H
Hiroko Murakami
Researcher at Sumitomo Chemical
Publications - 32
Citations - 3877
Hiroko Murakami is an academic researcher from Sumitomo Chemical. The author has contributed to research in topics: Reductase & Cytochrome. The author has an hindex of 16, co-authored 32 publications receiving 3757 citations.
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Journal ArticleDOI
Visfatin: a protein secreted by visceral fat that mimics the effects of insulin.
Atsunori Fukuhara,Morihiro Matsuda,Masako Nishizawa,Katsumori Segawa,Masaki Tanaka,Kae Kishimoto,Yasushi Matsuki,Mirei Murakami,Tomoko Ichisaka,Hiroko Murakami,Eijiro Watanabe,Toshiyuki Takagi,Megumi Akiyoshi,Tsuguteru Ohtsubo,Shinji Kihara,Shizuya Yamashita,Makoto Makishima,Tohru Funahashi,Shinya Yamanaka,Ryuji Hiramatsu,Yuji Matsuzawa,Iichiro Shimomura,Iichiro Shimomura +22 more
TL;DR: A newly identified adipocytokine, visfatin, that is highly enriched in the visceral fat of both humans and mice and whose expression level in plasma increases during the development of obesity is isolated.
Journal ArticleDOI
Visfatin : A protein secreted by visceral fat that mimics the effects of insulin
Atsunori Fukuhara,Morihiro Matsuda,Masako Nishizawa,Katsumori Segawa,Masaki Tanaka,Kae Kishimoto,Yasushi Matsuki,Mirei Murakami,Tomoko Ichisaka,Hiroko Murakami,Eijoro Watanabe,Toshiyuki Takagi,Megumi Akiyoshi,Tsuguteru Ohtsubo,Shinji Kiliara,Shizuya Yamashita,Makoto Makishima,Tohru Funahashi,Shinya Yamanaka,Ryuji Hiramatsu,Yuji Matsuzawa,Iichiro Shimomura +21 more
TL;DR: A newly identified adipocytokine, visfatin, that is highly enriched in the visceral fat of both humans and mice and whose expression level in plasma increases during the development of obesity is isolated.
Journal ArticleDOI
Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC
TL;DR: A full-length cDNA coding for 3-methylcholanthrene-inducible rat liver cytochrome P-450MC was constructed by the method of Okayama and Berg and revealed the amino acid sequence was composed of 523 amino acid residues, including the initial 22 N-terminal amino acids whose sequence was determined with the purified protein.
Journal ArticleDOI
A genetically engineered P450 monooxygenase: construction of the functional fused enzyme between rat cytochrome P450c and NADPH-cytochrome P450 reductase.
TL;DR: Results clearly indicate that the fused enzyme is a new self-catalytic P450 monooxygenase.
Journal ArticleDOI
Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene.
TL;DR: The possible functional domains related to binding of FAD, FMN, and NADPH were well conserved among all five species compared and showed 33-34% similarity with those of the rat, rabbit, pig, and trout reductases.