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Yasuo Mori

Researcher at Kyoto University

Publications -  414
Citations -  29254

Yasuo Mori is an academic researcher from Kyoto University. The author has contributed to research in topics: Transient receptor potential channel & Voltage-dependent calcium channel. The author has an hindex of 84, co-authored 386 publications receiving 26817 citations. Previous affiliations of Yasuo Mori include Laboratory of Molecular Biology & University of Cincinnati.

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Primary structure and functional expression of the cardiac dihydropyridine-sensitive calcium channel

TL;DR: It is shown that messenger RNA derived from the cardiac DHP receptor cDNA is sufficient to direct the formation of a functional DHP-sensitive calcium channel in Xenopus oocytes, and higher calcium-channel activity is observed when mRNA specific for the polypeptide of relative molecular mass associated with the skeletal muscle DHP receptors is co-injected.
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Primary structure and functional expression from complementary dna of a brain calcium channel

TL;DR: The primary structure of a voltage-dependent cal-cium channel from rabbit brain has been deduced by cloning and sequencing the complementary DNA and it is suggested that it is expressed predominantly in cerebellar Purkinje cells and granule cells.
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Time-reversal symmetry-breaking superconductivity in Sr2RuO4

TL;DR: In this paper, the spontaneous appearance of an internal magnetic field below the transition temperature of the superconductor Sr2RuO4 was observed, which indicated that the superconducting state in this material is characterized by the breaking of time-reversal symmetry.
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LTRPC2 Ca2+-permeable channel activated by changes in redox status confers susceptibility to cell death

TL;DR: It is reported that a widely expressed Ca2+-permeable cation channel, LTRPC2, activated by micromolar levels of H2O2 and agents that produce reactive oxygen/nitrogen species represents an important intrinsic mechanism that mediatesCa2+ and Na+ overload in response to disturbance of redox state in cell death.
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Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance.

TL;DR: The single-channel conductance properties of these AChR mutants expressed in Xenopus laevis oocytes indicate that three clusters of negatively charged and glutamine residues neighbouring segment M2 of the α-, β-, γ- and δ-subunits, probably forming three anionic rings, are major determinants of the rate of ion transport.