{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T10:37:35Z","timestamp":1773657455861,"version":"3.50.1"},"reference-count":36,"publisher":"Proceedings of the National Academy of Sciences","issue":"12","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1998,6,9]]},"abstract":"<jats:p>\n            Presenilins have been implicated in the genesis of Alzheimer\u2019s disease and in facilitating LIN-12\/Notch activity during development. All presenilins have multiple hydrophobic regions that could theoretically span a membrane, and a description of the membrane topology is a crucial step toward deducing the mechanism of presenilin function. Previously, we proposed an eight-transmembrane-domain model for presenilin, based on studies of the\n            <jats:italic>Caenorhabditis elegans<\/jats:italic>\n            SEL-12 presenilin. Here, we describe experiments that support the view that two of the hydrophobic regions of SEL-12 function as the seventh and eighth transmembrane domains. Furthermore, we have shown that human presenilin 1 behaves like SEL-12 presenilin when analyzed by our methods. Our results provide additional experimental support for the eight-transmembrane-domain model of presenilin topology.\n          <\/jats:p>","DOI":"10.1073\/pnas.95.12.7109","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:40:11Z","timestamp":1027694411000},"page":"7109-7114","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":123,"title":["Additional evidence for an eight-transmembrane-domain topology for\n            <i>Caenorhabditis elegans<\/i>\n            and human presenilins"],"prefix":"10.1073","volume":"95","author":[{"given":"Xiajun","family":"Li","sequence":"first","affiliation":[{"name":"Integrated Program in Cellular, Molecular and Biophysical Studies, Department of Biochemistry and Molecular Biophysics, and Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, New York, NY 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