H
Hisashi Umemori
Researcher at Boston Children's Hospital
Publications - 72
Citations - 6826
Hisashi Umemori is an academic researcher from Boston Children's Hospital. The author has contributed to research in topics: Tyrosine phosphorylation & Synapse. The author has an hindex of 36, co-authored 69 publications receiving 6242 citations. Previous affiliations of Hisashi Umemori include Washington University in St. Louis & Molecular and Behavioral Neuroscience Institute.
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Journal ArticleDOI
Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family.
Xiuqin Zhang,Omar A. Ibrahimi,Shaun K. Olsen,Hisashi Umemori,Moosa Mohammadi,David M. Ornitz +5 more
TL;DR: This study completes the mitogenesis-based comparison of receptor specificity of the entire FGF family under standard conditions and should help in interpreting and predicting in vivo biological activity.
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Characterization of Fyn-mediated tyrosine phosphorylation sites on GluRε2 (NR2B) subunit of the N-methyl-D-aspartate receptor
Takanobu Nakazawa,Shoji Komai,Tohru Tezuka,Chihiro Hisatsune,Hisashi Umemori,Kentaro Semba,Masayoshi Mishina,Toshiya Manabe,Tadashi Yamamoto +8 more
TL;DR: Tyr-1472 phosphorylation of GluRε2 was greatly reduced infyn mutant mice and significantly enhanced after induction of long term potentiation in the hippocampal CA1 region, suggesting that Tyr-1336, Tyr-1252, and Tyr- 1472 in Glu Rε2 were phosphorylated in human embryonic kidney fibroblasts when co-expressed with active Fyn, and its magnitude became larger in murine brain.
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Initial events of myelination involve Fyn tyrosine kinase signalling
TL;DR: This paper showed that Fyn tyrosine kinase is activated during the initial stages of myelination and that it is associated with the large myelin-associated glycoprotein (MAG), an adhesion molecule that has been implicated in myelinogenesis.
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PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-d-aspartate receptor subunit NR2A
TL;DR: Results suggest that PSD-95 is critical for regulation of NMDA receptor activity by Fyn and other Src-familyPTKs, serving as a molecular scaffold for anchoring these PTKs to NR2A.
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Negative regulation of BMP/Smad signaling by Tob in osteoblasts.
Yutaka Yoshida,Sakae Tanaka,Hisashi Umemori,Osamu Minowa,Michihiko Usui,Naoko Ikematsu,Eri Hosoda,Takeshi Imamura,Junko Kuno,Teruhito Yamashita,Kohei Miyazono,Masaki Noda,Tetsuo Noda,Tadashi Yamamoto +13 more
TL;DR: It is shown that Tob, a member of the emerging family of antiproliferative proteins, is a negative regulator of BMP/Smad signaling in osteoblasts and negatively regulates osteoblast proliferation and differentiation by suppressing the activity of the receptor-regulated Smad proteins.