{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T05:28:15Z","timestamp":1789190895586,"version":"build-2803163510"},"reference-count":33,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2015,7,26]],"date-time":"2015-07-26T00:00:00Z","timestamp":1437868800000},"content-version":"vor","delay-in-days":206,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004346","name":"Stiftung Rheinland-Pfalz f\u00fcr Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004346","id-type":"DOI","asserted-by":"publisher"}]},{"name":"COMATT"},{"name":"German Chemical Industrial Fund"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Open Bio"],"published-print":{"date-parts":[[2015,1]]},"abstract":"<jats:p>Several point mutations have been identified in human aquaporins, but their effects on the function of the respective aquaporins are mostly enigmatic. We analyzed the impact of the aquaporin 2 mutation V71M, which causes<jats:italic>nephrogenic diabetes insipidus<\/jats:italic> in humans, on aquaporin structure and activity, using the bacterial aquaglyceroporin GlpF as a model. Importantly, the sequence and structure around the V71M mutation is highly conserved between aquaporin 2 and GlpF. The V71M mutation neither impairs substrate flux nor oligomerization of the aquaglyceroporin. Therefore, the human aquaporin 2 mutant V71M is most likely active, but cellular trafficking is probably impaired.<\/jats:p>","DOI":"10.1016\/j.fob.2015.07.003","type":"journal-article","created":{"date-parts":[[2015,7,26]],"date-time":"2015-07-26T14:54:13Z","timestamp":1437922453000},"page":"640-646","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["The AQP2 mutation V71M causes<i>nephrogenic diabetes insipidus<\/i> in humans but does not impair the function of a bacterial homolog"],"prefix":"10.1002","volume":"5","author":[{"given":"Noreen","family":"Klein","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Pharmazie und Biochemie, Johannes Gutenberg-Universit\u00e4t Mainz, 55128 Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nadine","family":"K\u00fcmmerer","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Pharmazie und Biochemie, Johannes Gutenberg-Universit\u00e4t Mainz, 55128 Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominika","family":"Hobernik","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Pharmazie und Biochemie, Johannes Gutenberg-Universit\u00e4t Mainz, 55128 Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk","family":"Schneider","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Pharmazie und Biochemie, Johannes Gutenberg-Universit\u00e4t Mainz, 55128 Mainz, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2015,7,26]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.256.5055.385"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-440X(02)00355-X"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)36674-7"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.290.5491.481"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi201266m"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.51.33949"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1038\/35036519"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrd4226"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cub.2012.11.025"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/humu.20762"},{"key":"e_1_2_7_12_1","first-page":"622","article-title":"Folding and stability of the aquaglyceroporin GlpF: implications for human aqua(glycero)porin diseases","volume":"2015","author":"Klein N.","year":"1848","journal-title":"Biochim. 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