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Study for grain-filling of rice using 13C labeling flow-metabolome analysis
Okamura Masaki,Hirai Masami Yokota,Sawada Yuji,Okamoto Mami,Arai-Sanoh Yumiko,Yoshida Hiroe,Mukouyama Takehiro,Adachi Shunsuke,Fushimi Erina,Yabe Shiori,Nakagawa Hiroshi,Kobayashi Nobuya,Kondo Motohik 한국작물학회 2017 한국작물학회 학술발표대회 논문집 Vol.2017 No.-
Recent Trends in Elevator Group Control Systems
Sandor Markon,Ken’ichi Aoki,Masami Nakagawa,Takeshi Sudo 대한전자공학회 2008 ITC-CSCC :International Technical Conference on Ci Vol.2008 No.7
The latest elevator systems have structural differences from traditional systems, such as the use of destination calls, or multiple cars in the same hoistway. This requires the development of new elevator group control systems, which is best done by adopting modern soft-computing methods. We review some of these systems and the results of research so far, and suggest further directions of research.
Kazuhisa, Nakayama,Toshio, Watanabe,Tsutomu, Nakagawa,Kim, Won Sin,Masami, Nagahama,Masahiro, Hosaka,Kiyotaka, Hatsuzawa,Kiyomi, Kondoh-Hashiba,Kazuo, Murakami 圓光大學校 基礎自然科學硏究所 1993 基礎科學硏究誌 Vol.12 No.2
Many peptide hormones and neuropeptides are produced from larger, inactive precursors though endoproteolysis at sites usually marked by paired basic residues (primarily Lys-Arg and Arg-Arg), or occasionally by a monobasic residue (primarily Arg). Based upon data concerning processing of prorenin and its mutants around the native Lys-Arg cleavage site expressed in mouse pituitary AtT-20 cells, we present the following sequence rules that govern mono-arginyl cleavages: (a) a basic residue at the fourth (position-4) or the sixth(position-6) residue upstream of the cleavage site is required, (b) at position - 4, Arg ; more favorable than Lys, and (c) at position I, a hydrophobic aliphatic residue is not suitable. These rules are compatible with those proposed by comparison of precursor sequences around mono-arginyl cleavage sites. We also provide evidence that precursor cleavages at mono-arginly and dibasic sites can be catalyzed by the same Kex2-like processing endoprotease, PC1/PC3.