M
Michio Murata
Researcher at Osaka University
Publications - 299
Citations - 11594
Michio Murata is an academic researcher from Osaka University. The author has contributed to research in topics: Maitotoxin & Lipid bilayer. The author has an hindex of 50, co-authored 288 publications receiving 10668 citations. Previous affiliations of Michio Murata include Kitasato University & Tohoku University.
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Journal ArticleDOI
Membrane permeabilizing activity of amphotericin B is affected by chain length of phosphatidylcholine added as minor constituent.
Shigeru Matsuoka,Michio Murata +1 more
TL;DR: Clear distinction between the C(12) and C(14) lipids implies that molecular interaction between phospholipid and AmB is partly due to the matching of their hydrophobic length.
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Water‐Mediated Recognition of Simple Alkyl Chains by Heart‐Type Fatty‐Acid‐Binding Protein
Shigeru Matsuoka,Shigeru Sugiyama,Daisuke Matsuoka,Mika Hirose,Sébastien Lethu,Hikaru Ano,Toshiaki Hara,Osamu Ichihara,S. Roy Kimura,Satoshi Murakami,Hanako Ishida,Eiichi Mizohata,Tsuyoshi Inoue,Michio Murata +13 more
TL;DR: A newly developed calorimetric method is employed for comprehensively evaluating the affinity of FAs, sub-Angstrom X-ray crystallography to accurately determine their 3D structure, and energy calculations of the coexisting water molecules using the computer program WaterMap to gain a general understanding of how proteins recognize diverse lipids with different chain lengths.
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Cloning of modular type I polyketide synthase genes from salinomycin producing strain of Streptomyces albus.
TL;DR: Cloning of polyether polyketide synthase (PKS) genes for salinomycin biosynthetic gene cluster of Streptomyces albus showed high homology with bacterial type I PKSs and was deduced to code for KS, malonyl transferase, and ketoreductase motifs.
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Affinity of okadaic acid to type-1 and type-2A protein phosphatases is markedly reduced by oxidation of its 27-hydroxyl group.
TL;DR: The model of the three-dimensional conformation of OA appears to be present in a position relatively free from intramolecular bonding formation, in comparison with the other three hydroxyl groups, which may imply that the 27-hydroxyl group serves as a binding site with the phosphatase molecules.
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Interaction between the marine sponge cyclic peptide theonellamide A and sterols in lipid bilayers as viewed by surface plasmon resonance and solid-state (2)H nuclear magnetic resonance.
Rafael A. Espiritu,Nobuaki Matsumori,Michio Murata,Shinichi Nishimura,Hideaki Kakeya,Shigeki Matsunaga,Minoru Yoshida +6 more
TL;DR: This study demonstrates that TNM-A directly recognizes the 3β-OH moiety of sterols, which greatly facilitates its binding to bilayer membranes.