{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,30]],"date-time":"2025-07-30T14:38:33Z","timestamp":1753886313438,"version":"3.41.2"},"reference-count":30,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2011,10,5]],"date-time":"2011-10-05T00:00:00Z","timestamp":1317772800000},"content-version":"vor","delay-in-days":277,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"funder":[{"DOI":"10.13039\/501100001321","name":"National Research Foundation","doi-asserted-by":"publisher","award":["20110002144"],"award-info":[{"award-number":["20110002144"]}],"id":[{"id":"10.13039\/501100001321","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["BioMed Research International"],"published-print":{"date-parts":[[2011,1]]},"abstract":"<jats:p>Imperatoxin A (IpTx<jats:sub>a<\/jats:sub>) is known to modify the gating of skeletal ryanodine receptor (RyR1). In  this paper, the ability of charged aa residues of IpTx<jats:sub>a<\/jats:sub> to induce substate of native RyR1 in HSR was examined. Our results show that the basic residues (e.g., Lys<jats:sup>19<\/jats:sup>, Lys<jats:sup>20<\/jats:sup>, Lys<jats:sup>22<\/jats:sup>, Arg<jats:sup>23<\/jats:sup>, and Arg<jats:sup>24<\/jats:sup>) are important for producing substate of RyR1. In addition, other basic residues (e.g., Lys<jats:sup>30<\/jats:sup>, Arg<jats:sup>31<\/jats:sup>, and Arg<jats:sup>33<\/jats:sup>) near the C\u2010terminus and some acidic residues (e.g., Glu<jats:sup>29<\/jats:sup>, Asp<jats:sup>13<\/jats:sup>, and Asp<jats:sup>2<\/jats:sup>) are also involved in the generation of substate. Residues such as Lys<jats:sup>8<\/jats:sup> and Thr<jats:sup>26<\/jats:sup> may be involved in the self\u2010regulation of substate of RyR1, since alanine substitution of the aa residues led to a drastic conversion to the substate. The modifications of the channel gating by the wild\u2010type and mutant toxins were similar in purified RyR1. Taken together, the specific charge distributions on the surface of IpTx<jats:sub>a<\/jats:sub> are essential for regulation of the channel gating of RyR1.<\/jats:p>","DOI":"10.1155\/2011\/386384","type":"journal-article","created":{"date-parts":[[2011,10,5]],"date-time":"2011-10-05T19:03:40Z","timestamp":1317841420000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Both Basic and Acidic Amino Acid Residues of IpTx<sub>a<\/sub> Are Involved in Triggering Substate of RyR1"],"prefix":"10.1155","volume":"2011","author":[{"given":"In Ra","family":"Seo","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dae Eun","family":"Kang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dong Woo","family":"Song","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Do 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