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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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Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine in Vibrio alginolyticus.

TL;DR: Carboxynorspermidine synthase, mediates the nicotinamide-nucleotide-linked reduction of the Schiff base H2N(CH2)3N = CHCH2CH(NH2)COOH, an intermediate in the novel pathway for nSPD (NSPD) biosynthesis.
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Haemolysin produced by Vibrio mimicus activates two Cl- secretory pathways in cultured intestinal-like Caco-2 cells.

TL;DR: VMH stimulates Caco‐2 cells to secrete Cl– by activating both Ca2+‐dependent and cAMP‐dependent Cl– secretion mechanisms, and may be important therapeutic targets with regard to the diarrhoea that is induced by Vibrio mimicus.
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Protective immunity by oral immunization with heat‐killed Shigella strains in a guinea pig colitis model

TL;DR: Data indicate that a hexavalent mixture of heat‐killed cells of the six Shigella serogroups/serotypes studied would be a possible broad‐spectrum candidate vaccine against shigellosis.
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Properties of the membrane-bound 5'-nucleotidase and utilization of extracellular ATP in Vibrio parahaemolyticus.

TL;DR: It is concluded that extracellular ATP and other 5'-nucleotides are cleaved by the membrane-bound 5'- nucleotidase outside the cells and that the adenosine produced is then utilized.
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Isolation and partial characterization of a compound with siderophore activity from Vibrio parahaemolyticus.

TL;DR: A compound with siderophore activity was purified by successive column and thin layer chromatographic procedures from Dowex 1 x 8 extracts of culture supernatants of Vibrio parahaemolyticus AQ 3354 and indicated a prominent ion at m/z 477, probably corresponding to [M + 1] ion.