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Kiyoshi Okamoto

Researcher at Eisai

Publications -  27
Citations -  1253

Kiyoshi Okamoto is an academic researcher from Eisai. The author has contributed to research in topics: Lenvatinib & Angiogenesis. The author has an hindex of 10, co-authored 27 publications receiving 1010 citations.

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Antitumor Activity of Lenvatinib (E7080): An Angiogenesis Inhibitor That Targets Multiple Receptor Tyrosine Kinases in Preclinical Human Thyroid Cancer Models

TL;DR: Data demonstrate that lenvatinib provides antitumor activity mainly via angiogenesis inhibition but also inhibits FGFR and RET signaling pathway in preclinical human thyroid cancer models.
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Antitumor activities of the targeted multi-tyrosine kinase inhibitor lenvatinib (E7080) against RET gene fusion-driven tumor models.

TL;DR: It is demonstrated that lenvatinib can exert antitumor activity againstRET gene fusion-driven tumor models by inhibiting oncogenic RET gene fusion signaling.
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Eribulin mesylate reduces tumor microenvironment abnormality by vascular remodeling in preclinical human breast cancer models.

TL;DR: It is shown that eribulin induces remodeling of tumor vasculature through a novel antivascular activity in MX‐1 and MDA‐MB‐231 human breast cancer xenograft models, suggesting that Eribulin‐induced remodelling of abnormal tumor vasculation leads to a more functional microenvironment that may reduce the aggressiveness of tumors due to elimination of inner tumor hypoxia.
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Pladienolides, New Substances from Culture of Streptomyces platensis Mer-11107 : III. In Vitro and In Vivo Antitumor Activities

TL;DR: Seven novel 12-membered macrolides from Streptomyces platensis Mer-11107 are discovered, with pladienolide B the most potently inhibiting hypoxia induced-VEGF expression and proliferation of the U251 cancer cell line, and appear to have major potential for use in cancer treatment.
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Distinct binding mode of multikinase inhibitor lenvatinib revealed by biochemical characterization.

TL;DR: Kinetic analysis and X-ray analysis suggest that lenvatinib is very distinct in its binding mode of interaction compared to the several approved VEGFR2 kinase inhibitors.