F
Fumiko Itoh
Researcher at Tokyo University of Pharmacy and Life Sciences
Publications - 45
Citations - 3051
Fumiko Itoh is an academic researcher from Tokyo University of Pharmacy and Life Sciences. The author has contributed to research in topics: SMAD & Transforming growth factor. The author has an hindex of 23, co-authored 42 publications receiving 2821 citations. Previous affiliations of Fumiko Itoh include Kawasaki Medical School & Netherlands Cancer Institute.
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Journal ArticleDOI
Signaling of transforming growth factor-β family members through Smad proteins
TL;DR: The latest advances in the understanding of the Smad mechanism of action and their in vivo functions are reviewed, with a focus on the function of Smads as signal integrators.
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Regulation of cell proliferation by Smad proteins.
TL;DR: Important activities of TGF‐β are its potent anti‐mitogenic and pro‐apoptotic effects that, at least in part, are mediated via Smad proteins.
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Synergy and antagonism between Notch and BMP receptor signaling pathways in endothelial cells
Fumiko Itoh,Fumiko Itoh,Susumu Itoh,Susumu Itoh,Marie-José Goumans,Gudrun Valdimarsdottir,Tatsuya Iso,G. Paolo Dotto,Yasuo Hamamori,Larry Kedes,Mitsuyasu Kato,Peter ten Dijke +11 more
TL;DR: It is reported that expression of the Notch target gene, Herp2, is synergistically induced upon activation of Notch and BMP receptor signaling pathways in endothelial cells.
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Elucidation of Smad Requirement in Transforming Growth Factor-β Type I Receptor-induced Responses
Susumu Itoh,Midory Thorikay,Marcin Kowanetz,Aristidis Moustakas,Fumiko Itoh,Carl-Henrik Heldin,Peter ten Dijke +6 more
TL;DR: Mutation in the L45 loop region did not affect the binding of inhibitory Smads but did abrogate the weak binding of X-linked inhibitor of apoptosis protein and Disabled-2 to ALK5, which suggests that the L 45 loop in the kinase domain is important for docking of other binding proteins.
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Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads
TL;DR: The identification of a cytoplasmic protein, previously termed associated molecule with the SH3 domain of STAM (AMSH), as a direct binding partner for Smad6 is reported, suggesting that the molecular mechanism by which AMSH exerts its action is by inhibiting the binding of Smad 6 to activated type I receptors or activated R‐Smads.