Alpha Synuclein: References

Alessi, D.R. and Sammler, E. (2018). LRRK2 kinase in Parkinson’s disease. Neurodegeneration 360 (6384): 36 – 37.

Ariesandi, W., Change, C., Chen, T, and Chen, Y. (2013). Temperature-Dependent Structural Changes of Parkinson’s Alpha-Synuclein Reveal the Role of Pre- Existing Oligomers in Alpha-Synuclein Fibrillization. PLOS ONE 8(1): 1-10.

Baba, M., Nakajo, S., Tu, P., Tomita, T., Nakaya, K., Lee, V., Trojanowski, J.Q., Iwastsubo, T. (1998) Aggregation of a-Synuclein in Lewy Bodies of Sporadic Parkinson’s Disease and Dementia with Lewy Bodies. American Journal of Pathology 152(4): 879 -884.

Bae, E., Lee, H., Rockenstein, E., Ho, D., Park, E., Yang, N., Desplats, P., Masliah, E., and Lee, S. (2012) Antibody-Aided Clearance of Extracellular α-Synuclein Prevents Cell-to-Cell Aggregate Transmission. The Journal of Neuroscience 32(39): 13454 – 13469

Bendor, J.T., Logan, T., and Edwards, R.H. (2013). The Function of α-synuclein. Neuron 79: 1044 -1066.

Bonina F, Puglia C, Rimoli MG, Melisi D, Boatto G, Nieddu M, Calignano A, La Rana G, De Caprariis P (2003) Glycosyl derivatives of dopamine and L-dopa as anti-Parkinson prodrugs: synthesis, pharmacological activity and in vitro stability studies. J Drug Target 11:25–36.

Braak, H., Del Tredici, K., Rub, U., de Vos, R.A.I., Jansen Steur, E.N.H., and Braak, E. (2003). Staging of brain pathology related to sporadic Parkinson’s disease. Neurobiology of Aging 24: 197 – 211.

Dehay, B., Bourdenx, M., Gorry, P., Prezdborski, S., Vila, M., Hunot, S., Singleton, A., Olanow, C.W., Merchant., K.M., Bezard, E., Petsko, G.A., and Meissner, W.G. (2015). Targeting α-synuclein for treatment of Parkinson’s disease: mechanistic and therapeutic considerations. The Lancet 14: 855 – 866.

De Vos, K.J., Grierson, A.J., Ackerley, S., and Miller, C.C.  (2008) Role of axonal transport in neurodegenerative diseases. Annual Review of Neuroscience 31:151–73.

Galvin, J.E., Uryu, K., Lee, V.M., and Trojanowski, J,.Q. (1999) Axon pathology in Parkinson’s disease and Lewy body dementia hippocampus contains alpha-, beta-, and gamma-synuclein. Proc Natl Acad Sci USA 96:13450-13455.

George, J.M. (2002). The synucleins. Genome Biology 3(1): 1-6.

Goedert, M. (2001) Alpha-Synuclein and Neurodegenerative Diseases. Nature 2: 492 – 501.

Hawthrone, G.H., Bernuci, M.P., Bortolanza, M., Tumas, V., Issy, A.C., Del-Bel, E. (2016). Nanomedicine to Overcome Current Parkinson’s Treatment Liabilities: A Systematic Review. Neurotox Res 30: 715-729.

Iba, M., Guo, J.L., Mcbride, J.D., Zhang, B., Trojanowski, J.Q., and Lee, V.M.L. (2013). Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer’s-Like Tauopathy. The Journal of Neuroscience 33(3): 1034-1037.

Jensen, P.H., Hager, H., Nielsen, M.S., Hojrup, P., Gliemann, J., and Jakes, R. (1999) Alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356. The Journal of Biological Chemistry 274: 25481– 9.

Kahle, P.J., Haass, C., Kretzschmar, H.A., and Neumann, M. (2002). Structure/function of α‐synuclein in health and disease: rational development of animal models for Parkinson’s and related diseases. Journal of Neurochemistry 82 (3): 449 – 457.

Konno, M., Hasegawa, T., Baba, T., Miura, E., Sugeno, N., Kikuchi, A., et al. (2012). Suppression of dynamin GTPase decreases alpha-synuclein uptake by neuronal and oligodendroglial cells: a potent therapeutic target for synucleinopathy. Mol. Neurodegener 7:38.

Lee, H.J., Bae, E.J., Jang, A., Ho, D.H., Cho, E.D., Suk, J., Yun, Y., and Lee, S. (2011). Enzyme-linked immunosorbent assays for alpha-synuclein with species and multimeric state specificities. Journal of Neuroscience Methods 199: 249-257.

Lee, H., Shin, S.Y., Choi, C., Lee, Y.H., Lee, S.J. (2002). Formation and Removal of -Synuclein Aggregates in Cells Exposed to Mitochondrial Inhibitors. The Journal of Biological Chemistry 227 (7): 5411-5417.

Lei, P., Ayton, S., Finkelstein, D.I., Adlard, P.A., Masters, C.L. and Bush, A.I. (2010). Tau protein: Relevance to Parkinson’s disease. The International Journal of Biochemistry & Cell Biology 42: 1775 – 1778.

Luk, K.C., Song, C., O’Brien, P., Stieber, A., Branch, J.R., Brunden, K.R., Trojanowski, J.Q., and Lee, V.M.Y. (2009). Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. PNAS 106 (47): 20051-20056.

Mahul-Mellier, A-L., Vercruysse, F., Maco, B., Ait-Bouzaid, N., De Roo, M., Muller, D., Lasheul, H.A. (2015). Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death. Cell Death and Differentiation: 1-16.

Masuda-Suzukake, M., Nonaka, T., Hosokawa, M., Kubo, M., Shimozawa., Akiyama, H., and Hasegawa, M. (2014). Pathological alpha-synuclein propagates through neural networks. Acta Neuropathological Communications 2(88): 1 – 12.

Moriarty, G.M., Olson, M.P., Atieh, T.B., Janowska, M. K., Khare, S.D., and Baum, J. (2017). A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues. Journal of Biological Chemistry 292(39): 16378-16379.

Murray, I.V., Giasson, B.I., Quinn, S.M., Koppaka, V., Axelsen, P.H., Ischiropoulos, H., Trojanowski, J.Q., Lee, V. (2003). Role of α-Synuclein Carboxy-Terminus on Fibril Formation in Vitro. Biochemistry 42: 8530-8540

Paisán-Ruíz, C., Jain, S., Evans, E.W., Gilks, W.P., Simón, J., van der Brug, M., López de Munain, A., Aparicio, S., Gil, A.M., Khan, N., Johnson, J., Martinez, J.R., Nicholl, D., Carrera, I.M., Pena, A.S., de Silva, R., Lees, A., Martí-Massó, J.F., Pérez-Tur, J., Wood, N.W., Singleton, and A.B. (2004). Cloning of the gene containing mutations that cause PARK8-linked Parkinson’s disease. Neuron 44 (4): 595–600.

Pollanen, M.S., Dickson, D.W., and Bergeron, C. (1993). Pathology and Biology of the Lewy Body. Journal of Neuropathology and Experimental Neurology 52 (3): 183 – 191.

Qureshi, H.Y. and Paudel, H.K. (2010). Parkinsonian Neurotoxin 1-Methyl-4-phenyl-1,2,3,6- tetrahydropyridine (MPTP) and a-Synuclein Mutations Promote Tau Protein Phosphorylation at Ser262 and Destabilize Microtubule Cytoskeleton in Vitro. Journal of Biological Chemistry 286: 5055 – 5068.

Roostaee, A.R., Beaudoin, S., Staskeviscius, A., and Roucou, X. (2013). Aggregation and neurotoxicity of recombinant α-synuclein aggregates initiated by dimerization. Molecular Neurodegeneration 8(5): 1-12.

Senior, S.L., Ninkina, N., Deacon R., Bannerman, D., Buchman, V.L., Cragg, S.J., and Wade-Martins, R. (2008). Increased striatal dopamine release and hyperdopaminergic‐like behaviour in mice lacking both alpha‐synuclein and gamma‐synuclein. European Journal of Neuroscience 27(4).

Sharma, S., Lohan, S., and Murthy, R.S.R. Formulation and characterization of intranasal mucoadhesive nanoparticulates and thermo-reversible gel of levodopa for brain delivery. Drug Development and Industrial Pharmacy 40 (7): 869 – 878.

Sidhu, A., Segers-Nolten, I., Subramaniam V. (2014) Solution conditions define morphological homogeneity of α-synuclein fibrils. Biochimica et Biophysica Acta 1844: 2127-2134.

Tatenhorst, L., Eckermann, K., Dambeck, V., Fonseca-Orn, L., Walle, H., Lopes da Fonseca, T., Koch, J.C., Becker, S., Tonges, L., Baher, M., Outeiro, T.F., Zweckstetter, M., and Lingor, P. (2016). Fasudil attenuates aggregation of α-synuclein in models of Parkinson’s disease. Acta Neuropathologica Communications 4 (39): 1-17.

Taymans, J.M. and Greggio, E. (2015) LRRK2 kinase inhibition as a therapeutic strategy for Parkinson’s disease, where do we stand? Curr. Neuropharmacol. 14: 214–225.

Theillet, F., Binolifi, A., Bekei, B., Martorana, A., Rose, H.M., and Stuiver, M. (2016). Structural disorder of monomeric [alpha]-synuclein persists in mammalian cells. Nature 530: 1 – 6.

Tremlett, H., Bauer, K.C., Appel-Cresswell, S., Finlay, B.B., and Waubant, E. (2017). The gut microbiome in human neurological disease: A review. Annals of Neurology 81 (3): 369 – 382.

Ubhi, K., Low, P., and Masliah, E. (2011). Multiple system atrophy: a clinical and neuropathological perspective. Trends Neurosci 34: 581–590.

Volpicelli-Daley, Luk, K.C., Patel, T.P., Tanik, S.A., Riddle, D.M., Steiber, A., Meaney, D.F., Trojanowski, J.Q. and Lee, V. (2011). Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death. Neuron 72: 57 – 71.

Wang W, Perovic I, Chittuluru J, et al. (2011) A soluble α-synuclein construct forms a dynamic tetramer. Proc Natl Acad Sci USA 108: 17797–802.

Winner B, Jappelli R, Maji SK, et al. (2011). In vivo demonstration that alpha-synuclein oligomers are toxic. Proc Natl Acad Sci USA 108: 4194–99.

Witman, G.B., Cleveland, D.W., Weingarten, M.D., and Kirschner, M.W. (1976) Tubulin requires tau for growth onto microtubule initiating sites. Proc Natl Acad Sci USA 73: 4070 –4074.

Yamada, K., and Iwatsubo, T. (2018) Extracellular α-synuclein levels are regulated by neuronal activity. Molecular Neurodegeneration 13(9): 1-8.