Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Tanaka, Taiki*; Narikiyo, Yoshihiro*; Morita, Kosuke*; Fujita, Kunihiro*; Kaji, Daiya*; Morimoto, Koji*; Yamaki, Sayaka*; Wakabayashi, Yasuo*; Tanaka, Kengo*; Takeyama, Mirei*; et al.
Journal of the Physical Society of Japan, 87(1), p.014201_1 - 014201_9, 2018/01
Times Cited Count:18 Percentile:74.47(Physics, Multidisciplinary)Excitation functions of quasielastic scattering cross sections for the Ca + Pb, Ti + Pb, and Ca + Cm reactions were successfully measured by using the gas-filled recoil-ion separator GARIS. Fusion barrier distributions were extracted from these data, and compared with the coupled-channels calculations. It was found that the peak energies of the barrier distributions for the Ca + Pb and Ti + Pb systems coincide with those of the 2n evaporation channel cross sections for the systems, while that of the Ca + Cm is located slightly below the 4n evaporation ones. This results provide us helpful information to predict the optimum beam energy to synthesize superheavy nuclei.
Yamazaki, Yuji*; Tamada, Taro; Kasai, Noriyuki*; Urakawa, Itaru*; Aono, Yukiko*; Hasegewa, Hisashi*; Fujita, Toshiro*; Kuroki, Ryota; Yamashita, Takeyoshi*; Fukumoto, Seiji*; et al.
Journal of Bone and Mineral Research, 23(9), p.1509 - 1518, 2008/09
Times Cited Count:150 Percentile:94.53Fibroblast growth factor (FGF)23 is proposed to play a physiological role in the regulation of phosphate and vitamin D metabolism; deranged circulatory levels of FGF23 cause several diseases with abnormal mineral metabolism. We developed two antibodies (FN1 and FC1) that recognize the N- and C-terminal regions of FGF23, respectively. Both FN1 and FC1 inhibited FGF23 activity in a cell-based Klotho-dependent reporter assay. The present study using neutralizing antibodies confirms that FGF23 is a physiological regulator of phosphate and vitamin D metabolism. Then, we addressed the mechanism of action for these neutralizing antibodies. Structural analysis of the FGF23/FN1-Fab complex revealed that FN1 masked putative FGF receptor-binding sites in the N-terminal domain of FGF23, while biochemical analyses showed that FC1 interfered with the association between FGF23 and Klotho by binding to the C-terminal domain of FGF23. Taken together, our results suggest that the N- and C-terminal domains of FGF23 are responsible for association with cognate FGF receptors and Klotho, respectively, and that these interactions are indispensable for FGF23 activity.
Yonezawa, Chushiro*; Kakita, Kazutoshi*; Takahashi, Takanori*; Aono, Tatsuo*; Maeda, Satoshi; Abe, Takaaki*; Arakawa, Fumihiro*; Kiho, Nobuharu*; Akiyama, Masakazu*; Muramatsu, Isamu*; et al.
no journal, ,
no abstracts in English