T
Tadashi Yamamoto
Researcher at Okinawa Institute of Science and Technology
Publications - 626
Citations - 41630
Tadashi Yamamoto is an academic researcher from Okinawa Institute of Science and Technology. The author has contributed to research in topics: Tyrosine phosphorylation & Gene. The author has an hindex of 102, co-authored 612 publications receiving 40060 citations. Previous affiliations of Tadashi Yamamoto include American Cyanamid & University of Tokyo.
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Journal ArticleDOI
Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
Dusko Ilic,Yasuhide Furuta,Satoshi Kanazawa,Naoki Takeda,Kenji Sobue,Norio Nakatsuji,S Nomura,Jiro Fujimoto,Masato Okada,Tadashi Yamamoto +9 more
TL;DR: Surprisingly, the number of focal adhesions was increased in FAK-deficient cells, suggesting that FAK may be involved in the turnover of focalAdhesion contacts during cell migration.
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Similarity of protein encoded by the human c-erb-B-2 gene to epidermal growth factor receptor.
Tadashi Yamamoto,Shuntaro Ikawa,Tetsu Akiyama,Tetsu Akiyama,Kentaro Semba,Nobuo Nomura,Nobuo Nomura,Nobuyuki Miyajima,Toshiyuki Saito,Kumao Toyoshima +9 more
TL;DR: Its sequence shows that the c-erb-B-2 gene encodes a possible receptor protein and allows an analysis of the similarity of the protein to the EGF receptor and the neu product.
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A cAMP-response element binding protein-induced microRNA regulates neuronal morphogenesis
Ngan Vo,Matthew E. Klein,Matthew E. Klein,Olga Varlamova,David M. Keller,Tadashi Yamamoto,Richard H. Goodman,Soren Impey +7 more
TL;DR: Evidence is provided that miR132 regulates neuronal morphogenesis by decreasing levels of the GTPase-activating protein, p250GAP, which reveals that a CREB-regulated miRNA regulates neuronal Morphogenesis by responding to extrinsic trophic cues.
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The product of the human c-erbB-2 gene: a 185-kilodalton glycoprotein with tyrosine kinase activity.
TL;DR: Although the c-erbB-2 protein was predicted to encode a protein very similar to epidermal growth factor (EGF) receptor, EGF did not stimulate this kinase activity either in vivo or in vitro.
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Molecular Characterization of ALK, a Receptor Tyrosine Kinase Expressed Specifically in the Nervous System
Toshinori Iwahara,Jiro Fujimoto,Duanzhi Wen,Rod Cupples,Nathan Bucay,Tsutomu Arakawa,Shigeo Mori,Barry J. Ratzkin,Tadashi Yamamoto +8 more
TL;DR: Molecular cloning of cDNAs for both the human and mouse ALK proteins reveal that ALK is a novel receptor protein-tyrosine kinase having a putative transmembrane domain and an extracellular domain and shows the greatest sequence similarity to LTK (leukocyte tyrosine Kinase) whose biological function is presently unknown.