Mayumi Uno

Site-specific Inhibitory Mechanism for Amyloid β42 Aggregation by Catechol-type Flavonoids Targeting the Lys Residues*

K. Irie, Y. Masuda, K. Takegoshi, 2013, Journal of Biological Chemistry.

Isomerization and/or racemization at Asp23 of Abeta42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro.

T. Shirasawa, Takahiko Shimizu, K. Irie, 2008, Biochemical and biophysical research communications.

Structure–Activity Relationship for (+)-Taxifolin Isolated from Silymarin as an Inhibitor of Amyloid β Aggregation

K. Irie, K. Murakami, Y. Nakagawa, 2013, Bioscience, biotechnology, and biochemistry.

Random mutagenesis improves the low-temperature activity of the tetrameric 3-isopropylmalate dehydrogenase from the hyperthermophile Sulfolobus tokodaii.

S. Akanuma, A. Yamagishi, Mayumi Uno, 2008, Protein engineering, design & selection : PEDS.

Site-specific Inhibitory Mechanism for Amyloid β42 Aggregation by Catechol-type Flavonoids Targeting the Lys Residues*

K. Irie, Y. Masuda, K. Takegoshi, 2013, The Journal of Biological Chemistry.