{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T15:28:20Z","timestamp":1781105300051,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"21","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1992,11]]},"abstract":"<jats:p>Charybdotoxin (ChTX), a K+ channel blocker, depolarizes human peripheral T lymphocytes and renders them insensitive to activation by mitogen. We observed four types of K+ channels in human T cells: one voltage-activated, and three Ca(2+)-activated. To discern the mechanism by which ChTX depolarizes T cells, we examined the sensitivity of both the voltage-activated and Ca(2+)-activated K+ channels to ChTX and other peptide channel blockers. All four types were blocked by ChTX, whereas noxiustoxin and margatoxin blocked only the voltage-activated channels. All three toxins, however, produced equivalent depolarization in human T cells. We conclude that the membrane potential of resting T cells is set by voltage-activated channels and that blockade of these channels is sufficient to depolarize resting human T cells and prevent activation.<\/jats:p>","DOI":"10.1073\/pnas.89.21.10094","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T08:11:21Z","timestamp":1149063081000},"page":"10094-10098","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":191,"title":["Selective blockers of voltage-gated K+ channels depolarize human T lymphocytes: mechanism of the antiproliferative effect of charybdotoxin."],"prefix":"10.1073","volume":"89","author":[{"given":"R J","family":"Leonard","sequence":"first","affiliation":[{"name":"Department of Membrane Biochemistry and Biophysics, Merck Research Laboratories, Rahway, NJ 07065."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M L","family":"Garcia","sequence":"additional","affiliation":[{"name":"Department of Membrane Biochemistry and Biophysics, Merck Research Laboratories, Rahway, NJ 07065."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R S","family":"Slaughter","sequence":"additional","affiliation":[{"name":"Department of Membrane Biochemistry and Biophysics, Merck Research Laboratories, Rahway, NJ 07065."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J P","family":"Reuben","sequence":"additional","affiliation":[{"name":"Department of Membrane Biochemistry and Biophysics, Merck Research Laboratories, Rahway, NJ 07065."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1992,11]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.89.21.10094","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T13:48:17Z","timestamp":1649857697000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.89.21.10094"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,11]]},"references-count":0,"journal-issue":{"issue":"21","published-print":{"date-parts":[[1992,11]]}},"alternative-id":["10.1073\/pnas.89.21.10094"],"URL":"https:\/\/doi.org\/10.1073\/pnas.89.21.10094","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,11]]},"assertion":[{"value":"1992-11-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}