{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T20:47:10Z","timestamp":1789418830133,"version":"build-2803163510"},"reference-count":61,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2025,3,7]],"date-time":"2025-03-07T00:00:00Z","timestamp":1741305600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Institutes of Health\/National Institute of Diabetes and Digestive and Kidney Diseases (NIH\/NIDDK)","award":["DK135751"],"award-info":[{"award-number":["DK135751"]}]},{"name":"National Institutes of Health\/National Institute of Diabetes and Digestive and Kidney Diseases (NIH\/NIDDK)","award":["DK136755"],"award-info":[{"award-number":["DK136755"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Inositol phosphates are critical signaling messengers involved in a wide range of biological pathways, and inositol polyphosphate multikinase (IPMK) functions as a rate-limiting enzyme for inositol polyphosphate metabolism. IPMK has been implicated in cellular metabolism, but its function at the systemic level is still poorly understood. Since skeletal muscle is a major contributor to energy homeostasis, we have developed a mouse model in which skeletal muscle IPMK is specifically deleted and examined how a loss of IPMK affects whole-body metabolism. Here, we report that skeletal-muscle-specific IPMK knockout mice exhibited a ~12% increase in body weight compared to WT controls (p &lt; 0.05). These mice also showed a significantly impaired glucose tolerance, as indicated by their ~50% higher blood glucose levels during GTT. Additionally, exercise capacity was reduced by ~45% in IPMK-MKO mice, demonstrating a decline in endurance. Moreover, these metabolic alterations were accompanied by a 2.5-fold increase in skeletal muscle triglyceride accumulation, suggesting impaired lipid metabolism. Further analysis revealed that IPMK-deficient myocytes exhibited 30% lower \u03b2-oxidation rates. Thus, our results suggest that IPMK mediates whole-body metabolism by regulating muscle metabolism and may be potentially targeted for the treatment of metabolic syndromes.<\/jats:p>","DOI":"10.3390\/ijms26062395","type":"journal-article","created":{"date-parts":[[2025,3,7]],"date-time":"2025-03-07T07:05:46Z","timestamp":1741331146000},"page":"2395","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Loss of Skeletal Muscle Inositol Polyphosphate Multikinase Disrupts Glucose Regulation and Limits Exercise Capacity"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-7235-995X","authenticated-orcid":false,"given":"Ji-Hyun","family":"Lee","sequence":"first","affiliation":[{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7541-2251","authenticated-orcid":false,"given":"Ik-Rak","family":"Jung","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Becky","family":"Tu-Sekine","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sunghee","family":"Jin","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3992-9234","authenticated-orcid":false,"given":"Frederick","family":"Anokye-Danso","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rexford S.","family":"Ahima","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3887-6556","authenticated-orcid":false,"given":"Sangwon F.","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,3,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1016\/j.cell.2010.11.045","article-title":"SnapShot: Inositol phosphates","volume":"143","author":"Hatch","year":"2010","journal-title":"Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"19938","DOI":"10.1073\/pnas.1320171110","article-title":"Inositol polyphosphate multikinase is a coactivator for serum response factor-dependent induction of immediate early genes","volume":"110","author":"Kim","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2036","DOI":"10.1073\/pnas.1700165114","article-title":"Neuronal migration is mediated by inositol hexakisphosphate kinase 1 via alpha-actinin and focal adhesion kinase","volume":"114","author":"Fu","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.1073\/pnas.1017831108","article-title":"Inositol polyphosphate multikinase is a physiologic PI3-kinase that activates Akt\/PKB","volume":"108","author":"Maag","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1038\/35073015","article-title":"Back in the water: The return of the inositol phosphates","volume":"2","author":"Irvine","year":"2001","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"315","DOI":"10.14348\/molcells.2017.0066","article-title":"The Expanding Significance of Inositol Polyphosphate Multikinase as a Signaling Hub","volume":"40","author":"Kim","year":"2017","journal-title":"Mol. Cells"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1073\/pnas.1119751109","article-title":"AMP-activated protein kinase is physiologically regulated by inositol polyphosphate multikinase","volume":"109","author":"Bang","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"14137","DOI":"10.1096\/fj.201900717RR","article-title":"Inositol polyphosphate multikinase is a metformin target that regulates cell migration","volume":"33","author":"Padhi","year":"2019","journal-title":"FASEB J."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1126\/science.1146824","article-title":"Requirement of inositol pyrophosphates for full exocytotic capacity in pancreatic beta cells","volume":"318","author":"Illies","year":"2007","journal-title":"Science"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"38541","DOI":"10.18632\/oncotarget.15872","article-title":"Metabolomics uncovers a link between inositol metabolism and osteosarcoma metastasis","volume":"8","author":"Ren","year":"2017","journal-title":"Oncotarget"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1773","DOI":"10.1073\/pnas.1424642112","article-title":"Inositol pyrophosphates promote tumor growth and metastasis by antagonizing liver kinase B1","volume":"112","author":"Rao","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1021\/cb5001907","article-title":"Inositol phosphate recycling regulates glycolytic and lipid metabolism that drives cancer aggressiveness","volume":"9","author":"Benjamin","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1046\/j.1365-2958.2003.03562.x","article-title":"Arg82p is a bifunctional protein whose inositol polyphosphate kinase activity is essential for nitrogen and PHO gene expression but not for Mcm1p chaperoning in yeast","volume":"49","author":"El","year":"2003","journal-title":"Mol. Microbiol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/S0014-5793(00)02318-8","article-title":"Inositol polyphosphate kinase activity of Arg82\/ArgRIII is not required for the regulation of the arginine metabolism in yeast","volume":"486","author":"Dubois","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1038\/nrendo.2017.132","article-title":"Targeting thermogenesis in brown fat and muscle to treat obesity and metabolic disease","volume":"14","author":"Betz","year":"2018","journal-title":"Nat. Rev. Endocrinol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"R67","DOI":"10.1530\/JOE-17-0147","article-title":"Skeletal energy homeostasis: A paradigm of endocrine discovery","volume":"234","author":"Suchacki","year":"2017","journal-title":"J. Endocrinol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/nrendo.2016.162","article-title":"Exercise-stimulated glucose uptake\u2014Regulation and implications for glycaemic control","volume":"13","author":"Sylow","year":"2017","journal-title":"Nat. Rev. Endocrinol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1152\/physrev.00031.2010","article-title":"Fiber types in mammalian skeletal muscles","volume":"91","author":"Schiaffino","year":"2011","journal-title":"Physiol. Rev."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1645","DOI":"10.1002\/cphy.c130009","article-title":"Mechanisms modulating skeletal muscle phenotype","volume":"3","author":"Blaauw","year":"2013","journal-title":"Compr. Physiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/nrendo.2012.49","article-title":"Muscles, exercise and obesity: Skeletal muscle as a secretory organ","volume":"8","author":"Pedersen","year":"2012","journal-title":"Nat. Rev. Endocrinol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"235","DOI":"10.3803\/EnM.2015.30.3.235","article-title":"Connecting Myokines and Metabolism","volume":"30","author":"Ahima","year":"2015","journal-title":"Endocrinol. Metab."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1172\/JCI114857","article-title":"Skeletal muscle metabolism is a major determinant of resting energy expenditure","volume":"86","author":"Zurlo","year":"1990","journal-title":"J. Clin. Investig."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.1096\/fj.201700442R","article-title":"AMPK in skeletal muscle function and metabolism","volume":"32","author":"Kjobsted","year":"2018","journal-title":"FASEB J."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/j.molmet.2016.06.007","article-title":"mTORC2 and AMPK differentially regulate muscle triglyceride content via Perilipin 3","volume":"5","author":"Kleinert","year":"2016","journal-title":"Mol. Metab."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1111\/acel.12342","article-title":"Longevity and skeletal muscle mass: The role of IGF signalling, the sirtuins, dietary restriction and protein intake","volume":"14","author":"Sharples","year":"2015","journal-title":"Aging Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2764","DOI":"10.1172\/JCI67227","article-title":"AMPK, insulin resistance, and the metabolic syndrome","volume":"123","author":"Ruderman","year":"2013","journal-title":"J. Clin. Investig."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1016\/j.molcel.2017.05.032","article-title":"AMPK: Mechanisms of Cellular Energy Sensing and Restoration of Metabolic Balance","volume":"66","author":"Garcia","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.cmet.2004.12.003","article-title":"AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism","volume":"1","author":"Kahn","year":"2005","journal-title":"Cell Metab."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/nrm2249","article-title":"AMP-activated\/SNF1 protein kinases: Conserved guardians of cellular energy","volume":"8","author":"Hardie","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1016\/j.cmet.2015.05.005","article-title":"Beyond energy homeostasis: The expanding role of AMP-activated protein kinase in regulating metabolism","volume":"21","author":"Carling","year":"2015","journal-title":"Cell Metab."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1242\/jeb.128207","article-title":"Molecular networks in skeletal muscle plasticity","volume":"219","author":"Hoppeler","year":"2016","journal-title":"J. Exp. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1002\/9780470725207.ch5","article-title":"Transcriptional control of mitochondrial energy metabolism through the PGC1 coactivators","volume":"287","author":"Spiegelman","year":"2007","journal-title":"Novartis Found. Symp."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"3421","DOI":"10.1002\/jcp.30827","article-title":"IPMK modulates hepatic glucose production and insulin signaling","volume":"237","author":"Jung","year":"2022","journal-title":"J. Cell Physiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molmet.2019.08.001","article-title":"The role of skeletal muscle Akt in the regulation of muscle mass and glucose homeostasis","volume":"28","author":"Jaiswal","year":"2019","journal-title":"Mol. Metab."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"e96805","DOI":"10.1172\/jci.insight.96805","article-title":"Intracellular localization of diacylglycerols and sphingolipids influences insulin sensitivity and mitochondrial function in human skeletal muscle","volume":"3","author":"Perreault","year":"2018","journal-title":"JCI Insight"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/s001250051123","article-title":"Intramyocellular lipid concentrations are correlated with insulin sensitivity in humans: A 1H NMR spectroscopy study","volume":"42","author":"Krssak","year":"1999","journal-title":"Diabetologia"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"3440","DOI":"10.1210\/jc.2009-0053","article-title":"Influence of gender, obesity, and muscle lipase activity on intramyocellular lipids in sedentary individuals","volume":"94","author":"Moro","year":"2009","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"E1076","DOI":"10.1152\/ajpendo.00177.2004","article-title":"Impaired plasma fatty acid oxidation in extremely obese women","volume":"287","author":"Thyfault","year":"2004","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"E1039","DOI":"10.1152\/ajpendo.2000.279.5.E1039","article-title":"Lipid oxidation is reduced in obese human skeletal muscle","volume":"279","author":"Kim","year":"2000","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2944","DOI":"10.2337\/diabetes.51.10.2944","article-title":"Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes","volume":"51","author":"Kelley","year":"2002","journal-title":"Diabetes"},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Fujimoto, B.A., Young, M., Nakamura, N., Ha, H., Carter, L., Pitts, M.W., Torres, D., Noh, H.L., Suk, S., and Kim, J.K. (2021). Disrupted glucose homeostasis and skeletal-muscle-specific glucose uptake in an exocyst knockout mouse model. J. Biol. Chem., 296.","DOI":"10.1016\/j.jbc.2021.100482"},{"key":"ref_42","first-page":"2463","article-title":"Effects of resistance training and endurance training on insulin sensitivity in nonobese, young women: A controlled randomized trial","volume":"85","author":"Poehlman","year":"2000","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"S157","DOI":"10.2337\/dc09-S302","article-title":"Skeletal muscle insulin resistance is the primary defect in type 2 diabetes","volume":"32","author":"DeFronzo","year":"2009","journal-title":"Diabetes Care"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"909","DOI":"10.7326\/0003-4819-113-12-909","article-title":"Slow glucose removal rate and hyperinsulinemia precede the development of type II diabetes in the offspring of diabetic parents","volume":"113","author":"Warram","year":"1990","journal-title":"Ann. Intern. Med."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1220","DOI":"10.1016\/j.celrep.2015.04.037","article-title":"Differential Role of Insulin\/IGF-1 Receptor Signaling in Muscle Growth and Glucose Homeostasis","volume":"11","author":"Lauritzen","year":"2015","journal-title":"Cell Rep."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1093\/embo-reports\/kvf078","article-title":"Genetic manipulation of insulin signaling, action and secretion in mice. Insights into glucose homeostasis and pathogenesis of type 2 diabetes","volume":"3","author":"Baudry","year":"2002","journal-title":"EMBO Rep."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1926","DOI":"10.1101\/gad.908001","article-title":"Functional inactivation of the IGF-I and insulin receptors in skeletal muscle causes type 2 diabetes","volume":"15","author":"Fernandez","year":"2001","journal-title":"Genes Dev."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2397","DOI":"10.1210\/endo.137.6.8641192","article-title":"Transgenic mice with muscle-specific insulin resistance develop increased adiposity, impaired glucose tolerance, and dyslipidemia","volume":"137","author":"Moller","year":"1996","journal-title":"Endocrinology"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1695","DOI":"10.1002\/jcb.30478","article-title":"Inositol polyphosphate multikinase modulates free fatty acids-induced insulin resistance in primary mouse hepatocytes","volume":"124","author":"Jung","year":"2023","journal-title":"J. Cell. Biochem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1210\/me.2014-1134","article-title":"Convergence of IPMK and LKB1-AMPK signaling pathways on metformin action","volume":"28","author":"Bang","year":"2014","journal-title":"Mol. Endocrinol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1016\/j.cell.2014.11.034","article-title":"Metabolic inflexibility: When mitochondrial indecision leads to metabolic gridlock","volume":"159","author":"Muoio","year":"2014","journal-title":"Cell"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1172\/JCI13505","article-title":"Role of AMP-activated protein kinase in mechanism of metformin action","volume":"108","author":"Zhou","year":"2001","journal-title":"J. Clin. Investig."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2958","DOI":"10.2337\/db07-1187","article-title":"Ablation of AMP-activated protein kinase alpha2 activity exacerbates insulin resistance induced by high-fat feeding of mice","volume":"57","author":"Fujii","year":"2008","journal-title":"Diabetes"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"ra22","DOI":"10.1126\/scisignal.2003405","article-title":"Inositol polyphosphate multikinase is a coactivator of p53-mediated transcription and cell death","volume":"6","author":"Xu","year":"2013","journal-title":"Sci.Signal."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"16181","DOI":"10.1073\/pnas.1315551110","article-title":"Inositol polyphosphate multikinase is a transcriptional coactivator required for immediate early gene induction","volume":"110","author":"Xu","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1073\/pnas.0409103102","article-title":"Requirement for serum response factor for skeletal muscle growth and maturation revealed by tissue-specific gene deletion in mice","volume":"102","author":"Li","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"107199","DOI":"10.1016\/j.isci.2023.107199","article-title":"Inositol polyphosphate multikinase modulates redox signaling through nuclear factor erythroid 2-related factor 2 and glutathione metabolism","volume":"26","author":"Tyagi","year":"2023","journal-title":"iScience"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"817","DOI":"10.2337\/diabetes.50.4.817","article-title":"Skeletal muscle lipid content and oxidative enzyme activity in relation to muscle fiber type in type 2 diabetes and obesity","volume":"50","author":"He","year":"2001","journal-title":"Diabetes"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1152\/jappl.1997.83.1.166","article-title":"Altered glycolytic and oxidative capacities of skeletal muscle contribute to insulin resistance in NIDDM","volume":"83","author":"Simoneau","year":"1997","journal-title":"J. Appl. Physiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1096\/fasebj.9.2.7781930","article-title":"Skeletal muscle glycolytic and oxidative enzyme capacities are determinants of insulin sensitivity and muscle composition in obese women","volume":"9","author":"Simoneau","year":"1995","journal-title":"FASEB J."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"McPherron, A.C., Huynh, T.V., and Lee, S.J. (2009). Redundancy of myostatin and growth\/differentiation factor 11 function. BMC Dev. Biol., 9.","DOI":"10.1186\/1471-213X-9-24"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/6\/2395\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T16:48:58Z","timestamp":1760028538000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/6\/2395"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,3,7]]},"references-count":61,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2025,3]]}},"alternative-id":["ijms26062395"],"URL":"https:\/\/doi.org\/10.3390\/ijms26062395","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,3,7]]}}}