{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T05:04:27Z","timestamp":1780463067368,"version":"3.54.1"},"reference-count":61,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2026,5,31]],"date-time":"2026-05-31T00:00:00Z","timestamp":1780185600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Ministry of Education and Science","award":["PM-II\/SP\/0061\/2024\/02"],"award-info":[{"award-number":["PM-II\/SP\/0061\/2024\/02"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Xanthine oxidase (XO) and aldehyde oxidase (AO) are molybdenum-dependent flavoenzymes involved in purine catabolism and hepatic xenobiotic metabolism. This study aimed to assess XO and AO activities and molybdenum (Mo) content in liver tissue from liver graft donors and recipients with end-stage liver failure (ESLF). Liver tissue samples were obtained from 10 liver donors (LD; control group) and 30 patients with ESLF undergoing liver transplantation. The ESLF cohort was further divided by primary liver disease: hepatitis B or C viral infection (HBV\/HCV), alcohol-associated liver disease (ALD), primary sclerosing cholangitis (PSC), Wilson\u2019s disease (WD), and primary biliary cholangitis (PBC). Enzymatic activity was determined by spectrofluorometry, and hepatic Mo content was measured by inductively coupled plasma mass spectrometry. Compared with LD controls, ESLF recipients showed a significant decrease in both hepatic XO activity and Mo content. At the subgroup level, XO activity was significantly reduced in ALD, PSC, and PBC, whereas HBV\/HCV and WD showed lower but non-significant values. Mo content was significantly reduced in the overall ESLF cohort and in the WD subgroup, although disease-specific variability was observed, including relatively high Mo content in PSC. AO activity was assessed in a subset of samples and did not differ significantly between donor and recipient liver tissues. Correlation analyses did not demonstrate a statistically significant association between hepatic Mo content and XO activity, suggesting that total tissue Mo content may not directly reflect Mo-dependent enzymatic activity. These findings indicate that ESLF is associated with altered hepatic trace-element composition, including Mo, and with disturbances in Mo-dependent enzymatic activity. Future studies should combine liver tissue analysis with matched serum and portal blood samples to better characterise hepatic Mo metabolism and the systemic biological effects of trace elements.<\/jats:p>","DOI":"10.3390\/ijms27114998","type":"journal-article","created":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T12:45:08Z","timestamp":1780404308000},"page":"4998","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Homeostasis of Molybdenum, Xanthine Oxidase and Aldehyde Oxidase Activity Levels in the Livers of Patients with End-Stage Liver Failure and Healthy Controls"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-3142-9892","authenticated-orcid":false,"given":"Jakub Piotr","family":"Adamus","sequence":"first","affiliation":[{"name":"Department of Clinical Immunology, Medical University of Warsaw, 59 Nowogrodzka Street, 02-006 Warsaw, Poland"},{"name":"Clinical Immunology Student Scientific Association, Medical University of Warsaw, 59 Nowogrodzka Street, 02-006 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aleksandra","family":"Wycza\u0142kowska-Tomasik","sequence":"additional","affiliation":[{"name":"Department of Clinical Immunology, Medical University of Warsaw, 59 Nowogrodzka Street, 02-006 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5199-9681","authenticated-orcid":false,"given":"Anna","family":"Ruszczy\u0144ska","sequence":"additional","affiliation":[{"name":"University of Warsaw, Faculty of Chemistry, Biological and Chemical Research Centre, 101 Zwirki i Wigury Street, 02-089 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4872-5521","authenticated-orcid":false,"given":"Ewa","family":"Bulska","sequence":"additional","affiliation":[{"name":"University of Warsaw, Faculty of Chemistry, Biological and Chemical Research Centre, 101 Zwirki i Wigury Street, 02-089 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-3855-6632","authenticated-orcid":false,"given":"Zuzanna","family":"Z\u0105bek","sequence":"additional","affiliation":[{"name":"Clinical Immunology Student Scientific Association, Medical University of Warsaw, 59 Nowogrodzka Street, 02-006 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-8784-3898","authenticated-orcid":false,"given":"Karolina","family":"Pastwa","sequence":"additional","affiliation":[{"name":"Clinical Immunology Student Scientific Association, Medical University of Warsaw, 59 Nowogrodzka Street, 02-006 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dariusz","family":"So\u0142dacki","sequence":"additional","affiliation":[{"name":"Longevity Center Europe, 9 Belwederska Street, 00-761 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0160-3009","authenticated-orcid":false,"given":"Leszek","family":"P\u0105czek","sequence":"additional","affiliation":[{"name":"Department of Clinical Immunology, Medical University of Warsaw, 59 Nowogrodzka Street, 02-006 Warsaw, Poland"},{"name":"Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5A Pawinskiego Street, 02-106 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,5,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.cbpa.2016.03.016","article-title":"Molybdenum Cofactor and Human Disease","volume":"31","author":"Schwarz","year":"2016","journal-title":"Curr. Opin. Chem. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/nature08302","article-title":"Molybdenum Cofactors, Enzymes and Pathways","volume":"460","author":"Schwarz","year":"2009","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Clement, B., and Struwe, M.A. (2023). The History of mARC. Molecules, 28.","DOI":"10.3390\/molecules28124713"},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Mendel, R.R., and Schwarz, G. (2023). The History of Animal and Plant Sulfite Oxidase\u2014A Personal View. Molecules, 28.","DOI":"10.3390\/molecules28196998"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Johannes, L., Fu, C.-Y., and Schwarz, G. (2022). Molybdenum Cofactor Deficiency in Humans. Molecules, 27.","DOI":"10.3390\/molecules27206896"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/S0891-5849(02)00956-5","article-title":"Structure and Function of Xanthine Oxidoreductase: Where Are We Now?","volume":"33","author":"Harrison","year":"2002","journal-title":"Free Radic. Biol. Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1081\/DMR-120037569","article-title":"Physiological Roles of Xanthine Oxidoreductase","volume":"36","author":"Harrison","year":"2004","journal-title":"Drug Metab. Rev."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Hille, R. (2023). Xanthine Oxidase-A Personal History. Molecules, 28.","DOI":"10.3390\/molecules28041921"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2606","DOI":"10.2174\/1381612811319140010","article-title":"Chemical Nature and Reaction Mechanisms of the Molybdenum Cofactor of Xanthine Oxidoreductase","volume":"19","author":"Okamoto","year":"2013","journal-title":"Curr. Pharm. Des."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Adamus, J.P., Ruszczy\u0144ska, A., and Wycza\u0142kowska-Tomasik, A. (2024). Molybdenum\u2019s Role as an Essential Element in Enzymes Catabolizing Redox Reactions: A Review. Biomolecules, 14.","DOI":"10.3390\/biom14070869"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/0016-5085(81)90648-X","article-title":"Superoxide Radicals in Feline Intestinal Ischemia","volume":"81","author":"Granger","year":"1981","journal-title":"Gastroenterology"},{"key":"ref_12","first-page":"G768","article-title":"Conversion of Xanthine Dehydrogenase to Oxidase in Ischemic Rat Intestine: A Reevaluation","volume":"254","author":"Parks","year":"1988","journal-title":"Am. J. Physiol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/0003-9861(72)90078-1","article-title":"A Comparison of the Specificities of Xanthine Oxidase and Aldehyde Oxidase","volume":"150","author":"Krenitsky","year":"1972","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"83","DOI":"10.2133\/dmpk.21.83","article-title":"Drug-Metabolizing Ability of Molybdenum Hydroxylases","volume":"21","author":"Kitamura","year":"2006","journal-title":"Drug Metab. Pharmacokinet."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Ioannides, C. (2002). Enzyme Systems That Metabolise Drugs and Other Xenobiotics: Molybdenum Hydroxylases, John Wiley & Sons.","DOI":"10.1002\/0470846305"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1172\/JCI111494","article-title":"High Concentrations of Antibodies to Xanthine Oxidase in Human and Animal Sera. Molecular Characterization","volume":"74","author":"Bruder","year":"1984","journal-title":"J. Clin. Investig."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1042\/bj2890523","article-title":"Binding of Human Xanthine Oxidase to Sulphated Glycosaminoglycans on the Endothelial-Cell Surface","volume":"289","author":"Adachi","year":"1993","journal-title":"Biochem. J."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"6420","DOI":"10.1073\/pnas.1100700108","article-title":"Algae and Humans Share a Molybdate Transporter","volume":"108","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1568","DOI":"10.1016\/j.bbamcr.2012.02.007","article-title":"Cell Biology of Molybdenum in Plants and Humans","volume":"1823","author":"Mendel","year":"2012","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Res."},{"key":"ref_20","first-page":"164","article-title":"Molybdenum Nutriture in Humans","volume":"16","author":"Novotny","year":"2011","journal-title":"J. Evid. Based. Integr. Med."},{"key":"ref_21","first-page":"745","article-title":"Widespread Cellular Distribution of Aldehyde Oxidase in Human Tissues Found by Immunohistochemistry Staining","volume":"16","author":"Moriwaki","year":"2001","journal-title":"Histol. Histopathol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/clpt.1991.205","article-title":"Human Liver Xanthine Oxidase: Nature and Extent of Individual Variation","volume":"50","author":"Guerciolini","year":"1991","journal-title":"Clin. Pharmacol. Ther."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1007\/BF02899240","article-title":"Distribution of Xanthine Oxidoreductase Activity in Human Tissues\u2014A Histochemical and Biochemical Study","volume":"63","author":"Kooij","year":"1993","journal-title":"Virchows Arch. B Cell Pathol. Incl. Mol. Pathol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1111\/j.1572-0241.2002.05925.x","article-title":"Xanthine Oxidoreductase Activity in Human Liver Disease","volume":"97","author":"Stirpe","year":"2002","journal-title":"Am. J. Gastroenterol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"G753","DOI":"10.1152\/ajpgi.1988.254.5.G753","article-title":"Mechanisms of Conversion of Xanthine Dehydrogenase to Xanthine Oxidase in Ischemic Rat Liver and Kidney","volume":"254","author":"McKelvey","year":"1988","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1111\/j.1572-0241.2001.03700.x","article-title":"Serum Xanthine Oxidase in Human Liver Disease","volume":"96","author":"Battelli","year":"2001","journal-title":"Am. J. Gastroenterol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1111\/j.1600-0463.2006.apm_457.x","article-title":"Levels and Interactions of Plasma Xanthine Oxidase, Catalase and Liver Function Parameters in Nigerian Children with Plasmodium Falciparum Infection","volume":"114","author":"Iwalokun","year":"2006","journal-title":"APMIS"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1412","DOI":"10.1016\/j.jhep.2015.01.019","article-title":"Xanthine Oxidase in Non-Alcoholic Fatty Liver Disease and Hyperuricemia: One Stone Hits Two Birds","volume":"62","author":"Xu","year":"2015","journal-title":"J. Hepatol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"12282","DOI":"10.1038\/s41598-022-16688-0","article-title":"Xanthine Oxidoreductase Activity Is Correlated with Hepatic Steatosis","volume":"12","author":"Yagi","year":"2022","journal-title":"Sci. Rep."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Sato, K., Naganuma, A., Nagashima, T., Arai, Y., Mikami, Y., Nakajima, Y., Kanayama, Y., Murakami, T., Uehara, S., and Uehara, D. (2023). A Newly Developed Method-Based Xanthine Oxidoreductase Activities in Various Human Liver Diseases. Biomedicines, 11.","DOI":"10.3390\/biomedicines11051445"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1797","DOI":"10.1124\/dmd.113.053082","article-title":"Aldehyde Oxidase 1 (AOX1) in Human Liver Cytosols: Quantitative Characterization of AOX1 Expression Level and Activity Relationship","volume":"41","author":"Fu","year":"2013","journal-title":"Drug Metab. Dispos."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1177\/0091270003260336","article-title":"Human Liver Aldehyde Oxidase: Inhibition by 239 Drugs","volume":"44","author":"Obach","year":"2004","journal-title":"J. Clin. Pharmacol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1040","DOI":"10.1016\/j.jhep.2024.07.032","article-title":"EASL Clinical Practice Guidelines on Liver Transplantation","volume":"81","author":"Samuel","year":"2024","journal-title":"J. Hepatol."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Pozna\u0144ski, J., So\u0142dacki, D., Czarkowska-P\u0105czek, B., Bonna, A., Kornasiewicz, O., Krawczyk, M., Bal, W., and P\u0105czek, L. (2021). Cirrhotic Liver of Liver Transplant Recipients Accumulate Silver and Co-Accumulate Copper. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22041782"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"20126","DOI":"10.1073\/pnas.0704646104","article-title":"A High-Affinity Molybdate Transporter in Eukaryotes","volume":"104","author":"Llamas","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Leon-Miranda, E., Tejada-Jimenez, M., and Llamas, A. (2025). Insertional Mutagenesis as a Strategy to Open New Paths in Microalgal Molybdenum and Nitrate Homeostasis. Curr. Issues Mol. Biol., 47.","DOI":"10.20944\/preprints202504.2140.v1"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/0009-8981(75)90375-7","article-title":"Serum Xanthine Oxidase in Jaundice","volume":"63","author":"Giler","year":"1975","journal-title":"Clin. Chim. Acta"},{"key":"ref_38","first-page":"183","article-title":"Serum Xanthine Oxidase and Liver Disease","volume":"7","author":"Ramboer","year":"1972","journal-title":"Digestion"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1334","DOI":"10.1124\/dmd.114.058107","article-title":"In Vitro Oxidative Metabolism of 6-Mercaptopurine in Human Liver: Insights into the Role of the Molybdoflavoenzymes Aldehyde Oxidase, Xanthine Oxidase, and Xanthine Dehydrogenase","volume":"42","author":"Choughule","year":"2014","journal-title":"Drug Metab. Dispos."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1517\/17425255.2012.663352","article-title":"The Role of Aldehyde Oxidase in Drug Metabolism","volume":"8","author":"Garattini","year":"2012","journal-title":"Expert Opin. Drug Metab. Toxicol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1016\/S2468-1253(22)00165-0","article-title":"The Prevalence and Incidence of NAFLD Worldwide: A Systematic Review and Meta-Analysis","volume":"7","author":"Riazi","year":"2022","journal-title":"Lancet Gastroenterol. Hepatol."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Marelja, Z., Leimk\u00fchler, S., and Missirlis, F. (2018). Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism. Front. Physiol., 9.","DOI":"10.3389\/fphys.2018.00050"},{"key":"ref_43","first-page":"1","article-title":"Bacterial Molybdoenzymes: Old Enzymes for New Purposes","volume":"40","year":"2016","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_44","first-page":"415","article-title":"Molybdenum in Human Health and Disease","volume":"13","author":"Schwarz","year":"2013","journal-title":"Met. Ions Life Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.abb.2004.08.012","article-title":"Molybdenum-Containing Hydroxylases","volume":"433","author":"Hille","year":"2005","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"10326","DOI":"10.29219\/fnr.v67.10326","article-title":"Molybdenum\u2014A Scoping Review for Nordic Nutrition Recommendations 2023","volume":"67","author":"Oskarsson","year":"2023","journal-title":"Food Nutr. Res."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0003-9861(53)80001-9","article-title":"Identification of the Xanthine Oxidase Factor as Molybdenum","volume":"45","author":"Kaleita","year":"1953","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"16357","DOI":"10.1016\/S0021-9258(18)49263-0","article-title":"The Structure of the Molybdenum Cofactor. Characterization of Di-(Carboxamidomethyl)Molybdopterin from Sulfite Oxidase and Xanthine Oxidase","volume":"262","author":"Kramer","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/S0021-9258(19)52361-4","article-title":"Isolation and Identification of the Xanthine Oxidase Factor as Molybdenum","volume":"203","author":"Richert","year":"1953","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1007\/s12011-015-0450-0","article-title":"Mitochondrial Oxidative Stress-Induced Hepatocyte Apoptosis Reflects Increased Molybdenum Intake in Caprine","volume":"170","author":"Zhuang","year":"2016","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/0021-9681(70)90056-1","article-title":"Essential Trace Metals in Man: Molybdenum","volume":"23","author":"Schroeder","year":"1970","journal-title":"J. Chronic Dis."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"109079","DOI":"10.1016\/j.ymgme.2025.109079","article-title":"Early Postnatal Hepatocyte Transplantation in a Child with Molybdenum Cofactor Deficiency Type B","volume":"145","author":"Selvanathan","year":"2025","journal-title":"Mol. Genet. Metab."},{"key":"ref_53","first-page":"535","article-title":"Serum Molybdenum in Diseases of the Liver and Biliary System","volume":"97","author":"Versieck","year":"1981","journal-title":"J. Lab. Clin. Med."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"141035","DOI":"10.1016\/j.ijbiomac.2025.141035","article-title":"Based on the Sam50-MICOS-ATAD3-MtDNA Axis: Exploring Oligomeric Proanthocyanidins to Alleviate Molybdenum and Cadmium Co-Induced Liver Inflammation in Sheep","volume":"304","author":"Liu","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1007\/s12011-015-0237-3","article-title":"Study of Trace Elements in Liver Cirrhosis Patients and Their Role in Prognosis of Disease","volume":"165","author":"Nangliya","year":"2015","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1080\/17474124.2018.1497483","article-title":"The Role of the Chronic Care Model in Promoting the Management of the Patient with Rare Liver Disease","volume":"12","author":"Pericleous","year":"2018","journal-title":"Expert Rev. Gastroenterol. Hepatol."},{"key":"ref_57","unstructured":"American Liver Foundation (2024, August 30). Rare Liver Diseases. Available online: https:\/\/liverfoundation.org\/about-your-liver\/facts-about-liver-disease\/rare-liver-diseases\/."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Li, S., Lv, J., Yang, X., Yang, C., and Yin, M. (2025). Inflammatory and Metabolic Markers Mediate the Association between Urinary Metals and Non-Alcoholic Fatty Liver Disease in U.S. Adults: A Cross-Sectional Study. Front. Public Health, 13.","DOI":"10.3389\/fpubh.2025.1564302"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1038\/s41598-018-37516-4","article-title":"Alteration of Trace Elements during Pathogenesis of N-Nitrosodimethylamine Induced Hepatic Fibrosis","volume":"9","author":"George","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"e202402771","DOI":"10.26508\/lsa.202402771","article-title":"Examining the Liver\u2013Pancreas Crosstalk Reveals a Role for the Molybdenum Cofactor in \u03b2-Cell Regeneration","volume":"7","author":"Karampelias","year":"2024","journal-title":"Life Sci. Alliance"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"126816","DOI":"10.1016\/j.jtemb.2021.126816","article-title":"Evaluation of the Influence of Diet Supplementation with Conjugated Linoleic Acid Isomers on Elemental Composition in the Cardio-Oncological Nutritional Programming Rat\u2019 Model","volume":"68","author":"Bulska","year":"2021","journal-title":"J. Trace Elem. Med. Biol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/11\/4998\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T04:18:55Z","timestamp":1780460335000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/11\/4998"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5,31]]},"references-count":61,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2026,6]]}},"alternative-id":["ijms27114998"],"URL":"https:\/\/doi.org\/10.3390\/ijms27114998","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,5,31]]}}}