N
Naoya Fujita
Researcher at Japanese Foundation for Cancer Research
Publications - 159
Citations - 12199
Naoya Fujita is an academic researcher from Japanese Foundation for Cancer Research. The author has contributed to research in topics: Cancer & Protein kinase B. The author has an hindex of 58, co-authored 146 publications receiving 11096 citations. Previous affiliations of Naoya Fujita include Pharmaceuticals and Medical Devices Agency & Meiji Pharmaceutical University.
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Journal ArticleDOI
Modulation of Akt kinase activity by binding to Hsp90
TL;DR: Results indicate that Hsp90 plays an important role in maintaining Akt kinase activity by preventing PP2A-mediated dephosphorylation.
Journal ArticleDOI
The ALK Inhibitor Ceritinib Overcomes Crizotinib Resistance in Non–Small Cell Lung Cancer
Luc Friboulet,Nanxin Li,Ryohei Katayama,Christian C. Lee,Justin F. Gainor,Adam S. Crystal,Pierre-Yves Michellys,Mark M. Awad,Noriko Yanagitani,Sungjoon Kim,AnneMarie Culazzo Pferdekamper,Jie Li,Shailaja Kasibhatla,Frank Sun,Xiuying Sun,Su Hua,Peter McNamara,Sidra Mahmood,Elizabeth L. Lockerman,Naoya Fujita,Makoto Nishio,Jennifer L. Harris,Alice T. Shaw,Jeffrey A. Engelman +23 more
TL;DR: The first preclinical evaluation of the next-generation ALK TKI, ceritinib (LDK378), in the setting of crizotinib resistance demonstrates that ceritInib can overcome crizotib resistance, consistent with clinical data showing marked efficacy of cerit inib in patients with crizotonib-resistant disease.
Journal ArticleDOI
Molecular targeting therapy of cancer: drug resistance, apoptosis and survival signal.
Takashi Tsuruo,Mikihiko Naito,Akihiro Tomida,Naoya Fujita,Tetsuo Mashima,Hiroshi Sakamoto,Hiroshi Sakamoto,Naomi Haga +7 more
TL;DR: In this article, a review on molecular cancer therapeutics, including molecular mechanisms and therapeutic approaches, is presented, focusing on the areas of drug resistance, apoptosis and apoptosis resistance, and survival-signaling.
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Rap1 translates chemokine signals to integrin activation, cell polarization, and motility across vascular endothelium under flow
Mika Shimonaka,Mika Shimonaka,Koko Katagiri,Toshinori Nakayama,Naoya Fujita,Takashi Tsuruo,Osamu Yoshie,Tatsuo Kinashi +7 more
TL;DR: It is demonstrated that Rap1 plays a pivotal role in chemokine-induced integrin activation and migration and induced a polarized morphology, accompanied by the redistribution of CXCR4 and CD44 to the leading edge and uropod, respectively.
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Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization.
TL;DR: Akt promotes cell-cycle progression through the mechanisms of phosphorylation-dependent 14-3-3 binding to p27Kip1 and cytoplasmic localization and the COOH-terminal Thr198 residue as a novel site.