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Polymeropoulos, M.H., Lavedan, C., Leroy, E., Ide, S.E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., Stenroos, E.S., Chandrasekharappa, S., Athanassiadou, A., Papapetropoulos, T., Johnson, W.G., Lazzarini, A.M., Duvoisin, R.C., Di Iorio, G., Golbe, L.I. and Nussbaum, R.L. (1997) Mutation in the α-synuclein gene identified in families with Parkinson’s disease. Science, 276, 2045-2047. doi:10.1126/science.276.5321.2045

has been cited by the following article:

• TITLE: Demonstration of three dopamine molecules bound to α-Synuclein: Implication of oligomerization at the initial stage

  AUTHORS: Sakurako Shimotakahara, Yuuki Shiroyama, Takashi Fujimoto, Mai Akai, Takaya Onoue, Hiroko Seki, Sayaka Kado, Tomoya Machinami, Yoichi Shibusawa, Kenji Uéda, Mitsuru Tashiro

  KEYWORDS: α-Synuclein; Dopamine; Fibrillation; Oligomerization; Mass Spectrometry

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.3 No.2, May 29, 2012

  ABSTRACT: α-Synuclein is the major component of the filamentous Lewy bodies and Lewy neurites that define neuropathological features and dementia with Lewy bodies. To investigate the role of dopamine (DA) in α-synuclein fibrillation, the structural propensities to form oligomers at the initial stage fibrillation were studied using size exclusion chromatography and various biophysical techniques. Interactions with DA were observed for wild-type α-synuclein and its mutants, A30P, E46K and A53T, using electrospray ionization mass spectrometry (ESI-MS). The results of ESI-MS indicate that an intact α-synuclein, which was not oxidized, had an ability to bind with three molecules of DA at the initial stage. Furthermore, upon binding to DA, α-synuclein oligomerizes to higher molecular weight species. These oligomers are structurally different from amyloid fibrils, as confirmed by thioflavin T and CD analysis.