{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T20:13:52Z","timestamp":1789935232285,"version":"4.0.1"},"reference-count":28,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2017,10,10]],"date-time":"2017-10-10T00:00:00Z","timestamp":1507593600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100004412","name":"Human Frontier Science Program","doi-asserted-by":"publisher","award":["RGP0029\u20102014"],"award-info":[{"award-number":["RGP0029\u20102014"]}],"id":[{"id":"10.13039\/100004412","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Open Bio"],"published-print":{"date-parts":[[2017,11]]},"abstract":"<jats:p>\n                    The B subunit of the bacterial cholera toxin (CTxB) is responsible for the toxin binding to the cell membrane and its intracellular trafficking.\n                    <jats:styled-content style=\"fixed-case\">CT<\/jats:styled-content>\n                    xB binds to the monosialotetrahexosyl ganglioside at the plasma membrane of the target cell and mediates toxin internalization by endocytosis.\n                    <jats:styled-content style=\"fixed-case\">CT<\/jats:styled-content>\n                    xB induces a local membrane curvature that is essential for its clathrin\u2010independent uptake. Using all\u2010atom molecular dynamics, we show that\n                    <jats:styled-content style=\"fixed-case\">CT<\/jats:styled-content>\n                    xB induces local curvature, with the radius of curvature around 36\u00a0nm. The main feature of the\n                    <jats:styled-content style=\"fixed-case\">CT<\/jats:styled-content>\n                    xB molecular structure that causes membrane bending is the protruding alpha helices in the middle of the protein. Our study points to a generic protein design principle for generating local membrane curvature through specific binding to their lipid anchors.\n                  <\/jats:p>","DOI":"10.1002\/2211-5463.12321","type":"journal-article","created":{"date-parts":[[2017,9,26]],"date-time":"2017-09-26T04:22:47Z","timestamp":1506399767000},"page":"1638-1645","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":46,"title":["Cholera toxin B subunit induces local curvature on lipid bilayers"],"prefix":"10.1002","volume":"7","author":[{"given":"Weria","family":"Pezeshkian","sequence":"first","affiliation":[{"name":"Center for Biomembrane Physics (MEMPHYS) Department of Physics, Chemistry and Pharmacy (FKF) University of Southern Denmark Odense Odense M Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lina J.","family":"N\u00e5bo","sequence":"additional","affiliation":[{"name":"Center for Biomembrane Physics (MEMPHYS) 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