{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T14:10:58Z","timestamp":1770819058602,"version":"3.50.1"},"reference-count":49,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T00:00:00Z","timestamp":1767916800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T00:00:00Z","timestamp":1770768000000},"content-version":"vor","delay-in-days":33,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"DOI":"10.13039\/501100003716","name":"Korea Basic Science Institute","doi-asserted-by":"crossref","award":["RS-2023-NF001356"],"award-info":[{"award-number":["RS-2023-NF001356"]}],"id":[{"id":"10.13039\/501100003716","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["RS-2025-00557077"],"award-info":[{"award-number":["RS-2025-00557077"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["npj Sci Food"],"DOI":"10.1038\/s41538-025-00701-7","type":"journal-article","created":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T22:44:12Z","timestamp":1767998652000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Novel \u03b1-amylolyzates derived from enzymatically synthesized \u03b1-glucans using diverse glycogen branching enzymes decelerate glucose release by modulation of intestinal \u03b1-glucosidases"],"prefix":"10.1038","volume":"10","author":[{"given":"Young-Bo","family":"Song","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Moon-Gi","family":"Hong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Won-Min","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nardo Esmeralda","family":"Nava Rodriguez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David R.","family":"Rose","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sang-Ho","family":"Yoo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Byung-Hoo","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2026,1,9]]},"reference":[{"key":"701_CR1","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/0308-8146(96)00056-8","volume":"57","author":"HN Englyst","year":"1996","unstructured":"Englyst, H. N. & Hudson, G. J. The classification and measurement of dietary carbohydrates. Food Chem. 57, 15\u201321 (1996).","journal-title":"Food Chem."},{"key":"701_CR2","doi-asserted-by":"publisher","first-page":"306","DOI":"10.1159\/000477386","volume":"42","author":"X Yang","year":"2017","unstructured":"Yang, X. et al. Resistant starch regulates gut microbiota: structure, biochemistry and cell signalling. Cell. Physiol. Biochem. 42, 306\u2013318 (2017).","journal-title":"Cell. Physiol. Biochem."},{"key":"701_CR3","doi-asserted-by":"publisher","first-page":"852","DOI":"10.1080\/10408390903372466","volume":"49","author":"G Zhang","year":"2009","unstructured":"Zhang, G. & Hamaker, B. R. Slowly digestible starch: concept, mechanism, and proposed extended glycemic index. Crit. Rev. Food Sci. Nutr. 49, 852\u2013867 (2009).","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"701_CR4","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1111\/j.1753-4887.1999.tb01810.x","volume":"57","author":"KL Morris","year":"1999","unstructured":"Morris, K. L. & Zemel, M. B. Glycemic index, cardiovascular disease, and obesity. Nutr. Rev. 57, 273\u2013276 (1999).","journal-title":"Nutr. Rev."},{"key":"701_CR5","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1079\/PNS2005485","volume":"65","author":"LM Aston","year":"2006","unstructured":"Aston, L. M. Glycaemic index and metabolic disease risk. Proc. Nutr. Soc. 65, 125\u2013134 (2006).","journal-title":"Proc. Nutr. Soc."},{"key":"701_CR6","doi-asserted-by":"publisher","first-page":"S262","DOI":"10.2337\/dc08-s264","volume":"31","author":"MH Shanik","year":"2008","unstructured":"Shanik, M. H. et al. Insulin resistance and hyperinsulinemia: Is hyperinsulinemia the cart or the horse? Diabetes Care 31, S262\u2013S268 (2008).","journal-title":"Diabetes Care"},{"key":"701_CR7","doi-asserted-by":"publisher","first-page":"1873","DOI":"10.1093\/ajcn\/nqab270","volume":"114","author":"DS Ludwig","year":"2021","unstructured":"Ludwig, D. S. et al. The carbohydrate-insulin model: a physiological perspective on the obesity pandemic. Am. J. Clin. Nutr. 114, 1873\u20131885 (2021).","journal-title":"Am. J. Clin. Nutr."},{"key":"701_CR8","doi-asserted-by":"publisher","first-page":"1700117","DOI":"10.1002\/mnfr.201700117","volume":"62","author":"LY Hasek","year":"2018","unstructured":"Hasek, L. Y. et al. Dietary slowly digestible starch triggers the gut\u2013brain axis in obese rats with accompanied reduced food intake. Mol. Nutr. Food Res. 62, 1700117 (2018).","journal-title":"Mol. Nutr. Food Res."},{"key":"701_CR9","first-page":"338","volume":"27","author":"M Chisbert","year":"2024","unstructured":"Chisbert, M. et al. The impact of slowly digestible and resistant starch on glucose homeostasis and insulin resistance. Curr. Opin. Clin. Nutr. Metab. Care 27, 338\u2013343 (2024).","journal-title":"Curr. Opin. Clin. Nutr. Metab. Care"},{"key":"701_CR10","doi-asserted-by":"publisher","first-page":"1072","DOI":"10.1039\/C4FO00803K","volume":"6","author":"G Zhang","year":"2015","unstructured":"Zhang, G. et al. Gut feedback mechanisms and food intake: a physiological approach to slow carbohydrate bioavailability. Food Funct. 6, 1072\u20131089 (2015).","journal-title":"Food Funct."},{"key":"701_CR11","doi-asserted-by":"publisher","first-page":"1051","DOI":"10.1093\/jn\/133.4.1051","volume":"133","author":"BW Wolf","year":"2003","unstructured":"Wolf, B. W. et al. Pullulan is a slowly digested carbohydrate in humans. J. Nutr. 133, 1051\u20131055 (2003).","journal-title":"J. Nutr."},{"key":"701_CR12","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1016\/j.nutres.2017.06.009","volume":"45","author":"F Cisse","year":"2017","unstructured":"Cisse, F. et al. Preload of slowly digestible carbohydrate microspheres decreases gastric emptying rate of subsequent meal in humans. Nutr. Res. 45, 46\u201351 (2017).","journal-title":"Nutr. Res."},{"key":"701_CR13","doi-asserted-by":"publisher","first-page":"1152","DOI":"10.1136\/gut.24.12.1152","volume":"24","author":"B Jones","year":"1983","unstructured":"Jones, B. et al. Glucose absorption from starch hydrolysates in the human jejunum. Gut 24, 1152\u20131160 (1983).","journal-title":"Gut"},{"key":"701_CR14","doi-asserted-by":"publisher","first-page":"3076","DOI":"10.1074\/jbc.273.5.3076","volume":"273","author":"BL Nichols","year":"1998","unstructured":"Nichols, B. L. et al. Human small intestinal maltase-glucoamylase cDNA cloning homology to sucrase-isomaltase. J. Biol. Chem. 273, 3076\u20133081 (1998).","journal-title":"J. Biol. Chem."},{"key":"701_CR15","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1016\/0092-8674(86)90739-7","volume":"46","author":"W Hunziker","year":"1986","unstructured":"Hunziker, W. et al. The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein. Cell 46, 227\u2013234 (1986).","journal-title":"Cell"},{"key":"701_CR16","doi-asserted-by":"publisher","first-page":"182","DOI":"10.1016\/j.carbpol.2014.02.033","volume":"107","author":"P Kittisuban","year":"2014","unstructured":"Kittisuban, P. et al. Slow glucose release property of enzyme-synthesized highly branched maltodextrins differs among starch sources. Carbohydr. Polym. 107, 182\u2013191 (2014).","journal-title":"Carbohydr. Polym."},{"key":"701_CR17","doi-asserted-by":"publisher","first-page":"17763","DOI":"10.1074\/jbc.M109.078980","volume":"285","author":"L Sim","year":"2010","unstructured":"Sim, L. et al. Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains. J. Biol. Chem. 285, 17763\u201317770 (2010).","journal-title":"J. Biol. Chem."},{"key":"701_CR18","doi-asserted-by":"crossref","unstructured":"Lee, B.-H. et al. Contribution of the individual small intestinal \u03b1-glucosidases to digestion of unusual \u03b1-linked glycemic disaccharides. J. Agric. Food Chem. 64, 6487\u20136494 (2016).","DOI":"10.1021\/acs.jafc.6b01816"},{"key":"701_CR19","doi-asserted-by":"publisher","first-page":"1355","DOI":"10.1128\/AEM.02141-08","volume":"75","author":"M Palomo","year":"2009","unstructured":"Palomo, M. et al. The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains. Appl. Environ. Microbiol. 75, 1355\u20131362 (2009).","journal-title":"Appl. Environ. Microbiol."},{"key":"701_CR20","doi-asserted-by":"publisher","first-page":"2167","DOI":"10.1016\/j.bbagen.2012.09.022","volume":"1830","author":"X Roussel","year":"2013","unstructured":"Roussel, X. et al. Characterization of substrate and product specificity of the purified recombinant glycogen branching enzyme of Rhodothermus obamensis. Biochim. Biophys. Acta Gen. Subj. 1830, 2167\u20132177 (2013).","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"701_CR21","doi-asserted-by":"crossref","unstructured":"Sorndech, W. et al. Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates. Carbohydr. Polym. 152, 51\u201361 (2016).","DOI":"10.1016\/j.carbpol.2016.06.097"},{"key":"701_CR22","doi-asserted-by":"publisher","first-page":"1758","DOI":"10.1016\/j.ijbiomac.2017.10.049","volume":"107","author":"Y Li","year":"2018","unstructured":"Li, Y. et al. Modification by \u03b1-d-glucan branching enzyme lowers the in vitro digestibility of starch from different sources. Int. J. Biol. Macromol. 107, 1758\u20131764 (2018).","journal-title":"Int. J. Biol. Macromol."},{"key":"701_CR23","doi-asserted-by":"publisher","first-page":"106057","DOI":"10.1016\/j.foodhyd.2020.106057","volume":"108","author":"Y-E Shim","year":"2020","unstructured":"Shim, Y.-E. et al. Highly branched \u03b1-limit dextrins attenuate the glycemic response and stimulate the secretion of satiety hormone peptide YY. Food Hydrocoll. 108, 106057 (2020).","journal-title":"Food Hydrocoll."},{"key":"701_CR24","doi-asserted-by":"publisher","first-page":"89","DOI":"10.3390\/foods12010089","volume":"12","author":"Y Wang","year":"2022","unstructured":"Wang, Y. et al. Association of slowly digestible starch intake with reduction of postprandial glycemic response: an update meta-analysis. Foods 12, 89 (2022).","journal-title":"Foods"},{"key":"701_CR25","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s10068-019-00686-6","volume":"29","author":"D-H Seo","year":"2020","unstructured":"Seo, D.-H. et al. Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase. Food Sci. Biotechnol. 29, 1\u201316 (2020).","journal-title":"Food Sci. Biotechnol."},{"key":"701_CR26","doi-asserted-by":"publisher","first-page":"119016","DOI":"10.1016\/j.carbpol.2021.119016","volume":"278","author":"M-G Hong","year":"2022","unstructured":"Hong, M.-G. et al. Effect of highly branched \u03b1-glucans synthesized by dual glycosyltransferases on the glucose release rate. Carbohydr. Polym. 278, 119016 (2022).","journal-title":"Carbohydr. Polym."},{"key":"701_CR27","doi-asserted-by":"publisher","first-page":"109882","DOI":"10.1016\/j.enzmictec.2021.109882","volume":"150","author":"ALO Gaenssle","year":"2021","unstructured":"Gaenssle, A. L. O. et al. GH13 Glycogen branching enzymes can adapt the substrate chain length towards their preferences via \u03b1-1, 4-transglycosylation. Enz. Microb. Technol. 150, 109882 (2021).","journal-title":"Enz. Microb. Technol."},{"key":"701_CR28","first-page":"1386","volume":"18","author":"B-H Lee","year":"2008","unstructured":"Lee, B.-H. et al. Heterologous expression and characterization of glycogen branching enzyme from Synechocystis sp. PCC6803. J. Microb. Biotechnol. 18, 1386\u20131392 (2008).","journal-title":"J. Microb. Biotechnol."},{"key":"701_CR29","unstructured":"Yoo, S. Expression, Characterization, and Application of Bifidobacterium Glycogen Branching Enzyme. Master\u2019s degree thesis, Sejong Univ. (2020)."},{"key":"701_CR30","doi-asserted-by":"publisher","first-page":"120730","DOI":"10.1016\/j.carbpol.2023.120730","volume":"310","author":"Y-E Shim","year":"2023","unstructured":"Shim, Y.-E. et al. Production of highly branched \u03b1-limit dextrins with enhanced slow digestibility by various glycogen-branching enzymes. Carbohydr. Polym. 310, 120730 (2023).","journal-title":"Carbohydr. Polym."},{"key":"701_CR31","doi-asserted-by":"crossref","unstructured":"Song, Y.-B. et al. Enzymatic amplification of \u03b1-1, 6 linkages by glycosyltransferases on banana starches to enhance slow digestibility at the small intestinal \u03b1-glucosidase level. Food Hydrocoll. 168, 111518 (2025).","DOI":"10.1016\/j.foodhyd.2025.111518"},{"key":"701_CR32","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/j.carbpol.2016.09.088","volume":"157","author":"B-H Lee","year":"2017","unstructured":"Lee, B.-H. & Hamaker, B. R. Number of branch points in \u03b1-limit dextrins impact glucose generation rates by mammalian mucosal \u03b1-glucosidases. Carbohydr. Polym. 157, 207\u2013213 (2017).","journal-title":"Carbohydr. Polym."},{"key":"701_CR33","doi-asserted-by":"publisher","first-page":"31929","DOI":"10.1074\/jbc.M112.351858","volume":"287","author":"B-H Lee","year":"2012","unstructured":"Lee, B.-H. et al. Modulation of starch digestion for slow glucose release through \u201ctoggling\u201d of activities of mucosal \u03b1-glucosidases. J. Biol. Chem. 287, 31929\u201331938 (2012).","journal-title":"J. Biol. Chem."},{"key":"701_CR34","doi-asserted-by":"publisher","first-page":"1111","DOI":"10.1002\/mnfr.201300599","volume":"58","author":"BH Lee","year":"2014","unstructured":"Lee, B. H. et al. Mucosal C-terminal maltase-glucoamylase hydrolyzes large size starch digestion products that may contribute to rapid postprandial glucose generation. Mol. Nutr. Food Res. 58, 1111\u20131121 (2014).","journal-title":"Mol. Nutr. Food Res."},{"key":"701_CR35","doi-asserted-by":"publisher","first-page":"782","DOI":"10.1016\/j.jmb.2007.10.069","volume":"375","author":"L Sim","year":"2008","unstructured":"Sim, L. et al. Human intestinal maltase\u2013glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. J. Mol. Biol. 375, 782\u2013792 (2008).","journal-title":"J. Mol. Biol."},{"key":"701_CR36","doi-asserted-by":"publisher","first-page":"1612","DOI":"10.1016\/j.carres.2009.04.019","volume":"344","author":"J-H Jung","year":"2009","unstructured":"Jung, J.-H. et al. Enzymatic synthesis of salicin glycosides through transglycosylation catalyzed by amylosucrases from Deinococcus geothermalis and Neisseria polysaccharea. Carbohydr. Res. 344, 1612\u20131619 (2009).","journal-title":"Carbohydr. Res."},{"key":"701_CR37","doi-asserted-by":"publisher","first-page":"1000","DOI":"10.1021\/bm049326g","volume":"6","author":"G Potocki-Veronese","year":"2005","unstructured":"Potocki-Veronese, G. et al. Amylose synthesized in vitro by amylosucrase: morphology, structure, and properties. Biomacromolecules 6, 1000\u20131011 (2005).","journal-title":"Biomacromolecules"},{"key":"701_CR38","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/S0021-9258(18)75307-6","volume":"108","author":"JB Sumner","year":"1935","unstructured":"Sumner, J. B. & Howell, S. F. A method for determination of saccharase activity. J. Biol. Chem. 108, 51\u201354 (1935).","journal-title":"J. Biol. Chem."},{"key":"701_CR39","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1016\/j.carbpol.2006.05.018","volume":"67","author":"J-H Park","year":"2007","unstructured":"Park, J.-H. et al. The action mode of Thermus aquaticus YT-1 4-\u03b1-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin. Carbohydr. Polym. 67, 164\u2013173 (2007).","journal-title":"Carbohydr. Polym."},{"key":"701_CR40","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.jcs.2004.04.001","volume":"40","author":"A Rolland-Sabat\u00e9","year":"2004","unstructured":"Rolland-Sabat\u00e9, A. et al. Elongation and insolubilisation of \u03b1-glucans by the action of Neisseria polysaccharea amylosucrase. J. Cereal Sci. 40, 17\u201330 (2004).","journal-title":"J. Cereal Sci."},{"key":"701_CR41","doi-asserted-by":"publisher","first-page":"e59745","DOI":"10.1371\/journal.pone.0059745","volume":"8","author":"B-H Lee","year":"2013","unstructured":"Lee, B.-H. et al. Enzyme-synthesized highly branched maltodextrins have slow glucose generation at the mucosal \u03b1-glucosidase level and are slowly digestible in vivo. PloS ONE 8, e59745 (2013).","journal-title":"PloS ONE"},{"key":"701_CR42","doi-asserted-by":"publisher","first-page":"422","DOI":"10.1016\/0304-4165(71)90259-5","volume":"237","author":"H Akai","year":"1971","unstructured":"Akai, H. et al. Complete hydrolysis of branching linkages in glycogen by Pseudomonas isoamylase: distribution of linear chains. Biochim. Biophys. Acta Gen. Subj. 237, 422\u2013429 (1971).","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"701_CR43","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1002\/star.200900182","volume":"62","author":"JH Ryu","year":"2010","unstructured":"Ryu, J. H. et al. Production and characterization of digestion-resistant starch by the reaction of Neisseria polysaccharea amylosucrase. Starch-St\u00e4rke 62, 221\u2013228 (2010).","journal-title":"Starch-St\u00e4rke"},{"key":"701_CR44","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1016\/0008-6215(85)90009-6","volume":"139","author":"MJ Gidley","year":"1985","unstructured":"Gidley, M. J. Quantification of the structural features of starch polysaccharides by NMR spectroscopy. Carbohydr. Res. 139, 85\u201393 (1985).","journal-title":"Carbohydr. Res."},{"key":"701_CR45","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1016\/S0144-8617(01)00339-3","volume":"49","author":"S-H Yoo","year":"2002","unstructured":"Yoo, S.-H. & Jane, J. -l Molecular weights and gyration radii of amylopectins determined by high-performance size-exclusion chromatography equipped with multi-angle laser-light scattering and refractive index detectors. Carbohydr. Polym. 49, 307\u2013314 (2002).","journal-title":"Carbohydr. Polym."},{"key":"701_CR46","doi-asserted-by":"publisher","first-page":"132456","DOI":"10.1016\/j.foodchem.2022.132456","volume":"383","author":"Y-B Song","year":"2022","unstructured":"Song, Y.-B. et al. New insights suggest isomaltooligosaccharides are slowly digestible carbohydrates, rather than dietary fibers, at constitutive mammalian \u03b1-glucosidase levels. Food Chem. 383, 132456 (2022).","journal-title":"Food Chem."},{"key":"701_CR47","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1016\/j.foodhyd.2018.08.033","volume":"87","author":"H Shin","year":"2019","unstructured":"Shin, H. et al. Optimization of in vitro carbohydrate digestion by mammalian mucosal \u03b1-glucosidases and its applications to hydrolyze the various sources of starches. Food Hydrocoll.87, 470\u2013476 (2019).","journal-title":"Food Hydrocoll."},{"key":"701_CR48","doi-asserted-by":"crossref","unstructured":"Vasanthan, T. Enzymatic quantitation of total starch in plant products. Curr. Protoc. Food Anal. Chem. 1, E2\u20132 (2001).","DOI":"10.1002\/0471142913.fae0202s00"},{"key":"701_CR49","unstructured":"Nava Rodriguez, N. E. Engineered Expression System in K. phaffii for Expression of Human Alpha-glucosidases, Their Characterization and Inhibition. Doctoral dissertation, University of Waterloo (2020)."}],"container-title":["npj Science of Food"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41538-025-00701-7","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41538-025-00701-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41538-025-00701-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T13:04:33Z","timestamp":1770815073000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41538-025-00701-7"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1,9]]},"references-count":49,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["701"],"URL":"https:\/\/doi.org\/10.1038\/s41538-025-00701-7","relation":{},"ISSN":["2396-8370"],"issn-type":[{"value":"2396-8370","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,1,9]]},"assertion":[{"value":"4 November 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 December 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 January 2026","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":"54"}}