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beta-Helix is a likely core structure of yeast prion Sup35 amyloid fibers.

• Aiko Kishimoto, Kazuya Hasegawa, Hirofumi Suzuki, Hideki Taguchi, Keiichi Namba, Masasuke Yoshida
• Biochemical and biophysical research…
• 2004

We have studied the core structure of amyloid fibers of yeast prion protein Sup35. We developed procedures to prepare straight fibers of relatively uniform diameters from three kinds of fragments; N… (More)

Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it.

• Yuji Inoue, Hideki Taguchi, Aiko Kishimoto, Masasuke Yoshida
• The Journal of biological chemistry
• 2004

The interaction of Hsp104 with yeast prion fibers made of Sup35NM, a prion-inducing domain of Sup35, was tested. When fluorescently labeled Hsp104 was added to the preformed fibers, individual fibers… (More)

Strong growth polarity of yeast prion fiber revealed by single fiber imaging.

• Yuji Inoue, Aiko Kishimoto, Jun Hirao, Masasuke Yoshida, Hideki Taguchi
• The Journal of biological chemistry
• 2001

Using the yeast prion as a model, we have developed a novel system to observe the growth of individual prion fibers directly. NM fragments, the prion-determining region of the yeast protein Sup35p,… (More)

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