{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T09:35:08Z","timestamp":1787477708191,"version":"build-2736575974"},"reference-count":77,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,8,11]],"date-time":"2025-08-11T00:00:00Z","timestamp":1754870400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004794","name":"National Centre for Scientific Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004794","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011658","name":"French Infrastructure for Integrated Structural Biology","doi-asserted-by":"publisher","award":["ANR-10-INBS-000502"],"award-info":[{"award-number":["ANR-10-INBS-000502"]}],"id":[{"id":"10.13039\/501100011658","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011658","name":"French Infrastructure for Integrated Structural Biology","doi-asserted-by":"publisher","award":["ANR-17-EURE-0003"],"award-info":[{"award-number":["ANR-17-EURE-0003"]}],"id":[{"id":"10.13039\/501100011658","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2025,9]]},"DOI":"10.1016\/j.jbc.2025.110587","type":"journal-article","created":{"date-parts":[[2025,8,12]],"date-time":"2025-08-12T15:34:01Z","timestamp":1755012841000},"page":"110587","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Molecular recognition of fungal methylated glucosylceramides by ETD151 defensin"],"prefix":"10.1016","volume":"301","author":[{"given":"Ons","family":"Kharrat","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fran\u00e7oise","family":"Paquet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1382-4036","authenticated-orcid":false,"given":"Rouba","family":"Nasreddine","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9503-2619","authenticated-orcid":false,"given":"Jean-Baptiste","family":"Madinier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5288-7702","authenticated-orcid":false,"given":"Reine","family":"Nehm\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2647-0188","authenticated-orcid":false,"given":"Vincent","family":"Aucagne","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philippe","family":"Bulet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4363-4965","authenticated-orcid":false,"given":"Dror","family":"Warschawski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e9line","family":"Landon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2025.110587_bib1","doi-asserted-by":"crossref","first-page":"57","DOI":"10.3390\/jof3040057","article-title":"Global and multi-national prevalence of fungal Diseases\u2014estimate precision","volume":"3","author":"Bongomin","year":"2017","journal-title":"J. Fungi"},{"key":"10.1016\/j.jbc.2025.110587_bib2","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/S1473-3099(23)00692-8","article-title":"Global incidence and mortality of severe fungal disease","volume":"24","author":"Denning","year":"2024","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.jbc.2025.110587_bib3","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1038\/s41579-024-01062-w","article-title":"The pathobiology of human fungal infections","volume":"22","author":"Brown","year":"2024","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib4","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a019703","article-title":"Antifungal drug development: challenges, unmet clinical needs, and new approaches","volume":"4","author":"Roemer","year":"2014","journal-title":"Cold Spring Harb Perspect. Med."},{"key":"10.1016\/j.jbc.2025.110587_bib5","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/S0966-842X(03)00117-3","article-title":"Antifungal agents: mechanisms of action","volume":"11","author":"Odds","year":"2003","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib6","doi-asserted-by":"crossref","first-page":"3","DOI":"10.2174\/187152106774755554","article-title":"Azoles: mode of antifungal action and resistance development. Effect of miconazole on endogenous reactive oxygen species production in Candida albicans","volume":"5","author":"Francois","year":"2006","journal-title":"AIAMC"},{"key":"10.1016\/j.jbc.2025.110587_bib7","doi-asserted-by":"crossref","first-page":"321","DOI":"10.3390\/jof6040321","article-title":"Amphotericin B and other polyenes\u2014Discovery, clinical use, mode of action and drug resistance","volume":"6","author":"Carolus","year":"2020","journal-title":"J. Fungi"},{"key":"10.1016\/j.jbc.2025.110587_bib8","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/nyas.12831","article-title":"Mechanisms of echinocandin antifungal drug resistance","volume":"1354","author":"Perlin","year":"2015","journal-title":"Ann. N. Y Acad. Sci."},{"key":"10.1016\/j.jbc.2025.110587_bib9","doi-asserted-by":"crossref","first-page":"106","DOI":"10.3390\/metabo10030106","article-title":"Antifungal drugs","volume":"10","author":"Hou\u0161\u0165","year":"2020","journal-title":"Metabolites"},{"key":"10.1016\/j.jbc.2025.110587_bib10","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1038\/s41579-023-00960-9","article-title":"The rapid emergence of antifungal-resistant human-pathogenic fungi","volume":"21","author":"Lockhart","year":"2023","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib11","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1038\/s44259-023-00007-2","article-title":"Molecular mechanisms governing antifungal drug resistance","volume":"1","author":"Lee","year":"2023","journal-title":"NPJ Antimicrob. Resist."},{"key":"10.1016\/j.jbc.2025.110587_bib12","doi-asserted-by":"crossref","DOI":"10.1128\/microbiolspec.FUNK-0002-2016","article-title":"Antifungal drugs: the Current armamentarium and development of new agents","volume":"4","author":"Robbins","year":"2016","journal-title":"Microbiol. Spectr."},{"key":"10.1016\/j.jbc.2025.110587_bib13","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1038\/nri1180","article-title":"Defensins: antimicrobial peptides of innate immunity","volume":"3","author":"Ganz","year":"2003","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.jbc.2025.110587_bib14","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1016\/j.drudis.2007.07.016","article-title":"Therapeutic potential of antifungal plant and insect defensins","volume":"12","author":"Thevissen","year":"2007","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.jbc.2025.110587_bib15","doi-asserted-by":"crossref","first-page":"97","DOI":"10.3389\/fmicb.2014.00097","article-title":"Defensins: antifungal lessons from eukaryotes","volume":"5","author":"Silva","year":"2014","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib16","doi-asserted-by":"crossref","first-page":"12280","DOI":"10.3390\/molecules190812280","article-title":"Antifungal plant defensins: mechanisms of action and production","volume":"19","author":"Vriens","year":"2014","journal-title":"Molecules"},{"key":"10.1016\/j.jbc.2025.110587_bib17","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00642-18","article-title":"Biological roles played by sphingolipids in dimorphic and filamentous fungi","volume":"9","author":"Fernandes","year":"2018","journal-title":"mBio"},{"key":"10.1016\/j.jbc.2025.110587_bib18","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.4155\/fmc-2016-0053","article-title":"Sphingolipids as targets for treatment of fungal infections","volume":"8","author":"Rollin-Pinheiro","year":"2016","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.jbc.2025.110587_bib19","doi-asserted-by":"crossref","first-page":"3900","DOI":"10.1074\/jbc.M311165200","article-title":"Defensins from insects and plants interact with fungal glucosylceramides","volume":"279","author":"Thevissen","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110587_bib20","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1002\/bip.22570","article-title":"Psd1 binding affinity toward fungal membrane components as assessed by SPR: the role of glucosylceramide in fungal recognition and entry","volume":"102","author":"Neves de Medeiros","year":"2014","journal-title":"Biopolymers"},{"key":"10.1016\/j.jbc.2025.110587_bib21","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1111\/j.1365-2958.2007.05955.x","article-title":"Glucosylceramide synthase is essential for alfalfa defensin-mediated growth inhibition but not for pathogenicity of Fusarium graminearum","volume":"66","author":"Ramamoorthy","year":"2007","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib22","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/1471-2091-15-7","article-title":"Functional expression and activity of the recombinant antifungal defensin PvD1r from Phaseolus vulgaris L. (common bean) seeds","volume":"15","author":"Mello Ede","year":"2014","journal-title":"BMC Biochem."},{"key":"10.1016\/j.jbc.2025.110587_bib23","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.bbamem.2018.12.020","article-title":"Psd2 pea defensin shows a preference for mimetic membrane rafts enriched with glucosylceramide and ergosterol","volume":"1861","author":"Amaral","year":"2019","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.jbc.2025.110587_bib24","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1110\/ps.03404404","article-title":"Lead optimization of antifungal peptides with 3D NMR structures analysis","volume":"13","author":"Landon","year":"2004","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2025.110587_bib25","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2415524122","article-title":"The antimicrobial activity of ETD151 defensin is dictated by the presence of glycosphingolipids in the targeted organisms","volume":"122","author":"Kharrat","year":"2025","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2025.110587_bib27","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1007\/s10096-011-1430-8","article-title":"Cationic antimicrobial peptides in clinical development, with special focus on thanatin and heliomicin","volume":"31","author":"Andr\u00e8s","year":"2012","journal-title":"Eur. J. Clin. Microbiol. Infect. Dis."},{"key":"10.1016\/j.jbc.2025.110587_bib28","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1021\/acs.jproteome.9b00638","article-title":"Impact of an antifungal insect defensin on the proteome of the phytopathogenic fungus Botrytis cinerea","volume":"19","author":"Aumer","year":"2020","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jbc.2025.110587_bib29","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1111\/j.1364-3703.2007.00417.x","article-title":"Botrytis cinerea: the cause of grey mould disease","volume":"8","author":"Williamson","year":"2007","journal-title":"Mol. Plant Pathol."},{"key":"10.1016\/j.jbc.2025.110587_bib30","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/s12154-014-0113-1","article-title":"The rising threat of fungicide resistance in plant pathogenic fungi: botrytis as a case study","volume":"7","author":"Hahn","year":"2014","journal-title":"J. Chem. Biol."},{"key":"10.1016\/j.jbc.2025.110587_bib31","doi-asserted-by":"crossref","first-page":"441","DOI":"10.2217\/fmb-2016-0181","article-title":"Antifungal plant defensins: increased insight in their mode of action as a basis for their use to combat fungal infections","volume":"12","author":"Cools","year":"2017","journal-title":"Future Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib32","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1590\/S0001-37652004000100007","article-title":"Structure and biological functions of fungal cerebrosides","volume":"76","author":"Barreto-Bergter","year":"2004","journal-title":"Acad. Bras Cienc."},{"key":"10.1016\/j.jbc.2025.110587_bib33","doi-asserted-by":"crossref","first-page":"5582","DOI":"10.1074\/jbc.M512864200","article-title":"Identification of fungal sphingolipid C9-methyltransferases by phylogenetic profiling","volume":"281","author":"Ternes","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110587_bib34","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1111\/mmi.13474","article-title":"Functional characterization of the Aspergillus nidulans glucosylceramide pathway reveals that LCB \u03948-desaturation and C9-methylation are relevant to filamentous growth, lipid raft localization and Psd1 defensin activity","volume":"102","author":"Fernandes","year":"2016","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib35","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1111\/j.1462-5822.2011.01735.x","article-title":"Methylation of glycosylated sphingolipid modulates membrane lipid topography and pathogenicity of Cryptococcus neoformans","volume":"14","author":"Singh","year":"2012","journal-title":"Cell Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib36","doi-asserted-by":"crossref","first-page":"605","DOI":"10.3389\/fmicb.2019.00605","article-title":"Membrane sphingolipids regulate the fitness and antifungal protein susceptibility of Neurospora crassa","volume":"10","author":"Huber","year":"2019","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib37","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1128\/EC.00255-08","article-title":"Sphingolipid C-9 methyltransferases are important for growth and virulence but not for sensitivity to antifungal plant defensins in Fusarium graminearum","volume":"8","author":"Ramamoorthy","year":"2009","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.jbc.2025.110587_bib38","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1007\/s00294-013-0416-8","article-title":"Antifungal activity of plant defensin AFP1 in Brassica juncea involves the recognition of the methyl residue in glucosylceramide of target pathogen Candida albicans","volume":"60","author":"Oguro","year":"2014","journal-title":"Curr. Genet."},{"key":"10.1016\/j.jbc.2025.110587_bib39","doi-asserted-by":"crossref","first-page":"1957","DOI":"10.1016\/j.bbamem.2011.03.016","article-title":"Choosing membrane mimetics for NMR structural studies of transmembrane proteins","volume":"1808","author":"Warschawski","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110587_bib40","doi-asserted-by":"crossref","first-page":"3171","DOI":"10.1016\/j.bbamem.2014.08.023","article-title":"Complementary biophysical tools to investigate lipid specificity in the interaction between bioactive molecules and the plasma membrane: a review","volume":"1838","author":"Deleu","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110587_bib41","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.biochi.2016.05.013","article-title":"Antifungal peptides: to be or not to be membrane active","volume":"130","author":"Rautenbach","year":"2016","journal-title":"Biochimie"},{"key":"10.1016\/j.jbc.2025.110587_bib42","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1046\/j.0014-2956.2001.02715.x","article-title":"Lipid rafts and little caves","volume":"269","author":"Zajchowski","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2025.110587_bib43","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/j.jmb.2009.05.066","article-title":"Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy","volume":"390","author":"Bodner","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2025.110587_bib44","doi-asserted-by":"crossref","first-page":"238","DOI":"10.3389\/fchem.2019.00238","article-title":"Elucidating the lipid binding properties of membrane-active peptides using cyclised nanodiscs","volume":"7","author":"Zhang","year":"2019","journal-title":"Front. Chem."},{"key":"10.1016\/j.jbc.2025.110587_bib45","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.chemphyslip.2003.10.012","article-title":"Insights on the interaction of met-enkephalin with negatively charged membranes--an infrared and solid-state NMR spectroscopic study","volume":"127","author":"Marcotte","year":"2004","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jbc.2025.110587_bib46","doi-asserted-by":"crossref","first-page":"888","DOI":"10.1016\/S0006-3495(99)76940-7","article-title":"31P NMR first spectral moment Study of the partial magnetic orientation of phospholipid membranes","volume":"77","author":"Picard","year":"1999","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2025.110587_bib47","doi-asserted-by":"crossref","first-page":"21896","DOI":"10.1073\/pnas.2004807117","article-title":"How cholesterol stiffens unsaturated lipid membranes","volume":"117","author":"Chakraborty","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2025.110587_bib26","series-title":"WHO Fungal Priority Pathogens List to Guide Research, Development and Public Health Action","year":"2022"},{"key":"10.1016\/j.jbc.2025.110587_bib48","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2021.690211","article-title":"Glycosphingolipids in filamentous fungi: biological roles and potential applications in cosmetics and health foods","volume":"12","author":"Jiang","year":"2021","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2025.110587_bib49","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.str.2010.11.011","article-title":"Portrayal of complex dynamic properties of sugarcane defensin 5 by NMR: multiple motions associated with membrane interaction","volume":"19","author":"Silva de Paula","year":"2011","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2025.110587_bib50","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1016\/j.bbamem.2012.02.012","article-title":"Evaluation of the membrane lipid selectivity of the pea defensin Psd1","volume":"1818","author":"Gon\u00e7alves","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110587_bib51","article-title":"Comparative analysis of the techniques for the determination of binding affinity between a small molecule inhibitor and a protein target","author":"Luo","year":"2024","journal-title":"bioRxiv"},{"key":"10.1016\/j.jbc.2025.110587_bib52","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/s12551-025-01280-3","article-title":"Differential scanning fluorimetry followed by microscale thermophoresis and\/or isothermal titration calorimetry as an efficient tool for ligand screening","volume":"17","author":"Winiewska-Szajewska","year":"2025","journal-title":"Biophys. Rev."},{"key":"10.1016\/j.jbc.2025.110587_bib53","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0173260","article-title":"ITC-derived binding affinity may be biased due to titrant (nano)-aggregation. Binding of halogenated benzotriazoles to the catalytic domain of human protein kinase CK2","volume":"12","author":"Winiewska","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.110587_bib54","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2020.583826","article-title":"Enzyme kinetics by isothermal titration calorimetry: allostery, inhibition, and dynamics","author":"Wang","year":"2020","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2025.110587_bib55","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1007\/s12551-017-0296-0","article-title":"Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides","volume":"9","author":"Alvares","year":"2017","journal-title":"Biophys. Rev."},{"key":"10.1016\/j.jbc.2025.110587_bib56","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1074\/jbc.272.2.1171","article-title":"Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity","volume":"272","author":"De Samblanx","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110587_bib57","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/j.febslet.2010.12.039","article-title":"Ultra-high resolution crystal structure of a dimeric defensin SPE10","volume":"585","author":"Song","year":"2011","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2025.110587_bib58","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.bbamem.2009.07.013","article-title":"Backbone dynamics of the antifungal Psd1 pea defensin and its correlation with membrane interaction by NMR spectroscopy","volume":"1798","author":"Neves de Medeiros","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110587_bib59","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1002\/prot.25783","article-title":"Nuclear magnetic resonance solution structure of Pisum sativum defensin 2 provides evidence for the presence of hydrophobic surface-clusters","volume":"88","author":"Pinheiro-Aguiar","year":"2020","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2025.110587_bib60","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0005-2736(99)00205-9","article-title":"The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy","volume":"1462","author":"Bechinger","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110587_bib61","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1016\/j.bbamem.2008.02.009","article-title":"The impact of peptides on lipid membranes","volume":"1778","author":"Khandelia","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110587_bib62","doi-asserted-by":"crossref","first-page":"10320","DOI":"10.1039\/D4TB01107D","article-title":"Influence of lipid vesicle properties on the function of conjugation dependent membrane active peptides","volume":"12","author":"Iversen","year":"2024","journal-title":"J. Mater. Chem. B."},{"key":"10.1016\/j.jbc.2025.110587_bib63","doi-asserted-by":"crossref","first-page":"13723","DOI":"10.1021\/bi9620621","article-title":"Membrane pores induced by Magainin","volume":"35","author":"Ludtke","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.110587_bib64","doi-asserted-by":"crossref","first-page":"2959","DOI":"10.1016\/j.bbamem.2016.09.009","article-title":"Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by 2H solid-state NMR","volume":"1858","author":"Laadhari","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110587_bib65","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/s42003-019-0653-6","article-title":"Integrated solid-state NMR and molecular dynamics modeling determines membrane insertion of human \u03b2-defensin analog","volume":"2","author":"Kang","year":"2019","journal-title":"Commun. Biol."},{"key":"10.1016\/j.jbc.2025.110587_bib66","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.3390\/ijms20051009","article-title":"Exploring the dual interaction of natural rhamnolipids with plant and fungal biomimetic plasma membranes through biophysical studies","volume":"20","author":"Monnier","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2025.110587_bib67","doi-asserted-by":"crossref","first-page":"3698","DOI":"10.1002\/1873-3468.13986","article-title":"Sphingolipid-enriched domains in fungi","volume":"594","author":"Santos","year":"2020","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2025.110587_bib68","doi-asserted-by":"crossref","first-page":"2224","DOI":"10.1016\/j.bbamem.2017.08.017","article-title":"Changes in glucosylceramide structure affect virulence and membrane biophysical properties of Cryptococcus neoformans","volume":"1859","author":"Raj","year":"2017","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.110587_bib69","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1002\/prot.20449","article-title":"The CCPN Data Model for NMR spectroscopy: development of a software pipeline","volume":"59","author":"Vranken","year":"2005","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2025.110587_bib70","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/s10858-005-4425-x","article-title":"SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation spectra of proteins within a few seconds","volume":"33","author":"Schanda","year":"2006","journal-title":"J. Biomol. NMR."},{"key":"10.1016\/j.jbc.2025.110587_bib71","series-title":"The Pymol Molecular Graphics System","author":"Delano","year":"2002"},{"key":"10.1016\/j.jbc.2025.110587_bib72","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.1093\/bioinformatics\/btt286","article-title":"ShereKhan - calculating exchange parameters in relaxation dispersion data from CPMG experiments","volume":"29","author":"Mazur","year":"2013","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jbc.2025.110587_bib73","first-page":"89","article-title":"A general two-site solution for the chemical exchange produced dependence of T2 upon the carr-Purcell pulse separation","volume":"6","author":"Carver","year":"1972","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.jbc.2025.110587_bib74","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.1016\/j.bpj.2018.01.025","article-title":"A new method of assessing lipid mixtures by 31P magic-angle spinning NMR","volume":"114","author":"Warschawski","year":"2018","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2025.110587_bib75","first-page":"221","article-title":"Obtaining high-fidelity powder spectra in anisotropic media: Phase-cycled Hahn echo spectroscopy","volume":"52","author":"Rance","year":"1983","journal-title":"J. Magn. Reson"},{"key":"10.1016\/j.jbc.2025.110587_bib76","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1016\/0009-2614(76)80392-2","article-title":"Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains","volume":"42","author":"Davis","year":"1976","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.jbc.2025.110587_bib77","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.bbamem.2015.10.020","article-title":"A (2)H magic-angle spinning solid-state NMR characterisation of lipid membranes in intact bacteria","volume":"1858","author":"Warnet","year":"2015","journal-title":"Biochim. Biophys. acta"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582502438X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582502438X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T21:17:29Z","timestamp":1772831849000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002192582502438X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9]]},"references-count":77,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2025,9]]}},"alternative-id":["S002192582502438X"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2025.110587","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2025,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Molecular recognition of fungal methylated glucosylceramides by ETD151 defensin","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2025.110587","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology\u00e9","name":"copyright","label":"Copyright"}],"article-number":"110587"}}