{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T10:07:29Z","timestamp":1789985249820,"version":"4.0.1"},"reference-count":166,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T00:00:00Z","timestamp":1789776000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Scientific Foundation of China","doi-asserted-by":"publisher","award":["U21A20336"],"award-info":[{"award-number":["U21A20336"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Basic Research Program of Shanxi Province","award":["202503021211133"],"award-info":[{"award-number":["202503021211133"]}]},{"name":"Shanxi Province Higher Education \u201cBillion Project\u201d Science and Technology Guidance Project","award":["SYBYRC-202501"],"award-info":[{"award-number":["SYBYRC-202501"]}]},{"name":"Shanxi Province Higher Education \u201cBillion Project\u201d Science and Technology Guidance Project","award":["SY-BYSL-2025001"],"award-info":[{"award-number":["SY-BYSL-2025001"]}]},{"name":"Shanxi Province Higher Education \u201cBillion Project\u201d Science and Technology Guidance Project","award":["2025005"],"award-info":[{"award-number":["2025005"]}]},{"name":"Shanxi Province Higher Education \u201cBillion Project\u201d Science and Technology Guidance Project","award":["BYJL011"],"award-info":[{"award-number":["BYJL011"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Methylation, catalyzed by a diverse family of S-adenosylmethionine (SAM)-dependent methyltransferases, is a fundamental biochemical process that regulates the function of proteins, DNA, and RNA. Among these modifications, protein arginine methylation, catalyzed by protein arginine methyltransferases (PRMTs), represents a critical post-translational mechanism regulating transcription, DNA repair, RNA splicing, and signal transduction. Emerging evidence highlights important roles of PRMTs in cardiovascular diseases (CVDs); however, current research is limited by several challenges, including the paradoxical and context-dependent functions of individual PRMTs and the lack of highly specific inhibitors or activators, leaving their therapeutic potential incompletely defined. This review summarizes the classification, structure, and functional characteristics of methyltransferases, with a particular focus on PRMTs and their roles in normal physiology and diverse CVDs. We integrate current knowledge to provide a comprehensive understanding of how PRMTs contribute to cardiovascular pathophysiology by methylating histones, transcription factors, and other functional proteins. Collectively, PRMTs emerge as pivotal regulators in CVD development and progression. Future studies should prioritize resolving the functional duality of specific PRMTs, developing targeted precision therapeutics, and elucidating the roles of less-characterized family members in CVDs.<\/jats:p>","DOI":"10.3390\/biom16091365","type":"journal-article","created":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T09:01:38Z","timestamp":1789981298000},"page":"1365","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["S-Adenosylmethionine-Dependent Methylation, Protein Arginine Methyltransferases and Cardiovascular Diseases"],"prefix":"10.3390","volume":"16","author":[{"given":"Zi","family":"Yan","sequence":"first","affiliation":[{"name":"Department of Physiology, Shanxi Medical University, Taiyuan 030001, China"},{"name":"MOE Key Laboratory of Cellular Physiology, Shanxi Medical University, Taiyuan 030001, China"},{"name":"Shanxi Key Laboratory of Aging-Related Diseases Mechanisms and Translation, Taiyuan 030001, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenhui","family":"Zhao","sequence":"additional","affiliation":[{"name":"Department of Physiology, Shanxi Medical University, Taiyuan 030001, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naixin","family":"Zhao","sequence":"additional","affiliation":[{"name":"Department of Physiology, Shanxi Medical University, Taiyuan 030001, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8401-0035","authenticated-orcid":false,"given":"Jianguo","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Physiology, Shanxi Medical University, Taiyuan 030001, China"},{"name":"MOE Key Laboratory of Cellular Physiology, Shanxi Medical University, Taiyuan 030001, China"},{"name":"Shanxi Key Laboratory of Aging-Related Diseases Mechanisms and Translation, Taiyuan 030001, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"108396","DOI":"10.1016\/j.mrrev.2021.108396","article-title":"Insights into S-adenosyl-L-methionine (SAM)-dependent methyltransferase related diseases and genetic polymorphisms","volume":"788","author":"Li","year":"2021","journal-title":"Mutat. Res. Rev. Mutat. Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1038\/s41392-023-01528-y","article-title":"Methylation across the central dogma in health and diseases: New therapeutic strategies","volume":"8","author":"Liu","year":"2023","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S1357-2725(99)00139-9","article-title":"S-Adenosylmethionine","volume":"32","author":"Lu","year":"2000","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"e12891","DOI":"10.1111\/cpr.12891","article-title":"S-adenosylmethionine: A metabolite critical to the regulation of autophagy","volume":"53","author":"Ouyang","year":"2020","journal-title":"Cell Prolif."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Dhayalan, A., and Jeltsch, A. (2022). Special Issue \u201cStructure, Activity, and Function of Protein Methyltransferases\u201d. Life, 12.","DOI":"10.3390\/life12030405"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1021\/acschembio.0c00771","article-title":"Non-Histone Protein Methylation: Biological Significance and Bioengineering Potential","volume":"16","author":"Blyuss","year":"2021","journal-title":"ACS Chem. Biol."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Micallef, I., Fenech, K., and Baron, B. (2024). Therapeutic targeting potential of the protein lysine and arginine methyltransferases to reverse cancer chemoresistance. Front. Mol. Biosci., 11.","DOI":"10.3389\/fmolb.2024.1455415"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Pham, H.Q.H., Tao, X., and Yang, Y. (2023). Protein arginine methylation in transcription and epigenetic regulation. Front. Epigenet. Epigenomics, 1.","DOI":"10.3389\/freae.2023.1245832"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1038\/s41573-021-00159-8","article-title":"Protein arginine methylation: From enigmatic functions to therapeutic targeting","volume":"20","author":"Wu","year":"2021","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"101016","DOI":"10.1016\/j.drup.2023.101016","article-title":"Promising role of protein arginine methyltransferases in overcoming anti-cancer drug resistance","volume":"72","author":"Zhu","year":"2024","journal-title":"Drug Resist. Updat."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.semcdb.2022.08.005","article-title":"The role of protein arginine N-methyltransferases in inflammation","volume":"154","author":"Chen","year":"2024","journal-title":"Semin. Cell. Dev. Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.molcel.2016.11.003","article-title":"Arginine Methylation: The Coming of Age","volume":"65","author":"Blanc","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1038\/s41929-019-0300-0","article-title":"S-adenosylhomocysteine as a methyl transfer catalyst in biocatalytic methylation reactions","volume":"2","author":"Liao","year":"2019","journal-title":"Nat. Catal."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1039\/D2NP00086E","article-title":"S-Adenosylmethionine: More than just a methyl donor","volume":"40","author":"Lee","year":"2023","journal-title":"Nat. Prod. Rep."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Dusa, F.C., Vellai, T., and Sipos, M. (2025). Nutrition and DNA Methylation: How Dietary Methyl Donors Affect Reproduction and Aging. Dietetics, 4.","DOI":"10.3390\/dietetics4030030"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Menezo, Y., Elder, K., Clement, A., and Clement, P. (2022). Folic Acid, Folinic Acid, 5 Methyl TetraHydroFolate Supplementation for Mutations That Affect Epigenesis Through the Folate and One-Carbon Cycles. Biomolecules, 12.","DOI":"10.3390\/biom12020197"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"11971","DOI":"10.1074\/jbc.RA120.012934","article-title":"MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase","volume":"295","author":"Kountz","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1186\/s40246-026-00949-4","article-title":"Update of the Methyltransferase Gene Family: Classification, Evolution and Biological Functions","volume":"20","author":"Katsafadou","year":"2026","journal-title":"Hum. Genom."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1021\/acs.chemrev.6b00801","article-title":"Inhibitors of Protein Methyltransferases and Demethylases","volume":"118","author":"Kaniskan","year":"2018","journal-title":"Chem. Rev."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1038\/s41392-020-00252-1","article-title":"The role of histone methylation in the development of digestive cancers: A potential direction for cancer management","volume":"5","author":"Chen","year":"2020","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"107354","DOI":"10.1016\/j.phrs.2024.107354","article-title":"Methylation modification of non-histone proteins in breast cancer: An emerging targeted therapeutic strategy","volume":"208","author":"Huang","year":"2024","journal-title":"Pharmacol. Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/s41573-020-00108-x","article-title":"Epigenetics and beyond: Targeting writers of protein lysine methylation to treat disease","volume":"20","author":"Bhat","year":"2021","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Kaganovski, A., Smith-Salzberg, B., Shimshon, H.K., Draheim, A., Spivak, M., Sapir, T., and Shifteh, D. (2025). Current and Emerging Therapies for Targeting Protein Arginine Methyltransferases (PRMTs) in Cancer. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26167907"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"116212","DOI":"10.1016\/j.ejmech.2024.116212","article-title":"Overview of the development of protein arginine methyltransferase modulators: Achievements and future directions","volume":"267","author":"Tong","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"108201","DOI":"10.1016\/j.jbc.2025.108201","article-title":"Biomedical effects of protein arginine methyltransferase inhibitors","volume":"301","author":"Cao","year":"2025","journal-title":"J. Biol. Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1093\/nar\/gkaa1154","article-title":"Staying true to yourself: Mechanisms of DNA methylation maintenance in mammals","volume":"49","author":"Petryk","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/nrg.2017.80","article-title":"The DNA methyltransferase family: A versatile toolkit for epigenetic regulation","volume":"19","author":"Lyko","year":"2018","journal-title":"Nat. Rev. Genet."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"105937","DOI":"10.1016\/j.phrs.2021.105937","article-title":"RNA methylation and cancer treatment","volume":"174","author":"Yang","year":"2021","journal-title":"Pharmacol. Res."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/s41573-025-01280-8","article-title":"RNA modification systems as therapeutic targets","volume":"25","author":"Zhang","year":"2026","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"e202200212","DOI":"10.1002\/cbic.202200212","article-title":"Methyltransferases: Functions and Applications","volume":"23","author":"Abdelraheem","year":"2022","journal-title":"ChemBioChem"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.apsb.2020.08.011","article-title":"Diversity of the reaction mechanisms of SAM-dependent enzymes","volume":"11","author":"Sun","year":"2021","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Fotiadou, R., Heinz, F., Weigmann, K.F.G., Doerr, M., Bornscheuer, U.T., and Pavlidis, I.V. (2026). High-throughput assays for SAM-dependent methyltransferases: Advances, challenges, and future perspectives. Nat. Prod. Rep.","DOI":"10.1039\/D6NP00006A"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1038\/s41467-020-14722-1","article-title":"Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site","volume":"11","author":"Pennington","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1038\/s41556-023-01299-2","article-title":"Vitamin B12 produced by gut bacteria modulates cholinergic signalling","volume":"26","author":"Kang","year":"2024","journal-title":"Nat. Cell Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1021\/acs.biochem.8b01047","article-title":"A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily","volume":"58","author":"Krishnamohan","year":"2019","journal-title":"Biochemistry"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.tibs.2022.10.003","article-title":"To incise or not and where: SET-domain methyltransferases know","volume":"48","author":"Yancoskie","year":"2023","journal-title":"Trends Biochem. Sci."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"690","DOI":"10.2174\/1389203720666191023150727","article-title":"Using Yeast to Define the Regulatory Role of Protein Lysine Methylation","volume":"21","author":"Jethmalani","year":"2020","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2611","DOI":"10.1021\/acs.accounts.8b00356","article-title":"Mechanism of Radical Initiation in the Radical S-Adenosyl-l-methionine Superfamily","volume":"51","author":"Broderick","year":"2018","journal-title":"Acc. Chem. Res."},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Nguyen, T.Q., and Nicolet, Y. (2022). Structure and Catalytic Mechanism of Radical SAM Methylases. Life, 12.","DOI":"10.3390\/life12111732"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"6656","DOI":"10.1021\/acs.chemrev.8b00008","article-title":"Chemical and Biochemical Perspectives of Protein Lysine Methylation","volume":"118","author":"Luo","year":"2018","journal-title":"Chem. Rev."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1016\/j.molcel.2019.08.026","article-title":"Lysine Methylation Regulators Moonlighting Outside the Epigenome","volume":"75","author":"Cornett","year":"2019","journal-title":"Mol. Cell"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.jpha.2022.11.009","article-title":"Novel insights into histone lysine methyltransferases in cancer therapy: From epigenetic regulation to selective drugs","volume":"13","author":"Liao","year":"2023","journal-title":"J. Pharm. Anal."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Song, C., Kim, M.Y., and Cho, J.Y. (2024). The Role of Protein Methyltransferases in Immunity. Molecules, 29.","DOI":"10.3390\/molecules29020360"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Thiebaut, C., Eve, L., Poulard, C., and Le Romancer, M. (2021). Structure, Activity, and Function of PRMT1. Life, 11.","DOI":"10.3390\/life11111147"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1038\/s12276-021-00613-y","article-title":"Protein arginine methyltransferases: Promising targets for cancer therapy","volume":"53","author":"Hwang","year":"2021","journal-title":"Exp. Mol. Med."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2917","DOI":"10.1007\/s00018-019-03145-x","article-title":"Protein arginine methyltransferases: Insights into the enzyme structure and mechanism at the atomic level","volume":"76","author":"Tewary","year":"2019","journal-title":"Cell Mol. Life Sci."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/s13072-024-00530-0","article-title":"Intrafamily heterooligomerization as an emerging mechanism of methyltransferase regulation","volume":"17","author":"Hobble","year":"2024","journal-title":"Epigenet. Chromatin"},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Qualmann, B., and Kessels, M. (2021). The Role of Protein Arginine Methylation as Post-Translational Modification on Actin Cytoskeletal Components in Neuronal Structure and Function. Cells, 10.","DOI":"10.3390\/cells10051079"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"13665","DOI":"10.1021\/acs.jmedchem.3c01030","article-title":"Identification of a Protein Arginine Methyltransferase 7 (PRMT7)\/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor","volume":"66","author":"Feoli","year":"2023","journal-title":"J. Med. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Timm, D.E., Bowman, V., Madsen, R., and Rauch, C. (2018). Cryo-electron microscopy structure of a human PRMT5:MEP50 complex. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0193205"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.1038\/s41467-024-47107-9","article-title":"Loss-of-function mutation in PRMT9 causes abnormal synapse development by dysregulation of RNA alternative splicing","volume":"15","author":"Shen","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"107947","DOI":"10.1016\/j.jbc.2024.107947","article-title":"Oligomerization of protein arginine methyltransferase 1 and its functional impact on substrate arginine methylation","volume":"300","author":"Dang","year":"2024","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1038\/s41580-019-0155-x","article-title":"The regulation, functions and clinical relevance of arginine methylation","volume":"20","author":"Guccione","year":"2019","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"4357","DOI":"10.1016\/j.molcel.2021.09.011","article-title":"Cellular pathways influenced by protein arginine methylation: Implications for cancer","volume":"81","author":"Xu","year":"2021","journal-title":"Mol. Cell"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1753","DOI":"10.1002\/pro.2970","article-title":"Geometry of guanidinium groups in arginines","volume":"25","author":"Malinska","year":"2016","journal-title":"Protein Sci."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1038\/s42004-026-02075-7","article-title":"Molecular determinants of arginine versus lysine cation\u2013\u03c0 interactions in biomolecular condensates","volume":"9","author":"Armentia","year":"2026","journal-title":"Commun. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1186\/s40364-025-00860-5","article-title":"Arginine methylation in cancer: Mechanisms and therapeutic implications","volume":"13","author":"Xu","year":"2025","journal-title":"Biomark. Res."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1042\/BST20221147","article-title":"Effectors and effects of arginine methylation","volume":"51","author":"Wang","year":"2023","journal-title":"Biochem. Soc. Trans."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"15571","DOI":"10.1038\/ncomms15571","article-title":"Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition","volume":"8","author":"Shishkova","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Wang, X., Zhu, B., Winn, R., Lu, S., and Wang, H. (2025). Functional Dynamics of Arginine Mono- and Di-Methylation. Cells, 14.","DOI":"10.3390\/cells14110796"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"102971","DOI":"10.1016\/j.isci.2021.102971","article-title":"Independent transcriptomic and proteomic regulation by type I and II protein arginine methyltransferases","volume":"24","author":"Maron","year":"2021","journal-title":"iScience"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1139\/bcb-2023-0212","article-title":"Protein arginine methyltransferase 1, a major regulator of biological processes","volume":"102","author":"Sudhakar","year":"2024","journal-title":"Biochem. Cell Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.gene.2019.02.072","article-title":"Novel alternative splice variants of the human protein arginine methyltransferase 1 (PRMT1) gene, discovered using next-generation sequencing","volume":"699","author":"Adamopoulos","year":"2019","journal-title":"Gene"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.devcel.2018.03.007","article-title":"Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl","volume":"45","author":"Hou","year":"2018","journal-title":"Dev. Cell"},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Cura, V., and Cavarelli, J. (2021). Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase. Life, 11.","DOI":"10.3390\/life11111263"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1111\/febs.13953","article-title":"Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors","volume":"284","author":"Cura","year":"2017","journal-title":"FEBS J."},{"key":"ref_67","first-page":"17","article-title":"PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X","volume":"162","author":"Vhuiyan","year":"2017","journal-title":"J. Biochem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1038\/s41467-021-21873-2","article-title":"Protein context shapes the specificity of SH3 domain-mediated interactions in vivo","volume":"12","author":"Dionne","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"8693","DOI":"10.1038\/s41467-024-52945-8","article-title":"AtPRMT3-RPS2B promotes ribosome biogenesis and coordinates growth and cold adaptation trade-off","volume":"15","author":"Wang","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1038\/s42003-020-01644-3","article-title":"PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting retinoic acid signaling","volume":"4","author":"Verma","year":"2021","journal-title":"Commun. Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"216008","DOI":"10.1016\/j.canlet.2022.216008","article-title":"Protein arginine methyltransferase 3: A crucial regulator in metabolic reprogramming and gene expression in cancers","volume":"554","author":"Hsu","year":"2023","journal-title":"Cancer Lett."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1007\/s13402-024-00943-9","article-title":"The emerging role of CARM1 in cancer","volume":"47","author":"Xie","year":"2024","journal-title":"Cell Oncol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1161\/CIRCULATIONAHA.121.055738","article-title":"Epigenetic Regulation of Cardiomyocyte Maturation by Arginine Methyltransferase CARM1","volume":"149","author":"Garbutt","year":"2024","journal-title":"Circulation"},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Gupta, S., Kadumuri, R.V., Singh, A.K., Chavali, S., and Dhayalan, A. (2021). Structure, Activity and Function of the Protein Arginine Methyltransferase 6. Life, 11.","DOI":"10.3390\/life11090951"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Chen, Z., Gan, J., Wei, Z., Zhang, M., Du, Y., Xu, C., and Zhao, H. (2022). The Emerging Role of PRMT6 in Cancer. Front. Oncol., 12.","DOI":"10.3389\/fonc.2022.841381"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Dong, R., Li, X.J., and Lai, K.O. (2021). Activity and Function of the PRMT8 Protein Arginine Methyltransferase in Neurons. Life, 11.","DOI":"10.3390\/life11111132"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"2068","DOI":"10.1038\/s12276-026-01762-8","article-title":"Protein arginine methyltransferases coordinate mitochondrial stress adaptation and neuromuscular function","volume":"58","author":"Bae","year":"2026","journal-title":"Exp. Mol. Med."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"11106","DOI":"10.1093\/nar\/gkx727","article-title":"The PRMT5\/WDR77 complex regulates alternative splicing through ZNF326 in breast cancer","volume":"45","author":"Rengasamy","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"9674","DOI":"10.1074\/jbc.M115.636894","article-title":"Histone H2A and H4 N-Terminal Tails Are Positioned by the MEP50 WD Repeat Protein for Efficient Methylation by the PRMT5 Arginine Methyltransferase","volume":"290","author":"Burgos","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"4016","DOI":"10.1016\/j.molcel.2025.09.021","article-title":"Productive mRNA chromatin escape is promoted by PRMT5 activity","volume":"85","author":"DeAngelo","year":"2025","journal-title":"Mol. Cell"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"6428","DOI":"10.1038\/ncomms7428","article-title":"PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145","volume":"6","author":"Yang","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Halabelian, L., and Barsyte-Lovejoy, D. (2021). Structure and Function of Protein Arginine Methyltransferase PRMT7. Life, 11.","DOI":"10.3390\/life11080768"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"18299","DOI":"10.1074\/jbc.M116.740399","article-title":"Protein Arginine Methyltransferase Product Specificity Is Mediated by Distinct Active-Site Architectures","volume":"291","author":"Jain","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.abb.2019.02.014","article-title":"PRMT7 as a unique member of the protein arginine methyltransferase family: A review","volume":"665","author":"Jain","year":"2019","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12933-017-0656-x","article-title":"Asymmetric dimethylarginine (ADMA), symmetric dimethylarginine (SDMA) and homoarginine (hArg): The ADMA, SDMA and hArg paradoxes","volume":"17","author":"Tsikas","year":"2018","journal-title":"Cardiovasc. Diabetol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1186\/s12933-017-0569-8","article-title":"Symmetric and asymmetric dimethylarginine as risk markers of cardiovascular disease, all-cause mortality and deterioration in kidney function in persons with type 2 diabetes and microalbuminuria","volume":"16","author":"Zobel","year":"2017","journal-title":"Cardiovasc. Diabetol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1042\/CS20241021","article-title":"SDMA as a marker and mediator in cerebrovascular disease","volume":"138","author":"Riddell","year":"2024","journal-title":"Clin. Sci."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Oliva-Damaso, E., Oliva-Damaso, N., Rodriguez-Esparragon, F., Payan, J., Baamonde-Laborda, E., Gonzalez-Cabrera, F., Santana-Estupi\u00f1an, R., and Rodriguez-Perez, J.C. (2019). Asymmetric (ADMA) and Symmetric (SDMA) Dimethylarginines in Chronic Kidney Disease: A Clinical Approach. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20153668"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2361","DOI":"10.1016\/j.jacc.2022.11.005","article-title":"The Global Burden of Cardiovascular Diseases and Risk A Compass for Future Health","volume":"80","author":"Vaduganathan","year":"2022","journal-title":"J. Am. Coll. Cardiol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1264","DOI":"10.1016\/S0140-6736(25)00055-8","article-title":"The Lancet Commission on rethinking coronary artery disease: Moving from ischaemia to atheroma","volume":"405","author":"Zaman","year":"2025","journal-title":"Lancet"},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Severino, P., D\u2019Amato, A., Pucci, M., Infusino, F., Adamo, F., Birtolo, L.I., Netti, L., Montefusco, G., Chimenti, C., and Lavalle, C. (2020). Ischemic Heart Disease Pathophysiology Paradigms Overview: From Plaque Activation to Microvascular Dysfunction. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21218118"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1161\/CIRCULATIONAHA.124.070368","article-title":"Immunomodulatory Therapy for Ischemic Heart Disease","volume":"150","author":"Zhao","year":"2024","journal-title":"Circulation"},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Tang, H.Y., Chen, A.Q., Zhang, H., Gao, X.F., Kong, X.Q., and Zhang, J.J. (2022). Vascular Smooth Muscle Cells Phenotypic Switching in Cardiovascular Diseases. Cells, 11.","DOI":"10.3390\/cells11244060"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Chen, X., Zhou, Y., Yang, J., Xue, S., Wang, Q., Guo, X., Zhang, Y., and Niu, W. (2025). Research Status and Latest Progress in the Regulatory Mechanisms of ABCA1. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms262210855"},{"key":"ref_95","first-page":"e00376-00318","article-title":"Common and Differential Transcriptional Actions of Nuclear Receptors Liver X Receptors \u03b1 and \u03b2 in Macrophages","volume":"39","author":"Tabraue","year":"2019","journal-title":"Mol. Cell. Biol."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Bilotta, M.T., Petillo, S., Santoni, A., and Cippitelli, M. (2020). Liver X Receptors: Regulators of Cholesterol Metabolism, Inflammation, Autoimmunity, and Cancer. Front. Immunol., 11.","DOI":"10.3389\/fimmu.2020.584303"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.bbrc.2020.01.040","article-title":"PRMT2 inhibits the formation of foam cell induced by ox-LDL in RAW 264.7 macrophage involving ABCA1 mediated cholesterol efflux","volume":"524","author":"Li","year":"2020","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"12031","DOI":"10.1038\/s41598-022-15349-6","article-title":"Loss of PRMT2 in myeloid cells in normoglycemic mice phenocopies impaired regression of atherosclerosis in diabetic mice","volume":"12","author":"Vurusaner","year":"2022","journal-title":"Sci. Rep."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1716","DOI":"10.1007\/s12035-019-01850-z","article-title":"Protein Arginine Methyltransferases in Cardiovascular and Neuronal Function","volume":"57","author":"Wu","year":"2020","journal-title":"Mol. Neurobiol."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Hou, H., Meng, J., Chen, Y., Zhang, X., Yang, Z., Wang, Q., Zheng, M., and Jiang, Z. (2025). PRMT3 at the crossroads of inflammation: Dual roles in metabolic reprogramming and immune dysregulation in chronic diseases. Front. Immunol., 16.","DOI":"10.3389\/fimmu.2025.1663258"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"e001569","DOI":"10.1161\/CIRCGENETICS.116.001569","article-title":"Admixture Mapping of Subclinical Atherosclerosis and Subsequent Clinical Events Among African Americans in 2 Large Cohort Studies","volume":"10","author":"Shendre","year":"2017","journal-title":"Circ. Cardiovasc. Genet."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.1016\/j.bbadis.2019.02.012","article-title":"Inhibition of PRMT3 activity reduces hepatic steatosis without altering atherosclerosis susceptibility in apoE knockout mice","volume":"1865","author":"Hoekstra","year":"2019","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1038\/nrendo.2017.91","article-title":"SREBP-regulated lipid metabolism: Convergent physiology\u2014Divergent pathophysiology","volume":"13","author":"Shimano","year":"2017","journal-title":"Nat. Rev. Endocrinol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1158\/0008-5472.CAN-15-1766","article-title":"Arginine Methylation of SREBP1a via PRMT5 Promotes De Novo Lipogenesis and Tumor Growth","volume":"76","author":"Liu","year":"2016","journal-title":"Cancer Res."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"110529","DOI":"10.1016\/j.intimp.2023.110529","article-title":"PRMT5 knockdown enhances cell viability and suppresses cell apoptosis, oxidative stress, inflammation and endothelial dysfunction in ox-LDL-induced vascular endothelial cells via interacting with PDCD4","volume":"122","author":"Fei","year":"2023","journal-title":"Int. Immunopharmacol."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Wang, Q., and Yang, H.-S. (2024). The Impact of Pdcd4, a Translation Inhibitor, on Drug Resistance. Pharmaceuticals, 17.","DOI":"10.20944\/preprints202409.1669.v1"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"e2055","DOI":"10.1038\/cddis.2015.416","article-title":"Pdcd4 deficiency enhances macrophage lipoautophagy and attenuates foam cell formation and atherosclerosis in mice","volume":"7","author":"Wang","year":"2016","journal-title":"Cell Death Dis."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1038\/s41418-020-00646-2","article-title":"Programmed cell death 4 modulates lysosomal function by inhibiting TFEB translation","volume":"28","author":"Chen","year":"2021","journal-title":"Cell Death Differ."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"15328","DOI":"10.1074\/jbc.M114.547349","article-title":"Tumor necrosis factor (TNF)-\u03b1 induction of CXCL10 in endothelial cells requires protein arginine methyltransferase 5 (PRMT5)-mediated nuclear factor (NF)-\u03baB p65 methylation","volume":"289","author":"Harris","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Harris, D.P., Chandrasekharan, U.M., Bandyopadhyay, S., Willard, B., and DiCorleto, P.E. (2016). PRMT5-Mediated Methylation of NF-\u03baB p65 at Arg174 Is Required for Endothelial CXCL11 Gene Induction in Response to TNF-\u03b1 and IFN-\u03b3 Costimulation. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0148905"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1038\/s41419-022-04719-7","article-title":"PRMT5 critically mediates TMAO-induced inflammatory response in vascular smooth muscle cells","volume":"13","author":"Liu","year":"2022","journal-title":"Cell Death Dis."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"4028353","DOI":"10.1155\/2016\/4028353","article-title":"The Role of Protein Arginine Methyltransferases in Inflammatory Responses","volume":"2016","author":"Kim","year":"2016","journal-title":"Mediat. Inflamm."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"113562","DOI":"10.1016\/j.intimp.2024.113562","article-title":"Macrophages after myocardial infarction: Mechanisms for repairing and potential as therapeutic approaches","volume":"143","author":"Yang","year":"2024","journal-title":"Int. Immunopharmacol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"40531","DOI":"10.1038\/srep40531","article-title":"Protein arginine methyltransferase 1 (PRMT1) represses MHC II transcription in macrophages by methylating CIITA","volume":"7","author":"Fan","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"e32073","DOI":"10.1016\/j.heliyon.2024.e32073","article-title":"Macrophage polarisation and inflammatory mechanisms in atherosclerosis: Implications for prevention and treatment","volume":"10","author":"Yang","year":"2024","journal-title":"Heliyon"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1186\/s13072-025-00575-9","article-title":"Crosstalk between metabolism and epigenetics during macrophage polarization","volume":"18","author":"Zhang","year":"2025","journal-title":"Epigenet. Chromatin"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1161\/CIRCULATIONAHA.125.076101","article-title":"Macrophage PRMT9 Ameliorates Acute Myocardial Infarction by Promoting Symmetric Dimethylation and Degradation of STAT1","volume":"153","author":"Bai","year":"2026","journal-title":"Circulation"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1093\/eurheartj\/ehac647","article-title":"Vinculin phosphorylation impairs vascular endothelial junctions promoting atherosclerosis","volume":"44","author":"Shih","year":"2023","journal-title":"Eur. Heart J."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1161\/CIRCRESAHA.124.324773","article-title":"Kindlin-2 Phase Separation in Response to Flow Controls Vascular Stability","volume":"135","author":"Ma","year":"2024","journal-title":"Circ. Res."},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Quillien, A., Gilbert, G., Boulet, M., Ethuin, S., Waltzer, L., and Vandel, L. (2021). Prmt5 promotes vascular morphogenesis independently of its methyltransferase activity. PLoS Genet., 17.","DOI":"10.1371\/journal.pgen.1009641"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"e152481","DOI":"10.1172\/jci.insight.152481","article-title":"Endothelial PRMT5 plays a crucial role in angiogenesis after acute ischemic injury","volume":"7","author":"Ye","year":"2022","journal-title":"JCI Insight"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1358","DOI":"10.1091\/mbc.E15-10-0738","article-title":"Cross-talk between Arg methylation and Ser phosphorylation modulates apoptosis signal-regulating kinase 1 activation in endothelial cells","volume":"27","author":"Chen","year":"2016","journal-title":"Mol. Biol. Cell"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"104736","DOI":"10.1016\/j.isci.2022.104736","article-title":"PRMT4-mediated arginine methylation promotes tyrosine phosphorylation of VEGFR-2 and regulates filopodia protrusions","volume":"25","author":"Hartsough","year":"2022","journal-title":"iScience"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1038\/s12276-025-01517-x","article-title":"Endothelial PRMT7 prevents dysfunction, promotes revascularization and enhances cardiac recovery post-myocardial infarction","volume":"57","author":"Tran","year":"2025","journal-title":"Exp. Mol. Med."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"2244","DOI":"10.1093\/cvr\/cvad110","article-title":"Epigenetic regulation of vascular smooth muscle cell phenotypic switch and neointimal formation by PRMT5","volume":"119","author":"Zhu","year":"2023","journal-title":"Cardiovasc. Res."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"2142","DOI":"10.1093\/cvr\/cvad080","article-title":"Protein arginine methyltransferase 5-mediated arginine methylation stabilizes Kruppel-like factor 4 to accelerate neointimal formation","volume":"119","author":"Liu","year":"2023","journal-title":"Cardiovasc. Res."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/j.bbrc.2019.10.085","article-title":"PRMT4 overexpression aggravates cardiac remodeling following myocardial infarction by promoting cardiomyocyte apoptosis","volume":"520","author":"Wang","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1038\/s41418-019-0373-y","article-title":"Prmt7 promotes myoblast differentiation via methylation of p38MAPK on arginine residue 70","volume":"27","author":"Jeong","year":"2020","journal-title":"Cell Death Differ."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"110412","DOI":"10.1016\/j.cellsig.2022.110412","article-title":"PRMT1 suppresses doxorubicin-induced cardiotoxicity by inhibiting endoplasmic reticulum stress","volume":"98","author":"Kim","year":"2022","journal-title":"Cell. Signal."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"1840","DOI":"10.1016\/j.apsb.2021.10.016","article-title":"Prmt1 upregulated by Hdc deficiency aggravates acute myocardial infarction via NETosis","volume":"12","author":"Zhang","year":"2022","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Nemtsova, V., Vischer, A.S., and Burkard, T. (2023). Hypertensive Heart Disease: A Narrative Review Series\u2014Part 1: Pathophysiology and Microstructural Changes. J. Clin. Med., 12.","DOI":"10.3390\/jcm12072606"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1038\/s41569-018-0007-y","article-title":"Mechanisms of physiological and pathological cardiac hypertrophy","volume":"15","author":"Nakamura","year":"2018","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"93","DOI":"10.31083\/j.rcm2503093","article-title":"Hypertensive Heart Disease: Mechanisms, Diagnosis and Treatment","volume":"25","author":"Huang","year":"2024","journal-title":"Rev. Cardiovasc. Med."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s00395-018-0688-8","article-title":"Physiological and unappreciated roles of CaMKII in the heart","volume":"113","author":"Beckendorf","year":"2018","journal-title":"Basic Res. Cardiol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"5107","DOI":"10.1038\/s41467-018-07606-y","article-title":"Cardiac specific PRMT1 ablation causes heart failure through CaMKII dysregulation","volume":"9","author":"Pyun","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.3724\/abbs.2024175","article-title":"PRMT1 alleviates isoprenaline-induced myocardial hypertrophy by methylating SRSF1","volume":"57","author":"Yan","year":"2024","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.ijcard.2019.01.102","article-title":"The inhibitory subunit of cardiac troponin (cTnI) is modified by arginine methylation in the human heart","volume":"282","author":"Onwuli","year":"2019","journal-title":"Int. J. Cardiol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1016\/j.hrthm.2024.02.034","article-title":"Tropomyosin-troponin complex in inherited cardiomyopathies","volume":"21","author":"Sequeira","year":"2024","journal-title":"Heart Rhythm"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Paar, V., Haslinger, M., Krombholz-Reindl, P., Pittner, S., Neuner, M., Jirak, P., Kolbitsch, T., Minnich, B., Schr\u00f6dl, F., and Kaser-Eichberger, A. (2023). Hypertrophic cardiomyopathy is characterized by alterations of the mitochondrial calcium uniporter complex proteins: Insights from patients with aortic valve stenosis versus hypertrophic obstructive cardiomyopathy. Front. Pharmacol., 14.","DOI":"10.3389\/fphar.2023.1264216"},{"key":"ref_140","doi-asserted-by":"crossref","unstructured":"Cai, S.D., Liu, R., Wang, P.X., Li, J.Y., Xie, T.T., Wang, M.H., Cao, Y.J., Li, Z.M., and Liu, P.Q. (2020). PRMT5 Prevents Cardiomyocyte Hypertrophy via Symmetric Dimethylating HoxA9 and Repressing HoxA9 Expression. Front. Pharmacol., 11.","DOI":"10.3389\/fphar.2020.600627"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"105104","DOI":"10.1016\/j.phrs.2020.105104","article-title":"Histone H4R3 symmetric di-methylation by Prmt5 protects against cardiac hypertrophy via regulation of Filip1L\/\u03b2-catenin","volume":"161","author":"Cai","year":"2020","journal-title":"Pharmacol. Res."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"107553","DOI":"10.1016\/j.ypmed.2023.107553","article-title":"PRMT5 up-regulation improves myocardial hypertrophy by mediating E2F-1\/NF-\u03baB\/NLRP3 pathway","volume":"172","author":"Zhang","year":"2023","journal-title":"Prev. Med."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Motolani, A., Martin, M., Sun, M., and Lu, T. (2021). The Structure and Functions of PRMT5 in Human Diseases. Life, 11.","DOI":"10.3390\/life11101074"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.carpath.2017.07.003","article-title":"Increased \u03b2-catenin accumulation and nuclear translocation are associated with concentric hypertrophy in cardiomyocytes","volume":"31","author":"Lee","year":"2017","journal-title":"Cardiovasc. Pathol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1016\/j.jacbts.2023.05.008","article-title":"TAK1 Activation by NLRP3 Deficiency Confers Cardioprotection Against Pressure Overload-Induced Cardiomyocyte Pyroptosis and Hypertrophy","volume":"8","author":"Li","year":"2023","journal-title":"JACC Basic Transl. Sci."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"2472","DOI":"10.1038\/s41467-024-46711-z","article-title":"Fibroblast-specific PRMT5 deficiency suppresses cardiac fibrosis and left ventricular dysfunction in male mice","volume":"15","author":"Katanasaka","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1161\/CIRCRESAHA.117.305349","article-title":"Cardiac Nonmyocytes in the Hub of Cardiac Hypertrophy","volume":"117","author":"Kamo","year":"2015","journal-title":"Circ. Res."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"e03864","DOI":"10.1016\/j.heliyon.2020.e03864","article-title":"Protein arginine methyltransferase 6 mediates cardiac hypertrophy by differential regulation of histone H3 arginine methylation","volume":"6","author":"Raveendran","year":"2020","journal-title":"Heliyon"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"3339","DOI":"10.1016\/j.celrep.2018.08.052","article-title":"Genomic Location of PRMT6-Dependent H3R2 Methylation Is Linked to the Transcriptional Outcome of Associated Genes","volume":"24","author":"Bouchard","year":"2018","journal-title":"Cell Rep."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/s00018-021-04097-x","article-title":"PRMT7 ablation in cardiomyocytes causes cardiac hypertrophy and fibrosis through \u03b2-catenin dysregulation","volume":"79","author":"Ahn","year":"2022","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Qian, J., Jackson-Weaver, O., Shen, Y., Jin, J., Chen, Y., Li, M., Subramanyan, R.K., and Xu, J. (2024). Inactivation of PRMT1 inhibits cardiac fibrosis via transcriptional regulation and perturbation of FBL activity in fibroblast-to-myofibroblast transition. bioRxiv.","DOI":"10.1101\/2024.05.24.595777"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"e71174","DOI":"10.1111\/jcmm.71174","article-title":"Matrifibrocytes Redefine Cardiac Fibrosis: From Terminal Differentiation to Translational Modulation","volume":"30","author":"Zhang","year":"2026","journal-title":"J. Cell. Mol. Med."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1186\/s12964-020-00555-4","article-title":"TGF-\u03b2 and WNT signaling pathways in cardiac fibrosis: Non-coding RNAs come into focus","volume":"18","author":"Yousefi","year":"2020","journal-title":"Cell Commun. Signal."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1982","DOI":"10.1038\/s41418-022-00990-5","article-title":"PRMT4 promotes ferroptosis to aggravate doxorubicin-induced cardiomyopathy via inhibition of the Nrf2\/GPX4 pathway","volume":"29","author":"Wang","year":"2022","journal-title":"Cell Death Differ."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/j.isci.2018.09.023","article-title":"PRMT1 Deficiency in Mouse Juvenile Heart Induces Dilated Cardiomyopathy and Reveals Cryptic Alternative Splicing Products","volume":"8","author":"Murata","year":"2018","journal-title":"iScience"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.coph.2020.08.005","article-title":"Role of O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins in diabetic cardiovascular complications","volume":"57","author":"Chatham","year":"2021","journal-title":"Curr. Opin. Pharmacol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1161\/CIRCRESAHA.121.319456","article-title":"PRMT5 Prevents Dilated Cardiomyopathy via Suppression of Protein O-GlcNAcylation","volume":"129","author":"Li","year":"2021","journal-title":"Circ. Res."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1083\/jcb.201406020","article-title":"GSK3- and PRMT-1-dependent modifications of desmoplakin control desmoplakin-cytoskeleton dynamics","volume":"208","author":"Albrecht","year":"2015","journal-title":"J. Cell Biol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"12720","DOI":"10.1038\/s41598-023-37874-8","article-title":"PP2A-B55alpha controls keratinocyte adhesion through dephosphorylation of the Desmoplakin C-terminus","volume":"13","author":"Perl","year":"2023","journal-title":"Sci. Rep."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1038\/s41401-022-00963-x","article-title":"Adriamycin induces cardiac fibrosis in mice via PRMT5-mediated cardiac fibroblast activation","volume":"44","author":"Dong","year":"2023","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1038\/s12276-024-01193-3","article-title":"Prmt7 regulates the JAK\/STAT\/Socs3 signaling pathway in postmenopausal cardiomyopathy","volume":"56","author":"Ahn","year":"2024","journal-title":"Exp. Mol. Med."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"20220164","DOI":"10.1098\/rstb.2022.0164","article-title":"SCN5A channelopathy: Arrhythmia, cardiomyopathy, epilepsy and beyond","volume":"378","author":"Remme","year":"2023","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"3069","DOI":"10.1002\/jcp.30775","article-title":"Modulation of I(Ks) channel-PIP(2) interaction by PRMT1 plays a critical role in the control of cardiac repolarization","volume":"237","author":"An","year":"2022","journal-title":"J. Cell. Physiol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1735","DOI":"10.1016\/j.drudis.2020.06.031","article-title":"Modulating the modulators: Regulation of protein arginine methyltransferases by post-translational modifications","volume":"25","author":"Hartley","year":"2020","journal-title":"Drug Discov. Today"},{"key":"ref_165","doi-asserted-by":"crossref","unstructured":"Dong, C., Wang, Y., Ma, A., and Wang, T. (2020). Life Cycle of the Cardiac Voltage-Gated Sodium Channel NaV1.5. Front. Physiol., 11.","DOI":"10.3389\/fphys.2020.609733"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"1569","DOI":"10.1038\/s12276-021-00684-x","article-title":"Inducible Prmt1 ablation in adult vascular smooth muscle leads to contractile dysfunction and aortic dissection","volume":"53","author":"Pyun","year":"2021","journal-title":"Exp. Mol. Med."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/16\/9\/1365\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T09:58:36Z","timestamp":1789984716000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/16\/9\/1365"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,19]]},"references-count":166,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2026,9]]}},"alternative-id":["biom16091365"],"URL":"https:\/\/doi.org\/10.3390\/biom16091365","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,19]]}}}