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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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Gambierol: A New Toxic Polyether Compound Isolated from the Marine Dinoflagellate Gambierdiscus toxicus.

TL;DR: This paper showed that the act of binding to one sequence precludes the binding of the other, even though the necessary bases are unpaired in the loops of the unbound nine-base domains.
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Convergent synthesis of the FGHI ring system of yessotoxin: Stereoselective construction of the G ring

TL;DR: In this paper, a convergent synthetic route to the FGHI ring system of yessotoxin, a marine ladder polyether, has been developed, which features convergent coupling of the diol and the aldehyde to form α-cyano ethers via acetal formation followed by ring closing metathesis and reductive etherification to construct the oxocane ring G and tetrahydropyran ring H.
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Synthesis of 28-19F-amphotericin B methyl ester

TL;DR: A fluorinated amphotericin B (AmB) derivative, 28-19F-AmB methyl ester (3), labeled at the polyene moiety, was synthesized by combining chemical synthesis with degradation of a natural product via cross-coupling reactions and macrolactonization as discussed by the authors.
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Amphotericin B Dimers with Bisamide Linkage Bearing Powerful Membrane-Permeabilizing Activity

TL;DR: Covalently linked dimers of amphotericin B were prepared by cross-linking its carboxylic acid, and a dimer with a linkage of 1,6-hexanediamine revealed potent hemolytic activity while its N-acetyl derivative gave rise to large K+ ion flux in phosphatidylcholine liposomes, suggesting that the dimers may serve as a tool for elucidating the structure of the ion channel assemblage formed by amph
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Evidence of lipid rafts based on the partition and dynamic behavior of sphingomyelins.

TL;DR: A review of the recent advances in microscopic techniques to visualize the partition and dynamic behavior of SMs, disclosing the detailed structure of lipid rafts and elucidate the importance of SM-SM interactions in the stabilization of signaling platforms as lipid rafting.