T
Tsutomu Kabashima
Researcher at Nagasaki International University
Publications - 65
Citations - 2127
Tsutomu Kabashima is an academic researcher from Nagasaki International University. The author has contributed to research in topics: Catalytic triad & Peptide sequence. The author has an hindex of 19, co-authored 62 publications receiving 1990 citations. Previous affiliations of Tsutomu Kabashima include Nagasaki University & University of Texas Southwestern Medical Center.
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Journal ArticleDOI
Mechanism for fatty acid "sparing" effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase.
TL;DR: The results strongly suggested that the fatty acid inhibition of glucose-induced l-PK transcription resulted from AMPK phosphorylation of ChREBP at Ser568, which inactivated the DNA binding activity.
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Xylulose 5-phosphate mediates glucose-induced lipogenesis by xylulose 5-phosphate-activated protein phosphatase in rat liver.
TL;DR: The results suggest that (ia) Xu5P-dependent PPase is responsible for activation of transcription of the L-type pyruvate kinase gene and lipogenic enzyme genes, and (ii) Xu 5P is the glucose signaling compound.
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Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein
TL;DR: Mechanisms for regulation of ChREBP and the L-PK transcription by excess carbohydrate and cAMP are revealed.
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Inhibition of HIV-1 protease expression in T cells owing to DNA aptamer-mediated specific delivery of siRNA.
TL;DR: This study provides the first evidence that the DNA aptamer with intrinsic stability has a greater potential to be used for siRNA delivery and specifically enter into CD4(+) T cells specifically.
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Roles of the Ser146, Tyr159, and Lys163 Residues in the Catalytic Action of 7α-Hydroxysteroid Dehydrogenase from Escherichia coli
Tetsurou Tanabe,Nobutaka Tanaka,Kouichiro Uchikawa,Tsutomu Kabashima,Kiyoshi Ito,Takamasa Nonaka,Yukio Mitsui,Masato Tsuru,Tadashi Yoshimoto +8 more
TL;DR: The data presented in this paper confirm that Tyr159 acts as a basic catalyst, that Lys163 binds to NAD(H) and lowers the pKa value of Tyr159, and that Ser146 stabilizes the substrate, reaction intermediate and product in catalysis.