Haruko Masumiya
University of Calgary
7 Papers
190 Citations
Haruko Masumiya is an academic researcher from University of Calgary. The author has contributed to research in topics: Ryanodine receptor & Ryanodine receptor 2. The author has an hindex of 6, co-authored 7 publications. Previous affiliations of Haruko Masumiya include Tokyo Medical and Dental University.
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Papers
Nitric oxide-dependent modulation of the delayed rectifier K+ current and the L-type Ca2+ current by ginsenoside Re, an ingredient of Panax ginseng, in guinea-pig cardiomyocytes
TL;DR: Direct S‐nitrosylation of channel protein appears to be the main mechanism for IKs enhancement, while a cGMP‐dependent pathway is responsible for ICa,L inhibition.
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Localization of the 12.6-kDa FK506-binding Protein (FKBP12.6) Binding Site to the NH2-terminal Domain of the Cardiac Ca2+ Release Channel (Ryanodine Receptor)
TL;DR: To systematically define the molecular determinants of FKBP12.6 binding, a series of internal and NH2- and COOH-terminal deletion mutants of RyR2 were constructed and the effect of these deletions on GST-FKBP 12.6binding was examined.
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Three-dimensional Localization of Divergent Region 3 of the Ryanodine Receptor to the Clamp-shaped Structures Adjacent to the FKBP Binding Sites
Jing Zhang,Zheng Liu,Haruko Masumiya,Ruiwu Wang,Dawei Jiang,Fei Li,Terence Wagenknecht,Terence Wagenknecht,S.R. Wayne Chen +8 more
TL;DR: A structural basis is determined for the role of the DR3 region in excitation-contraction coupling and in channel regulation and it is demonstrated that a region between 1815 and 1855 near DR3 is essential for GST-FKBP12.6 binding sites.
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Ryanodine Sensitizes the Ca2+ Release Channel (Ryanodine Receptor) to Ca2+ Activation
TL;DR: Results demonstrate that ryanodine does not “lock” the RyR channel into an open state as generally believed; rather, it sensitizes dramatically the channel to activation by Ca2+.
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Isoform dependent formation of heteromeric Ca2+ release channels (ryanodine receptors)
Bailong Xiao,Haruko Masumiya,Dawei Jiang,Ruiwu Wang,Yoshitatsu Sei,Lin Zhang,Takashi Murayama,Yasuo Ogawa,F. Anthony Lai,Terence Wagenknecht,S.R. Wayne Chen +10 more
TL;DR: Observations demonstrate that RyR2 is capable of forming functional heteromeric channels with RyR3 and RyR1, whereasRyR1 is incapable of forming heteromerics channels withRyR3.
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