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Bisaglia, M., Tosatto, L., Munari, F., Tessari, I., de Laureto, P.P., Mammi, S. and Bubacco, L. (2010) Dopamine quinones interact with α-synuclein to form unstructured adducts. Biochemical and Biophysical Research Communications, 394, 424-428. doi:10.1016/j.bbrc.2010.03.044

has been cited by the following article:

• TITLE: Dopamine cannot promote oligomerization of unoxidized α-synuclein

  AUTHORS: Sakurako Shimotakahara, Mika Matsui, Chiseko Sakuma, Teruaki Takahashi, Takashi Fujimoto, Kazuo Furihata, Masaki Kojima, Shohei Seino, Tomoya Machinami, Yoichi Shibusawa, Kenji Uéda, Mitsuru Tashiro

  KEYWORDS: α-Synuclein; Dopamine; Glutathione; Oligomerization

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.4 No.3, August 9, 2013

  ABSTRACT: α-Synuclein is the major component of the filamentous Lewy bodies and Lewy neurites that define neuropathological features of Parkinson’s disease and dementia with Lewy bodies. To investigate the oligomerization process of α-synuclein in association with dopamine (DA), the structural propensities to form oligomers were studied using NMR and other biophysical techniques. The1H-15N HSQC spectra indicated that both N- and C-termini interacted with DA. Although interactions with DA were also observed in the presence of glutathione by ESI-MS, the significant suppression of oligomerization was observed in the size exclusion chromatography, suggesting that oxidations of α-synuclein are required for its oligomerization.