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Naotaka Hamasaki
Researcher at Kyushu University
Publications - 8
Citations - 1240
Naotaka Hamasaki is an academic researcher from Kyushu University. The author has contributed to research in topics: Protein S & Mutant. The author has an hindex of 8, co-authored 8 publications receiving 1181 citations.
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Mitochondrial DNA damage and dysfunction associated with oxidative stress in failing hearts after myocardial infarction.
Tomomi Ide,Hiroyuki Tsutsui,Shunji Hayashidani,Dongchon Kang,Nobuhiro Suematsu,Kei-ichiro Nakamura,Hideo Utsumi,Naotaka Hamasaki,Akira Takeshita +8 more
TL;DR: It is hypothesized that ROS may induce mitochondrial DNA (mtDNA) damage, which leads to defects of mtDNA-encoded gene expression and respiratory chain complex enzymes and thus may contribute to the progression of left ventricular remodeling and failure after myocardial infarction.
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Genetic variants of IL-13 signalling and human asthma and atopy
Andrea Heinzmann,X. Q. Mao,Mina Akaiwa,R. T. Kreomer,Peisong Gao,Koichi Ohshima,R. Umeshita,R. Umeshita,Yoshito Abe,Sandra Braun,Tetsuji Yamashita,Mark H. Roberts,Rie Sugimoto,Kazuhiko Arima,Yojiro Arinobu,Bin Yu,S. Kruse,Tadao Enomoto,Y. Dake,M. Kawai,S. Shimazu,S. Sasaki,Chaker N. Adra,M. Kitaichi,Hiroshi Inoue,Kohei Yamauchi,Nobukazu Tomichi,Fumihiko Kurimoto,Naotaka Hamasaki,Julian M. Hopkin,Kenji Izuhara,T. Shirakawa,Klaus A. Deichmann +32 more
TL;DR: Detailed molecular modelling analyses indicate that residue 110 of IL-13, the site of the charge-modifying variants Arg and Gln, is important in the internal constitution of the ligand and crucial in ligand-receptor interaction, likely to be important promoters of human asthma.
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Four missense mutations identified in the protein S gene of thrombosis patients with protein S deficiency: effects on secretion and anticoagulant activity of protein S.
Hiroko Tsuda,Michiyo Urata,Tomohide Tsuda,Machiko Wakiyama,Hiroko Iida,Mutsuko Nakahara,Sachiko Kinoshita,Naotaka Hamasaki +7 more
TL;DR: Results indicate that the Y595C and the K155E mutations are responsible for a secretion defect and a decreased anticoagulant activity of PS, respectively.
Journal ArticleDOI
The N-terminal region of the transmembrane domain of human erythrocyte band 3: Residues critical for membrane insertion and transport activity
TL;DR: It is found that the hydrophobic length of TM1 was critical for membrane insertion and that formation of a transport-active structure also depended on the presence of specific amino acid sequences in TM1.
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A case of congenital afibrinogenemia : Fibrinogen Hakata, a novel nonsense mutation of the fibrinogen γ-chain gene
Hiroko Iida,Eiichi Ishii,Mutsuko Nakahara,Michiyo Urata,Machiko Wakiyama,Masako Kurihara,Kumiko Watanabe,Takeshi Kai,Kenji Ihara,Sachiko Kinoshita,Naotaka Hamasaki +10 more
TL;DR: Congenital afibrinogenemia due to a novel homozygous nonsense mutation of the fibrinagen gamma-chain gene, fibr inogen Hakata, was found in an 18-year-old Japanese girl who had received supplemental fibrInogen therapy since she was 4 months old.