S
Shunichi Shimasaki
Researcher at University of California, San Diego
Publications - 164
Citations - 17381
Shunichi Shimasaki is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Granulosa cell & Follistatin. The author has an hindex of 71, co-authored 164 publications receiving 16797 citations. Previous affiliations of Shunichi Shimasaki include Scripps Health & McGill University.
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Journal ArticleDOI
Pituitary FSH is released by a heterodimer of the β-subunits from the two forms of inhibin
Nicholas Ling,Shao-Yao Ying,Naoto Ueno,Shunichi Shimasaki,Frederick Esch,Mari Hotta,Roger Guillemin +6 more
TL;DR: It is proposed that the FSH-releasing substance, which is active in picomolar concentrations, is a heterodimeric protein composed of the two β-subunits of inhibins A and B linked by interchain disulphide bond(s).
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The bone morphogenetic protein system in mammalian reproduction
TL;DR: The physiological importance of the BMP system for mammalian reproduction has been further highlighted by the elucidation of the aberrant reproductive phenotypes of animals with naturally occurring mutations or targeted deletions of certain BMP family genes.
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Identification and molecular characterization of insulin-like growth factor binding proteins (IGFBP-1, -2, -3, -4, -5 and -6).
Shunichi Shimasaki,Nicholas Ling +1 more
TL;DR: In this paper, six different insulin-like growth factor binding proteins (IGFBPs) have been identified by molecular cloning of their cDNAs from rat and human tissues and designated as IGFBP-1, -2, -3, -4, -5 and -6.
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Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo
Shun-ichiro Iemura,Takamasa S. Yamamoto,Chiyo Takagi,Hideho Uchiyama,Tohru Natsume,Shunichi Shimasaki,Hiromu Sugino,Naoto Ueno +7 more
TL;DR: The results suggest that follistatin acts as an organizer factor in early amphibian embryogenesis by inhibiting BMP activities by a different mechanism from that used by chordin and noggin.
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Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone.
TL;DR: A Mr 35,000 protein with follicle-stimulating hormone release-inhibitory activity was isolated from porcine ovarian follicular fluid by heparin-Sepharose affinity chromatography, gel filtration on Sephacryl S-200, and multiple steps of high-performance liquid chromatography to signify its structural difference from inhibin.