S
Sueharu Horinouchi
Researcher at University of Tokyo
Publications - 355
Citations - 25647
Sueharu Horinouchi is an academic researcher from University of Tokyo. The author has contributed to research in topics: Streptomyces griseus & Streptomyces. The author has an hindex of 77, co-authored 355 publications receiving 24536 citations.
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Journal ArticleDOI
Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region
Nobuaki Kudo,Nobuaki Matsumori,Hiroshi Taoka,Daisuke Fujiwara,Erwin P. Schreiner,Barbara Wolff,Minoru Yoshida,Sueharu Horinouchi +7 more
TL;DR: Results show that the single cysteine residue determines LMB sensitivity and is selectively alkylated by LMB, leading to CRM1 inactivation.
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Leptomycin B Inhibition of Signal-Mediated Nuclear Export by Direct Binding to CRM1
Nobuaki Kudo,Barbara Wolff,Toshihiro Sekimoto,Erwin P. Schreiner,Yoshihiro Yoneda,Mitsuhiro Yanagida,Sueharu Horinouchi,Minoru Yoshida +7 more
TL;DR: Evidence is shown that LMB binds directly to CRM1 and thatCRM1 is essential for NES-dependent nuclear export of proteins in both yeast and mammalian cells, and is an essential factor for nuclear exported proteins in eukaryotes.
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Nucleotide sequence and functional map of pC194, a plasmid that specifies inducible chloramphenicol resistance.
TL;DR: The genetic determinant of chloramphenicol (CAM) resistance, which includes the chlorampshenicol acetyl transferase (CAT) structural gene, the putative promoter and controlling element of this determinant, have been mapped functionally by subcloning a 1,035-nucleotide fragment which specifies the resistance phenotype using plasmid pBR322 as vector.
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Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function.
TL;DR: Trichostatin A and trapoxin are useful in analyzing the role of histone acetylation in chromatin structure and function as well as in determining the genes whose activities are regulated by histoneacetylation.
Journal Article
FK228 (Depsipeptide) as a Natural Prodrug That Inhibits Class I Histone Deacetylases
Ryohei Furumai,Akihisa Matsuyama,Nobuyuki Kobashi,Kun-Hyung Lee,Makoto Nishiyama,Hidenori Nakajima,Akito Tanaka,Yasuhiko Komatsu,Norikazu Nishino,Minoru Yoshida,Sueharu Horinouchi +10 more
TL;DR: FK228 serves as a stable prodrug to inhibit class I enzymes and is activated by reduction after uptake into the cells and implicates its clinical usefulness for counteracting glutathione-mediated drug resistance in chemotherapy.