{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T20:51:01Z","timestamp":1792270261829,"version":"4.4.0"},"reference-count":51,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,1,2]],"date-time":"2025-01-02T00:00:00Z","timestamp":1735776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2025,1,2]],"date-time":"2025-01-02T00:00:00Z","timestamp":1735776000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Commun"],"DOI":"10.1038\/s41467-024-55673-1","type":"journal-article","created":{"date-parts":[[2025,1,2]],"date-time":"2025-01-02T20:15:13Z","timestamp":1735848913000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Structural basis for catalysis and selectivity of phospholipid synthesis by eukaryotic choline-phosphotransferase"],"prefix":"10.1038","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9976-5828","authenticated-orcid":false,"given":"Jacquelyn R.","family":"Roberts","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-3384-4354","authenticated-orcid":false,"given":"Yasuhiro","family":"Horibata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank E.","family":"Kwarcinski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8228-2133","authenticated-orcid":false,"given":"Vinson","family":"Lam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ashleigh M.","family":"Raczkowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-5855-6022","authenticated-orcid":false,"given":"Akane","family":"Hubbard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Betsy","family":"White","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroyuki","family":"Sugimoto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6540-4896","authenticated-orcid":false,"given":"Gregory G.","family":"Tall","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1750-4793","authenticated-orcid":false,"given":"Melanie D.","family":"Ohi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7762-9793","authenticated-orcid":false,"given":"Shoji","family":"Maeda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,1,2]]},"reference":[{"key":"55673_CR1","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1038\/nrm2330","volume":"9","author":"G van Meer","year":"2008","unstructured":"van Meer, G., Voelker, D. R. & Feigenson, G. W. Membrane lipids: where they are and how they behave. Nat. Rev. Mol. Cell Biol. 9, 112\u2013124 (2008).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"55673_CR2","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1038\/nrm4080","volume":"16","author":"A-E Saliba","year":"2015","unstructured":"Saliba, A.-E., Vonkova, I. & Gavin, A.-C. The systematic analysis of protein\u2013lipid interactions comes of age. Nat. Rev. Mol. Cell Biol. 16, 753\u2013761 (2015).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"55673_CR3","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1111\/tra.12230","volume":"16","author":"JE Vance","year":"2015","unstructured":"Vance, J. E. Phospholipid synthesis and transport in mammalian cells. Traffic 16, 1\u201318 (2015).","journal-title":"Traffic"},{"key":"55673_CR4","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1146\/annurev.pharmtox.011008.145616","volume":"49","author":"T Shimizu","year":"2009","unstructured":"Shimizu, T. Lipid mediators in health and disease: enzymes and receptors as therapeutic targets for the regulation of immunity and inflammation. Annu. Rev. Pharmacol. Toxicol. 49, 123\u2013150 (2009).","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"55673_CR5","doi-asserted-by":"publisher","first-page":"411","DOI":"10.1007\/s10545-012-9509-7","volume":"36","author":"F Lamari","year":"2013","unstructured":"Lamari, F., Mochel, F., Sedel, F. & Saudubray, J. M. Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases. J. Inherit. Metab. Dis. 36, 411\u2013425 (2013).","journal-title":"J. Inherit. Metab. Dis."},{"key":"55673_CR6","doi-asserted-by":"crossref","unstructured":"Gibellini, F. & Smith, T. K. The Kennedy pathway\u2014De novo synthesis of phosphatidylethanolamine and phosphatidylcholine. IUBMB Life 62, 414\u2013428 (2010).","DOI":"10.1002\/iub.337"},{"key":"55673_CR7","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1016\/S0021-9258(19)50785-2","volume":"222","author":"EP Kennedy","year":"1956","unstructured":"Kennedy, E. P. & Weiss, S. B. The function of cytidine coenzymes in the biosynthesis of phospholipides. J. Biol. Chem. 222, 193\u2013214 (1956).","journal-title":"J. Biol. Chem."},{"key":"55673_CR8","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1146\/annurev.bi.64.070195.001531","volume":"64","author":"C Kent","year":"1995","unstructured":"Kent, C. Eukaryotic phospholipid biosynthesis. Annu. Rev. Biochem. 64, 315\u2013343 (1995).","journal-title":"Annu. Rev. Biochem."},{"key":"55673_CR9","doi-asserted-by":"publisher","first-page":"14776","DOI":"10.1016\/S0021-9258(17)36692-9","volume":"269","author":"CR McMaster","year":"1994","unstructured":"McMaster, C. R. & Bell, R. M. Phosphatidylcholine biosynthesis via the CDP-choline pathway in Saccharomyces cerevisiae. Multiple mechanisms of regulation. J. Biol. Chem. 269, 14776\u201314783 (1994).","journal-title":"J. Biol. Chem."},{"key":"55673_CR10","doi-asserted-by":"publisher","first-page":"29808","DOI":"10.1074\/jbc.M005786200","volume":"275","author":"AL Henneberry","year":"2000","unstructured":"Henneberry, A. L., Wistow, G. & McMaster, C. R. Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J. Biol. Chem. 275, 29808\u201329815 (2000).","journal-title":"J. Biol. Chem."},{"key":"55673_CR11","doi-asserted-by":"publisher","first-page":"28010","DOI":"10.1016\/S0021-9258(18)46888-3","volume":"269","author":"CR McMaster","year":"1994","unstructured":"McMaster, C. R. & Bell, R. M. Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases. J. Biol. Chem. 269, 28010\u201328016 (1994).","journal-title":"J. Biol. Chem."},{"key":"55673_CR12","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1042\/bj3390291","volume":"339","author":"AL Henneberry","year":"1999","unstructured":"Henneberry, A. L. & McMaster, C. R. Cloning and expression of a human choline\/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem. J. 339, 291\u2013298 (1999).","journal-title":"Biochem. J."},{"key":"55673_CR13","doi-asserted-by":"publisher","first-page":"13482","DOI":"10.1074\/jbc.273.22.13482","volume":"273","author":"JG Williams","year":"1998","unstructured":"Williams, J. G. & McMaster, C. R. Scanning alanine mutagenesis of the CDP-alcohol phosphotransferase motif of saccharomyces cerevisiaeCholinephosphotransferase*. J. Biol. Chem. 273, 13482\u201313487 (1998).","journal-title":"J. Biol. Chem."},{"key":"55673_CR14","doi-asserted-by":"publisher","first-page":"20995","DOI":"10.1016\/S0021-9258(17)31920-8","volume":"269","author":"RH Hjelmstad","year":"1994","unstructured":"Hjelmstad, R. H., Morash, S. C., McMaster, C. R. & Bell, R. M. Chimeric enzymes. Structure-function analysis of segments of sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases. J. Biol. Chem. 269, 20995\u201321002 (1994).","journal-title":"J. Biol. Chem."},{"key":"55673_CR15","doi-asserted-by":"publisher","first-page":"4357","DOI":"10.1016\/S0021-9258(20)64330-7","volume":"266","author":"RH Hjelmstad","year":"1991","unstructured":"Hjelmstad, R. H. & Bell, R. M. sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae: mixed micellar analysis of the CPT1 and EPT1 gene products*. J. Biol. Chem. 266, 4357\u20134365 (1991).","journal-title":"J. Biol. Chem."},{"key":"55673_CR16","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1016\/j.febslet.2004.05.043","volume":"569","author":"HA Boumann","year":"2004","unstructured":"Boumann, H. A., de Kruijff, B., Heck, A. J. R. & de Kroon, A. I. P. M. The selective utilization of substrates in vivo by the phosphatidylethanolamine and phosphatidylcholine biosynthetic enzymes Ept1p and Cpt1p in yeast. FEBS Lett. 569, 173\u2013177 (2004).","journal-title":"FEBS Lett."},{"key":"55673_CR17","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s42003-019-0427-1","volume":"2","author":"K Gr\u0101ve","year":"2019","unstructured":"Gr\u0101ve, K., Bennett, M. D. & H\u00f6gbom, M. Structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase reveals mechanism of substrate binding and metal catalysis. Commun. Biol. 2, 1\u201311 (2019).","journal-title":"Commun. Biol."},{"key":"55673_CR18","doi-asserted-by":"publisher","first-page":"5137","DOI":"10.1016\/j.jmb.2020.04.028","volume":"432","author":"M Belcher Dufrisne","year":"2020","unstructured":"Belcher Dufrisne, M. et al. Structural and functional characterization of phosphatidylinositol-phosphate biosynthesis in mycobacteria. J. Mol. Biol. 432, 5137\u20135151 (2020).","journal-title":"J. Mol. Biol."},{"key":"55673_CR19","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms9505","volume":"6","author":"OB Clarke","year":"2015","unstructured":"Clarke, O. B. et al. Structural basis for phosphatidylinositol-phosphate biosynthesis. Nat. Commun. 6, 8505 (2015).","journal-title":"Nat. Commun."},{"key":"55673_CR20","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-27281-w","volume":"12","author":"M Centola","year":"2021","unstructured":"Centola, M., van Pee, K., Betz, H. & Yildiz, \u00d6. Crystal structures of phosphatidyl serine synthase PSS reveal the catalytic mechanism of CDP-DAG alcohol O-phosphatidyl transferases. Nat. Commun. 12, 6982 (2021).","journal-title":"Nat. Commun."},{"key":"55673_CR21","doi-asserted-by":"publisher","first-page":"312","DOI":"10.1016\/j.crstbi.2021.11.005","volume":"3","author":"B Yang","year":"2021","unstructured":"Yang, B., Yao, H., Li, D. & Liu, Z. The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interface. Curr. Res. Struct. Biol. 3, 312\u2013323 (2021).","journal-title":"Curr. Res. Struct. Biol."},{"key":"55673_CR22","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms5068","volume":"5","author":"G Sciara","year":"2014","unstructured":"Sciara, G. et al. Structural basis for catalysis in a CDP-alcohol phosphotransferase. Nat. Commun. 5, 4068 (2014).","journal-title":"Nat. Commun."},{"key":"55673_CR23","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms5169","volume":"5","author":"P Nogly","year":"2014","unstructured":"Nogly, P. et al. X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism. Nat. Commun. 5, 4169 (2014).","journal-title":"Nat. Commun."},{"key":"55673_CR24","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-38290-2","volume":"14","author":"Z Wang","year":"2023","unstructured":"Wang, Z., Yang, M., Yang, Y., He, Y. & Qian, H. Structural basis for catalysis of human choline\/ethanolamine phosphotransferase 1. Nat. Commun. 14, 2529 (2023).","journal-title":"Nat. Commun."},{"key":"55673_CR25","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-38003-9","volume":"14","author":"L Wang","year":"2023","unstructured":"Wang, L. & Zhou, M. Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis. Nat. Commun. 14, 2753 (2023).","journal-title":"Nat. Commun."},{"key":"55673_CR26","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1007\/s11745-002-0947-6","volume":"37","author":"MM Wright","year":"2002","unstructured":"Wright, M. M. & McMaster, C. R. PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline\/ethanolamine phosphotransferase 1 (CEPT1). Lipids 37, 663\u2013672 (2002).","journal-title":"Lipids"},{"key":"55673_CR27","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1038\/s41594-018-0028-6","volume":"25","author":"C McMahon","year":"2018","unstructured":"McMahon, C. et al. Yeast surface display platform for rapid discovery of conformationally selective nanobodies. Nat. Struct. Mol. Biol. 25, 289\u2013296 (2018).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"55673_CR28","doi-asserted-by":"publisher","first-page":"729","DOI":"10.1042\/bj3130729","volume":"313","author":"CR McMASTER","year":"1996","unstructured":"McMASTER, C. R., MORASH, S. C. & BELL, R. M. Phospholipid and cation activation of chimaeric choline\/ethanolamine phosphotransferases. Biochem. J. 313, 729\u2013735 (1996).","journal-title":"Biochem. J."},{"key":"55673_CR29","doi-asserted-by":"crossref","unstructured":"Hjelmstad, R. H. & Bell, R. M. Choline- and ethanolaminephosphotransferases from Saccharomyces cerevisiae. in Methods in Enzymology (eds Dennis, E. A. & Vance, ennis E.) vol. 209, 272\u2013279 (Academic Press, 1992).","DOI":"10.1016\/0076-6879(92)09034-Z"},{"key":"55673_CR30","doi-asserted-by":"publisher","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","volume":"372","author":"E Krissinel","year":"2007","unstructured":"Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774\u2013797 (2007).","journal-title":"J. Mol. Biol."},{"key":"55673_CR31","doi-asserted-by":"publisher","unstructured":"Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 1\u201311 https:\/\/doi.org\/10.1038\/s41586-021-03819-2 (2021).","DOI":"10.1038\/s41586-021-03819-2"},{"key":"55673_CR32","doi-asserted-by":"publisher","first-page":"3909","DOI":"10.1016\/S0021-9258(18)61443-7","volume":"262","author":"RH Hjelmstad","year":"1987","unstructured":"Hjelmstad, R. H. & Bell, R. M. Mutants of Saccharomyces cerevisiae defective in sn-1,2-diacylglycerol cholinephosphotransferase. Isolation, characterization, and cloning of the CPT1 gene. J. Biol. Chem. 262, 3909\u20133917 (1987).","journal-title":"J. Biol. Chem."},{"key":"55673_CR33","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1093\/brain\/aww263","volume":"140","author":"MY Ahmed","year":"2017","unstructured":"Ahmed, M. Y. et al. A mutation of EPT1 (SELENOI) underlies a new disorder of Kennedy pathway phospholipid biosynthesis. Brain 140, 547\u2013554 (2017).","journal-title":"Brain"},{"key":"55673_CR34","doi-asserted-by":"publisher","first-page":"503","DOI":"10.1194\/jlr.C600019-JLR200","volume":"48","author":"Y Horibata","year":"2007","unstructured":"Horibata, Y. & Hirabayashi, Y. Identification and characterization of human ethanolaminephosphotransferase1. J. Lipid Res. 48, 503\u2013508 (2007).","journal-title":"J. Lipid Res."},{"key":"55673_CR35","doi-asserted-by":"publisher","DOI":"10.1126\/science.aao6326","volume":"359","author":"MS Rana","year":"2018","unstructured":"Rana, M. S. et al. Fatty acyl recognition and transfer by an integral membrane S-acyltransferase. Science 359, eaao6326 (2018).","journal-title":"Science"},{"key":"55673_CR36","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1038\/s41586-020-2280-2","volume":"581","author":"L Wang","year":"2020","unstructured":"Wang, L. et al. Structure and mechanism of human diacylglycerol O-acyltransferase 1. Nature 581, 329\u2013332 (2020).","journal-title":"Nature"},{"key":"55673_CR37","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1038\/s41594-022-00884-7","volume":"30","author":"ZL Johnson","year":"2023","unstructured":"Johnson, Z. L. et al. Structural basis of the acyl-transfer mechanism of human GPAT1. Nat. Struct. Mol. Biol. 30, 22\u201330 (2023).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"55673_CR38","doi-asserted-by":"publisher","first-page":"6064","DOI":"10.1021\/cr200296t","volume":"111","author":"PE Selvy","year":"2011","unstructured":"Selvy, P. E., Lavieri, R. R., Lindsley, C. W. & Brown, H. A. Phospholipase D: enzymology, functionality, and chemical modulation. Chem. Rev. 111, 6064\u20136119 (2011).","journal-title":"Chem. Rev."},{"key":"55673_CR39","doi-asserted-by":"publisher","first-page":"S199","DOI":"10.1002\/mrc.951","volume":"39","author":"WW Bachovchin","year":"2001","unstructured":"Bachovchin, W. W. Review: contributions of NMR spectroscopy to the study of hydrogen bonds in serine protease active sites. Magn. Reson. Chem. 39, S199\u2013S213 (2001).","journal-title":"Magn. Reson. Chem."},{"key":"55673_CR40","doi-asserted-by":"publisher","first-page":"4501","DOI":"10.1021\/cr000033x","volume":"102","author":"L Hedstrom","year":"2002","unstructured":"Hedstrom, L. Serine protease mechanism and specificity. Chem. Rev. 102, 4501\u20134524 (2002).","journal-title":"Chem. Rev."},{"key":"55673_CR41","doi-asserted-by":"publisher","first-page":"290","DOI":"10.1038\/nmeth.4169","volume":"14","author":"A Punjani","year":"2017","unstructured":"Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290\u2013296 (2017).","journal-title":"Nat. Methods"},{"key":"55673_CR42","doi-asserted-by":"publisher","first-page":"218","DOI":"10.1038\/s42003-019-0437-z","volume":"2","author":"T Wagner","year":"2019","unstructured":"Wagner, T. et al. SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM. Commun. Biol. 2, 218 (2019).","journal-title":"Commun. Biol."},{"key":"55673_CR43","doi-asserted-by":"publisher","first-page":"1214","DOI":"10.1038\/s41592-020-00990-8","volume":"17","author":"A Punjani","year":"2020","unstructured":"Punjani, A., Zhang, H. & Fleet, D. J. Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction. Nat. Methods 17, 1214\u20131221 (2020).","journal-title":"Nat. Methods"},{"key":"55673_CR44","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1002\/pro.3943","volume":"30","author":"EF Pettersen","year":"2021","unstructured":"Pettersen, E. F. et al. UCSF ChimeraX: structure visualization for researchers, educators, and developers. Protein Sci. 30, 70\u201382 (2021).","journal-title":"Protein Sci."},{"key":"55673_CR45","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"PD Adams","year":"2010","unstructured":"Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213\u2013221 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"55673_CR46","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1107\/S0907444909042073","volume":"66","author":"VB Chen","year":"2010","unstructured":"Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"55673_CR47","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1002\/pro.3235","volume":"27","author":"TD Goddard","year":"2017","unstructured":"Goddard, T. D. et al. UCSF ChimeraX: meeting modern challenges in visualization and analysis. Protein Sci. 27, 14\u201325 (2017).","journal-title":"Protein Sci."},{"key":"55673_CR48","doi-asserted-by":"publisher","first-page":"W344","DOI":"10.1093\/nar\/gkw408","volume":"44","author":"H Ashkenazy","year":"2016","unstructured":"Ashkenazy, H. et al. ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules. Nucleic Acids Res. 44, W344\u2013W350 (2016).","journal-title":"Nucleic Acids Res."},{"key":"55673_CR49","doi-asserted-by":"crossref","unstructured":"Horibata, Y. & Sugimoto, H. Differential contributions of choline phosphotransferases CPT1 and CEPT1 to the biosynthesis of choline phospholipids. J. Lipid Res. 62, 100100 (2021).","DOI":"10.1016\/j.jlr.2021.100100"},{"key":"55673_CR50","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","volume":"25","author":"EF Pettersen","year":"2004","unstructured":"Pettersen, E. F. et al. UCSF Chimera?A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605\u20131612 (2004).","journal-title":"J. Comput. Chem."},{"key":"55673_CR51","doi-asserted-by":"publisher","first-page":"2778","DOI":"10.1021\/ci200227u","volume":"51","author":"RA Laskowski","year":"2011","unstructured":"Laskowski, R. A. & Swindells, M. B. LigPlot+: multiple ligand\u2013protein interaction diagrams for drug discovery. J. Chem. Inf. Model. 51, 2778\u20132786 (2011).","journal-title":"J. Chem. Inf. Model."}],"container-title":["Nature Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-55673-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-55673-1","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-55673-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,2,10]],"date-time":"2025-02-10T07:46:27Z","timestamp":1739173587000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-55673-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1,2]]},"references-count":51,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["55673"],"URL":"https:\/\/doi.org\/10.1038\/s41467-024-55673-1","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2024.05.09.593427","asserted-by":"object"}]},"ISSN":["2041-1723"],"issn-type":[{"value":"2041-1723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1,2]]},"assertion":[{"value":"1 May 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 December 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"2 January 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"S.M. is an employee of Xaira Therapeutics. The remaining authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"111"}}