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Shosaku Numa

Researcher at Kyoto University

Publications -  191
Citations -  33526

Shosaku Numa is an academic researcher from Kyoto University. The author has contributed to research in topics: Complementary DNA & Acetylcholine receptor. The author has an hindex of 81, co-authored 191 publications receiving 33141 citations. Previous affiliations of Shosaku Numa include National Institutes of Natural Sciences, Japan & Mitsubishi.

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Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-lipotropin precursor.

TL;DR: The nucleotide sequence of a 1,091-base pair cloned cDNA insert encoding bovine corticotropin-β-lipotropin precursor mRNA indicates that the precursor protein consists of repetitive units and includes a third melanotropin sequence in its cryptic portion.
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Primary structure of the receptor for calcium channel blockers from skeletal muscle

TL;DR: Structural and sequence similarities to the voltage-dependent sodium channel suggest that in the transverse tubule membrane of skeletal muscle the dihydropyridine receptor may act both as voltage sensor in excitation-contraction coupling and as a calcium channel.
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Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence.

TL;DR: Cloning and sequence analysis of cDNA for the Electrophorus electricus electroplax sodium channel indicate that this protein exhibits four repeated homology units, which are presumably oriented in a pseudosymmetric fashion across the membrane.
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Structural parts involved in activation and inactivation of the sodium channel.

TL;DR: Evidence is provided that the positive charges in segment S4 are involved in the voltage–sensing mechanism for activation of the channel and that the region between repeats III and IV is important for its inactivation.
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Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor.

TL;DR: The predicted structure suggests that the calcium release channel activity resides in the C-terminal region of the receptor molecule, whereas the remaining portion constitutes the 'foot' structure spanning the junctional gap between the sarcoplasmic reticulum and the transverse tubule.