Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Fujio Sekiya"'
Publikováno v:
Proceedings of the National Academy of Sciences. 102:4276-4281
Phospholipase C-γ1 (PLC-γ1) contains two tandem Src homology 2 (SH2) domains. The NH2-terminal SH2 domain has been known to mediate the binding of PLC-γ1 to receptor protein tyrosine kinases, which then activate PLC-γ1 via phosphorylation at Y783
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::433d67642b29507428e907a49ebd8742
https://doi.org/10.1073/pnas.0409590102
https://doi.org/10.1073/pnas.0409590102
Publikováno v:
Journal of Biological Chemistry. 279:32181-32190
Phospholipase C-gamma 1 (PLC-gamma 1) is phosphorylated on three tyrosine residues: Tyr-771, Tyr-783, and Tyr-1253. With the use of antibodies specific for each of these phosphorylation sites, we have now determined the kinetics and magnitude of phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cac41ce3bce3b33f32427f04e662fb39
https://doi.org/10.1074/jbc.m405116200
https://doi.org/10.1074/jbc.m405116200
Publikováno v:
Journal of Biological Chemistry. 275:6411-6416
Upon stimulation of cells with platelet-derived growth factor (PDGF), phospholipase C-gamma1 (PLC-gamma1) binds to the tyrosine-phosphorylated PDGF receptor through one or both of its Src homology 2 (SH2) domains, is phosphorylated by the receptor ki
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::772b11d7bc4404570a7a65f75d61f4de
https://doi.org/10.1074/jbc.275.9.6411
https://doi.org/10.1074/jbc.275.9.6411
Publikováno v:
Journal of Biological Chemistry. 274:13900-13907
We have recently shown that phospholipase C-gamma (PLC-gamma) is activated by tau, a neuronal cell-specific microtubule-associated protein, in the presence of arachidonic acid. We now report that non-neuronal tissues also contain a protein that can a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe964406fb75be1b4792f64f47928ba5
https://doi.org/10.1074/jbc.274.20.13900
https://doi.org/10.1074/jbc.274.20.13900
Autor:
Heun Soo Kang, Joong-Soo Han, Sue Goo Rhee, Seung Ryul Kim, Chunghee Lee, Andrew J. Morris, Yun Soo Bae, Jae Ryong Kim, Joon Ki Chung, Fujio Sekiya
Publikováno v:
Journal of Biological Chemistry. 272:15986-15992
In the accompanying paper (Chung, J.-K., Sekiya, F., Kang, H.-S., Lee, C., Han, J.-S., Kim, S. R., Bae, Y. S., Morris, A. J., and Rhee, S. G. (1997) J. Biol. Chem. 272, 15980-15985), synaptojanin is identified as a protein that inhibits phospholipase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2fc668027a0101123c32250c64f182a
https://doi.org/10.1074/jbc.272.25.15986
https://doi.org/10.1074/jbc.272.25.15986
Publikováno v:
FEBS Letters. 392:205-208
We demonstrated recently that coagulation factor IX has a specific binding site(s) for Mg2+ ions, independent of the (Ca2+)-binding sites, and that binding of Mg2+ ions is very important for expression of the functional conformation of this protein.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74ee002690f797c71c098a1a97d6d451
https://doi.org/10.1016/0014-5793(96)00813-7
https://doi.org/10.1016/0014-5793(96)00813-7
Publikováno v:
Journal of Biological Chemistry. 271:8541-8544
We recently showed that not only Ca ions but also Mg ions play a crucial role in stabilizing the native conformation of coagulation factor IX. We here report that Mg ions at physiological concentrations greatly augment the biological activities of fa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::31d6991f9a7e5b68ccdf8d7b09f6dbf0
https://doi.org/10.1074/jbc.271.15.8541
https://doi.org/10.1074/jbc.271.15.8541
Publikováno v:
Journal of Biological Chemistry. 271:5200-5207
The venom of the viper Echis carinatus contains a metalloprotease, ecarin, that is a potent prothrombin activator. We here show that the venom is also rich in another prothrombin activator, which does not belong to any known category of prothrombin a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17bc8bf74ef91d3cf00da4cd3d34e847
https://doi.org/10.1074/jbc.271.9.5200
https://doi.org/10.1074/jbc.271.9.5200
Publikováno v:
Journal of Biological Chemistry. 270:14325-14331
The indispensable role of Ca2+ ions in the maintenance of the functional tertiary structures of vitamin K-dependent coagulation factors has been definitively established but the participation of Mg2+ ions, another alkaline-earth metal that is present
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f51ae285a5f42e71988d447c38e3887
https://doi.org/10.1074/jbc.270.24.14325
https://doi.org/10.1074/jbc.270.24.14325
Autor:
Takashi Morita, Fujio Sekiya
Publikováno v:
Japanese Journal of Thrombosis and Hemostasis. 6:485-488
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::564afcc5f432f9189f1e0877e650369b
https://doi.org/10.2491/jjsth.6.485
https://doi.org/10.2491/jjsth.6.485