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Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/28495
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dc.contributor.authorGerke, V-
dc.contributor.authorGavins, FNE-
dc.contributor.authorGeisow, M-
dc.contributor.authorGrewal, T-
dc.contributor.authorJaiswal, JK-
dc.contributor.authorNylandsted, J-
dc.contributor.authorRescher, U-
dc.date.accessioned2024-03-08T15:27:51Z-
dc.date.available2024-03-08T15:27:51Z-
dc.date.issued2024-02-21-
dc.identifierORCiD: Volker Gerke https://orcid.org/0000-0001-7208-8206-
dc.identifier1574 ORCiD: Felicity N. E. Gavins https://orcid.org/0000-0001-7008-5423-
dc.identifierORCiD: Michael Geisow https://orcid.org/0009-0001-6218-8200-
dc.identifierORCiD: Thomas Grewal https://orcid.org/0000-0002-7937-8887-
dc.identifierORCiD: Jyoti K. Jaiswal https://orcid.org/0000-0002-5992-5185-
dc.identifierORCiD: Jesper Nylandsted https://orcid.org/0000-0001-6474-5093-
dc.identifierORCiD: Ursula Rescher https://orcid.org/0000-0001-8892-319X-
dc.identifier1574-
dc.identifier.citationGerke, V. et al. (2024) 'Annexins-a family of proteins with distinctive tastes for cell signaling and membrane dynamics', Nature communications, 15 (1), 1574, pp. 1 - 15. doi: 10.1038/s41467-024-45954-0.en_US
dc.identifier.urihttps://bura.brunel.ac.uk/handle/2438/28495-
dc.description.abstractAnnexins are cytosolic proteins with conserved three-dimensional structures that bind acidic phospholipids in cellular membranes at elevated Ca2+ levels. Through this they act as Ca2+-regulated membrane binding modules that organize membrane lipids, facilitating cellular membrane transport but also displaying extracellular activities. Recent discoveries highlight annexins as sensors and regulators of cellular and organismal stress, controlling inflammatory reactions in mammals, environmental stress in plants, and cellular responses to plasma membrane rupture. Here, we describe the role of annexins as Ca2+-regulated membrane binding modules that sense and respond to cellular stress and share our view on future research directions in the field.en_US
dc.description.sponsorshipWork in our laboratories was supported by grants from the German Research Foundation to V.G. (CRC1348/A04, GE514/6-3) and U.R. (CRC1009/A06, CRC1348/A11); the Interdisciplinary Center for Clinical Research of the Münster Medical School to U.R. (Re2/022/20); the Danish Council for Independent Research (6108-00378A, 9040-00252B), Scientific Committee Danish Cancer Society (R90-A5847-14-S2, R269-A15812), and the Novo Nordisk Foundation (NNF18OC0034936) to J.N.; the Royal Society and Wolfson Foundation (RSWF\R3\183001) to F.N.E.G.; the National Institute of Health (NIH R01AR055686) to J.K.J.; the Ara Parseghian Medical Research Fund (G217137) to T.G.en_US
dc.format.extent1 - 15-
dc.format.mediumElectronic-
dc.languageEnglish-
dc.language.isoen_USen_US
dc.publisherSpringer Natureen_US
dc.rightsCopyright © The Author(s) 2024. Rights and permissions: Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit https://creativecommons.org/licenses/by/4.0/.-
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/-
dc.subjectcalciumen_US
dc.subjectcell biologyen_US
dc.subjectdrug discoveryen_US
dc.subjectmembrane lipidsen_US
dc.titleAnnexins-a family of proteins with distinctive tastes for cell signaling and membrane dynamicsen_US
dc.typeArticleen_US
dc.identifier.doihttps://doi.org/10.1038/s41467-024-45954-0-
dc.relation.isPartOfNature communications-
pubs.issue1-
pubs.publication-statusPublished-
pubs.volume15-
dc.identifier.eissn2041-1723-
dc.rights.licensehttps://creativecommons.org/licenses/by/4.0/.legalcode.en-
dc.rights.holderThe Author(s)-
Appears in Collections:Dept of Life Sciences Research Papers

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