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Megumi Funakoshi-Tago

Showing results (31-40 of 106) with videos related to

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The EMBO Journal|October 7, 2006
Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2Megumi Funakoshi-Tago, Stephane Pelletier, Tadashi Matsuda, et al.
Cellular Signalling|August 7, 2008
Negative regulation of Jak2 by its auto-phosphorylation at tyrosine 913 via the Epo signaling pathwayMegumi Funakoshi-Tago, Kenji Tago, Tadashi Kasahara, et al.
Cellular Signalling|October 14, 2010
JAK2 is an important signal transducer in IL-33-induced NF-κB activationMegumi Funakoshi-Tago, Kenji Tago, Yoshinori Sato, et al.
European Journal of Biochemistry|March 13, 2003
TRAF6 and C-SRC induce synergistic AP-1 activation via PI3-kinase-AKT-JNK pathwayMegumi Funakoshi-Tago, Kenji Tago, Yoshiko Sonoda, et al.
Molecular and Cellular Biology|September 20, 2006
Two domains of the erythropoietin receptor are sufficient for Jak2 binding/activation and functionStéphane Pelletier, Sébastien Gingras, Megumi Funakoshi-Tago, et al.
Molecular and Cellular Biology|December 28, 2007
Jak2 FERM domain interaction with the erythropoietin receptor regulates Jak2 kinase activityMegumi Funakoshi-Tago, Stéphane Pelletier, Hiroshi Moritake, et al.
Neurochemistry International|September 29, 2023
The citrus flavonoid, nobiletin inhibits neuronal inflammation by preventing the activation of NF-κBTaisuke Murata, Sho Ishiwa, Xin Lin, et al.
European Journal of Pharmacology|February 15, 2018
A major component of vitamin E, α-tocopherol inhibits the anti-tumor activity of crizotinib against cells transformed by EML4-ALKYuki Uchihara, Takayuki Kidokoro, Kenji Tago, et al.
Cellular Signalling|January 1, 2017
Phosphorylated CIS suppresses the Epo or JAK2 V617F mutant-triggered cell proliferation through binding to EpoRMegumi Funakoshi-Tago, Takuro Moriwaki, Fumihito Ueda, et al.
International Journal of Molecular Sciences|April 13, 2024
FL118 Is a Potent Therapeutic Agent against Chronic Myeloid Leukemia Resistant to BCR-ABL Inhibitors through Targeting RNA Helicase DDX5Kengo Takeda, Satoshi Ohta, Miu Nagao, et al.
Pageof 11

Showing results (31-40 of 106) with videos related to

Sort By:
Pageof 11
The EMBO Journal|October 7, 2006
Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2Megumi Funakoshi-Tago, Stephane Pelletier, Tadashi Matsuda, et al.
Cellular Signalling|August 7, 2008
Negative regulation of Jak2 by its auto-phosphorylation at tyrosine 913 via the Epo signaling pathwayMegumi Funakoshi-Tago, Kenji Tago, Tadashi Kasahara, et al.
Cellular Signalling|October 14, 2010
JAK2 is an important signal transducer in IL-33-induced NF-κB activationMegumi Funakoshi-Tago, Kenji Tago, Yoshinori Sato, et al.
European Journal of Biochemistry|March 13, 2003
TRAF6 and C-SRC induce synergistic AP-1 activation via PI3-kinase-AKT-JNK pathwayMegumi Funakoshi-Tago, Kenji Tago, Yoshiko Sonoda, et al.
Molecular and Cellular Biology|September 20, 2006
Two domains of the erythropoietin receptor are sufficient for Jak2 binding/activation and functionStéphane Pelletier, Sébastien Gingras, Megumi Funakoshi-Tago, et al.
Molecular and Cellular Biology|December 28, 2007
Jak2 FERM domain interaction with the erythropoietin receptor regulates Jak2 kinase activityMegumi Funakoshi-Tago, Stéphane Pelletier, Hiroshi Moritake, et al.
Neurochemistry International|September 29, 2023
The citrus flavonoid, nobiletin inhibits neuronal inflammation by preventing the activation of NF-κBTaisuke Murata, Sho Ishiwa, Xin Lin, et al.
European Journal of Pharmacology|February 15, 2018
A major component of vitamin E, α-tocopherol inhibits the anti-tumor activity of crizotinib against cells transformed by EML4-ALKYuki Uchihara, Takayuki Kidokoro, Kenji Tago, et al.
Cellular Signalling|January 1, 2017
Phosphorylated CIS suppresses the Epo or JAK2 V617F mutant-triggered cell proliferation through binding to EpoRMegumi Funakoshi-Tago, Takuro Moriwaki, Fumihito Ueda, et al.
International Journal of Molecular Sciences|April 13, 2024
FL118 Is a Potent Therapeutic Agent against Chronic Myeloid Leukemia Resistant to BCR-ABL Inhibitors through Targeting RNA Helicase DDX5Kengo Takeda, Satoshi Ohta, Miu Nagao, et al.
Pageof 11