S
Sumio Shinoda
Researcher at Okayama University
Publications - 182
Citations - 4958
Sumio Shinoda is an academic researcher from Okayama University. The author has contributed to research in topics: Vibrio vulnificus & Vibrio parahaemolyticus. The author has an hindex of 36, co-authored 178 publications receiving 4665 citations. Previous affiliations of Sumio Shinoda include Okayama University of Science.
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Interactions between chromosomal omnipotent suppressors and extrachromosomal effectors in Saccharomyces cerevisiae.
Bun ichiro Ono,Yury O. Chernoff,Yury O. Chernoff,Yumiko Ishino-Arao,Noriko Yamagishi,Sumio Shinoda,Sergey G. Inge-Vechtomov +6 more
TL;DR: SUP46, SUP138 and SUP139 acted as dominant omnipotent suppressors in the ψ− cytoplasm though their suppressor activity was substantially reduced, and a multicopy plasmid carrying the wild-type SUP35 gene enhanced the efficiency of sup111 in ψ+ cy toplasm.
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Lateral flagella of vibrios: serological classification and genetical similarity.
TL;DR: Results suggest conservation of DNA sequence of the L‐flagellar gene of vibrios, which was demonstrated by dot blot hybridization test with a DNA probe of HL2 L‐ FlageLLar gene fragment.
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Purification and Some Properties of a Novel l-2,4-Diaminobutyric Acid Decarboxylase from Vibrio alginolyticus
TL;DR: Cultivation of this bacterium in the presence of added DABA brought about increased production of norspermidine (NSPD), characteristically present in this species as well as DAP, suggesting that the enzyme may be functionally implicated in the formation of D AP, a biosynthetic precursor of NSPD.
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Purification and properties of carboxynorspermidine decarboxylase, a novel enzyme involved in norspermidine biosynthesis, from Vibrio alginolyticus
TL;DR: A novel enzyme which catalyses the decarboxylation of carboxynorspermidine to yield nors permidine, one of the unusual polyamines, was purified to apparent homogeneity (3100-fold) from cells of Vibrio alginolyticus.
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Molecular cloning and functional analysis of cytochrome P450 1A2 from Japanese monkey liver: comparison with marmoset cytochrome P450 1A2.
Shizuo Narimatsu,Maiko Oda,Hiroyuki Hichiya,Takashi Isobe,Kazuo Asaoka,Nobumitsu Hanioka,Shigeru Yamano,Sumio Shinoda,Shigeo Yamamoto +8 more
TL;DR: Kinetic studies demonstrated that the enzymatic properties as ER and PN O-deethylases were considerably different between the Japanese monkey and the marmoset CYP1A2, and it was suggested that Japanese monkey CYP 1A2 is a high-K(m) enzyme in both ER andPN O -deethylations, whereas marmosett CYP