{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T05:39:53Z","timestamp":1779341993762,"version":"3.51.4"},"reference-count":3,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"4980","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[1990,10,26]]},"abstract":"<jats:p>\n            Site-directed mutagenesis experiments have suggested a model for the inactivation mechanism of\n            <jats:italic>Shaker<\/jats:italic>\n            potassium channels from\n            <jats:italic>Drosophila melanogaster<\/jats:italic>\n            . In this model, the first 20 amino acids form a cytoplasmic domain that interacts with the open channel to cause inactivation. The model was tested by the internal application of a synthetic peptide, with the sequence of the first 20 residues of the ShB alternatively spliced variant, to noninactivating mutant channels expressed in\n            <jats:italic>Xenopus<\/jats:italic>\n            oocytes. The peptide restored inactivation in a concentration-dependent manner. Like normal inactivation, peptide-induced inactivation was not noticeably voltage-dependent. Trypsin-treated peptide and peptides with sequences derived from the first 20 residues of noninactivating mutants did not restore inactivation. These results support the proposal that inactivation occurs by a cytoplasmic domain that occludes the ion-conducting pore of the channel.\n          <\/jats:p>","DOI":"10.1126\/science.2122520","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T22:10:14Z","timestamp":1160086214000},"page":"568-571","source":"Crossref","is-referenced-by-count":595,"title":["Restoration of Inactivation in Mutants of\n            <i>Shaker<\/i>\n            Potassium Channels by a Peptide Derived from ShB"],"prefix":"10.1126","volume":"250","author":[{"given":"William N.","family":"Zagotta","sequence":"first","affiliation":[{"name":"Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Toshinori","family":"Hoshi","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard W.","family":"Aldrich","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"221","reference":[{"key":"e_1_2_1_1_1","doi-asserted-by":"publisher","DOI":"10.1085\/jgp.70.5.567"},{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.2539643"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.2122519"}],"container-title":["Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.science.org\/doi\/pdf\/10.1126\/science.2122520","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,12]],"date-time":"2024-01-12T09:48:22Z","timestamp":1705052902000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.science.org\/doi\/10.1126\/science.2122520"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,10,26]]},"references-count":3,"journal-issue":{"issue":"4980","published-print":{"date-parts":[[1990,10,26]]}},"alternative-id":["10.1126\/science.2122520"],"URL":"https:\/\/doi.org\/10.1126\/science.2122520","relation":{},"ISSN":["0036-8075","1095-9203"],"issn-type":[{"value":"0036-8075","type":"print"},{"value":"1095-9203","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,10,26]]}}}