Masatoshi Saiki

发表

Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains.

Shinya Honda, Deshan Zhou, H. Morii, 2005, Journal of molecular biology.

Peripheral region for core cross-β plays important role in amyloidogenicity

H. Morii, T. Konakahara, M. Ishimura, 2006 .

Irradiation effect of a submillimeter wave from 420 GHz gyrotron on amyloid peptides in vitro.

M. Tani, T. Yaji, T. Ohta, 2020, Biomedical optics express.

Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding

M. Hagiwara, M. Okumura, K. Inaba, 2013, Scientific Reports.

Acceleration of disulfide‐coupled protein folding using glutathione derivatives

H. Yamaguchi, M. Okumura, Y. Hidaka, 2011, The FEBS journal.

The potential stem-forming sequence consists of the polymerization in Pmel17

Masatoshi Saiki, Ikumi Shibatate, Takafumi Shizuma, 2020, Journal of Biorheology.

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.

H. Yamaguchi, M. Okumura, Shingo Kanemura, 2014, Structure.

Fiber formation of a synthetic spider peptide derived from Nephila clavata

H. Yamaguchi, M. Miyazawa, Y. Hidaka, 2011, Biopolymers.

Recognition of the N-terminal histone H2A and H3 peptides by peptidylarginine deiminase IV.

Y. Hidaka, Masatoshi Saiki, Mayumi Watase, 2009, Protein and peptide letters.

Thiamine tetrahydrofurfuryl disulfide promotes voluntary activity through dopaminergic activation in the medial prefrontal cortex

T. Matsui, H. Soya, Takeru Shima, 2018, Scientific Reports.

Interaction-based evaluation of the propensity for amyloid formation with cross-beta structure.

H. Morii, T. Konakahara, Masatoshi Saiki, 2006, Biochemical and biophysical research communications.

Stem-forming regions that are essential for the amyloidogenesis of prion proteins.

H. Morii, M. Nara, Y. Hidaka, 2012, Biochemistry.