{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T11:13:48Z","timestamp":1791371628365,"version":"4.3.1"},"reference-count":43,"publisher":"National Academy of Sciences","issue":"24","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2003,11,25]]},"abstract":"<jats:p>\n                    Microbial-type rhodopsins are found in archaea, prokaryotes, and eukaryotes. Some of them represent membrane ion transport proteins such as bacteriorhodopsin, a light-driven proton pump, or channelrhodopsin-1 (ChR1), a recently identified light-gated proton channel from the green alga\n                    <jats:italic>Chlamydomonas reinhardtii<\/jats:italic>\n                    . ChR1 and ChR2, a related microbial-type rhodopsin from\n                    <jats:italic>C. reinhardtii<\/jats:italic>\n                    , were shown to be involved in generation of photocurrents of this green alga. We demonstrate by functional expression, both in oocytes of\n                    <jats:italic>Xenopus laevis<\/jats:italic>\n                    and mammalian cells, that ChR2 is a directly light-switched cation-selective ion channel. This channel opens rapidly after absorption of a photon to generate a large permeability for monovalent and divalent cations. ChR2 desensitizes in continuous light to a smaller steady-state conductance. Recovery from desensitization is accelerated by extracellular H\n                    <jats:sup>+<\/jats:sup>\n                    and negative membrane potential, whereas closing of the ChR2 ion channel is decelerated by intracellular H\n                    <jats:sup>+<\/jats:sup>\n                    . ChR2 is expressed mainly in\n                    <jats:italic>C. reinhardtii<\/jats:italic>\n                    under low-light conditions, suggesting involvement in photoreception in dark-adapted cells. The predicted seven-transmembrane \u03b1 helices of ChR2 are characteristic for G protein-coupled receptors but reflect a different motif for a cation-selective ion channel. Finally, we demonstrate that ChR2 may be used to depolarize small or large cells, simply by illumination.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1936192100","type":"journal-article","created":{"date-parts":[[2003,11,25]],"date-time":"2003-11-25T15:59:06Z","timestamp":1069775946000},"page":"13940-13945","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":2447,"title":["Channelrhodopsin-2, a directly light-gated cation-selective membrane channel"],"prefix":"10.1073","volume":"100","author":[{"given":"Georg","family":"Nagel","sequence":"first","affiliation":[{"name":"Max-Planck-Institut f\u00fcr Biophysik, Marie-Curie-Strasse 15, 60439 Frankfurt, Germany; Institut f\u00fcr Biochemie, Universit\u00e4t Regensburg; Universit\u00e4tsstrasse 31, 93040 Regensburg, Germany; and Institut f\u00fcr Biophysikalische Chemie, Johann Wolfgang Goethe-Universit\u00e4t, Biozentrum, D-60439 Frankfurt, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tanjef","family":"Szellas","sequence":"additional","affiliation":[{"name":"Max-Planck-Institut f\u00fcr Biophysik, Marie-Curie-Strasse 15, 60439 Frankfurt, Germany; 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