Article citationsMore>>

Zarranz, J.J., Alegre, J., Gomez-Esteban, J.C., Lezcano, E., Ros, R., Ampuero, I., Vidal, L., Hoenicka, J., Rodriguez, O., Atares, B., Llorens, V., Gomez Tortosa, E., del Ser, T., Munoz, D.G. and De Yebenes, J.G. (2004) The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia. Annals of Neurology, 55, 164-173. doi:10.1002/ana.10795

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.