Ryousuke Ito

β-Amyrin biosynthesis: the critical role of steric volume at C-19 of 2,3-oxidosqualene for its correct folding to generate the pentacyclic scaffold.

T. Hoshino, Y. Yamaguchi, Kazunari Takahashi, 2014, Organic letters.

β-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the π-electrons of Phe, at position 474 has a key role in affording the correct folding of the substrate to complete the normal polycyclization cascade.

Chiaki Nakano, T. Hoshino, Chika Nakada, 2014, Organic & biomolecular chemistry.

Triterpene cyclases from Oryza sativa L.: cycloartenol, parkeol and achilleol B synthases.

Chiaki Nakano, T. Hoshino, Tsutomu Sato, 2011, Organic letters.

Oryza sativa Parkeol Cyclase: Changes in the Substrate‐Folding Conformation and the Deprotonation Sites on Mutation at Tyr257: Importance of the Hydroxy Group and Steric Bulk

T. Hoshino, Asuka Suzuki, Ryousuke Ito, 2019, Chembiochem : a European journal of chemical biology.

Purification, kinetics, inhibitors and CD for recombinant β‐amyrin synthase from Euphorbia tirucalli L and functional analysis of the DCTA motif, which is highly conserved among oxidosqualene cyclases

T. Hoshino, Yukari Masukawa, Ryousuke Ito, 2013, The FEBS journal.

Effect of cation-π interactions and steric bulk on the catalytic action of oxidosqualene cyclase: a case study of Phe728 of β-amyrin synthase from Euphorbia tirucalli L.

T. Hoshino, Yukari Masukawa, Ryousuke Ito, 2013, Chemistry.