{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T21:53:44Z","timestamp":1788558824416,"version":"build-2803163510"},"reference-count":47,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2019,4,10]],"date-time":"2019-04-10T00:00:00Z","timestamp":1554854400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2019,4,10]],"date-time":"2019-04-10T00:00:00Z","timestamp":1554854400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31030025"],"award-info":[{"award-number":["31030025"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31320103901"],"award-info":[{"award-number":["31320103901"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31630016"],"award-info":[{"award-number":["31630016"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>In fungi many proteins, which play important roles in maintaining the function of the cell wall and participating in pathogenic processes, are anchored to the cell surface by a glycosylphosphatidylinositol (GPI) anchor. It has been known that modification and removal of phosphoethanolamine (EtN-P) on the second mannose residue in GPI anchors is important for maturation and sorting of GPI anchored proteins in yeast and mammalian cells, but is a step absent from some protist parasites. In <jats:italic>Aspergillus fumigatus<\/jats:italic>, an opportunistic fungal pathogen causing invasive aspergillosis in humans, GPI-anchored proteins are known to be involved in cell wall synthesis and virulence. In this report the gene encoding <jats:italic>A. fumigatus<\/jats:italic> EtN-P transferase GPI7 was investigated. By deletion of the <jats:italic>gpi7<\/jats:italic> gene, we evaluated the effects of EtN-P modification on the morphogenesis of <jats:italic>A. fumigatus<\/jats:italic> and localization of GPI proteins. Our results showed that deletion of the <jats:italic>gpi7<\/jats:italic> gene led to reduced cell membrane GPI anchored proteins, the mis-localization of the cell wall GPI anchored protein Mp1, abnormal polarity, and autophagy in <jats:italic>A. fumigatus<\/jats:italic>. Our results suggest that addition of EtN-P of the second mannose on the GPI anchor is essential for transportation and localization of the cell wall GPI-anchored proteins.<\/jats:p>","DOI":"10.1038\/s41598-019-42344-1","type":"journal-article","created":{"date-parts":[[2019,4,10]],"date-time":"2019-04-10T10:18:48Z","timestamp":1554891528000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Aspergillus fumigatus phosphoethanolamine transferase gene gpi7 is required for proper transportation of the cell wall GPI-anchored proteins and polarized growth"],"prefix":"10.1038","volume":"9","author":[{"given":"Haomiao","family":"Ouyang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ting","family":"Du","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8996-1518","authenticated-orcid":false,"given":"Iain B. H.","family":"Wilson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7140-5548","authenticated-orcid":false,"given":"Jinghua","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Paul","family":"Latg\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1514-6374","authenticated-orcid":false,"given":"Cheng","family":"Jin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,4,10]]},"reference":[{"issue":"6229","key":"42344_CR1","doi-asserted-by":"publisher","first-page":"1414","DOI":"10.1126\/science.aaa6097","volume":"347","author":"DW Denning","year":"2015","unstructured":"Denning, D. W. & Bromley, M. J. How to bolster the antifungal pipeline. Science 347(6229), 1414\u20131416 (2015).","journal-title":"Science"},{"key":"42344_CR2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1126\/scitranslmed.3004404","volume":"4","author":"GD Brown","year":"2012","unstructured":"Brown, G. D. et al. Hidden killers: Human fungal infections. Sci. Transl. Med. 4, 1\u20139 (2012).","journal-title":"Sci. Transl. Med."},{"key":"42344_CR3","doi-asserted-by":"publisher","first-page":"S36","DOI":"10.1016\/j.jinf.2014.07.011","volume":"69","author":"A Warris","year":"2014","unstructured":"Warris, A. The biology of pulmonary aspergillus infections. J. Infect. 69, S36\u2013S41 (2014).","journal-title":"J. Infect."},{"issue":"3","key":"42344_CR4","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1007\/s12275-016-0647-8","volume":"54","author":"J-Y Kim","year":"2016","unstructured":"Kim, J.-Y. Human fungal pathogens: Why should we learn? J. Microbiol. 54(3), 145\u2013148 (2016).","journal-title":"J. Microbiol."},{"key":"42344_CR5","doi-asserted-by":"publisher","first-page":"232","DOI":"10.1007\/s12275-016-6045-4","volume":"54","author":"MJ Lee","year":"2016","unstructured":"Lee, M. J. & Sheppard, D. C. Recent advances in the understanding of the Aspergillus fumigatus cell wall. J. Microbiol. 54, 232\u2013242 (2016).","journal-title":"J. Microbiol."},{"key":"42344_CR6","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1007\/s12275-016-5510-4","volume":"54","author":"NA Brown","year":"2016","unstructured":"Brown, N. A. & Goldman, G. H. The contribution of Aspergillus fumigatus stress responses to virulence and antifungal resistance. J. Microbiol. 54, 243\u2013253 (2016).","journal-title":"J. Microbiol."},{"key":"42344_CR7","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1007\/s12275-016-5619-5","volume":"54","author":"HS Park","year":"2016","unstructured":"Park, H. S. & Yu, J. H. Developmental regulators in Aspergillus fumigatus. J. Microbiol. 54, 223\u2013231 (2016).","journal-title":"J. Microbiol."},{"key":"42344_CR8","first-page":"438","volume":"7","author":"N Escobar","year":"2016","unstructured":"Escobar, N. et al. Hide, keep quiet, and keep low: properties that make Aspergillus fumigatus a successful lung pathogen. Frontiers in Microbiology 7, 438 (2016).","journal-title":"Frontiers in Microbiology"},{"key":"42344_CR9","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1016\/j.fgb.2005.04.002","volume":"42","author":"PWJ De Groot","year":"2005","unstructured":"De Groot, P. W. J., Ram, A. F. & Klis, F. M. Features and functions of covalently linked proteins in fungal cell walls. Fungal Genet. Biol. 42, 657\u2013675 (2005).","journal-title":"Fungal Genet. Biol."},{"key":"42344_CR10","doi-asserted-by":"publisher","first-page":"993","DOI":"10.1194\/jlr.R700002-JLR200","volume":"48","author":"P Orlean","year":"2007","unstructured":"Orlean, P. & Menon, A. K. Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J. Lipid Res. 48, 993\u20131011 (2007).","journal-title":"J. Lipid Res."},{"issue":"3","key":"42344_CR11","doi-asserted-by":"publisher","first-page":"e59013","DOI":"10.1371\/journal.pone.0059013","volume":"8","author":"J Yan","year":"2013","unstructured":"Yan, J. et al. Transcriptome and biochemical analysis reveals that suppression of GPI-anchor synthesis leads to autophagy and possible necroptosis in Aspergillus fumigatus. PLoS One 8(3), e59013 (2013).","journal-title":"PLoS One"},{"key":"42344_CR12","doi-asserted-by":"publisher","first-page":"4701","DOI":"10.1038\/sj.emboj.7600456","volume":"23","author":"TK Smith","year":"2004","unstructured":"Smith, T. K., Crossman, A., Brimacombe, J. S. & Ferguson, M. A. J. Chemical validation of GPI biosynthesis as a drug target against African sleeping sickness. EMBO J. 23, 4701\u20134708 (2004).","journal-title":"EMBO J."},{"key":"42344_CR13","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1021\/id5000212","volume":"1","author":"PA Mann","year":"2015","unstructured":"Mann, P. A. et al. Chemical genomics-based antifungal drug discovery: targeting glycosylphosphatidylinositol (GPI) precursor biosynthesis. ACS Infect. Dis. 1, 59\u201372 (2015).","journal-title":"ACS Infect. Dis."},{"key":"42344_CR14","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1093\/jb\/mvn090","volume":"144","author":"T Kinoshita","year":"2008","unstructured":"Kinoshita, T., Fujita, M. & Maeda, Y. Biosynthesis, remodeling and functions of mammalian GPI-anchored proteins: Recent progress. J. Biochem. 144, 287\u2013294 (2008).","journal-title":"J. Biochem."},{"key":"42344_CR15","doi-asserted-by":"publisher","first-page":"130","DOI":"10.2183\/pjab.90.130","volume":"90","author":"T Kinoshita","year":"2014","unstructured":"Kinoshita, T. Biosynthesis and deficiencies of glycosylphosphatidylinositol. Proc. Jpn. Acad. Ser. B Phy.s Biol. Sci. 90, 130\u2013143 (2014).","journal-title":"Proc. Jpn. Acad. Ser. B Phy.s Biol. Sci."},{"issue":"10","key":"42344_CR16","doi-asserted-by":"publisher","first-page":"9728","DOI":"10.1074\/jbc.M413755200","volume":"280","author":"N Shishioh","year":"2005","unstructured":"Shishioh, N. et al. GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J. Biol. Chem. 280(10), 9728\u20139734 (2005).","journal-title":"J. Biol. Chem."},{"issue":"5","key":"42344_CR17","doi-asserted-by":"publisher","first-page":"1611","DOI":"10.1091\/mbc.11.5.1611","volume":"11","author":"CH Taron","year":"2000","unstructured":"Taron, C. H., Wiedman, J. M., Grimme, S. J. & Orlean, P. Glycosylphosphatidylinositol biosynthesis defects in Gpi11p- and Gpi13p-deficient yeast suggest a branched pathway and implicate gpi13p in phosphoethanolamine transfer to the third mannose. Mol. Biol. Cell 11(5), 1611\u20131630 (2000).","journal-title":"Mol. Biol. Cell"},{"issue":"8","key":"42344_CR18","doi-asserted-by":"publisher","first-page":"e2369","DOI":"10.1371\/journal.pntd.0002369","volume":"7","author":"MS Cardoso","year":"2013","unstructured":"Cardoso, M. S. et al. Identification and Functional Analysis of Trypanosoma cruzi Genes That Encode Proteins of the Glycosylphosphatidylinositol Biosynthetic Pathway. PLOS Neglected Tropical Diseases 7(8), e2369 (2013).","journal-title":"PLOS Neglected Tropical Diseases"},{"issue":"3","key":"42344_CR19","doi-asserted-by":"publisher","first-page":"627","DOI":"10.1091\/mbc.10.3.627","volume":"10","author":"E Gaynor","year":"1999","unstructured":"Gaynor, E. et al. MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast. Mol. Biol. Cell 10(3), 627\u201348 (1999).","journal-title":"Mol. Biol. Cell"},{"issue":"32","key":"42344_CR20","doi-asserted-by":"publisher","first-page":"24458","DOI":"10.1074\/jbc.M003844200","volume":"275","author":"I Flury","year":"2000","unstructured":"Flury, I., Benachour, A. & Conzelmann, A. YLL031c belongs to a novel family of membrane proteins involved in the transfer of ethanolaminephosphate onto the core structure of glycosylphosphatidylinositol anchors in yeast. J. Biol. Chem. 275(32), 24458\u201324465 (2000).","journal-title":"J. Biol. Chem."},{"issue":"5","key":"42344_CR21","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1266\/ggs.77.309","volume":"77","author":"A Toh-e","year":"2002","unstructured":"Toh-e, A. & Oguchi, T. Genetic characterization of genes encoding enzymes catalyzing addition of phosphoethanolamine to the glycosylphosphatidylinositol anchor in Saccharomyces cerevisiae. Genes Genet. Syst. 77(5), 309\u2013322 (2002).","journal-title":"Genes Genet. Syst."},{"issue":"6","key":"42344_CR22","doi-asserted-by":"publisher","first-page":"1333","DOI":"10.1083\/jcb.130.6.1333","volume":"130","author":"M Benghezal","year":"1995","unstructured":"Benghezal, M., Lipke, P. & Conzelmann, A. Identification of six complementation classes involved in the biosynthesis of glycosylphosphatidyl- inositol anchors in Saccharomyces cerevisiae. J. Cell Biol. 130(6), 1333\u201344 (1995).","journal-title":"J. Cell Biol."},{"issue":"3","key":"42344_CR23","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1046\/j.1365-2958.2002.02926.x","volume":"44","author":"M Richard","year":"2002","unstructured":"Richard, M. et al. Complete glycosylphosphatidylinositol anchors are required in Candida albicans for full morphogenesis, virulence and resistance to macrophages. Mol. Microbiol. 44(3), 841\u2013853 (2002).","journal-title":"Mol. Microbiol."},{"issue":"1","key":"42344_CR24","doi-asserted-by":"publisher","first-page":"140","DOI":"10.1111\/mmi.12175","volume":"88","author":"T Yoko-o","year":"2013","unstructured":"Yoko-o, T. et al. Determination and physiological roles of the glycosylphosphatidylinositol lipid remodelling pathway in yeast. Mol. Microbiol. 88(1), 140\u2013155 (2013).","journal-title":"Mol. Microbiol."},{"issue":"50","key":"42344_CR25","doi-asserted-by":"publisher","first-page":"51869","DOI":"10.1074\/jbc.M405232200","volume":"279","author":"M Fujita","year":"2004","unstructured":"Fujita, M., Yoko-o, T., Okamoto, M. & Jigami, Y. GPI7 involved in glycosylphosphatidylinositol biosynthesis is essential for yeast cell separation. J. Biol. Chem. 279(50), 51869\u201379 (2004).","journal-title":"J. Biol. Chem."},{"issue":"21","key":"42344_CR26","doi-asserted-by":"publisher","first-page":"15251","DOI":"10.1074\/jbc.274.21.15251","volume":"274","author":"A Benachour","year":"1999","unstructured":"Benachour, A. et al. Deletion of GPI7, a yeast gene required for addition of a side chain to the glycosylphosphatidylinositol (GPI) core structure, affects GPI protein transport, remodeling, and cell wall integrity. J Biol. Chem. 274(21), 15251\u201315261 (1999).","journal-title":"J Biol. Chem."},{"issue":"22","key":"42344_CR27","doi-asserted-by":"crossref","first-page":"15277","DOI":"10.1016\/S0021-9258(19)49529-X","volume":"267","author":"A Menon","year":"1992","unstructured":"Menon, A. & Stevens, V. Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein. J. Biol. Chem. 267(22), 15277\u201315280 (1992).","journal-title":"J. Biol. Chem."},{"issue":"12","key":"42344_CR28","doi-asserted-by":"publisher","first-page":"1271","DOI":"10.1093\/glycob\/10.12.1271","volume":"10","author":"I Imhof","year":"2000","unstructured":"Imhof, I., Canivenc-Gansel, E., Meyer, U. & Conzelmann, A. Phosphatidylethanolamine is the donor of the phosphorylethanolamine linked to the alpha1,4-linked mannose of yeast GPI structures. Glycobiology 10(12), 1271\u20131275 (2000).","journal-title":"Glycobiology"},{"key":"42344_CR29","doi-asserted-by":"publisher","first-page":"15267","DOI":"10.1021\/bi0486029","volume":"43","author":"T Fontaine","year":"2004","unstructured":"Fontaine, T. et al. In vitro biosynthesis of glycosylphosphatidylinositol in Aspergillus fumigatus. Biochemistry 43, 15267\u201315275 (2004).","journal-title":"Biochemistry"},{"issue":"9","key":"42344_CR30","doi-asserted-by":"publisher","first-page":"859","DOI":"10.1038\/embor.2008.163","volume":"9","author":"J Geng","year":"2008","unstructured":"Geng, J. & Klionsky, D. J. The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. \u2018Protein modifications: beyond the usual suspects\u2019 review series. EMBO Rep. 9(9), 859\u201364 (2008).","journal-title":"EMBO Rep."},{"key":"42344_CR31","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/S1937-6448(07)66005-5","volume":"266","author":"EL Eskelinen","year":"2008","unstructured":"Eskelinen, E. L. New insights into the mechanisms of macroautophagy in mammalian cells. International Review of Cell and Molecular Biology 266, 207\u2013247 (2008).","journal-title":"International Review of Cell and Molecular Biology"},{"key":"42344_CR32","doi-asserted-by":"publisher","first-page":"14882","DOI":"10.1074\/jbc.275.20.14882","volume":"275","author":"I Mouyna","year":"2000","unstructured":"Mouyna, I. et al. Glycosylphosphatidylinositol anchored glucanosyltransferases play an active role in the biosynthesis of the fungal cell wall. J. Biol. Chem. 275, 14882\u201314889 (2000).","journal-title":"J. Biol. Chem."},{"key":"42344_CR33","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1093\/glycob\/cwg004","volume":"13","author":"T Fontaine","year":"2003","unstructured":"Fontaine, T. et al. Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins. Glycobiol. 13, 169\u2013177 (2003).","journal-title":"Glycobiol."},{"key":"42344_CR34","doi-asserted-by":"publisher","first-page":"3830","DOI":"10.1128\/JCM.39.11.3830-3837.2001","volume":"39","author":"K Yuen","year":"2001","unstructured":"Yuen, K. et al. Characterization of AFMP1: a novel target for serodiagnosis of aspergillosis. J. Clin. Microbiol. 39, 3830\u20133837 (2001).","journal-title":"J. Clin. Microbiol."},{"key":"42344_CR35","doi-asserted-by":"publisher","first-page":"889","DOI":"10.1128\/EC.00351-12","volume":"12","author":"H Ouyang","year":"2013","unstructured":"Ouyang, H. et al. One single basic amino acid at \u03c9-1 or \u03c9-2 site is a signal that retains glycosylphosphatidylinositol (GPI) anchored protein in plasma membrane of Aspergillus fumigatus. Eukaryotic cell 12, 889\u2013899 (2013).","journal-title":"Eukaryotic cell"},{"key":"42344_CR36","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/j.fgb.2015.02.006","volume":"76","author":"J Wang","year":"2015","unstructured":"Wang, J. et al. Kexin-like endoprotease KexB is required for N-glycan processing, morphogenesis and virulence in Aspergillus fumigatus. Fungal Genetics and Biology 76, 57\u201369 (2015).","journal-title":"Fungal Genetics and Biology"},{"key":"42344_CR37","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1016\/j.cell.2009.08.040","volume":"139","author":"M Fujita","year":"2009","unstructured":"Fujita, M. et al. GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi. Cell 139, 352\u2013365 (2009).","journal-title":"Cell"},{"key":"42344_CR38","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1083\/jcb.201012074","volume":"194","author":"M Fujita","year":"2011","unstructured":"Fujita, M. et al. Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI. J. Cell Biol. 194, 61\u201375 (2011).","journal-title":"J. Cell Biol."},{"key":"42344_CR39","doi-asserted-by":"publisher","first-page":"2924","DOI":"10.1091\/mbc.e11-04-0294","volume":"22","author":"GA Castillon","year":"2011","unstructured":"Castillon, G. A. et al. The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling. Mol. Biol. Cell 22, 2924\u20132936 (2011).","journal-title":"Mol. Biol. Cell"},{"key":"42344_CR40","doi-asserted-by":"publisher","first-page":"14256","DOI":"10.1074\/jbc.M313755200","volume":"279","author":"S Tanaka","year":"2004","unstructured":"Tanaka, S., Maeda, Y., Tashima, Y. & Kinoshita, T. Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p. J. Biol. Chem. 279, 14256\u201314263 (2004).","journal-title":"J. Biol. Chem."},{"key":"42344_CR41","doi-asserted-by":"publisher","first-page":"3506","DOI":"10.1093\/emboj\/16.12.3506","volume":"16","author":"F Reggiori","year":"1997","unstructured":"Reggiori, F., Canivenc-Gansel, E. & Conzelmann, A. Lipid remodeling leads to the introduction and exchange of defined ceramides on GPI proteins in the ER and Golgi of Saccharomyces cerevisiae. EMBO J. 16, 3506\u20133518 (1997).","journal-title":"EMBO J."},{"key":"42344_CR42","doi-asserted-by":"publisher","first-page":"1050","DOI":"10.1016\/j.bbalip.2012.01.004","volume":"1821","author":"M Fujita","year":"2012","unstructured":"Fujita, M. & Kinoshita, T. GPI-anchor remodeling: potential functions of GPI-anchors in intracellular trafficking and membrane dynamics. Biochim. Biophys. Acta 1821, 1050\u20131058 (2012).","journal-title":"Biochim. Biophys. Acta"},{"key":"42344_CR43","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1016\/j.cub.2014.11.039","volume":"25","author":"J Manzano-Lopez","year":"2015","unstructured":"Manzano-Lopez, J. et al. COPII coat composition is actively regulated by luminal cargo maturation. Curr. Biol. 25, 152\u2013162 (2015).","journal-title":"Curr. Biol."},{"key":"42344_CR44","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1007\/s002940050350","volume":"33","author":"G Weidner","year":"1998","unstructured":"Weidner, G., d\u2019Enfert, C., Koch, A., Mol, P. & Brakhage, A. Development of a homologous transformation system for the human pathogenic fungus Aspergillus fumigatus based on the pyrG gene encoding orotidine 5\u2032-monophosphate decarboxylase. Curr. Genet. 33, 378\u201385 (1998).","journal-title":"Curr. Genet."},{"key":"42344_CR45","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/S0926-6593(66)80120-0","volume":"113","author":"D Cove","year":"1966","unstructured":"Cove, D. The induction and repression of nitrate reductase in the fungus Aspergillus nidulans. Biochim. Biophys. Acta 113, 51\u201356 (1966).","journal-title":"Biochim. Biophys. Acta"},{"key":"42344_CR46","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1007\/s002940050103","volume":"30","author":"C d\u2019Enfert","year":"1996","unstructured":"d\u2019Enfert, C. Selection of multiple disruption events in Aspergillus fumigatus using the orotidine-50-decarboxylase gene, pyrG, as a unique transformation marker. Curr. Genet. 30, 76\u201382 (1996).","journal-title":"Curr. Genet."},{"key":"42344_CR47","doi-asserted-by":"publisher","first-page":"1470","DOI":"10.1073\/pnas.81.5.1470","volume":"81","author":"M Yelton","year":"1984","unstructured":"Yelton, M., Hamer, J. & Timerberlake, W. Transformation of Aspergillus nidulans by using a trpC plasmid. Proc. Natl. Acad. Sci. USA 81, 1470\u20131474 (1984).","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-42344-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-42344-1","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-42344-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,12,17]],"date-time":"2022-12-17T08:33:04Z","timestamp":1671265984000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-42344-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,4,10]]},"references-count":47,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2019,12]]}},"alternative-id":["42344"],"URL":"https:\/\/doi.org\/10.1038\/s41598-019-42344-1","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,4,10]]},"assertion":[{"value":"19 October 2018","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"21 February 2019","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"10 April 2019","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}],"article-number":"5857"}}