Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Seiyu Imoto"'
Autor:
Tadashi Matsuda, Yuichi Sekine, Shinya Kamitani, Seiyu Imoto, Ryuta Muromoto, Osamu Ikeda, Norihiko Ohbayashi
Publikováno v:
Biochemical and Biophysical Research Communications. 370(2):359-365
Sma- and MAD-related protein 3 (Smad3) plays crucial roles in the transforming growth factor-beta (TGF-beta)-mediated signaling pathway, which produce a variety of cellular responses, including cell proliferation and differentiation. In our previous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79e45a387f5c21567e3b55559f29acae
http://hdl.handle.net/2115/33892
http://hdl.handle.net/2115/33892
Autor:
Osamu Ikeda, Taichiro Okayama, Yuichi Sekine, Seiyu Imoto, Ryuta Muromoto, Tadashi Matsuda, Noriko Sato
Publikováno v:
International Immunology. 20:395-403
Signal transducers and activators of transcription (STATs) mediate cell proliferation, differentiation, and survival in immune responses, hematopoiesis, neurogenesis, and other biological processes. STAT3, for example, is involved in the epithelialme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9ee47035791c167bddf1bce3b4ed849
https://doi.org/10.1093/intimm/dxm154
https://doi.org/10.1093/intimm/dxm154
Autor:
Seiyu Imoto, Naohito Aoki, Yuichi Sekine, Tadashi Matsuda, Kenji Sugiyama, Osamu Ikeda, Yoshihiro Hayakawa, Satoshi Tsuji
Publikováno v:
Oncogene. 26:6038-6049
In the previous study, we demonstrated the involvement of dual specificity phosphatase 22 (DUSP22/LMW-DSP2) in regulating the leukemia inhibitory factor/interleukin-6/signal transducer and activator of transcription 3-mediated signaling pathway. In t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f893a98c81505b997ac36a81071d31bb
https://doi.org/10.1038/sj.onc.1210426
https://doi.org/10.1038/sj.onc.1210426
Autor:
Shizuo Akira, Ryuta Muromoto, Seiyu Imoto, Yuichi Sekine, Noriko Sato, Tadashi Matsuda, Taro Kawai, Tadashi Watanabe, Masato Ishida, Nobuyuki Kamada, Norihiko Ohbayashi, Kenji Sugiyama
Publikováno v:
Immunology Letters. 103(2):127-134
Zipper-interacting protein kinase (ZIPK) is a widely expressed serine/threonine kinase that has been implicated in cell death and transcriptional regulation, but its mechanism of regulation remains unknown. Here, we identified threonine-265 (Thr265)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaeba78fe6c6b018a7308038ae0f3dcf
http://hdl.handle.net/2115/8407
http://hdl.handle.net/2115/8407
Autor:
Noriko Sato, Tadashi Matsuda, Yuichi Sekine, Ryuta Muromoto, Kenji Sugiyama, Seiyu Imoto, Rieko Tsuruma
Publikováno v:
Biochemical and Biophysical Research Communications. 336(2):617-624
Signal transducer and activator of transcription 3 (STAT3), which mediates biological actions in many physiological processes, is activated by cytokines and growth factors via specific tyrosine phosphorylation, dimerization, and nuclear translocation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78909db87fe73eed188d1b5e5f6afcb0
http://hdl.handle.net/2115/22106
http://hdl.handle.net/2115/22106
Publikováno v:
Biochemical and Biophysical Research Communications. 319:275-282
Bone morphogenetic proteins (BMPs) play central roles in differentiation, development, and physiologic tissue remodeling. Recently, we have demonstrated that a protein inhibitor of activated STAT, PIASy, suppresses TGF-β signaling by interacting wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e133fa3b868117100c1950718eac1edd
https://doi.org/10.1016/j.bbrc.2004.04.161
https://doi.org/10.1016/j.bbrc.2004.04.161
Publikováno v:
Journal of Biological Chemistry. 278:34253-34258
Smads proteins play a key role in the intracellular signaling of the transforming growth factor (TGF)-beta family of growth factors, which exhibits a diverse set of cellular responses, including cell proliferation and differentiation. In particular,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4860e25f7c5dab437f8daf6396a323ac
https://doi.org/10.1074/jbc.m304961200
https://doi.org/10.1074/jbc.m304961200
Publikováno v:
Biochemical Journal. 374:261-268
XB51 (derived from X11-like binding protein of clone number 51) was isolated by yeast two-hybrid cDNA screening using the N-terminal domain of X11L (X11-like protein) as a bait. X11L is a neuron-specific adaptor protein that is known to down-regulate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c03cd471b2db13799b2ab3bf07ff245
https://doi.org/10.1042/bj20030489
https://doi.org/10.1042/bj20030489
Molecular interactions between STAT3 and protein inhibitor of activated STAT3, and androgen receptor
Autor:
Hideki Fuse, Tadashi Matsuda, Taro Yumioka, Akira Junicho, Noriko Sato, Seiyu Imoto, Yuichi Sekine, Takashi Yamamoto
Publikováno v:
Biochemical and Biophysical Research Communications. 306(2):610-615
STAT3 mainly acts as a signal transducer of IL-6 family cytokines and transcriptionally activates specific target genes. The recently discovered protein inhibitor of activated STAT3 (PIAS3) binds directly to STAT3 and blocks transcriptional activatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::551c2370010dc8fd37844d1466f024a9
http://hdl.handle.net/2115/28119
http://hdl.handle.net/2115/28119
Autor:
Shizuo Akira, Kenji Sugiyma, Takashi Yamamoto, Tadashi Matsuda, Seiyu Imoto, Kazuya Shimoda, Taro Yumioka, Kenji Oritani, Yuichi Sekine, Akihiko Yoshimura, Ryuta Muromoto, Mayu Minoguchi
Publikováno v:
ResearcherID
Signal-transducing adaptor protein-2 (STAP-2) is a recently identified adaptor protein that contains pleckstrin and Src homology 2-like domains as well as a YXXQ motif in its C-terminal region. Our previous studies have demonstrated that STAP-2 binds
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d360180267de534748d261684a4c292d
https://pubmed.ncbi.nlm.nih.gov/16365431
https://pubmed.ncbi.nlm.nih.gov/16365431