Nobuyoshi Shimizu
Keio University
504 Papers
6.6K Citations
Nobuyoshi Shimizu is an academic researcher from Keio University. The author has contributed to research in topics: Gene & Biology. The author has an hindex of 84, co-authored 504 publications. Previous affiliations of Nobuyoshi Shimizu include Juntendo University & Nagahama Institute of Bio-Science and Technology.
Chat about Author
Papers
•Journal Article
Telomerase activity and bcl-2 expression in non-small cell lung cancer
TL;DR: The results suggest that the biological role of the Bcl-2 protein alters according to tumor aggressiveness, thereby cofunctioning with telomerase against genetic instability.
40
Mutant analyses reveal different functions of fgfr1 in medaka and zebrafish despite conserved ligand-receptor relationships.
Hayato Yokoi,Atsuko Shimada,Matthias Carl,Shigeo Takashima,Daisuke Kobayashi,Takanori Narita,Tomoko Jindo,Tetsuaki Kimura,Tadao Kitagawa,Takahiro Kage,Atsushi Sawada,Kiyoshi Naruse,Shuichi Asakawa,Nobuyoshi Shimizu,Hiroshi Mitani,Akihiro Shima,Makiko Tsutsumi,Hiroshi Hori,Joachim Wittbrodt,Yumiko Saga,Yuji Ishikawa,Kazuo Araki,Hiroyuki Takeda +22 more
TL;DR: Results provide evidence that teleost fish have evolved divergent functions of Fgf8-Fgfr1 while maintaining the ligand-receptor relationships, and are invaluable for shedding light on evolutionary diversification of gene function.
40
Evolutionary conservation of a unique amino acid sequence in human DICER protein essential for binding to Argonaute family proteins.
Takashi Sasaki,Nobuyoshi Shimizu +1 more
TL;DR: A unique amino acid sequence of 127 amino acids in the RIBOc-A domain of human DICER protein is identified as a "binding site" to Argonaute proteins, which is highly conserved in the vertebrates, but not found in the non-vertebrate species.
39
Expression of epidermal growth factor (EGF) and the EGF receptor in human tissues.
TL;DR: The EGF-EGF receptor system has been widely examined for signal transduction, control of cell growth and differentiation, and in vivo physiological function and carcinogenesis in human tissues.
38
Binding sites on tau proteins as components for antimicrobial peptides.
TL;DR: The finding demonstrates that the binding sites on tau proteins possess high potential for becoming components in antimicrobial peptides, and could become a useful method in peptide antibiotic research.
38