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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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Book ChapterDOI

Regulation of oocyte growth and maturation in fish

TL;DR: Of considerable interest is the finding that MIH, unlike most steroid hormones, acts on its receptors at the surface of oocytes, and the mechanism of MIH-induced MPF activation in fish oocytes differs from that in Xenopus and starfish.
Journal ArticleDOI

Cytoplasmic Lipid Droplets Are Sites of Convergence of Proteasomal and Autophagic Degradation of Apolipoprotein B

TL;DR: Observations indicate that both proteasomal and autophagy/lysosomal degradation of ApoB occur around CLDs and that the CLD surface functions as a unique platform for convergence of the two pathways.
Journal ArticleDOI

Induction of Female-to-Male Sex Change in Adult Zebrafish by Aromatase Inhibitor Treatment

TL;DR: Results demonstrated that sex plasticity remains in the mature ovaries of this species.
Journal ArticleDOI

Cloning and identification of a membrane progestin receptor in goldfish ovaries and evidence it is an intermediary in oocyte meiotic maturation

TL;DR: Results with the goldfish mPRalpha protein are similar to those obtained previously with spotted seatrout, further supporting the hypothesis that the mPR alpha acts as an intermediary in MIH induction of oocyte maturation in teleosts.
Journal ArticleDOI

Initiation of Cyclin B Degradation by the 26S Proteasome upon Egg Activation

TL;DR: The results of this study indicate that Mutant cyclin at K57 was resistant to both digestion by the 26S proteasome and degradation at metaphase/anaphase transition in Xenopus egg extracts, indicating that the destruction of cyclin B is initiated by the ATP-dependent and ubiquitin-independent proteolytic activity of 26S Proteasome through the first cutting in the NH2 terminus ofcyclin.