Naoko Doi

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Because intracellular [Na(+)] is kept low by Na(+)/K(+)-ATPase, Na(+) dependence is generally considered a property of extracellular enzymes. However, we found that p94/calpain 3, a skeletal-muscle-specific member of the Ca(2+)-activated intracellular "modulator proteases" that is responsible for a limb-girdle muscular dystrophy ("calpainopathy"), underwent(More)
  • Page Ii Disclaimer, Keiichi Yokobori, Jung Yonghun, Abd Korea, Shawal, Yaman +19 others
  • 2000
Centre has endeavoured to ensure that the updated information is accurate and up to date, but cannot be held responsible for the validity of material provided by other parties. The objective of the study is to evaluate electricity sector reform processes in APEC member economies, in an effort to provide a useful description and analysis of the growing trend(More)
Calpain represents a family of Ca(2+)-dependent cytosolic cysteine proteases found in almost all eukaryotes and some bacteria, and is involved in a variety of biological phenomena, including brain function. Several substrates of calpain are aggressively proteolyzed under pathological conditions, e.g., in neurodegenerating processes, fodrin is proteolyzed by(More)
Calpains are intracellular Ca(2+)-regulated cysteine proteases that are essential for various cellular functions. Mammalian conventional calpains (calpain-1 and calpain-2) modulate the structure and function of their substrates by limited proteolysis. Thus, it is critically important to determine the site(s) in proteins at which calpains cleave. However,(More)
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