{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:22:46Z","timestamp":1792783366192,"version":"4.5.0"},"reference-count":87,"publisher":"Springer Science and Business Media LLC","issue":"11","license":[{"start":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T00:00:00Z","timestamp":1792454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T00:00:00Z","timestamp":1792454400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"name":"Ministry of Earth Sciences","award":["MoES\/PAMC\/DOM\/89\/2023)"],"award-info":[{"award-number":["MoES\/PAMC\/DOM\/89\/2023)"]}],"id":[{"id":"https:\/\/ror.org\/013cf5k59","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Med Oncol"],"DOI":"10.1007\/s12032-026-03456-7","type":"journal-article","created":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T04:40:35Z","timestamp":1792471235000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Marine microbial arginase: a metabolic therapeutic strategy for oral squamous cell carcinoma"],"prefix":"10.1007","volume":"43","author":[{"given":"R.","family":"Priya","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G.","family":"Ragul","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G.","family":"Ritika","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kamala","family":"Kannan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dhanraj","family":"Ganapathy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sivaperumal","family":"Pitchiah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,10,20]]},"reference":[{"key":"3456_CR1","doi-asserted-by":"publisher","first-page":"100476","DOI":"10.1016\/j.oor.2024.100476","volume":"10","author":"S Sivasakthivel","year":"2024","unstructured":"Sivasakthivel S, Ramani P, Jayaraman S. Expression of angiotensin converting enzyme 2 in patients with oral squamous cell carcinoma. Oral Oncol Rep. 2024;10:100476. https:\/\/doi.org\/10.1016\/j.oor.2024.100476.","journal-title":"Oral Oncol Rep"},{"key":"3456_CR2","doi-asserted-by":"publisher","first-page":"84","DOI":"10.1016\/j.oooo.2024.05.005","volume":"138","author":"K Gopalakrishnan","year":"2024","unstructured":"Gopalakrishnan K, Kannan B, Pandi C, Pandi A, Ramasubramanian A, Jayaseelan VP, Arumugam P. Aberrant expression of VASP serves as a potential prognostic biomarker and therapeutic target for oral squamous cell carcinoma. Oral Surgery, Oral Medicine, Oral Pathology and Oral Radiology. 2024 Sep 1;138(3):391-402. https:\/\/doi.org\/10.1016\/j.oooo.2024.05.005","journal-title":"Oral Surgery, Oral Medicine, Oral Pathology and Oral Radiology<br>"},{"key":"3456_CR3","doi-asserted-by":"publisher","first-page":"829","DOI":"10.1016\/j.cell.2016.09.031","volume":"167","author":"R Geiger","year":"2016","unstructured":"Geiger R, Rieckmann JC, Wolf T, Basso C, Feng Y, Fuhrer T, et al. L-Arginine modulates T Cell metabolism and enhances survival and anti-tumor activity. Cell. 2016;167:829\u2013e84213. https:\/\/doi.org\/10.1016\/j.cell.2016.09.031.","journal-title":"Cell"},{"key":"3456_CR4","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1016\/j.fsi.2021.06.013","volume":"115","author":"H Li","year":"2021","unstructured":"Li H, Zhang M, Jiang H, Fan Y, Li X, Wang R, et al. Arginase plays an important role in ammonia detoxification of yellow catfish Pelteobagrus fulvidraco. Fish Shellfish Immunol. 2021;115:171\u20138. https:\/\/doi.org\/10.1016\/j.fsi.2021.06.013.","journal-title":"Fish Shellfish Immunol"},{"key":"3456_CR5","doi-asserted-by":"publisher","first-page":"266","DOI":"10.1038\/s41577-024-01098-2","volume":"25","author":"S Can\u00e8","year":"2025","unstructured":"Can\u00e8 S, Geiger R, Bronte V. The roles of arginases and arginine in immunity. Nat Rev Immunol. 2025;25:266\u201384. https:\/\/doi.org\/10.1038\/s41577-024-01098-2.","journal-title":"Nat Rev Immunol"},{"key":"3456_CR6","doi-asserted-by":"publisher","first-page":"5291","DOI":"10.3390\/ijms21155291","volume":"21","author":"S Clemente","year":"2020","unstructured":"Clemente S, van Waarde G, Antunes AF, D\u00f6mling I, Elsinga AH. Arginase as a potential biomarker of disease progression: a molecular imaging perspective. Int J Mol Sci. 2020;21:5291. https:\/\/doi.org\/10.3390\/ijms21155291.","journal-title":"Int J Mol Sci"},{"key":"3456_CR7","doi-asserted-by":"publisher","first-page":"1287","DOI":"10.1007\/s00109-015-1354-3","volume":"93","author":"YY Sin","year":"2015","unstructured":"Sin YY, Baron G, Schulze A, Funk CD. Arginase-1 deficiency. J Mol Med. 2015;93:1287\u201396. https:\/\/doi.org\/10.1007\/s00109-015-1354-3.","journal-title":"J Mol Med"},{"key":"3456_CR8","doi-asserted-by":"publisher","first-page":"5303","DOI":"10.1007\/s00018-021-03828-4","volume":"78","author":"A-A Mart\u00ed i L\u00edndez","year":"2021","unstructured":"Mart\u00ed i L\u00edndez A-A, Reith W. Arginine-dependent immune responses. Cell Mol Life Sci. 2021;78:5303\u201324. https:\/\/doi.org\/10.1007\/s00018-021-03828-4.","journal-title":"Cell Mol Life Sci"},{"key":"3456_CR9","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1016\/j.advms.2018.08.018","volume":"64","author":"J Szefel","year":"2019","unstructured":"Szefel J, Danielak A, Kruszewski WJ. Metabolic pathways of L-arginine and therapeutic consequences in tumors. Adv Med Sci. 2019;64:104\u201310. https:\/\/doi.org\/10.1016\/j.advms.2018.08.018.","journal-title":"Adv Med Sci"},{"key":"3456_CR10","doi-asserted-by":"publisher","first-page":"565","DOI":"10.1007\/s00280-021-04335-w","volume":"88","author":"N Kumari","year":"2021","unstructured":"Kumari N, Bansal S. Arginine depriving enzymes: applications as emerging therapeutics in cancer treatment. Cancer Chemother Pharmacol. 2021;88:565\u201394. https:\/\/doi.org\/10.1007\/s00280-021-04335-w.","journal-title":"Cancer Chemother Pharmacol"},{"key":"3456_CR11","doi-asserted-by":"publisher","first-page":"2857","DOI":"10.1007\/s00253-020-10432-2","volume":"104","author":"R Dhankhar","year":"2020","unstructured":"Dhankhar R, Gupta V, Kumar S, Kapoor RK, Gulati P. Microbial enzymes for deprivation of amino acid metabolism in malignant cells: biological strategy for cancer treatment. Appl Microbiol Biotechnol. 2020;104:2857\u201369. https:\/\/doi.org\/10.1007\/s00253-020-10432-2.","journal-title":"Appl Microbiol Biotechnol"},{"key":"3456_CR12","doi-asserted-by":"publisher","first-page":"3541","DOI":"10.3390\/cancers13143541","volume":"13","author":"C-L Chen","year":"2021","unstructured":"Chen C-L, Hsu S-C, Ann DK, Yen Y, Kung H-J. Arginine Signaling and Cancer Metabolism. Cancers (Basel). 2021;13:3541. https:\/\/doi.org\/10.3390\/cancers13143541.","journal-title":"Cancers (Basel)"},{"key":"3456_CR13","doi-asserted-by":"publisher","unstructured":"Kim S-H, Roszik J, Grimm EA, Ekmekcioglu S. Impact of l-Arginine Metabolism on Immune Response and Anticancer Immunotherapy. Front Oncol. 2018;8. https:\/\/doi.org\/10.3389\/fonc.2018.00067.","DOI":"10.3389\/fonc.2018.00067"},{"key":"3456_CR14","doi-asserted-by":"publisher","first-page":"25","DOI":"10.3390\/microorganisms5020025","volume":"5","author":"A Poli","year":"2017","unstructured":"Poli A, Finore I, Romano I, Gioiello A, Lama L, Nicolaus B. Microbial diversity in extreme marine habitats and their biomolecules. Microorganisms. 2017;5:25. https:\/\/doi.org\/10.3390\/microorganisms5020025.","journal-title":"Microorganisms"},{"key":"3456_CR15","doi-asserted-by":"publisher","first-page":"1957","DOI":"10.3390\/microorganisms8121957","volume":"8","author":"C Lauritano","year":"2020","unstructured":"Lauritano C, Rizzo C, Lo Giudice A, Saggiomo M. Physiological and molecular responses to main environmental stressors of microalgae and bacteria in polar marine environments. Microorganisms. 2020;8:1957. https:\/\/doi.org\/10.3390\/microorganisms8121957.","journal-title":"Microorganisms"},{"key":"3456_CR16","doi-asserted-by":"publisher","first-page":"656","DOI":"10.3390\/md17120656","volume":"17","author":"M Jin","year":"2019","unstructured":"Jin M, Gai Y, Guo X, Hou Y, Zeng R. Properties and applications of extremozymes from deep-sea extremophilic microorganisms: a mini review. Mar Drugs. 2019;17:656. https:\/\/doi.org\/10.3390\/md17120656.","journal-title":"Mar Drugs"},{"key":"3456_CR17","doi-asserted-by":"publisher","first-page":"261","DOI":"10.3390\/encyclopedia1010024","volume":"1","author":"EA Permyakov","year":"2021","unstructured":"Permyakov EA. Metal Binding Proteins. Encyclopedia. 2021;1:261\u201392. https:\/\/doi.org\/10.3390\/encyclopedia1010024.","journal-title":"Encyclopedia"},{"key":"3456_CR18","doi-asserted-by":"publisher","first-page":"110812","DOI":"10.1016\/j.jinorgbio.2019.110812","volume":"202","author":"E Uribe","year":"2020","unstructured":"Uribe E, Reyes M-B, Mart\u00ednez I, Mella K, Salas M, Tarife\u00f1o-Saldivia E, et al. Functional analysis of the Mn2\u2009+\u2009requirement in the catalysis of ureohydrolases arginase and agmatinase - a historical perspective. J Inorg Biochem. 2020;202:110812. https:\/\/doi.org\/10.1016\/j.jinorgbio.2019.110812.","journal-title":"J Inorg Biochem"},{"key":"3456_CR19","doi-asserted-by":"publisher","first-page":"8399","DOI":"10.1021\/bi301145n","volume":"51","author":"EL D\u2019Antonio","year":"2012","unstructured":"D\u2019Antonio EL, Hai Y, Christianson DW. Structure and function of non-native metal clusters in human arginase I. Biochemistry. 2012;51:8399\u2013409. https:\/\/doi.org\/10.1021\/bi301145n.","journal-title":"Biochemistry"},{"key":"3456_CR20","doi-asserted-by":"publisher","first-page":"5291","DOI":"10.3390\/ijms21155291","volume":"21","author":"S Clemente","year":"2020","unstructured":"Clemente S, van Waarde G, Antunes AF, D\u00f6mling I, Elsinga AH. Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective. Int J Mol Sci. 2020;21:5291. https:\/\/doi.org\/10.3390\/ijms21155291.","journal-title":"Int J Mol Sci"},{"key":"3456_CR21","doi-asserted-by":"publisher","unstructured":"Hern\u00e1ndez VM, Arteaga A, Dunn MF. Diversity, properties and functions of bacterial arginases. FEMS Microbiol Rev. 2021;45. https:\/\/doi.org\/10.1093\/femsre\/fuab034.","DOI":"10.1093\/femsre\/fuab034"},{"key":"3456_CR22","doi-asserted-by":"publisher","unstructured":"Hwangbo S-A, Kim J-W, Jung S-J, Jin KS, Lee J-O, Kim J-S, et al. Characterization of a Dimeric Arginase From Zymomonas mobilis ZM4. Front Microbiol. 2019;10. https:\/\/doi.org\/10.3389\/fmicb.2019.02755.","DOI":"10.3389\/fmicb.2019.02755"},{"key":"3456_CR23","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1186\/s12896-024-00829-6","volume":"24","author":"MS Selim","year":"2024","unstructured":"Selim MS, Mounier MM, Abdelhamid SA, Hamed AA, Abo Elsoud MM, Mohamed SS. Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2. BMC Biotechnol. 2024;24:6. https:\/\/doi.org\/10.1186\/s12896-024-00829-6.","journal-title":"BMC Biotechnol"},{"key":"3456_CR24","doi-asserted-by":"publisher","first-page":"995","DOI":"10.1016\/j.biocel.2013.02.008","volume":"45","author":"X Zhang","year":"2013","unstructured":"Zhang X, Zhang J, Zhang R, Guo Y, Wu C, Mao X, et al. Structural, enzymatic and biochemical studies on Helicobacter pylori arginase. Int J Biochem Cell Biol. 2013;45:995\u20131002. https:\/\/doi.org\/10.1016\/j.biocel.2013.02.008.","journal-title":"Int J Biochem Cell Biol"},{"key":"3456_CR25","doi-asserted-by":"publisher","first-page":"528","DOI":"10.1021\/acschembio.2c00879","volume":"18","author":"S Mordhorst","year":"2023","unstructured":"Mordhorst S, Badmann T, B\u00f6sch NM, Morinaka BI, Rauch H, Piel J, et al. Structural and biochemical insights into post-translational arginine-to-ornithine peptide modifications by an atypical arginase. ACS Chem Biol. 2023;18:528\u201336. https:\/\/doi.org\/10.1021\/acschembio.2c00879.","journal-title":"ACS Chem Biol"},{"key":"3456_CR26","doi-asserted-by":"publisher","first-page":"2113","DOI":"10.1074\/jbc.RA119.011752","volume":"295","author":"N Zhuang","year":"2020","unstructured":"Zhuang N, Zhang H, Li L, Wu X, Yang C, Zhang Y. Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a bond rotation catalytic mechanism. J Biol Chem. 2020;295:2113\u201324. https:\/\/doi.org\/10.1074\/jbc.RA119.011752.","journal-title":"J Biol Chem"},{"key":"3456_CR27","doi-asserted-by":"publisher","first-page":"3595","DOI":"10.1042\/BCJ20190545","volume":"476","author":"A Dutta","year":"2019","unstructured":"Dutta A, Mazumder M, Alam M, Gourinath S, Sau AK. Metal-induced change in catalytic loop positioning in Helicobacter pylori arginase alters catalytic function. Biochem J. 2019;476:3595\u2013614. https:\/\/doi.org\/10.1042\/BCJ20190545.","journal-title":"Biochem J"},{"key":"3456_CR28","doi-asserted-by":"publisher","first-page":"1153","DOI":"10.1016\/j.bbapap.2018.08.006","volume":"1866","author":"V Sadarangani","year":"2018","unstructured":"Sadarangani V, Rahman S, Sau AK. Metal ions-induced stability and function of bimetallic human arginase-I, a therapeutically important enzyme. Biochim et Biophys Acta (BBA) - Proteins Proteom. 2018;1866:1153\u201364. https:\/\/doi.org\/10.1016\/j.bbapap.2018.08.006.","journal-title":"Biochim et Biophys Acta (BBA) - Proteins Proteom"},{"key":"3456_CR29","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1089\/ind.2024.0029","volume":"20","author":"M Kumari","year":"2024","unstructured":"Kumari M, Karn SK, Raj V. Extremophiles and related extremozymes: their structure-function relationship in industrial applications. Ind Biotechnol. 2024;20:279\u201395. https:\/\/doi.org\/10.1089\/ind.2024.0029.","journal-title":"Ind Biotechnol"},{"key":"3456_CR30","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1016\/j.ijbiomac.2017.11.141","volume":"108","author":"TM Maharem","year":"2018","unstructured":"Maharem TM, Zahran WE, Hassan RE, Abdel Fattah MM. Unique properties of arginase purified from camel liver cytosol. Int J Biol Macromol. 2018;108:88\u201397. https:\/\/doi.org\/10.1016\/j.ijbiomac.2017.11.141.","journal-title":"Int J Biol Macromol"},{"key":"3456_CR31","doi-asserted-by":"publisher","first-page":"3697","DOI":"10.1038\/s41598-018-22099-x","volume":"8","author":"S Tommasi","year":"2018","unstructured":"Tommasi S, Elliot DJ, Da Boit M, Gray SR, Lewis BC, Mangoni AA. Homoarginine and inhibition of human arginase activity: kinetic characterization and biological relevance. Sci Rep. 2018;8:3697. https:\/\/doi.org\/10.1038\/s41598-018-22099-x.","journal-title":"Sci Rep"},{"key":"3456_CR32","doi-asserted-by":"publisher","first-page":"228","DOI":"10.1016\/j.bbrep.2017.10.006","volume":"12","author":"N Verma","year":"2017","unstructured":"Verma N, Singh AK, Singh M. L-arginine biosensors: A comprehensive review. Biochem Biophys Rep. 2017;12:228\u201339. https:\/\/doi.org\/10.1016\/j.bbrep.2017.10.006.","journal-title":"Biochem Biophys Rep"},{"key":"3456_CR33","doi-asserted-by":"publisher","first-page":"S2579","DOI":"10.3945\/jn.115.226621","volume":"146","author":"SM Morris","year":"2016","unstructured":"Morris SM. Arginine Metabolism Revisited. J Nutr. 2016;146:S2579\u201386. https:\/\/doi.org\/10.3945\/jn.115.226621.","journal-title":"J Nutr"},{"key":"3456_CR34","doi-asserted-by":"publisher","unstructured":"Buijs N, Brinkmann SJH, Ligthart-Melis GC, Schierbeek H. Metabolism of Glutamine, Citrulline, and Arginine; Stable Isotopes Analyzing the Intestinal\u2013Renal Axis. Mass Spectrometry and Stable Isotopes in Nutritional and Pediatric Research. Wiley; 2017. pp. 139\u201374. https:\/\/doi.org\/10.1002\/9781119341185.ch6.","DOI":"10.1002\/9781119341185.ch6"},{"key":"3456_CR35","doi-asserted-by":"publisher","unstructured":"Rath M, M\u00c3\u00bcller I, Kropf P, Closs EI, Munder M. Metabolism via Arginase or Nitric Oxide Synthase: Two Competing Arginine Pathways in Macrophages. Front Immunol. 2014;5. https:\/\/doi.org\/10.3389\/fimmu.2014.00532.","DOI":"10.3389\/fimmu.2014.00532"},{"key":"3456_CR36","doi-asserted-by":"publisher","first-page":"7068","DOI":"10.3390\/ijms22137068","volume":"22","author":"CL McGinity","year":"2021","unstructured":"McGinity CL, Palmieri EM, Somasundaram V, Bhattacharyya DD, Ridnour LA, Cheng RYS, et al. Nitric Oxide Modulates Metabolic Processes in the Tumor Immune Microenvironment. Int J Mol Sci. 2021;22:7068. https:\/\/doi.org\/10.3390\/ijms22137068.","journal-title":"Int J Mol Sci"},{"key":"3456_CR37","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1152\/physrev.00037.2016","volume":"98","author":"RW Caldwell","year":"2018","unstructured":"Caldwell RW, Rodriguez PC, Toque HA, Narayanan SP, Caldwell RB. Arginase: A Multifaceted enzyme important in health and disease. Physiol Rev. 2018;98:641\u201365. https:\/\/doi.org\/10.1152\/physrev.00037.2016.","journal-title":"Physiol Rev"},{"key":"3456_CR38","doi-asserted-by":"publisher","first-page":"4503","DOI":"10.3390\/nu13124503","volume":"13","author":"A Matos","year":"2021","unstructured":"Matos A, Carvalho M, Bicho M, Ribeiro R. Arginine and arginases modulate metabolism, tumor microenvironment and prostate cancer progression. Nutrients. 2021;13:4503. https:\/\/doi.org\/10.3390\/nu13124503.","journal-title":"Nutrients"},{"key":"3456_CR39","doi-asserted-by":"publisher","first-page":"12964","DOI":"10.1021\/acsnano.2c05408","volume":"16","author":"J Zhang","year":"2022","unstructured":"Zhang J, Wang S, Guo X, Lu Y, Liu X, Jiang M, et al. Arginine supplementation targeting tumor-killing immune cells reconstructs the tumor microenvironment and enhances the antitumor immune response. ACS Nano. 2022;16:12964\u201378. https:\/\/doi.org\/10.1021\/acsnano.2c05408.","journal-title":"ACS Nano"},{"key":"3456_CR40","doi-asserted-by":"publisher","first-page":"1316","DOI":"10.1158\/2326-6066.CIR-21-0280","volume":"9","author":"M Aaboe J\u00f8rgensen","year":"2021","unstructured":"Aaboe J\u00f8rgensen M, Ugel S, Linder H\u00fcbbe M, Carretta M, Perez-Penco M, Weis-Banke SE, et al. Arginase 1\u2013based immune modulatory vaccines induce anticancer immunity and synergize with anti\u2013PD-1 checkpoint blockade. Cancer Immunol Res. 2021;9:1316\u201326. https:\/\/doi.org\/10.1158\/2326-6066.CIR-21-0280.","journal-title":"Cancer Immunol Res"},{"key":"3456_CR41","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1158\/1538-7445.AM2016-552","volume":"76","author":"M Works","year":"2016","unstructured":"Works M, Bennett M, Chen J, Emberley E, Huang T, Janes J, et al. Abstract 552: Immuno-oncology agent CB-1158 is a potent and selective arginase inhibitor and causes an immune-mediated anti-tumor response. Cancer Res. 2016;76:552\u2013552. https:\/\/doi.org\/10.1158\/1538-7445.AM2016-552.","journal-title":"Cancer Res"},{"key":"3456_CR42","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1186\/s40425-019-0504-5","volume":"7","author":"JJ Miret","year":"2019","unstructured":"Miret JJ, Kirschmeier P, Koyama S, Zhu M, Li YY, Naito Y, et al. Suppression of myeloid cell arginase activity leads to therapeutic response in a NSCLC mouse model by activating anti-tumor immunity. J Immunother Cancer. 2019;7:32. https:\/\/doi.org\/10.1186\/s40425-019-0504-5.","journal-title":"J Immunother Cancer"},{"key":"3456_CR43","doi-asserted-by":"publisher","first-page":"e1404215","DOI":"10.1080\/2162402X.2017.1404215","volume":"7","author":"E Martinenaite","year":"2018","unstructured":"Martinenaite E, Mortensen REJ, Hansen M, Orebo Holmstr\u00f6m M, Munir Ahmad S, Gr\u00f8nne Dahlager J\u00f8rgensen N, et al. Frequent adaptive immune responses against arginase-1. Oncoimmunology. 2018;7:e1404215. https:\/\/doi.org\/10.1080\/2162402X.2017.1404215.","journal-title":"Oncoimmunology"},{"key":"3456_CR44","doi-asserted-by":"publisher","unstructured":"Weis-Banke SE, H\u00fcbbe ML, Holmstr\u00f6m MO, J\u00f8rgensen MA, Bendtsen SK, Martinenaite E, et al. The metabolic enzyme arginase-2 is a potential target for novel immune modulatory vaccines. Oncoimmunology. 2020;9. https:\/\/doi.org\/10.1080\/2162402X.2020.1771142.","DOI":"10.1080\/2162402X.2020.1771142"},{"key":"3456_CR45","doi-asserted-by":"publisher","first-page":"2762","DOI":"10.1002\/ijc.25202","volume":"126","author":"B Delage","year":"2010","unstructured":"Delage B, Fennell DA, Nicholson L, McNeish I, Lemoine NR, Crook T, et al. Arginine deprivation and argininosuccinate synthetase expression in the treatment of cancer. Int J Cancer. 2010;126:2762\u201372. https:\/\/doi.org\/10.1002\/ijc.25202.","journal-title":"Int J Cancer"},{"key":"3456_CR46","doi-asserted-by":"publisher","first-page":"72","DOI":"10.3390\/ph14010072","volume":"14","author":"M Kuo","year":"2021","unstructured":"Kuo M, Chen H, Feun L, Savaraj N. Targeting the proline\u2013glutamine\u2013asparagine\u2013arginine metabolic axis in amino acid starvation cancer therapy. Pharmaceuticals. 2021;14:72. https:\/\/doi.org\/10.3390\/ph14010072.","journal-title":"Pharmaceuticals"},{"key":"3456_CR47","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1186\/1756-8722-5-17","volume":"5","author":"EC Hsueh","year":"2012","unstructured":"Hsueh EC, Knebel SM, Lo W-H, Leung Y-C, Cheng PN-M, Hsueh C-T. Deprivation of arginine by recombinant human arginase in prostate cancer cells. J Hematol Oncol. 2012;5:17. https:\/\/doi.org\/10.1186\/1756-8722-5-17.","journal-title":"J Hematol Oncol"},{"key":"3456_CR48","doi-asserted-by":"publisher","first-page":"105926","DOI":"10.1016\/j.archoralbio.2024.105926","volume":"161","author":"B Kannan","year":"2024","unstructured":"Kannan B, Pandi C, Pandi A, Jayaseelan VP, Arumugam P. Triggering receptor expressed in myeloid cells 1 (TREM1) as a potential prognostic biomarker and association with immune infiltration in oral squamous cell carcinoma. Archives of oral biology. 2024 May 1;161:105926. https:\/\/doi.org\/10.1016\/j.archoralbio.2024.105926","journal-title":"Archives of oral biology<br>"},{"key":"3456_CR49","doi-asserted-by":"publisher","first-page":"S2837","DOI":"10.1093\/jn\/134.10.2837S","volume":"134","author":"DS Lind","year":"2004","unstructured":"Lind DS. Arginine and Cancer. J Nutr. 2004;134:S2837\u201341. https:\/\/doi.org\/10.1093\/jn\/134.10.2837S.","journal-title":"J Nutr"},{"key":"3456_CR50","doi-asserted-by":"publisher","first-page":"964","DOI":"10.1038\/s41419-020-03175-5","volume":"11","author":"M Cerezo","year":"2020","unstructured":"Cerezo M, Rocchi S. Cancer cell metabolic reprogramming: a keystone for the response to immunotherapy. Cell Death Dis. 2020;11:964. https:\/\/doi.org\/10.1038\/s41419-020-03175-5.","journal-title":"Cell Death Dis"},{"key":"3456_CR51","doi-asserted-by":"publisher","unstructured":"McNeal CJ, Meininger CJ, Reddy D, Wilborn CD, Wu G. Safety and effectiveness of arginine in adults. J Nutr. 2016;146. https:\/\/doi.org\/10.3945\/jn.116.234740. :2587S-2593S.","DOI":"10.3945\/jn.116.234740"},{"key":"3456_CR52","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1038\/s41568-022-00473-2","volume":"22","author":"CE Holbert","year":"2022","unstructured":"Holbert CE, Cullen MT, Casero RA, Stewart TM. Polyamines in cancer: integrating organismal metabolism and antitumour immunity. Nat Rev Cancer. 2022;22:467\u201380. https:\/\/doi.org\/10.1038\/s41568-022-00473-2.","journal-title":"Nat Rev Cancer"},{"key":"3456_CR53","doi-asserted-by":"publisher","first-page":"906","DOI":"10.1111\/j.1440-1681.2007.04638.x","volume":"34","author":"W Durante","year":"2007","unstructured":"Durante W, Johnson FK, Johnson RA, Arginase: a critical regulator, of nitric, oxide synthesis and vascular function. Clin Exp Pharmacol Physiol. 2007;34:906\u201311. https:\/\/doi.org\/10.1111\/j.1440-1681.2007.04638.x.","journal-title":"Clin Exp Pharmacol Physiol"},{"key":"3456_CR54","doi-asserted-by":"publisher","first-page":"3541","DOI":"10.3390\/cancers13143541","volume":"13","author":"C-L Chen","year":"2021","unstructured":"Chen C-L, Hsu S-C, Ann DK, Yen Y, Kung H-J. Arginine signaling and cancer metabolism. Cancers (Basel). 2021;13:3541. https:\/\/doi.org\/10.3390\/cancers13143541.","journal-title":"Cancers (Basel)"},{"key":"3456_CR55","doi-asserted-by":"publisher","first-page":"2156","DOI":"10.1002\/bit.27011","volume":"116","author":"F Cheng","year":"2019","unstructured":"Cheng F, Yang J, Schwaneberg U, Zhu L. Rational surface engineering of an arginine deiminase (an antitumor enzyme) for increased PEGylation efficiency. Biotechnol Bioeng. 2019;116:2156\u201366. https:\/\/doi.org\/10.1002\/bit.27011.","journal-title":"Biotechnol Bioeng"},{"key":"3456_CR56","doi-asserted-by":"publisher","first-page":"941","DOI":"10.1021\/acs.bioconjchem.3c00174","volume":"34","author":"R Tenchov","year":"2023","unstructured":"Tenchov R, Sasso JM, Zhou QA. PEGylated lipid nanoparticle formulations: immunological safety and efficiency perspective. Bioconjug Chem. 2023;34:941\u201360. https:\/\/doi.org\/10.1021\/acs.bioconjchem.3c00174.","journal-title":"Bioconjug Chem"},{"key":"3456_CR57","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1186\/1475-2867-9-9","volume":"9","author":"S-M Tsui","year":"2009","unstructured":"Tsui S-M, Lam W-M, Lam T-L, Chong H-C, So P-K, Kwok S-Y, et al. Pegylated derivatives of recombinant human arginase (rhArg1) for sustained in vivo activity in cancer therapy: preparation, characterization and analysis of their pharmacodynamics in vivo and in vitro and action upon hepatocellular carcinoma cell (HCC). Cancer Cell Int. 2009;9:9. https:\/\/doi.org\/10.1186\/1475-2867-9-9.","journal-title":"Cancer Cell Int"},{"key":"3456_CR58","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1007\/s00792-017-0939-x","volume":"21","author":"MF Siliakus","year":"2017","unstructured":"Siliakus MF, van der Oost J, Kengen SWM. Adaptations of archaeal and bacterial membranes to variations in temperature, pH and pressure. Extremophiles. 2017;21:651\u201370. https:\/\/doi.org\/10.1007\/s00792-017-0939-x.","journal-title":"Extremophiles"},{"key":"3456_CR59","doi-asserted-by":"publisher","first-page":"478","DOI":"10.3390\/md9040478","volume":"9","author":"A Trincone","year":"2011","unstructured":"Trincone A. Marine Biocatalysts: Enzymatic features and applications. Mar Drugs. 2011;9:478\u201399. https:\/\/doi.org\/10.3390\/md9040478.","journal-title":"Mar Drugs"},{"key":"3456_CR60","doi-asserted-by":"publisher","first-page":"2265","DOI":"10.21608\/nrmj.2024.336571","volume":"8","author":"S Sadaf Wajahat","year":"2024","unstructured":"Sadaf Wajahat S. Potentials of the marine microbial enzymes in therapeutics. Novel Res Microbiol J. 2024;8:2265\u201384. https:\/\/doi.org\/10.21608\/nrmj.2024.336571.","journal-title":"Novel Res Microbiol J"},{"key":"3456_CR61","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1007\/s42995-020-00058-8","volume":"2","author":"X-L Chen","year":"2020","unstructured":"Chen X-L, Wang Y, Wang P, Zhang Y-Z. Proteases from the marine bacteria in the genus Pseudoalteromonas: diversity, characteristics, ecological roles, and application potentials. Mar Life Sci Technol. 2020;2:309\u201323. https:\/\/doi.org\/10.1007\/s42995-020-00058-8.","journal-title":"Mar Life Sci Technol"},{"key":"3456_CR62","doi-asserted-by":"publisher","first-page":"656","DOI":"10.3390\/md17120656","volume":"17","author":"M Jin","year":"2019","unstructured":"Jin M, Gai Y, Guo X, Hou Y, Zeng R. Properties and applications of extremozymes from deep-sea extremophilic microorganisms: a mini review. Mar Drugs. 2019;17:656. https:\/\/doi.org\/10.3390\/md17120656.","journal-title":"Mar Drugs"},{"key":"3456_CR63","doi-asserted-by":"publisher","first-page":"201","DOI":"10.13005\/bbra\/2436","volume":"14","author":"R Unissa","year":"2017","unstructured":"Unissa R, Sowmya M, Sagarika Y, Divya V, Anusha M, Kumar Chauhan A, et al. Purification, kinetic characterization and anti-proliferative activity of a therapeutic protein from marine sources. Biosci Biotechnol Res Asia. 2017;14:201\u20138. https:\/\/doi.org\/10.13005\/bbra\/2436.","journal-title":"Biosci Biotechnol Res Asia"},{"key":"3456_CR64","doi-asserted-by":"publisher","first-page":"4234","DOI":"10.3390\/ijms21124234","volume":"21","author":"S-F Chung","year":"2020","unstructured":"Chung S-F, Kim C-F, Kwok S-Y, Tam S-Y, Chen YW, Chong H-C, et al. Mono-PEGylation of a thermostable arginine-depleting enzyme for the treatment of lung cancer. Int J Mol Sci. 2020;21:4234. https:\/\/doi.org\/10.3390\/ijms21124234.","journal-title":"Int J Mol Sci"},{"key":"3456_CR65","doi-asserted-by":"publisher","first-page":"895","DOI":"10.1007\/s10637-022-01265-z","volume":"40","author":"S-F Chung","year":"2022","unstructured":"Chung S-F, Tam S-Y, Kim C-F, Chong H-C, Lee LM-Y, Leung Y-C. Mono-PEGylated thermostable Bacillus caldovelox arginase mutant (BCA-M-PEG20) induces apoptosis, autophagy, cell cycle arrest and growth inhibition in gastric cancer cells. Invest New Drugs. 2022;40:895\u2013904. https:\/\/doi.org\/10.1007\/s10637-022-01265-z.","journal-title":"Invest New Drugs"},{"key":"3456_CR66","doi-asserted-by":"publisher","first-page":"1965","DOI":"10.3390\/microorganisms10101965","volume":"10","author":"CJC Rodrigues","year":"2022","unstructured":"Rodrigues CJC, de Carvalho CCCR. Marine bioprospecting, biocatalysis and process development. Microorganisms. 2022;10:1965. https:\/\/doi.org\/10.3390\/microorganisms10101965.","journal-title":"Microorganisms"},{"key":"3456_CR67","doi-asserted-by":"publisher","first-page":"1994","DOI":"10.1039\/D1NP00006C","volume":"38","author":"SL Robinson","year":"2021","unstructured":"Robinson SL, Piel J, Sunagawa S. A roadmap for metagenomic enzyme discovery. Nat Prod Rep. 2021;38:1994\u20132023. https:\/\/doi.org\/10.1039\/D1NP00006C.","journal-title":"Nat Prod Rep"},{"key":"3456_CR68","doi-asserted-by":"publisher","unstructured":"Bramhachari PV, Sheela GM, Satish T. Perspectives for novel enzyme discovery from marine environments through genome mining and metagenomics. Encyclopedia of Marine Biotechnology. Wiley; 2020. pp. 2423\u201342. https:\/\/doi.org\/10.1002\/9781119143802.ch109.","DOI":"10.1002\/9781119143802.ch109"},{"key":"3456_CR69","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1016\/j.gpb.2018.01.002","volume":"16","author":"TR Ngara","year":"2018","unstructured":"Ngara TR, Zhang H. Recent Advances in function-based metagenomic screening. Genomics Proteom Bioinf. 2018;16:405\u201315. https:\/\/doi.org\/10.1016\/j.gpb.2018.01.002.","journal-title":"Genomics Proteom Bioinf"},{"key":"3456_CR70","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1007\/s44288-025-00338-9","volume":"3","author":"T Saikia","year":"2025","unstructured":"Saikia T, Das S. A review of geomicrobial bioprospecting strategies for novel therapeutic discovery from Earth\u2019s extreme environments. Discover Geoscience. 2025;3:223. https:\/\/doi.org\/10.1007\/s44288-025-00338-9.","journal-title":"Discover Geoscience"},{"key":"3456_CR71","doi-asserted-by":"publisher","unstructured":"Bhatt HB, Sani RK, Amoozegar MA, Singh SP, Editorial. Extremozymes: characteristics, structure, protein engineering and applications. Front Microbiol. 2024;15. https:\/\/doi.org\/10.3389\/fmicb.2024.1423463.","DOI":"10.3389\/fmicb.2024.1423463"},{"key":"3456_CR72","doi-asserted-by":"publisher","first-page":"4623","DOI":"10.1021\/acs.jcim.3c00772","volume":"63","author":"D Platero-Rochart","year":"2023","unstructured":"Platero-Rochart D, Krivobokova T, Gastegger M, Reibnegger G, S\u00e1nchez-Murcia PA. Prediction of enzyme catalysis by computing reaction energy barriers via steered QM\/MM molecular dynamics simulations and machine learning. J Chem Inf Model. 2023;63:4623\u201332. https:\/\/doi.org\/10.1021\/acs.jcim.3c00772.","journal-title":"J Chem Inf Model"},{"key":"3456_CR73","doi-asserted-by":"publisher","first-page":"1049","DOI":"10.2174\/138161208784246199","volume":"14","author":"L Feun","year":"2008","unstructured":"Feun L, You M, Wu C, Kuo M, Wangpaichitr M, Spector S, et al. Arginine deprivation as a targeted therapy for cancer. Curr Pharm Des. 2008;14:1049\u201357. https:\/\/doi.org\/10.2174\/138161208784246199.","journal-title":"Curr Pharm Des"},{"key":"3456_CR74","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1111\/j.1755-148X.2010.00798.x","volume":"24","author":"T Lam","year":"2011","unstructured":"Lam T, Wong GKY, Chow H, Chong H, Chow T, Kwok S, et al. Recombinant human arginase inhibits the in vitro and in vivo proliferation of human melanoma by inducing cell cycle arrest and apoptosis. Pigment Cell Melanoma Res. 2011;24:366\u201376. https:\/\/doi.org\/10.1111\/j.1755-148X.2010.00798.x.","journal-title":"Pigment Cell Melanoma Res"},{"key":"3456_CR75","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1158\/0008-5472.CAN-06-1945","volume":"67","author":"PN-M Cheng","year":"2007","unstructured":"Cheng PN-M, Lam T-L, Lam W-M, Tsui S-M, Cheng AW-M, Lo W-H, et al. Pegylated Recombinant Human Arginase (rhArg-peg5,000mw) Inhibits the In vitro and In vivo Proliferation of Human Hepatocellular Carcinoma through Arginine Depletion. Cancer Res. 2007;67:309\u201317. https:\/\/doi.org\/10.1158\/0008-5472.CAN-06-1945.","journal-title":"Cancer Res"},{"key":"3456_CR76","doi-asserted-by":"publisher","first-page":"991","DOI":"10.1007\/s11030-024-10886-w","volume":"29","author":"S Muthumanickam","year":"2025","unstructured":"Muthumanickam S, Ramachandran B, Jeyakanthan J, Jegatheswaran S, Pandi B. Designing a novel drug\u2013drug conjugate as a prodrug for breast cancer therapy: in silico insights. Mol Divers. 2025;29:991\u20131007. https:\/\/doi.org\/10.1007\/s11030-024-10886-w.","journal-title":"Mol Divers"},{"key":"3456_CR77","doi-asserted-by":"publisher","unstructured":"Madesh S, Murugan R, Sau A, Jubie S, Swaroop AK, Rajagopal R, et al. Nano-encapsulated coumarin derivative, CS\u2010QM2 inhibits neoplasm growth: experimented in zebrafish model. J Biochem Mol Toxicol. 2025;39. https:\/\/doi.org\/10.1002\/jbt.70239.","DOI":"10.1002\/jbt.70239"},{"key":"3456_CR78","doi-asserted-by":"publisher","first-page":"1778","DOI":"10.1200\/JCO.2016.71.3230","volume":"35","author":"E Beddowes","year":"2017","unstructured":"Beddowes E, Spicer J, Chan PY, Khadeir R, Corbacho JG, Repana D, et al. Phase 1 Dose-Escalation Study of Pegylated Arginine Deiminase, Cisplatin, and Pemetrexed in Patients With Argininosuccinate Synthetase 1\u2013Deficient Thoracic Cancers. J Clin Oncol. 2017;35:1778\u201385. https:\/\/doi.org\/10.1200\/JCO.2016.71.3230.","journal-title":"J Clin Oncol"},{"key":"3456_CR79","doi-asserted-by":"publisher","first-page":"139171","DOI":"10.1016\/j.ijbiomac.2024.139171","volume":"292","author":"A KLG","year":"2025","unstructured":"KLG A, Priyadharshini B, Vasugi S, Dilipan E. Exploring the therapeutic potential of biosynthetic enzymes in cancer treatment: Innovations and implications. Int J Biol Macromol. 2025;292:139171. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.139171.","journal-title":"Int J Biol Macromol"},{"key":"3456_CR80","doi-asserted-by":"publisher","first-page":"4957","DOI":"10.1038\/onc.2016.37","volume":"35","author":"MD Patil","year":"2016","unstructured":"Patil MD, Bhaumik J, Babykutty S, Banerjee UC, Fukumura D. Arginine dependence of tumor cells: targeting a chink in cancer\u2019s armor. Oncogene. 2016;35:4957\u201372. https:\/\/doi.org\/10.1038\/onc.2016.37.","journal-title":"Oncogene"},{"key":"3456_CR81","doi-asserted-by":"publisher","first-page":"1375","DOI":"10.1007\/s10637-021-01111-8","volume":"39","author":"SL Chan","year":"2021","unstructured":"Chan SL, Cheng PNM, Liu AM, Chan LL, Li L, Chu CM, et al. A phase II clinical study on the efficacy and predictive biomarker of pegylated recombinant arginase on hepatocellular carcinoma. Invest New Drugs. 2021;39:1375\u201382. https:\/\/doi.org\/10.1007\/s10637-021-01111-8.","journal-title":"Invest New Drugs"},{"key":"3456_CR82","doi-asserted-by":"publisher","first-page":"314","DOI":"10.1007\/s10637-021-01178-3","volume":"40","author":"T Yau","year":"2022","unstructured":"Yau T, Cheng PNM, Chiu J, Kwok GGW, Leung R, Liu AM, et al. A phase 1 study of pegylated recombinant arginase (PEG-BCT-100) in combination with systemic chemotherapy (capecitabine and oxaliplatin)[PACOX] in advanced hepatocellular carcinoma patients. Invest New Drugs. 2022;40:314\u201321. https:\/\/doi.org\/10.1007\/s10637-021-01178-3.","journal-title":"Invest New Drugs"},{"key":"3456_CR83","doi-asserted-by":"publisher","first-page":"425","DOI":"10.1007\/s10637-012-9862-2","volume":"31","author":"PA Ott","year":"2013","unstructured":"Ott PA, Carvajal RD, Pandit-Taskar N, Jungbluth AA, Hoffman EW, Wu B-W, et al. Phase I\/II study of pegylated arginine deiminase (ADI-PEG 20) in patients with advanced melanoma. Invest New Drugs. 2013;31:425\u201334. https:\/\/doi.org\/10.1007\/s10637-012-9862-2.","journal-title":"Invest New Drugs"},{"key":"3456_CR84","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1001\/jamaoncol.2016.3049","volume":"3","author":"PW Szlosarek","year":"2017","unstructured":"Szlosarek PW, Steele JP, Nolan L, Gilligan D, Taylor P, Spicer J, et al. Arginine Deprivation With Pegylated Arginine Deiminase in Patients With Argininosuccinate Synthetase 1\u2013Deficient Malignant Pleural Mesothelioma. JAMA Oncol. 2017;3:58. https:\/\/doi.org\/10.1001\/jamaoncol.2016.3049.","journal-title":"JAMA Oncol"},{"key":"3456_CR85","doi-asserted-by":"publisher","first-page":"251","DOI":"10.4143\/crt.2013.45.4.251","volume":"45","author":"MM Phillips","year":"2013","unstructured":"Phillips MM, Sheaff MT, Szlosarek PW. Targeting arginine-dependent cancers with arginine-degrading enzymes: opportunities and challenges. Cancer Res Treat. 2013;45:251\u201362. https:\/\/doi.org\/10.4143\/crt.2013.45.4.251.","journal-title":"Cancer Res Treat"},{"key":"3456_CR86","doi-asserted-by":"publisher","first-page":"251","DOI":"10.4143\/crt.2013.45.4.251","volume":"45","author":"MM Phillips","year":"2013","unstructured":"Phillips MM, Sheaff MT, Szlosarek PW. Targeting arginine-dependent cancers with arginine-degrading enzymes: opportunities and challenges. Cancer Res Treat. 2013;45:251\u201362. https:\/\/doi.org\/10.4143\/crt.2013.45.4.251.","journal-title":"Cancer Res Treat"},{"key":"3456_CR87","doi-asserted-by":"publisher","first-page":"813","DOI":"10.1038\/nrd4333","volume":"13","author":"VP Torchilin","year":"2014","unstructured":"Torchilin VP. Multifunctional, stimuli-sensitive nanoparticulate systems for drug delivery. Nat Rev Drug Discov. 2014;13:813\u201327. https:\/\/doi.org\/10.1038\/nrd4333.","journal-title":"Nat Rev Drug Discov"}],"container-title":["Medical Oncology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12032-026-03456-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12032-026-03456-7","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12032-026-03456-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T17:02:04Z","timestamp":1792515724000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12032-026-03456-7"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,20]]},"references-count":87,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2026,11]]}},"alternative-id":["3456"],"URL":"https:\/\/doi.org\/10.1007\/s12032-026-03456-7","relation":{},"ISSN":["1559-131X"],"issn-type":[{"value":"1559-131X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,10,20]]},"assertion":[{"value":"26 November 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"28 September 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 October 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","label":"Competing interests","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"In the present review studies, we did not use any animal\/human. Therefore, we do not require any ethical approval.","order":2,"name":"Ethics","label":"Ethical Approval","group":{"name":"EthicsHeading","label":"Declarations"}}],"article-number":"343"}}