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Toshinobu Tokumoto

Researcher at Shizuoka University

Publications -  93
Citations -  2013

Toshinobu Tokumoto is an academic researcher from Shizuoka University. The author has contributed to research in topics: Oocyte & Zebrafish. The author has an hindex of 21, co-authored 87 publications receiving 1823 citations. Previous affiliations of Toshinobu Tokumoto include University of Texas at Austin & Graduate University for Advanced Studies.

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Fine selection of up-regulated genes during ovulation by in vivo induction of oocyte maturation and ovulation in zebrafish

TL;DR: In vivo induction techniques that permit the induction of oocyte maturation and ovulation in living zebrafish (in vivo assays) were used to select highly up-regulated genes (genes associated with ovulation) and made it possible for the first time to distinguish maturation-inducing genes from ovulation- inducing genes.
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Identification of α-type subunits of the Xenopus 20S proteasome and analysis of their changes during the meiotic cell cycle

TL;DR: Six of α-type subunits of the Xenopus 26S proteasome are modified in Xenopus immature oocytes and two subunits are modified meiotic cell cycle-dependently.
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The Role of DNA Methylation Reprogramming during Sex Determination and Transition in Zebrafish.

TL;DR: In this article, the authors used zebrafish to investigate DNA methylation reprogramming during juvenile germ cell development and adult female-to-male sex transition, and they found that methylation plays important roles in zebra fish embryo development and sexual plasticity.
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The cytoskeleton-dependent localization of cdc2/cyclin B in blastomere cortex during Xenopus embryonic cell cycle.

TL;DR: The distribution of several regulating factors for cell cycles around MBT was investigated using immunocytochemistry and confocal fluorescence microscopy and it is possible that the cortical MPF activity is regulated by the differential localization between cdc2 and cyclin B.
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Functional and biochemical characterization of the 20S proteasome in a yeast temperature-sensitive mutant, rpt6-1

TL;DR: Two α-subunits (α1 and α7) of the 20S proteasome in the rpt6-1 mutant differed from their wild-type counterparts and peptidase activities were found to be lower in the mutant than in the wild- type strain.