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Takashi Daiho

Researcher at Asahikawa Medical University

Publications -  40
Citations -  970

Takashi Daiho is an academic researcher from Asahikawa Medical University. The author has contributed to research in topics: Transmembrane domain & ATPase. The author has an hindex of 19, co-authored 39 publications receiving 913 citations. Previous affiliations of Takashi Daiho include Asahikawa Medical College.

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Journal ArticleDOI

Organization of cytoplasmic domains of sarcoplasmic reticulum Ca2+‐ATPase in E1P and E1ATP states: a limited proteolysis study

TL;DR: It is proposed that the A domain undergoes a large amount of rotation between E1P and E2P, which will be very useful for establishing the conditions for structural studies.
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Distinct natures of beryllium fluoride-bound, aluminum fluoride-bound, and magnesium fluoride-bound stable analogues of an ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase: changes in catalytic and transport sites during phosphoenzyme hydrolysis.

TL;DR: The structural natures of stable analogues for the ADP-insensitive phosphoenzyme (E2P) of Ca2+-ATPase formed in sarcoplasmic reticulum vesicles were explored and compared with those of actual E2P formed from Pi without Ca2+.
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ADP‐insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+‐ATPase has a compact conformation resistant to proteinase K, V8 protease and trypsin

TL;DR: Results show that the structure of the enzyme with bound decavanadate is very similar to ADP‐insensitive phosphoenzyme, and has a very compact form in the cytoplasmic region, being consistent with large domain motions.
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Comprehensive Analysis of Expression and Function of 51 Sarco(endo)plasmic Reticulum Ca2+-ATPase Mutants Associated with Darier Disease

TL;DR: The results indicated that in most cases (48 of 51) DD mutations cause severe disruption of Ca2+ homeostasis by the defects in protein expression and/or transport function and hence DD, but even a slight disturbance of theHomeostasis will result in the disease.
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Critical Role of Glu40-Ser48 Loop Linking Actuator Domain and First Transmembrane Helix of Ca2+-ATPase in Ca2+ Deocclusion and Release from ADP-insensitive Phosphoenzyme

TL;DR: The functional importance of the length of the A/M1 linker connecting the actuator domain and the first transmembrane helix of sarcoplasmic reticulum Ca2+-ATPase was explored by its elongation with glycine insertion at Pro42/Ala43 and Gly46/Lys47 and showed that these interactions at each site completely abolished ATPase activity.