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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · 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

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 · see citing works

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 1,360 · see citing works

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 1,350 · see citing works

Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease

Namba, Y., Tomonaga, M., Kawasaki, H., Otomo, E., & Ikeda, K. (1991) · Brain Research · doi:10.1016/0006-8993(91)91092-f · Cited by 1,157 · 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

Immunochemical identification of the serine protease inhibitor α1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease

Abraham, C. R., Selkoe, D. J., & Potter, H. (1988) · Cell · doi:10.1016/0092-8674(88)90462-x · Cited by 893 · see citing works

Immunogenic structure of the influenza virus hemagglutinin

Green, N. H., Alexander, H., Olson, A. J., Alexander, S. P. H., Shinnick, T. M., Sutcliffe, J. G., & Lerner, R. A. (1982) · Cell · doi:10.1016/0092-8674(82)90202-1 · Cited by 756 · see citing works

Sequence identification of 2,375 human brain genes

Adams, M. D., Dubnick, M., Kerlavage, A. R., Moreno, R., Kelley, J. M., Utterback, T. R., Nagle, J. W., Fields, C., & Venter, J. C. (1992) · Nature · doi:10.1038/355632a0 · Cited by 754 · see citing works

Precursor of amyloid protein in Alzheimer disease undergoes fast anterograde axonal transport.

Koo, E. H., Sisodia, S. S., Archer, D. R., Martin, L. J., Weidemann, A., Beyreuther, K., Fischer, P., Masters, C. L., & Price, D. L. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1561 · Cited by 733 · see citing works

Mass spectrometry of purified amyloid beta protein in Alzheimer's disease.

Mori, H., Takio, K., OGAWARA, M., & Selkoe, D. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41896-0 · Cited by 481 · see citing works

Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact.

Shivers, B. D., Hilbich, C., Multhaup, G., Salbaum, M., Beyreuther, K. T., & SEEBURG, P. H. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02952.x · Cited by 442 · see citing works

The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease.

Snow, A. D., Mar, H., Nochlin, D., Kimata, K., Kato, M., Suzuki, S., Hassell, J., & Wight, T. N. (1988) · PubMed Central · Cited by 418 · see citing works

Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation

Horstman, L. L., & Racker, E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63241-7 · Cited by 398 · see citing works

The rat brain synucleins; family of proteins transiently associated with neuronal membrane

Maroteaux, L., & Scheller, R. H. (1991) · Molecular Brain Research · doi:10.1016/0169-328x(91)90043-w · Cited by 334 · see citing works

Localization of Alzheimer βA4 amyloid precursor protein at central and peripheral synaptic sites

SCHUBERT, W. J., Prior, R., Weidemann, A., Dircksen, H., Multhaup, G., Masters, C. L., & Beyreuther, K. T. (1991) · Brain Research · doi:10.1016/0006-8993(91)91532-6 · Cited by 265 · see citing works

Patterns of aberrant sprouting in alzheimer's disease

Masliah, E., Mallory, M. E., Hansen, L. A., Alford, M. F., Albright, T., DeTeresa, R. M., Terry, R. D., Baudier, J., & Saitoh, T. (1991) · Neuron · doi:10.1016/0896-6273(91)90170-5 · Cited by 245 · see citing works

Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease.

Cataldo, A., Hamilton, D. J., & Nixon, R. (1994) · Brain Research · doi:10.1016/0006-8993(94)91858-9 · Cited by 225 · see citing works

Three-dimensional analysis of the relationship between synaptic pathology and neuropil threads in Alzheimer disease

Masliah, E., Ellisman, M., Carragher, B., Mallory, M., Young, S., Hansen, L., Deteresa, R., & Terry, R. D. (1992) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199207000-00003 · Cited by 183 · see citing works

Morphologic and biochemical analysis of the intracellular trafficking of the Alzheimer beta/A4 amyloid precursor protein

Caporaso, G., Takei, K., Gandy, S., Matteoli, M., Mundigl, O., Greengard, P., & Camilli, P. V. D. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-05-03122.1994 · Cited by 182 · see citing works

The Seminal Role of β-Amyloid in the Pathogenesis of Alzheimer Disease

Joachim, C. L., & Selkoe, D. J. (1992) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-199205000-00003 · Cited by 181 · see citing works

Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin

Cataldo, A. M., Thayer, C. Y., Bird, E. D., Wheelock, T. R., & Nixon, R. A. (1990) · Brain Research · doi:10.1016/0006-8993(90)90456-l · Cited by 176 · see citing works

A new brain‐specific 14‐kDa protein is a phosphoprotein

Nakajo, S., TSUKADA, K., Omata, K., Nakamura, Y., & Nakaya, K. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18337.x · Cited by 170 · see citing works

Synaptic pathology in alzheimer's disease: Immunological data for markers of synaptic and large dense-core vesicles

Lassmann, H., Weiler, R., Fischer, P. A., Bancher, C., Jellinger, K. A., Floor, E., Danielczyk, W., SEITELBERGER, F., & Winkler, H. J. S. (1992) · Neuroscience · doi:10.1016/0306-4522(92)90003-k · Cited by 160 · see citing works

SP-40,40 is a constituent of Alzheimer's amyloid

Choi-Miura, N. H., Ihara, Y., Fukuchi, K., Takeda, M., Nakano, Y., Tobe, T., & Tomita, M. (1992) · Acta Neuropathologica · doi:10.1007/bf00296787 · Cited by 158 · see citing works

Immunocytochemical localization of the precursor protein for β-amyloid in the rat central nervous system

Card, J. P., Meade, R. P., & Davis, L. G. (1988) · Neuron · doi:10.1016/0896-6273(88)90131-6 · Cited by 155 · see citing works

Protein kinase C alteration is an early biochemical marker in Alzheimer's disease

Masliah, E., Cole, G. M., Hansen, L. A., Mallory, M. E., Albright, T., Terry, R. D., & Saitoh, T. (1991) · Journal of Neuroscience · doi:10.1523/jneurosci.11-09-02759.1991 · Cited by 125 · see citing works

Cell and tissue distribution and developmental change of neuron specific 14 kDa protein (phosphoneuroprotein 14)

Shibayama‐Imazu, T., Okahashi, I., Omata, K., Nakajo, S., Ochiai, H., Nakai, Y., Hama, T., Nakamura, Y., & Nakaya, K. (1993) · Brain Research · doi:10.1016/0006-8993(93)90796-p · Cited by 117 · see citing works

Immunodetection of the amyloid P component in Alzheimer's disease

Duong, T., Pommier, E. C., & Scheibel, A. B. (1989) · Acta Neuropathologica · doi:10.1007/bf00688180 · Cited by 111 · see citing works

Identification of components of immunoglobulins in senile plaques by means of fluorescent antibody technique

Ishii, T., Haga, S., & Shimizu, F. (1975) · Acta Neuropathologica · doi:10.1007/bf00689569 · Cited by 110 · see citing works

Immunoreactive A4 and gamma-trace peptide colocalization in amyloidotic arteriolar lesions in brains of patients with Alzheimer's disease.

Vinters, H. V., Nishimura, G. S., Secor, D. L., & Pardridge, W. M. (1990) · Europe PMC (PubMed Central) · Cited by 110 · see citing works

Amyloid β-protein precursor accumulates in dystrophic neurites of senile plaques in Alzheimer-type dementia

Shoji, M., Hirai, S., Yamaguchi, H., Harigaya, Y., & Kawarabayashi, T. (1990) · Brain Research · doi:10.1016/0006-8993(90)91187-l · Cited by 99 · see citing works

Localization of amyloid precursor protein in GAP43-immunoreactive aberrant sprouting neurites in Alzheimer's disease

Masliah, E., Mallory, M. E., Hansen, L. A., Alford, M. F., DeTeresa, R. M., Terry, R. D., Baudier, J., & Saitoh, T. (1992) · Brain Research · doi:10.1016/0006-8993(92)90831-s · Cited by 91 · see citing works

A high ratio of chromogranin A to synaptin/synaptophysin is a common feature of brains in Alzheimer and Pick disease

Bellmann‐Weiler, R., Lassmann, H., Fischer, P. A., Jellinger, K. A., & Winkler, H. J. S. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)81408-g · Cited by 89 · see citing works

Antibodies to non-beta regions of the beta-amyloid precursor protein detect a subset of senile plaques.

Joachim, C. L., Games, D., Morris, J. R., Ward, P. J., Frenkel, D., & Selkoe, D. J. (1991) · PubMed Central · Cited by 88 · see citing works

Chromogranin A-like immunoreactive neurites are major constituents of senile plaques.

Muñoz, D. G. (1991) · PubMed · Cited by 82 · see citing works

Synaptophysin and chromogranin A immunoreactivities in senile plaques of Alzheimer's disease

Brion, J., Couck, A., Bruce, M. T., Anderton, B. H., & Flament-Durand, J. (1991) · Brain Research · doi:10.1016/0006-8993(91)90697-t · Cited by 71 · see citing works

Accumulation of amyloid precursor fragment in Alzheimer plaques

Cole, G. M., Masliah, E., Shelton, E. R., Chan, H. W., Terry, R. D., & Saitoh, T. (1991) · Neurobiology of Aging · doi:10.1016/0197-4580(91)90046-m · Cited by 64 · see citing works

Amyloid β/A4 protein precursor is widely distributed in both the central and peripheral nervous systems of the mouse

Kawarabayashi, T., Shoji, M., Harigaya, Y., Yamaguchi, H., & Hirai, S. (1991) · Brain Research · doi:10.1016/0006-8993(91)90651-b · Cited by 58 · see citing works

Amyloidosis in aging and Alzheimer's disease.

Price, D. L., Walker, L. C., Martin, L. J., & Sisodia, S. S. (1992) · PubMed Central · Cited by 32 · see citing works

Complements, microglial cells and amyloid fibril formation

Ishii, T., & Haga, S. (1992) · Research in Immunology · doi:10.1016/0923-2494(92)80043-k · Cited by 25 · 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

Neuropathological alterations in Alzheimer disease

Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345 · 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 1,763 · 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

The many faces of α-synuclein: from structure and toxicity to therapeutic target

Lashuel, H. A., Overk, C., Oueslati, A., & Masliah, E. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3406 · Cited by 1,623 · see citing works

Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.

(1998) · Europe PMC (PubMed Central) · Cited by 1,594 · 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

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. (2008) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.1437 · Cited by 1,424 · see citing works

Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein

Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105343200 · Cited by 1,103 · see citing works

Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation

Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096 · see citing works

A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly

Giasson, B. I., Murray, I. V. J., Trojanowski, J. Q., & Lee, V. M.-Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008919200 · Cited by 1,080 · see citing works

Increased Expression of α-Synuclein Reduces Neurotransmitter Release by Inhibiting Synaptic Vesicle Reclustering after Endocytosis

Nemani, V. M., Lü, W., Berge‐Seidl, V., Nakamura, K., Onoa, B., Lee, M. K., Chaudhry, F. A., Nicoll, R. A., & Edwards, R. H. (2010) · Neuron · doi:10.1016/j.neuron.2009.12.023 · Cited by 1,051 · see citing works

Structure and Dynamics of Micelle-bound Human α-Synuclein

Ulmer, T. S., Bax, A., Cole, N. B., & Nussbaum, R. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411805200 · Cited by 966 · see citing works

Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies

Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898 · see citing works

α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies

Wong, Y. C., & Krainc, D. (2017) · Nature Medicine · doi:10.1038/nm.4269 · Cited by 897 · see citing works

Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, Á., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 901 · see citing works

The function of α-synuclein

Bendor, J. T., Logan, T. P., & Edwards, R. H. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.004 · Cited by 825 · see citing works

Structural disorder of monomeric α-synuclein persists in mammalian cells

Theillet, F., Binolfi, A., Bekei, B., Martorana, A., Rose, H. M., Stuiver, M., Verzini, S., Lorenz, D., van Rossum, M., Goldfarb, D., et al. (2016) · Nature · doi:10.1038/nature16531 · Cited by 877 · see citing works

Characterization of a novel protein regulated during the critical period for song learning in the zebra finch

George, J. M., Jin, H., Woods, W. S., & Clayton, D. F. (1995) · Neuron · doi:10.1016/0896-6273(95)90040-3 · Cited by 844 · see citing works

Intravesicular Localization and Exocytosis of α-Synuclein and its Aggregates

Lee, H.-J., Patel, S. S., & Lee, S. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0692-05.2005 · Cited by 798 · see citing works

The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease

Clayton, D. F., & George, J. M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01213-7 · Cited by 779 · see citing works

α-Synuclein Promotes Mitochondrial Deficit and Oxidative Stress

Hsu, L. J., Sagara, Y., Arroyo, A., Rockenstein, E. M., Sisk, A., Mallory, M. E., Wong, J., Takenouchi, T., Hashimoto, M., & Masliah, E. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64553-1 · Cited by 716 · 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

Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases

Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641 · 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

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

The synaptic pathology of α-synuclein aggregation in dementia with Lewy bodies, Parkinson’s disease and Parkinson’s disease dementia

Schulz-Schaeffer, W. J. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0711-0 · Cited by 627 · see citing works

α-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease

Chen, L., & Feany, M. Β. (2005) · Nature Neuroscience · doi:10.1038/nn1443 · Cited by 614 · see citing works

What Genetics Tells us About the Causes and Mechanisms of Parkinson's Disease

Corti, O., Lesage, S., & Brice, A. (2011) · Physiological Reviews · doi:10.1152/physrev.00022.2010 · Cited by 610 · 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

Understanding Dopaminergic Cell Death Pathways in Parkinson Disease

Michel, P. P., Hirsch, É. C., & Hunot, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.038 · Cited by 594 · see citing works

Beclin 1 Gene Transfer Activates Autophagy and Ameliorates the Neurodegenerative Pathology in α-Synuclein Models of Parkinson's and Lewy Body Diseases

Spencer, B., Potkar, R., Trejo, M., Rockenstein, E., Patrick, C., Gindi, R., Adame, A., Wyss-Coray, T., & Masliah, E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4390-09.2009 · Cited by 595 · see citing works

α‐Synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma

El-Agnaf, O. M. A., Salem, S. A., Paleologou, K. E., Cooper, L. J., Fullwood, N. J., Gibson, M. J., Curran, M. D., Court, J. A., Mann, D. M. A., Ikeda, S.-I., et al. (2003) · The FASEB Journal · doi:10.1096/fj.03-0098fje · Cited by 590 · see citing works

Cell Biology and Pathophysiology of α-SynucleinPreprint

Burré, J., Sharma, M., & Südhof, T. C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024091 · Cited by 576 · see citing works

The Synaptic Function of α-Synuclein

Burré, J. (2015) · Journal of Parkinson s Disease · doi:10.3233/jpd-150642 · Cited by 579 · see citing works

Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation

Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 567 · 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

Microglia clear neuron-released α-synuclein via selective autophagy and prevent neurodegeneration

Choi, I., Zhang, Y., Seegobin, S. P., Pruvost, M., Wang, Q., Purtell, K., Zhang, B., & Yue, Z. (2020) · Nature Communications · doi:10.1038/s41467-020-15119-w · Cited by 549 · see citing works

Effects of α-Synuclein Immunization in a Mouse Model of Parkinson’s Disease

Masliah, E., Rockenstein, E., Adame, A., Alford, M., Crews, L., Hashimoto, M., Seubert, P., Lee, M., Goldstein, J., Chilcote, T., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.05.010 · Cited by 542 · see citing works

α-Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease

Bianco, C. L., Ridet, J.-L., Schneider, B. L., Déglon, N., & Aebischer, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152339799 · Cited by 533 · see citing works

Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations

Dehay, B., Bourdenx, M., Gorry, P., Przedborski, S., Vila, M., Hunot, S., Singleton, A., Olanow, C. W., Merchant, K., Bézard, E., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)00006-x · Cited by 530 · see citing works

Constitutive Phosphorylation of the Parkinson's Disease Associated α-Synuclein

Okochi, M., Walter, J., Koyama, A., Nakajo, S., Baba, M., Iwatsubo, T., Meijer, L., Kahle, P. J., & Haass, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.390 · Cited by 521 · see citing works

Lipid Rafts Mediate the Synaptic Localization of α-Synuclein

Fortin, D. L., Troyer, M. D., Nakamura, K., Kubo, S., Anthony, M. D., & Edwards, R. H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1594-04.2004 · Cited by 518 · see citing works

The Lewy body in Parkinson's disease: Molecules implicated in the formation and degradation of α‐synuclein aggregates

Wakabayashi, K., Tanji, K., Mori, F., & Takahashi, H. (2007) · Neuropathology · doi:10.1111/j.1440-1789.2007.00803.x · Cited by 516 · 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

Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)

Theillet, F., Binolfi, A., Frembgen-Kesner, T., Hingorani, K. S., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L. M., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 504 · see citing works

Antisense oligonucleotide therapy for neurodegenerative disease

Smith, R. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25424 · Cited by 506 · see citing works

Differential neuropathological alterations in transgenic mice expressing α‐synuclein from the platelet‐derived growth factor and Thy‐1 promoters

Rockenstein, E., Mallory, M., Hashimoto, M., Song, D., Shults, C. W., Lang, I., & Masliah, E. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10231 · Cited by 502 · see citing works

Role of Protein Aggregation in Mitochondrial Dysfunction and Neurodegeneration in Alzheimer's and Parkinson's Diseases

Hashimoto, M., Rockenstein, E. M., Crews, L. A., & Masliah, E. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:4:1-2:21 · Cited by 498 · see citing works

Structure of membrane-bound α-synuclein from site-directed spin labeling and computational refinement

Jao, C. C., Hegde, B. G., Chen, J., Haworth, I. S., & Langen, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807826105 · Cited by 501 · see citing works

Axon degeneration in Parkinson's disease

Burke, R. E., & O’Malley, K. L. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.01.011 · Cited by 494 · see citing works

The Lewy Body in Parkinson’s Disease and Related Neurodegenerative Disorders

Wakabayashi, K., Tanji, K., Odagiri, S., Miki, Y., Mori, F., & Takahashi, H. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8280-y · Cited by 478 · see citing works

Inhibition of mitochondrial fusion by α‐synuclein is rescued by PINK1, Parkin and DJ‐1

Kamp, F., Exner, N., Lutz, A., Wender, N., Hegermann, J., Brunner, B., Nuscher, B., Bartels, T., Giese, A., Beyer, K., et al. (2010) · EMBO Journal · doi:10.1038/emboj.2010.223 · Cited by 505 · see citing works

α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation

Burré, J., Sharma, M., & Südhof, T. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416598111 · Cited by 478 · see citing works

Poly(ADP-ribose) drives pathologic α-synuclein neurodegeneration in Parkinson’s disease

Kam, T.-I., Mao, X., Park, H., Chou, S.-C., Karuppagounder, S. S., Umanah, G. E., Yun, S. P., Brahmachari, S., Panicker, N., Chen, R., et al. (2018) · Science · doi:10.1126/science.aat8407 · Cited by 476 · see citing works

Lewy bodies

Shults, C. W. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509567103 · Cited by 476 · see citing works

Aggregation promoting C-terminal truncation of α-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

Li, W., West, N. C., Colla, E., Pletniková, O., Troncoso, J. C., Marsh, L., Dawson, T. M., Jäkälä, P., Hartmann, T., Price, D. L., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406976102 · Cited by 473 · see citing works

Biophysical Properties of the Synucleins and Their Propensities to Fibrillate

Uversky, V. N., Li, J., Souillac, P. O., Millett, I. S., Doniach, S., Jakes, R., Goedert, M., & Fink, A. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109541200 · Cited by 462 · see citing works

Development of α-synuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson’s disease

Braak, H., Sastre, M., & Del Tredici, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0244-3 · Cited by 462 · see citing works

Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson’s disease?

Goldberg, M. S., & Lansbury, P. T. (2000) · Nature Cell Biology · doi:10.1038/35017124 · Cited by 456 · see citing works

Direct binding and functional coupling of α-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis

Lee, F. J. S., Liu, F., Pristupa, Z. B., & Niznik, H. B. (2001) · The FASEB Journal · doi:10.1096/fj.00-0334com · Cited by 455 · see citing works

Membrane-bound α-Synuclein Has a High Aggregation Propensity and the Ability to Seed the Aggregation of the Cytosolic Form

Lee, H.-J., Choi, C., & Lee, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107045200 · Cited by 452 · see citing works

Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models

Karpinar, D. P., Balija, M. B. G., Kügler, S., Opazo, F., Rezaei‐Ghaleh, N., Wender, N., Kim, H., Taschenberger, G., Falkenburger, B. H., Heise, H., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.257 · Cited by 443 · see citing works

NACP/α-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson’s disease brains

Wakabayashi, K., Hayashi, S., Yoshimoto, M., Kudo, H., & Takahashi, H. (2000) · Acta Neuropathologica · doi:10.1007/pl00007400 · Cited by 439 · 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

The toxicity in vitro of β-amyloid protein

Iversen, L. L., Mortishire‐Smith, R. J., Pollack, S. J., & Shearman, M. S. (1995) · Biochemical Journal · doi:10.1042/bj3110001 · Cited by 425 · see citing works

Decreased α-synuclein in cerebrospinal fluid of aged individuals and subjects with Parkinson’s disease

Tokuda, T., Salem, S. A., Allsop, D., Mizuno, T., Nakagawa, M., Qureshi, M. M., Locascio, J. J., Schlossmacher, M. G., & El-Agnaf, O. M. A. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.024 · Cited by 425 · see citing works

α-Synuclein Overexpression in PC12 and Chromaffin Cells Impairs Catecholamine Release by Interfering with a Late Step in Exocytosis

Larsen, K. E., Schmitz, Y., Troyer, M. D., Mosharov, E. V., Dietrich, P., Quazi, A. Z., Savalle, M., Nemani, V. M., Chaudhry, F. A., Edwards, R. H., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3821-06.2006 · Cited by 415 · see citing works

Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders.

Takeda, A., Mallory, M. E., Sundsmo, M. P., Honer, W. G., Hansen, L. A., & Masliah, E. (1998) · Europe PMC (PubMed Central) · Cited by 404 · see citing works

Colocalization of Tau and Alpha-Synuclein Epitopes in Lewy Bodies

Ishizawa, T., Mattila, P. M., Davies, P., Wang, D., & Dickson, D. W. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.4.389 · Cited by 391 · see citing works

α‐Synuclein Up‐Regulation in Substantia Nigra Dopaminergic Neurons Following Administration of the Parkinsonian Toxin MPTP

Vila, M., Vukosavić, S., Jackson-Lewis, V. R., Neystat, M., Jakowec, M. W., & Przedborski, S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.740721.x · Cited by 388 · see citing works

Effects of Curvature and Composition on α-Synuclein Binding to Lipid Vesicles

Middleton, E. R., & Rhoades, E. R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.07.056 · Cited by 378 · see citing works

α-Synuclein Binds to Tau and Stimulates the Protein Kinase A-catalyzed Tau Phosphorylation of Serine Residues 262 and 356

Jensen, P. H., Hager, H., Nielsen, M. S., Højrup, P., Gliemann, J., & Jakes, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25481 · Cited by 377 · see citing works

Multiple Tight Phospholipid-Binding Modes of α-Synuclein Revealed by Solution NMR Spectroscopy

Bodner, C. R., Dobson, C. M., & Bax, A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.05.066 · Cited by 370 · see citing works

α-synuclein in the pathophysiology of Alzheimer’s disease

Twohig, D., & Nielsen, H. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0320-x · Cited by 374 · see citing works

Neuropathological Staging of Brain Pathology in Sporadic Parkinson’s disease: Separating the Wheat from the Chaff

Braak, H., & Del Tredici, K. (2017) · Journal of Parkinson’s Disease · doi:10.3233/jpd-179001 · Cited by 372 · see citing works

The E46K Mutation in α-Synuclein Increases Amyloid Fibril Formation

Greenbaum, E. A., Graves, C. L., Mishizen-Eberz, A. J., Lupoli, M. A., Lynch, D. R., Englander, S. W., Axelsen, P. H., & Giasson, B. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411638200 · Cited by 370 · see citing works

Iron Toxicity in Diseases of Aging: Alzheimer's Disease, Parkinson's Disease and Atherosclerosis

Altamura, S., & Muckenthaler, M. U. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-1010 · Cited by 369 · 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

Pathological roles of α-synuclein in neurological disorders

Vekrellis, K., Xilouri, M., Emmanouilidou, E., Rideout, H. J., & Stefanis, L. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70213-7 · Cited by 359 · see citing works

Effect of Mutant α-Synuclein on Dopamine Homeostasis in a New Human Mesencephalic Cell Line

Lotharius, J., Barg, S., Wiekop, P., Lundberg, C., Raymon, H. K., & Brundin, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205518200 · Cited by 349 · see citing works

Accumulation of α-synuclein/NACP is a cytopathological feature common to Lewy body disease and multiple system atrophy

Wakabayashi, K., Hayashi, S., Kakita, A., Yamada, M., Toyoshima, Y., Yoshimoto, M., & Takahashi, H. (1998) · Acta Neuropathologica · doi:10.1007/s004010050918 · Cited by 347 · see citing works

Neuropathology and molecular diagnosis of Synucleinopathies

Koga, S., Sekiya, H., Kondru, N. C., Ross, O. A., & Dickson, D. W. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00501-z · Cited by 338 · see citing works

Microglia Phenotypes in Aging and Neurodegenerative Diseases

Wendimu, M. Y., & Hooks, S. B. (2022) · Cells · doi:10.3390/cells11132091 · Cited by 336 · see citing works

Astrocytic expression of Parkinson's disease-related A53T α-synuclein causes neurodegeneration in mice

Gu, X., Long, C.-X., Sun, L., Xie, C., Lin, X. Z., & Cai, H. (2010) · Molecular Brain · doi:10.1186/1756-6606-3-12 · Cited by 341 · see citing works

Antibody-Aided Clearance of Extracellular α-Synuclein Prevents Cell-to-Cell Aggregate Transmission

Bae, E.-J., Lee, H.-J., Rockenstein, E., Ho, D.-H., Park, E.-B., Yang, N.-Y., Desplats, P., Masliah, E., & Lee, S.-J. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1292-12.2012 · Cited by 339 · see citing works

Copper(II)-induced self-oligomerization of α-synuclein

Paik, S. R., Shin, H.-J., Lee, J., Chang, C., & Kim, J. (1999) · Biochemical Journal · doi:10.1042/bj3400821 · Cited by 332 · see citing works

Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation

Flagmeier, P., Meisl, G., Vendruscolo, M., Knowles, T. P. J., Dobson, C. M., Buell, A. K., & Galvagnion, C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604645113 · Cited by 323 · see citing works

NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease

Wakabayashi, K., Matsumoto, K., Takayama, K., Yoshimoto, M., & Takahashi, H. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00891-4 · Cited by 331 · see citing works

α-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins

Sharon, R., Goldberg, M. S., Bar-Josef, I., Betensky, R. A., Shen, J., & Selkoe, D. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171300598 · Cited by 329 · see citing works

Impaired dopamine metabolism in Parkinson’s disease pathogenesis

Masato, A., Plotegher, N., Boassa, D., & Bubacco, L. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0332-6 · Cited by 331 · see citing works

Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling

Der-Sarkissian, A., Jao, C. C., Chen, J., & Langen, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305266200 · Cited by 328 · see citing works

Understanding the molecular causes of Parkinson's disease

Wood‐Kaczmar, A., Gandhi, S., & Wood, N. W. (2006) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.09.007 · Cited by 327 · see citing works

Reducing C-Terminal-Truncated Alpha-Synuclein by Immunotherapy Attenuates Neurodegeneration and Propagation in Parkinson's Disease-Like Models

Games, D., Valera, E., Spencer, B. J., Rockenstein, E. M., Mante, M., Adame, A., Patrick, C., Ubhi, K. K., Nuber, S., Sacayon, P., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5314-13.2014 · Cited by 322 · 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

The Synuclein FamilyPreprint

Lavedan, C. N. (1998) · Genome Research · doi:10.1101/gr.8.9.871 · Cited by 321 · see citing works

Expression of Concern: Antioxidant compounds have potent anti‐fibrillogenic and fibril‐destabilizing effects for α‐synuclein fibrils in vitro

Ono, K., & Yamada, M. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03707.x · Cited by 320 · see citing works

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 166 · see citing works

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 · see citing works

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 · see citing works

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 80 · see citing works

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 52 · see citing works