenko, I., Pletniková, O., Kawas, C. H., O’Brien, R., Resnick, S. M., Crain, B. J., & Troncoso, J. C. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.156 · Cited by 163
α-Synuclein–induced Aggregation of Cytoplasmic Vesicles inSaccharomyces cerevisiae
Soper, J. H., Roy, S., Stieber, A., Lee, E., Wilson, R. B., Trojanowski, J. Q., Burd, C. G., & Lee, V. M. ‐. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-08-0827 · Cited by 163
Li, J., Uversky, V. N., & Fink, A. L. (2002) · NeuroToxicology · doi:10.1016/s0161-813x(02)00066-9 · Cited by 155
Wakamatsu, M., Ishii, A., Iwata, S., Sakagami, J., Ukai, Y., Ono, M., Kambe, D., Muramatsu, S., Kobayashi, K., Iwatsubo, T., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.11.017 · Cited by 157
Self-citationUlmer, T. S., & Bax, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507624200 · Cited by 156
Zhang, Q.-S., Heng, Y., Yuan, Y.-H., & Chen, N.-H. (2017) · Toxicology Letters · doi:10.1016/j.toxlet.2016.11.002 · Cited by 156
Kuwahara, T., Koyama, A., Koyama, S., Yoshina, S., Ren, C.-H., Kato, T., Mitani, S., & Iwatsubo, T. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn198 · Cited by 158
Huang, M., Chiang, S., Kalinowski, D. S., Bae, D.-H., Sahni, S., & Richardson, D. R. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6392763 · Cited by 155
Genetics of Parkinson's disease
Nussbaum, R. L. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.10.1687 · Cited by 163
Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151
Emadi, S., Barkhordarian, H., Wang, M. S., Schulz, P., & Sierks, M. R. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.089 · Cited by 150
Schildknecht, S., Gerding, H. R., Karreman, C., Drescher, M., Lashuel, H. A., Outeiro, T. F., Di Monte, D. A., & Leist, M. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12226 · Cited by 148
TOM40 Mediates Mitochondrial Dysfunction Induced by α-Synuclein Accumulation in Parkinson’s Disease
Bender, A., Desplats, P., Spencer, B. J., Rockenstein, E. M., Adame, A., Elstner, M., Laub, C., Mueller, S. K., Koob, A. O., Mante, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062277 · Cited by 151
Self-citationRetractedMori, F., Tanji, K., Yoshimoto, M., Takahashi, H., & Wakabayashi, K. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.7929 · Cited by 149
Self-citationVamvaca, K., Volles, M. J., & Lansbury, P. T. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.03.021 · Cited by 149
Dutta, S., Verma, S., Jain, V., Surapaneni, B. K., Vinayek, R., Phillips, L. E., & Nair, P. P. (2019) · Journal of Neurogastroenterology and Motility · doi:10.5056/jnm19044 · Cited by 150
Paik, S. R., Lee, J., Kim, D.-H., Chang, C., & Kim, J. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0207 · Cited by 148
Mutant α-Synuclein Overexpression Mediates Early Proinflammatory Activity
Su, X., Federoff, H. J., & Maguire-Zeiss, K. A. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9053-x · Cited by 145
Moors, T. E., Maat, C. A., Niedieker, D., Mona, D., Petersen, D., Huisman, E., Kole, J., El‐Mashtoly, S. F., Spycher, L., Zago, W. M., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02329-9 · Cited by 155
Lee, J. C., Langen, R., Hummel, P. A., Gray, H. B., & Winkler, J. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407307101 · Cited by 141
Jensen, P. H., Højrup, P., Hager, H., Nielsen, M. S., JACOBSEN, L., Olesen, O. F., Gliemann, J., & Jakes, R. (1997) · Biochemical Journal · doi:10.1042/bj3230539 · Cited by 143
Malkus, K. A., Tsika, E., & Ischiropoulos, H. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-24 · Cited by 144
Helix periodicity, topology, and dynamics of membrane‐associated α‐Synuclein
Bussell, R., Ramlall, T. F., & Eliezer, D. (2005) · Protein Science · doi:10.1110/ps.041255905 · Cited by 142
Differential localization of α-, β- and γ-synucleins in the rat CNS
Li, J.-Y., Jensen, P. H., & Dahlström, A. B. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00143-4 · Cited by 141
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Prots, I., Veber, V., Brey, S., Campioni, S., Buder, K., Riek, R., Böhm, K. J., & Winner, B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.451815 · Cited by 140
Ren, X., Zhao, Y., Xue, F., Zheng, Y., Huang, H., Wang, W., Chang, Y., Yang, H., & Zhang, J. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.07.008 · Cited by 143
Djelloul, M., Holmqvist, S., Boza-Serrano, A., Azevedo, C., Yeung, M. S., Goldwurm, S., Frisén, J., Deierborg, T., & Roybon, L. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.07.002 · Cited by 138
Structural insights on physiological functions and pathological effects of ±‐synuclein
Bisaglia, M., Mammi, S., & Bubacco, L. (2008) · The FASEB Journal · doi:10.1096/fj.08-119784 · Cited by 143
Residual Structure, Backbone Dynamics, and Interactions within the Synuclein Family
Sung, Y., & Eliezer, D. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.07.008 · Cited by 137
Graham, D. R., & Sidhu, A. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22331 · Cited by 137
Atwood, C., Martins, R. N., Smith, M. A., & Perry, G. L. (2002) · Peptides · doi:10.1016/s0196-9781(02)00070-0 · Cited by 142
The AAA-ATPase VPS4 Regulates Extracellular Secretion and Lysosomal Targeting of α-Synuclein
Hasegawa, T., Konno, M., Baba, T., Sugeno, N., Kikuchi, A., Kobayashi, M., Miura, E., Tanaka, N., Tamai, K., Furukawa, K., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029460 · Cited by 138
Parkin is associated with cellular vesicles
Kubo, S., Kitami, T., Noda, S., Shimura, H., Uchiyama, Y., Asakawa, S., Minoshima, S., Shimizu, N., Mizuno, Y., & Hattori, N. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00364.x · Cited by 135
Activated Fyn Phosphorylates α-Synuclein at Tyrosine Residue 125
Nakamura, T., Yamashita, H., Takahashi, T., & Nakamura, S. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.4253 · Cited by 135
Emmer, K. L., Waxman, E. A., Covy, J. P., & Giasson, B. I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.247965 · Cited by 138
Alarcón-Arís, D., Recasens, A., Galofré, M., Carballo‐Carbajal, I., Zacchi, N., Ruiz‐Bronchal, E., Pavia-Collado, R., Chica, R., Ferrés‐Coy, A., Santos, M., et al. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2017.11.015 · Cited by 140
Could a loss of α‐synuclein function put dopaminergic neurons at risk?
Perez, R. G., & Hastings, T. G. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02423.x · Cited by 133
Kholodilov, N. G., Neystat, M., Tinmarla, F. O., Steven, E. L., Larsen, K. E., Sulzer, D. L., & Burke, R. E. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0732586.x · Cited by 133
Bioinorganic chemistry of copper coordination to alpha-synuclein: Relevance to Parkinson's disease
Binolfi, A., Quintanar, L., Bertoncini, C. W., Griesinger, C., & Fernández, C. O. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.004 · Cited by 133
Mukherjee, S., Sakunthala, A., Gadhe, L. G., Poudyal, M., Sawner, A. S., Kadu, P., & Maji, S. K. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167713 · Cited by 133
Jensen, P. H., Islam, K., Kenney, J. M., Nielsen, M. S., Power, J., & Gai, W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000099200 · Cited by 133
McFarland, N. R., Fan, Z., Xu, K., Schwarzschild, M. A., Feany, M. Β., Hyman, B. T., & McLean, P. J. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181a24b53 · Cited by 131
Immunotherapy for neurodegenerative diseases: Focus on α-synucleinopathies
Valera, E., & Masliah, E. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.01.013 · Cited by 132
Self-citationChanges in the solubility and phosphorylation of α-synuclein over the course of Parkinson’s disease
Zhou, J., Broe, M., Huang, Y. M., Anderson, J. P., Gai, W., Milward, E. A., Porritt, M. J., Howells, D. W., Hughes, A. J., Wang, X., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0815-1 · Cited by 132
The regulation of synaptic function by α-synuclein
Bellani, S., Sousa, V. L., Ronzitti, G., Valtorta, F., Meldolesi, J., & Chieregatti, E. (2010) · Communicative & Integrative Biology · doi:10.4161/cib.3.2.10964 · Cited by 133
Protein misfolding in Alzheimer’s and Parkinson’s disease: genetics and molecular mechanisms
Forloni, G., Terreni, L., Bertani, I., Fogliarino, S., Invernizzi, R. W., Assini, A., Ribizzi, G., Negro, A., Calabrese, E., & Volonté, M. A. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00076-3 · Cited by 132
Crews, L. A., Mizuno, H., Desplats, P., Rockenstein, E. M., Adame, A., Patrick, C., Winner, B., Winkler, J., & Masliah, E. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0066-08.2008 · Cited by 134
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Zhang, L., Zhang, C., Zhu, Y., Cai, Q., Chan, P., Uéda, K., Yu, S., & Yang, H. (2008) · Brain Research · doi:10.1016/j.brainres.2008.08.067 · Cited by 130
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Zhou, W., Schaack, J. B., Zawada, W. M., & Freed, C. R. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03292-9 · Cited by 129
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Farrand, A. Q., Helke, K. L., Gregory, R. A., Gooz, M. B., Hinson, V. K., & Boger, H. A. (2017) · Brain stimulation · doi:10.1016/j.brs.2017.08.008 · Cited by 130
Liang, T., Spence, J., Liu, L., Strother, W. N., Chang, H. W., Ellison, J. A., Lumeng, L., Li, T., Foroud, T., & Carr, L. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737182100 · Cited by 126
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Chen, X., de Silva, H. A. R., Pettenati, M. J., Rao, P. N., George‐Hyslop, P. S., Roses, A. D., Xia, Y., Horsburgh, K. J., Uéda, K., & Saitoh, T. (1995) · Genomics · doi:10.1016/0888-7543(95)80237-g · Cited by 125
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Nakai, M., Fujita, M., Waragai, M., Sugama, S., Wei, J., Akatsu, H., Ohtaka‐Maruyama, C., Okado, H., & Hashimoto, M. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.108 · Cited by 129
Metadata
- Authors
- Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T.
- Affiliations
- University of California San Diego (US)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1995-02
- Volume
- 14
- Issue
- 2
- Pages
- 467-475
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2059261643
- Cited by
- 1,316
- References
- 48
- Citations by year
- 2026: 21 · 2025: 23 · 2024: 34 · 2023: 36 · 2022: 60 · 2021: 56 · 2020: 69 · 2019: 59 · 2018: 62 · 2017: 49 · 2016: 53 · 2015: 61 · 2014: 52 · 2013: 41 · 2012: 47
- FWCI
- 12.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Health Assistance Foundation
- National Institutes of Health
- National Institute on Aging (AG10689, AG05131, R01AG010689, P50AG005131)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- presynaptic proteins, synaptic vesicles, synaptophysin, amyloidogenesis, amyloid plaques, brain distribution, Alzheimer's disease
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Antibodies, Antibody Specificity, Brain, Cattle, Humans, Molecular Sequence Data, Oligopeptides, Organ Specificity, Recombinant Proteins, Torpedo, Blotting, Western, Microscopy, Immunoelectron, Amyloid beta-Protein Precursor, Synaptophysin, Rats, Sprague-Dawley, Sequence Homology, Amino Acid, Microscopy, Confocal, Rats
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