PRMT1 in Health and Disease: Emerging Perspectives From Molecular Mechanisms to Therapeutic Strategies

Yanqun Luo , Ying Gao , Xiaoliang Deng , Lei Wang , Tao Wu

MedComm ›› 2025, Vol. 6 ›› Issue (12) : e70482

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MedComm ›› 2025, Vol. 6 ›› Issue (12) :e70482 DOI: 10.1002/mco2.70482
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PRMT1 in Health and Disease: Emerging Perspectives From Molecular Mechanisms to Therapeutic Strategies
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Abstract

Protein arginine methyltransferase 1 (PRMT1) serves as a critical epigenetic modulator involved in a wide range of physiological and pathological processes. Previous studies have established its fundamental roles in essential cellular mechanisms such as DNA repair, transcriptional regulation, and signal transduction. Dysregulation of PRMT1 has been further associated with the pathogenesis of various diseases, including cancer, metabolic disorders, and immune dysfunction. However, a systematic synthesis of the multifaceted functions of PRMT1 across these diverse pathological contexts remains lacking. This review seeks to address this gap by comprehensively examining the molecular mechanisms, biological functions, and context-dependent roles of PRMT1. We integrate recent advances spanning multiple disease domains, with a particular focus on cancer, chronic liver diseases, cardiovascular disorders, neurodegenerative conditions, and immune-related pathologies. In addition, we elucidate the mechanistic links between PRMT1 dysregulation and disease pathogenesis. Further, the development and clinical potential of small-molecule inhibitors are also summarized. This review offers new perspectives on PRMT1-related disease mechanisms and lays a theoretical foundation for the development of targeted therapies. Ultimately, this review aims to contribute to the progression of precision medicine and the enhancement of global health outcomes.

Keywords

cancer / chronic liver diseases / cardiovascular diseases / inhibitor / protein arginine methyltransferase 1

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Yanqun Luo, Ying Gao, Xiaoliang Deng, Lei Wang, Tao Wu. PRMT1 in Health and Disease: Emerging Perspectives From Molecular Mechanisms to Therapeutic Strategies. MedComm, 2025, 6(12): e70482 DOI:10.1002/mco2.70482

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References

[1]

J. M. Lee, H. M. Hammarén, M. M. Savitski, and S. H. Baek, “Control of Protein Stability by Post-Translational Modifications,” Nature Communications 14, no. 1 (2023): 201.

[2]

J. Xu and S. Richard, “Cellular Pathways Influenced by Protein Arginine Methylation: Implications for Cancer,” Molecular Cell 81, no. 21 (2021): 4357–4368.

[3]

C. Thiebaut, L. Eve, C. Poulard, and M. Le Romancer, “Structure, Activity, and Function of PRMT1,” Life (Basel) 11, no. 11 (2021): 1147.

[4]

W. J. Lin, J. D. Gary, M. C. Yang, S. Clarke, and H. R. Herschman, “The Mammalian Immediate-Early TIS21 Protein and the Leukemia-Associated BTG1 Protein Interact With a Protein-Arginine N-Methyltransferase,” The Journal of Biological Chemistry 271, no. 25 (1996): 15034–15044.

[5]

H. Liu, J. Jiang, and L. Zhao, “Protein Arginine Methyltransferase-1 Deficiency Restrains Depression-Like Behavior of Mice by Inhibiting Inflammation and Oxidative Stress via Nrf-2,” Biochemical and Biophysical Research Communications 518, no. 3 (2019): 430–437.

[6]

J. W. Hwang, Y. Cho, G. U. Bae, S. N. Kim, and Y. K. Kim, “Protein Arginine Methyltransferases: Promising Targets for Cancer Therapy,” Experimental & Molecular Medicine 53, no. 5 (2021): 788–808.

[7]

I. Goulet, G. Gauvin, S. Boisvenue, and J. Côté, “Alternative Splicing Yields Protein Arginine Methyltransferase 1 Isoforms With Distinct Activity, Substrate Specificity, and Subcellular Localization,” The Journal of Biological Chemistry 282, no. 45 (2007): 33009–33021.

[8]

J. Fuhrmann and P. R. Thompson, “Protein Arginine Methylation and Citrullination in Epigenetic Regulation,” American Chemical Society Chemical Biology 11, no. 3 (2016): 654–668.

[9]

H. Wang, Z. Q. Huang, L. Xia, et al., “Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone Receptor,” Science 293, no. 5531 (2001): 853–857.

[10]

S. R. N. Sudhakar, S. N. Khan, A. Clark, et al., “Protein Arginine Methyltransferase 1, a Major Regulator of Biological Processes,” Biochemistry and Cell Biology 102, no. 2 (2024): 106–126.

[11]

Z. Li, D. Wang, J. Lu, et al., “Methylation of EZH2 by PRMT1 Regulates its Stability and Promotes Breast Cancer Metastasis,” Cell Death and Differentiation 27, no. 12 (2020): 3226–3242.

[12]

L. Peng, Y. Zhao, J. Tan, et al., “PRMT1 Promotes Warburg effect by Regulating the PKM2/PKM1 ratio in Non-Small Cell Lung Cancer,” Cell Death & Disease 15, no. 7 (2024): 504.

[13]

B. Yao, T. Gui, X. Zeng, et al., “PRMT1-Mediated H4R3me2a Recruits SMARCA4 to Promote Colorectal Cancer Progression by Enhancing EGFR Signaling,” Genome Medicine 13, no. 1 (2021): 58.

[14]

S. Tang, V. Sethunath, N. Y. Metaferia, et al., “A Genome-Scale CRISPR Screen Reveals PRMT1 as a Critical Regulator of Androgen Receptor Signaling in Prostate Cancer,” Cell Reports 38, no. 8 (2022): 110417.

[15]

M. Zhou, Y. Huang, P. Xu, et al., “PRMT1 Promotes the Self-Renewal of Leukemia Stem Cells by Regulating Protein Synthesis,” Advanced Science (Weinh) 12, no. 5 (2025): e2308586.

[16]

R. H. Böger, S. M. Bode-Böger, A. Szuba, et al., “Asymmetric Dimethylarginine (ADMA): A Novel Risk Factor for Endothelial Dysfunction: Its Role in Hypercholesterolemia,” Circulation 98, no. 18 (1998): 1842–1847.

[17]

L. Xu, Z. Huang, T. H. Lo, et al., “Hepatic PRMT1 Ameliorates Diet-Induced Hepatic Steatosis Via Induction of PGC1α,” Theranostics 12, no. 6 (2022): 2502–2518.

[18]

J. H. Nho, M. J. Park, H. J. Park, et al., “Protein Arginine Methyltransferase-1 Stimulates Dopaminergic Neuronal Cell Death in a Parkinson's Disease Model,” Biochemical and Biophysical Research Communications 530, no. 2 (2020): 389–395.

[19]

Q. Sun, L. Liu, H. Wang, et al., “Constitutive High Expression of Protein Arginine Methyltransferase 1 in Asthmatic Airway Smooth Muscle Cells is Caused by Reduced microRNA-19a Expression and Leads to Enhanced Remodeling,” Journal of Allergy and Clinical Immunology 140, no. 2 (2017): 510–524.e3.

[20]

J. Jin, J. Yao, M. Wang, et al., “Preliminary Efficacy Results From an Ongoing Phase I/II Trial of CTS2190, a PRMT1 Inhibitor, in Patients With Advanced/Metastatic Solid Tumors,” Journal of Clinical Oncology 43 (2025): 3082.

[21]

A. Scorilas, M. H. Black, M. Talieri, and E. P. Diamandis, “Genomic Organization, Physical Mapping, and Expression Analysis of the Human Protein Arginine Methyltransferase 1 Gene,” Biochemical and Biophysical Research Communications 278, no. 2 (2000): 349–359.

[22]

X. Zhang and X. Cheng, “Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of its Binding to Substrate Peptides,” Structure (London, England) 11, no. 5 (2003): 509–520.

[23]

R. S. Blanc and S. Richard, “Arginine Methylation: The Coming of Age,” Molecular Cell 65, no. 1 (2017): 8–24.

[24]

J. Kargul, I. Irminger-Finger, and G. J. Laurent, “RNA Splicing: An Ingenious Gene Self Editing Tool,” The International Journal of Biochemistry & Cell Biology 91, no. Pt B (2017): 81.

[25]

R. K. Bradley and O. Anczuków, “RNA Splicing Dysregulation and the Hallmarks of Cancer,” Nature Reviews Cancer 23, no. 3 (2023): 135–155.

[26]

E. Fisher and J. Feng, “RNA Splicing Regulators Play Critical Roles in Neurogenesis,” Wiley Interdisciplinary Reviews RNA 13, no. 6 (2022): e1728.

[27]

J. Y. Fong, L. Pignata, P. A. Goy, et al., “Therapeutic Targeting of RNA Splicing Catalysis Through Inhibition of Protein Arginine Methylation,” Cancer Cell 36, no. 2 (2019): 194–209.e9.

[28]

W. J. Li, Y. Huang, Y. A. Lin, et al., “Targeting PRMT1-Mediated SRSF1 Methylation to Suppress Oncogenic Exon Inclusion Events and Breast Tumorigenesis,” Cell Reports 42, no. 11 (2023): 113385.

[29]

R. Sinha, E. Allemand, Z. Zhang, R. Karni, M. P. Myers, and A. R. Krainer, “Arginine Methylation Controls the Subcellular Localization and Functions of the Oncoprotein Splicing Factor SF2/ASF,” Molecular and Cellular Biology 30, no. 11 (2010): 2762–2774.

[30]

D. E. J. Williams, K. King, R. Jackson, et al., “PRMT1 Modulates Alternative Splicing to Enhance HPV18 mRNA Stability and Promote the Establishment of Infection,” BioRxiv (2024).

[31]

S. P. Jackson and J. Bartek, “The DNA-Damage Response in Human Biology and Disease,” Nature 461, no. 7267 (2009): 1071–1078.

[32]

F. Zhao, W. Kim, J. A. Kloeber, and Z. Lou, “DNA end Resection and its Role in DNA Replication and DSB Repair Choice in Mammalian Cells,” Experimental & Molecular Medicine 52, no. 10 (2020): 1705–1714.

[33]

Z. Yu, G. Vogel, Y. Coulombe, et al., “The MRE11 GAR Motif Regulates DNA Double-Strand Break Processing and ATR Activation,” Cell Research 22, no. 2 (2012): 305–320.

[34]

F. M. Boisvert, U. Déry, J. Y. Masson, and S. Richard, “Arginine Methylation of MRE11 by PRMT1 is Required for DNA Damage Checkpoint Control,” Genes & Development 19, no. 6 (2005): 671–676.

[35]

W. D. Wright, S. S. Shah, and W. D. Heyer, “Homologous Recombination and the Repair of DNA Double-Strand Breaks,” Journal of Biological Chemistry 293, no. 27 (2018): 10524–10535.

[36]

S. Yin, L. Liu, and W. Gan, “PRMT1 and PRMT5: On the Road of Homologous Recombination and Non-Homologous end Joining,” Genome Instability Disorders 4, no. 4 (2023): 197–209.

[37]

R. Scully, A. Panday, R. Elango, and N. A. Willis, “DNA Double-Strand Break Repair-Pathway Choice in Somatic Mammalian Cells,” Nature Reviews Molecular Cell Biology 20, no. 11 (2019): 698–714.

[38]

F. M. Boisvert, A. Rhie, S. Richard, and A. J. Doherty, “The GAR Motif of 53BP1 is Arginine Methylated by PRMT1 and is Necessary for 53BP1 DNA Binding Activity,” Cell Cycle 4, no. 12 (2005): 1834–1841.

[39]

Y. Zhang, Q. Zhang, L. Li, et al., “Arginine Methylation of APE1 Promotes its Mitochondrial Translocation to Protect Cells From Oxidative Damage,” Free Radical Biology and Medicine 158 (2020): 60–73.

[40]

B. Cha, W. Kim, Y. K. Kim, et al., “Methylation by Protein Arginine Methyltransferase 1 Increases Stability of Axin, a Negative Regulator of Wnt Signaling,” Oncogene 30, no. 20 (2011): 2379–2389.

[41]

J. Sakamaki, H. Daitoku, K. Ueno, A. Hagiwara, K. Yamagata, and A. Fukamizu, “Arginine Methylation of BCL-2 Antagonist of Cell Death (BAD) Counteracts its Phosphorylation and Inactivation by Akt,” Proceedings of the National Academy of Sciences of the United States of America 108, no. 15 (2011): 6085–6090.

[42]

T. Zhang, J. Wu, N. Ungvijanpunya, et al., “Smad6 Methylation Represses NFκB Activation and Periodontal Inflammation,” Journal of Dental Research 97, no. 7 (2018): 810–819.

[43]

L. V. Albrecht, D. Ploper, N. Tejeda-Muñoz, and E. M. De Robertis, “Arginine Methylation is Required for Canonical Wnt Signaling and Endolysosomal Trafficking,” Proceedings of the National Academy of Sciences of the United States of America 115, no. 23 (2018): E5317–E5325.

[44]

M. Le Romancer, I. Treilleux, N. Leconte, et al., “Regulation of Estrogen Rapid Signaling Through Arginine Methylation by PRMT1,” Molecular Cell 31, no. 2 (2008): 212–221.

[45]

M. Y. Liu, W. K. Hua, C. J. Chen, and W. J. Lin, “The MKK-Dependent Phosphorylation of p38α Is Augmented by Arginine Methylation on Arg49/Arg149 During Erythroid Differentiation,” International Journal of Molecular Sciences 21, no. 10 (2020): 3546.

[46]

A. Reintjes, J. E. Fuchs, L. Kremser, et al., “Asymmetric Arginine Dimethylation of RelA Provides a Repressive Mark to Modulate TNFα/NF-κB Response,” PNAS 113, no. 16 (2016): 4326–4331.

[47]

Y. Zhu, L. Wang, and R. Liu, “Inhibition of PRMT1 Alleviates Sepsis-Induced Acute Kidney Injury in Mice by Blocking the TGF-β1 and IL-6 Trans-Signaling Pathways,” FEBS Open Bio 13, no. 10 (2023): 1859–1873.

[48]

J. Liu, X. Bu, C. Chu, et al., “PRMT1 Mediated Methylation of cGAS Suppresses Anti-Tumor Immunity,” Nature Communications 14, no. 1 (2023): 2806.

[49]

L. Xue, L. Bao, J. Roediger, Y. Su, B. Shi, and Y. B. Shi, “Protein Arginine Methyltransferase 1 Regulates Cell Proliferation and Differentiation in Adult Mouse Adult Intestine,” Cell & Bioscience 11, no. 1 (2021): 113.

[50]

S. Infantino, A. Light, K. O'Donnell, et al., “Arginine Methylation Catalyzed by PRMT1 is Required for B Cell Activation and Differentiation,” Nature Communications 8, no. 1 (2017): 891.

[51]

R. S. Blanc, G. Vogel, X. Li, Z. Yu, S. Li, and S. Richard, “Arginine Methylation by PRMT1 Regulates Muscle Stem Cell Fate,” Molecular and Cellular Biology 37, no. 3 (2017): e00457 16.

[52]

X. Zhao, Z. Chong, Y. Chen, X. L. Zheng, Q. F. Wang, and Y. Li, “Protein Arginine Methyltransferase 1 in the Generation of Immune Megakaryocytes: A Perspective Review,” Journal of Biological Chemistry 298, no. 11 (2022): 102517.

[53]

M. Y. Liu, W. K. Hua, Y. Y. Chiou, et al., “Calcium-Dependent Methylation by PRMT1 Promotes Erythroid Differentiation Through the p38α MAPK Pathway,” FEBS Letters 594, no. 2 (2020): 301–316.

[54]

S. Sen, Z. He, S. Ghosh, et al., “PRMT1 Plays a Critical Role in Th17 Differentiation by Regulating Reciprocal Recruitment of STAT3 and STAT5,” Journal of Immunology (Baltimore, Md: 1950) 201, no. 2 (2018): 440–450.

[55]

E. Dolezal, S. Infantino, F. Drepper, et al., “The BTG2-PRMT1 Module Limits Pre-B Cell Expansion by Regulating the CDK4-Cyclin-D3 Complex,” Nature Immunology 18, no. 8 (2017): 911–920.

[56]

A. Plotnikov, N. Kozer, G. Cohen, et al., “PRMT1 Inhibition Induces Differentiation of Colon Cancer Cells,” Scientific Reports 10, no. 1 (2020): 20030.

[57]

F. Wang, S. Chen, S. Peng, et al., “PRMT1 Promotes the Proliferation and Metastasis of Gastric Cancer Cells by Recruiting MLXIP for the Transcriptional Activation of the β-Catenin Pathway,” Genes & Diseases 10, no. 6 (2023): 2622–2638.

[58]

H. Tao, C. Jin, L. Zhou, et al., “PRMT1 Inhibition Activates the Interferon Pathway to Potentiate Antitumor Immunity and Enhance Checkpoint Blockade Efficacy in Melanoma,” Cancer Research 84, no. 3 (2024): 419–433.

[59]

B. Yao, T. Gui, X. Zeng, et al., “Correction to: PRMT1-Mediated H4R3me2a Recruits SMARCA4 to Promote Colorectal Cancer Progression by Enhancing EGFR Signaling,” Genome Medicine 13, no. 1 (2021): 154.

[60]

Q. Cao, W. Xu, X. Chen, G. Luo, P. S. Reinach, and D. Yan, “PRMT1-Mediated Arginine Methylation Promotes Corneal Epithelial Wound Healing via Epigenetic Regulation of ANXA3,” Investigative Ophthalmology & Visual Science 66, no. 1 (2025): 22.

[61]

S. Liu, W. Zhang, W. Liu, et al., “PRMT1-Mediated SWI/SNF Complex Recruitment via SMARCC1 Drives IGF2BP2 Transcription to Enhance Carboplatin Resistance in Head and Neck Squamous Cell Carcinoma,” Advanced Science (Weinh) 12, no. 22 (2025): e2417460.

[62]

Y. Zhang, D. Wang, M. Zhang, et al., “Protein Arginine Methyltransferase 1 Coordinates the Epithelial-Mesenchymal Transition/Proliferation Dichotomy in Gastric Cancer Cells,” Experimental Cell Research 362, no. 1 (2018): 43–50.

[63]

D. de Korte and M. Hoekstra, “Protein Arginine Methyltransferase 1: A Multi-Purpose Player in the Development of Cancer and Metabolic Disease,” Biomolecules 15, no. 2 (2025): 185.

[64]

T. H. Beacon, G. P. Delcuve, C. López, et al., “The Dynamic Broad Epigenetic (H3K4me3, H3K27ac) Domain as a Mark of Essential Genes,” Clin Epigenetics 13, no. 1 (2021): 138.

[65]

S. Zheng, J. Moehlenbrink, Y. C. Lu, et al., “Arginine Methylation-Dependent Reader-Writer Interplay Governs Growth Control by E2F-1,” Molecular Cell 52, no. 1 (2013): 37–51.

[66]

J. Wang, Z. Wang, H. Inuzuka, W. Wei, and J. Liu, “PRMT1 Methylates METTL14 to Modulate its Oncogenic Function,” Neoplasia 42 (2023): 100912.

[67]

M. Yang, Y. Zhang, G. Liu, et al., “TIPE1 Inhibits Osteosarcoma Tumorigenesis and Progression by Regulating PRMT1 Mediated STAT3 Arginine Methylation,” Cell Death & Disease 13, no. 9 (2022): 815.

[68]

W. J. Li, Y. C. Chen, Y. A. Lin, et al., “Hypoxia-Induced PRMT1 Methylates HIF2β to Promote Breast Tumorigenesis Via Enhancing Glycolytic Gene Transcription,” Cell Reports 44, no. 4 (2025): 115487.

[69]

X. He, Y. Zhu, Y. C. Lin, et al., “PRMT1-Mediated FLT3 Arginine Methylation Promotes Maintenance of FLT3-ITD(+) Acute Myeloid Leukemia,” Blood 134, no. 6 (2019): 548–560.

[70]

J. Ling, S. Wang, C. Yi, et al., “PRMT1-Mediated Modification of H4R3me2a Promotes Liver Cancer Progression by Enhancing the Transcriptional Activity of SOX18,” Hepatology Communications 9, no. 4 (2025): e0647.

[71]

L. Li, J. Cui, X. Li, Y. Zhu, H. Wu, and L. Zhou, “Prmt1-Mediated Histone H4R3me2a Methylation Regulates the Proliferation, Migration and Invasion of Laryngeal Cancer Cells by Affecting the Expression Level of NCOA5,” Frontiers in Oncology 14 (2024): 1489164.

[72]

H. Liu, X. Chen, P. Wang, et al., “PRMT1-Mediated PGK1 Arginine Methylation Promotes Colorectal Cancer Glycolysis and Tumorigenesis,” Cell Death & Disease 15, no. 2 (2024): 170.

[73]

Z. Li, D. Wang, W. Wang, et al., “Macrophages-Stimulated PRMT1-Mediated EZH2 Methylation Promotes Breast Cancer Metastasis,” Biochemical and Biophysical Research Communications 533, no. 4 (2020): 679–684.

[74]

Z. Li, D. Wang, X. Chen, et al., “PRMT1-Mediated EZH2 Methylation Promotes Breast Cancer Cell Proliferation and Tumorigenesis,” Cell Death & Disease 12, no. 11 (2021): 1080.

[75]

L. M. Liu, W. Z. Sun, X. Z. Fan, Y. L. Xu, M. B. Cheng, and Y. Zhang, “Methylation of C/EBPα by PRMT1 Inhibits Its Tumor-Suppressive Function in Breast Cancer,” Cancer Research 79, no. 11 (2019): 2865–2877.

[76]

T. Hussain, S. Awasthi, F. Shahid, S. S. Yi, N. Sahni, and C. M. Aldaz, “Therapeutic Potential of PRMT1 as a Critical Survival Dependency Target in Multiple Myeloma,” BioRxiv (2025).

[77]

A. Scoumanne and X. Chen, “Protein Methylation: A New Mechanism of p53 Tumor Suppressor Regulation,” Histology and Histopathology 23, no. 9 (2008): 1143–1149.

[78]

L. M. Liu, Q. Tang, X. Hu, et al., “Arginine Methyltransferase PRMT1 Regulates p53 Activity in Breast Cancer,” Life (Basel) 11, no. 8 (2021): 789.

[79]

Y. Zhang, L. Mao, A. Jiang, et al., “PRMT1 Mediates the Proliferation of Y79 Retinoblastoma Cells by Regulating the p53/p21/CDC2/Cyclin B Pathway,” Experimental Eye Research 247 (2024): 110040.

[80]

Y. J. Lee, W. W. Chang, C. P. Chang, et al., “Downregulation of PRMT1 Promotes the Senescence and Migration of a Non-MYCN Amplified Neuroblastoma SK-N-SH Cells,” Scientific Reports 9, no. 1 (2019): 1771.

[81]

F. M. Boisvert, M. J. Hendzel, J. Y. Masson, and S. Richard, “Methylation of MRE11 Regulates its Nuclear Compartmentalization,” Cell Cycle 4, no. 7 (2005): 981–989.

[82]

J. Walton, A. S. N. Ng, K. Arevalo, et al., “PRMT1 Inhibition Perturbs RNA Metabolism and Induces DNA Damage in Clear Cell Renal Cell Carcinoma,” Nature Communications 15, no. 1 (2024): 8232.

[83]

V. Giuliani, M. A. Miller, C. Y. Liu, et al., “PRMT1-Dependent Regulation of RNA Metabolism and DNA Damage Response Sustains Pancreatic Ductal Adenocarcinoma,” Nature Communications 12, no. 1 (2021): 4626.

[84]

Z. Wang, X. Zhang, Y. Zhou, et al., “Energy Deficiency-Induced ATG4B Nuclear Translocation Inhibits PRMT1-Mediated DNA Repair and Promotes Leukemia Progression,” Advanced Science (Weinh) (2025): e09838.

[85]

M. Teeuwssen and R. Fodde, “Cell Heterogeneity and Phenotypic Plasticity in Metastasis Formation: The Case of Colon Cancer,” Cancers (Basel) 11, no. 9 (2019).

[86]

H. Wang, Y. Li, N. Wu, C. Lv, and Y. Wang, “P4HB Regulates the TGFβ/SMAD3 Signaling Pathway Through PRMT1 to Participate in High Glucose-Induced Epithelial-Mesenchymal Transition and Fibrosis of Renal Tubular Epithelial Cells,” BMC Nephrology [Electronic Resource] 25, no. 1 (2024): 297.

[87]

C. Xiong, H. Chen, B. Su, et al., “PRMT1-Mediated BRD4 Arginine Methylation and Phosphorylation Promote Partial Epithelial-Mesenchymal Transformation and Renal Fibrosis,” Faseb Journal 39, no. 1 (2025): e70293.

[88]

H. Wei, Y. Liu, J. Min, et al., “Protein Arginine Methyltransferase 1 Promotes Epithelial-Mesenchymal Transition Via TGF-β1/Smad Pathway in Hepatic Carcinoma Cells,” Neoplasma 66, no. 6 (2019): 918–929.

[89]

S. Avasarala, M. Van Scoyk, M. K. Karuppusamy Rathinam, et al., “PRMT1 Is a Novel Regulator of Epithelial-Mesenchymal-Transition in Non-small Cell Lung Cancer,” Journal of Biological Chemistry 290, no. 21 (2015): 13479–13489.

[90]

Y. Gao, Y. Zhao, J. Zhang, et al., “The Dual Function of PRMT1 in Modulating Epithelial-Mesenchymal Transition and Cellular Senescence in Breast Cancer Cells Through Regulation of ZEB1,” Scientific Reports 6 (2016): 19874.

[91]

R. Lugano, M. Ramachandran, and A. Dimberg, “Tumor Angiogenesis: Causes, Consequences, Challenges and Opportunities,” Cellular and Molecular Life Sciences 77, no. 9 (2020): 1745–1770.

[92]

H. Saman, S. S. Raza, S. Uddin, and K. Rasul, “Inducing Angiogenesis, a Key Step in Cancer Vascularization, and Treatment Approaches,” Cancers (Basel) 12, no. 5 (2020): 1172.

[93]

N. Sphyris, C. King, J. Hoar, et al., “Carcinoma Cells that have Undergone an Epithelial-Mesenchymal Transition Differentiate Into Endothelial Cells and Contribute to Tumor Growth,” Oncotarget 12, no. 8 (2021): 823–844.

[94]

K. Maphalala, D. P. Ramali, L. T. Maebele, et al., “Therapeutic Targeting of Protein Arginine Methyltransferases Reduces Breast Cancer Progression by Disrupting Angiogenic Pathways,” Biochemistry and Biophysics Reports 43 (2025): 102172.

[95]

H. Wang, H. Nie, X. Zhao, et al., “Tumor-Derived PRMT1 Suppresses Macrophage Antitumor Activity by Inhibiting cGAS/STING Signaling in Gastric Cancer Cells,” Cell Death & Disease 16, no. 1 (2025): 649.

[96]

J. Zhang, Z. Huang, C. Song, et al., “PRMT1-Mediated PARP1 Methylation Drives Lung Metastasis and Chemoresistance via P65 Activation in Triple-Negative Breast Cancer,” Research (Wash D C) 8 (2025): 0854.

[97]

N. Cao, F. Zhang, J. Yin, et al., “LPCAT2 Inhibits Colorectal Cancer Progression Via the PRMT1/SLC7A11 Axis,” Oncogene 43, no. 22 (2024): 1714–1725.

[98]

L. Zhang, Y. He, Y. Jiang, et al., “PRMT1 Reverts the Immune Escape of Necroptotic Colon Cancer Through RIP3 Methylation,” Cell Death & Disease 14, no. 4 (2023): 233.

[99]

C. Cheng, X. Pei, S. W. Li, et al., “CRISPR/Cas9 Library Screening Uncovered Methylated PKP2 as a Critical Driver of Lung Cancer Radioresistance by Stabilizing β-Catenin,” Oncogene 40, no. 16 (2021): 2842–2857.

[100]

S. Liang, Q. Wang, Y. Wen, et al., “Ligand-Independent EphA2 Contributes to Chemoresistance in Small-Cell Lung Cancer by Enhancing PRMT1-Mediated SOX2 Methylation,” Cancer Science 114, no. 3 (2023): 921–936.

[101]

Y. Sun, D. Dong, Y. Xia, L. Hao, W. Wang, and C. Zhao, “YTHDF1 Promotes Breast Cancer Cell Growth, DNA Damage Repair and Chemoresistance,” Cell Death & Disease 13, no. 3 (2022): 230.

[102]

S. Shen, H. Zhou, Z. Xiao, et al., “PRMT1 in Human Neoplasm: Cancer Biology and Potential Therapeutic Target,” Cell Communication and Signaling 22, no. 1 (2024): 102.

[103]

F. Zhu, X. Yang, Y. Yang, et al., “The Role of Histone Methyltransferases in Therapeutic Resistance of NSCLC,” Epigenetics 20, no. 1 (2025): 2536786.

[104]

C. D. K. Nguyen, B. A. Colón-Emeric, S. Murakami, M. N. Y. Shujath, and C. Yi, “PRMT1 Promotes Epigenetic Reprogramming Associated With Acquired Chemoresistance in Pancreatic Cancer,” Cell Reports 43, no. 5 (2024): 114176.

[105]

M. K. Aparnathi, S. Ul Haq, J. St-Germain, et al., “PRMT1 Inhibitor MS023 Suppresses RNA Splicing to Sensitize Small Cell Lung Cancer to DNA Damaging Agents,” Neoplasia 66 (2025): 101176.

[106]

Y. Zhang, M. Xu, J. Yuan, et al., “Repression of PRMT Activities Sensitize Homologous Recombination-Proficient Ovarian and Breast Cancer Cells to PARP Inhibitor Treatment,” BioRxiv (2025).

[107]

C. Dominici, N. Sgarioto, Z. Yu, et al., “Synergistic Effects of Type I PRMT and PARP Inhibitors Against Non-Small Cell Lung Cancer Cells,” Clin Epigenetics 13, no. 1 (2021): 54.

[108]

Y. Gao, C. Feng, J. Ma, and Q. Yan, “Protein Arginine Methyltransferases (PRMTs): Orchestrators of Cancer Pathogenesis, Immunotherapy Dynamics, and Drug Resistance,” Biochemical Pharmacology 221 (2024): 116048.

[109]

D. Huang, A. H. Rezaeian, J. Wang, et al., “Targeting the PRMT1-cGAS-STING Signaling Pathway to Enhance the Anti-Tumor Therapeutic Efficacy,” Journal of Cancer Biology 5, no. 2 (2024): 44–60.

[110]

H. Devarbhavi, S. K. Asrani, J. P. Arab, Y. A. Nartey, E. Pose, and P. S. Kamath, “Global Burden of Liver Disease: 2023 Update,” Journal of Hepatology 79, no. 2 (2023): 516–537.

[111]

Z. M. Younossi, G. Wong, Q. M. Anstee, and L. Henry, “The Global Burden of Liver Disease,” Clinical Gastroenterology and Hepatology 21, no. 8 (2023): 1978–1991.

[112]

M. Eslam, A. J. Sanyal, and J. George, “MAFLD: A Consensus-Driven Proposed Nomenclature for Metabolic Associated Fatty Liver Disease,” Gastroenterology 158, no. 7 (2020): 1999–2014.e1.

[113]

K. P. Matchett, J. Paris, S. A. Teichmann, and N. C. Henderson, “Spatial Genomics: Mapping Human Steatotic Liver Disease,” Nature Reviews Gastroenterology & Hepatology 21, no. 9 (2024): 646–660.

[114]

M. Noureddin and A. J. Sanyal, “Pathogenesis of NASH: The Impact of Multiple Pathways,” Current Hepatology Reports 17, no. 4 (2018): 350–360.

[115]

X. Guo, X. Yin, Z. Liu, and J. Wang, “Non-Alcoholic Fatty Liver Disease (NAFLD) Pathogenesis and Natural Products for Prevention and Treatment,” International Journal of Molecular Sciences 23, no. 24 (2022): 15489.

[116]

U. Sabir, H. M. Irfan, U. I. Alamgeer, Z. R. Niazi, and H. M. M. Asjad, “Phytochemicals Targeting NAFLD Through Modulating the Dual Function of Forkhead Box O1 (FOXO1) Transcription Factor Signaling Pathways,” Naunyn-Schmiedebergs Archives of Pharmacology 395, no. 7 (2022): 741–755.

[117]

X. Zhang, N. Tang, T. J. Hadden, and A. K. Rishi, “Akt, FoxO and Regulation of Apoptosis,” Biochimica Et Biophysica Acta 1813, no. 11 (2011): 1978–1986.

[118]

X. Pan, Y. Zhang, H. G. Kim, S. Liangpunsakul, and X. C. Dong, “FOXO Transcription Factors Protect Against the Diet-Induced Fatty Liver Disease,” Scientific Reports 7 (2017): 44597.

[119]

L. Liu, L. D. Zheng, P. Zou, et al., “FoxO1 Antagonist Suppresses Autophagy and Lipid Droplet Growth in Adipocytes,” Cell Cycle 15, no. 15 (2016): 2033–2041.

[120]

G. Alasiri, L. Y. Fan, S. Zona, et al., “ER Stress and Cancer: The FOXO Forkhead Transcription Factor Link,” Molecular and Cellular Endocrinology 462, no. Pt B (2018): 67–81.

[121]

D. T. Graves and T. N. Milovanova, “Mucosal Immunity and the FOXO1 Transcription Factors,” Frontiers in Immunology 10 (2019): 2530.

[122]

C. Zeng and M. Chen, “Progress in Nonalcoholic Fatty Liver Disease: SIRT Family Regulates Mitochondrial Biogenesis,” Biomolecules 12, no. 8 (2022).

[123]

H. S. Han, D. Choi, S. Choi, and S. H. Koo, “Roles of Protein Arginine Methyltransferases in the Control of Glucose Metabolism,” Endocrinology and Metabolism (Seoul) 29, no. 4 (2014): 435–440.

[124]

G. J. Kops and B. M. Burgering, “Forkhead Transcription Factors: New Insights Into Protein Kinase B (c-akt) Signaling,” Journal of Molecular Medicine (Berlin) 77, no. 9 (1999): 656–665.

[125]

D. Choi, K. J. Oh, H. S. Han, et al., “Protein Arginine Methyltransferase 1 Regulates Hepatic Glucose Production in a FoxO1-Dependent Manner,” Hepatology 56, no. 4 (2012): 1546–1556.

[126]

A. Brunet, A. Bonni, M. J. Zigmond, et al., “Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor,” Cell 96, no. 6 (1999): 857–868.

[127]

J. Zhao, A. Adams, S. A. Weinman, and I. Tikhanovich, “Hepatocyte PRMT1 Protects From Alcohol Induced Liver Injury by Modulating Oxidative Stress Responses,” Scientific Reports 9, no. 1 (2019): 9111.

[128]

S. Choi, D. Choi, Y. K. Lee, et al., “Depletion of Prmt1 in Adipocytes Impairs Glucose Homeostasis in Diet-Induced Obesity,” Diabetes 70, no. 8 (2021): 1664–1678.

[129]

Y. Ma, S. Liu, H. Jun, et al., “A Critical Role for Hepatic Protein Arginine Methyltransferase 1 Isoform 2 in Glycemic Control,” Faseb Journal 34, no. 11 (2020): 14863–14877.

[130]

C. Ye, W. Jiang, T. Hu, J. Liang, and Y. Chen, “The Regulatory Impact of CFLAR Methylation Modification on Liver Lipid Metabolism,” International Journal of Molecular Sciences 25, no. 14 (2024).

[131]

J. H. Zippin, J. Farrell, D. Huron, et al., “Bicarbonate-Responsive “Soluble” Adenylyl Cyclase Defines A Nuclear cAMP Microdomain,” Journal of Cell Biology 164, no. 4 (2004): 527–534.

[132]

D. Wu and Y. Qiu, “Type 2 Immune Regulation of Adipose Tissue Homeostasis,” Current Opinion in Physiology 12 (2019): 20–25.

[133]

E. E. Powell, V. W. Wong, and M. Rinella, “Non-Alcoholic Fatty Liver Disease,” Lancet 397, no. 10290 (2021): 2212–2224.

[134]

A. Hoffmann, G. Cheng, and D. Baltimore, “NF-κB: Master Regulator of Cellular Responses in Health and Disease,” Immunity & Inflammation 1, no. 1 (2025): 2.

[135]

P. O. Hassa, M. Covic, M. T. Bedford, and M. O. Hottiger, “Protein Arginine Methyltransferase 1 Coactivates NF-kappaB-Dependent Gene Expression Synergistically With CARM1 and PARP1,” Journal of Molecular Biology 377, no. 3 (2008): 668–678.

[136]

Z. Yan, H. Wu, H. Liu, et al., “The Protein Arginine Methyltransferase PRMT1 Promotes TBK1 Activation Through Asymmetric Arginine Methylation,” Cell reports 36, no. 12 (2021): 109731.

[137]

I. Tikhanovich, J. Zhao, J. Olson, et al., “Protein Arginine Methyltransferase 1 Modulates Innate Immune Responses Through Regulation of Peroxisome Proliferator-Activated Receptor γ-Dependent Macrophage Differentiation,” Journal of Biological Chemistry 292, no. 17 (2017): 6882–6894.

[138]

J. H. Cho, R. Lee, E. Kim, Y. E. Choi, and E. J. Choi, “PRMT1 Negatively Regulates Activation-Induced Cell Death in Macrophages by Arginine Methylation of GAPDH,” Experimental Cell Research 368, no. 1 (2018): 50–58.

[139]

Y. Aizawa, M. Mori, T. Suzuki, A. Saito, and H. Inoue, “Shotgun Proteomic Investigation of Methyltransferase and Methylation Profiles in Lipopolysaccharide Stimulated RAW264.7 Murine Macrophages,” Biomedical Research 43, no. 3 (2022): 73–80.

[140]

T. Yuan, Z. Ye, S. Mei, et al., “PRMT1-Mediated Methylation of UBE2m Promoting Calcium Oxalate Crystal-Induced Kidney Injury by Inhibiting Fatty Acid Metabolism,” Cell Death & Disease 16, no. 1 (2025): 579.

[141]

X. Qiao, D. I. Kim, H. Jun, et al., “Protein Arginine Methyltransferase 1 Interacts with PGC1α and Modulates Thermogenic Fat Activation,” Endocrinology 160, no. 12 (2019): 2773–2786.

[142]

R. Bataller and D. A. Brenner, “Liver Fibrosis,” Journal of Clinical Investigation 115, no. 2 (2005): 209–218.

[143]

F. Z. Yan, H. Qian, F. Liu, et al., “Inhibition of Protein Arginine Methyltransferase 1 Alleviates Liver Fibrosis by Attenuating the Activation of Hepatic Stellate Cells in Mice,” Faseb Journal 36, no. 9 (2022): e22489.

[144]

W. J. Li, Y. H. He, J. J. Yang, et al., “Profiling PRMT Methylome Reveals Roles of hnRNPA1 Arginine Methylation in RNA Splicing and Cell Growth,” Nature Communications 12, no. 1 (2021): 1946.

[145]

K. Wang, L. Luo, S. Fu, et al., “PHGDH Arginine Methylation by PRMT1 Promotes Serine Synthesis and Represents a Therapeutic Vulnerability in Hepatocellular Carcinoma,” Nature Communications 14, no. 1 (2023): 1011.

[146]

J. Yan, K. X. Li, L. Yu, et al., “PRMT1 Integrates Immune Microenvironment and Fatty Acid Metabolism Response in Progression of Hepatocellular Carcinoma,” Journal of Hepatocellular Carcinoma 11 (2024): 15–27.

[147]

L. Luo, X. Wu, J. Fan, et al., “FBXO7 Ubiquitinates PRMT1 to Suppress Serine Synthesis and Tumor Growth in Hepatocellular Carcinoma,” Nature Communications 15, no. 1 (2024): 4790.

[148]

J. Zhao, M. O'Neil, M. Schonfeld, A. Komatz, S. A. Weinman, and I. Tikhanovich, “Hepatocellular Protein Arginine Methyltransferase 1 Suppresses Alcohol-Induced Hepatocellular Carcinoma Formation by Inhibition of Inducible Nitric Oxide Synthase,” Hepatology Communications 4, no. 6 (2020): 790–808.

[149]

J. M. Jeong and C. Ju, “The Protective Function of PRMT1 in Alcohol-Induced Hepatocellular Carcinoma,” Hepatology Communications 4, no. 6 (2020): 787–789.

[150]

Q. Li, L. Zhang, Q. Yang, et al., “Thymidine Kinase 1 Drives Hepatocellular Carcinoma in Enzyme-Dependent and -Independent Manners,” Cell Metabolism 35, no. 6 (2023): 912–927.e7.

[151]

Y. Zhou, T. Zhang, S. Wang, et al., “Metal-Polyphenol-Network Coated R612F Nanoparticles Reduce Drug Resistance in Hepatocellular Carcinoma by Inhibiting Stress Granules,” Cell Death Discovery 10, no. 1 (2024): 384.

[152]

K. Murata, W. Lu, M. Hashimoto, et al., “PRMT1 Deficiency in Mouse Juvenile Heart Induces Dilated Cardiomyopathy and Reveals Cryptic Alternative Splicing Products,” Iscience 8 (2018): 200–213.

[153]

J. H. Pyun, H. J. Kim, M. H. Jeong, et al., “Cardiac Specific PRMT1 Ablation Causes Heart Failure Through CaMKII Dysregulation,” Nature Communications 9, no. 1 (2018): 5107.

[154]

M. H. Jeong, H. J. Jeong, B. Y. Ahn, et al., “PRMT1 Suppresses ATF4-Mediated Endoplasmic Reticulum Response in Cardiomyocytes,” Cell Death & Disease 10, no. 12 (2019): 903.

[155]

S. W. Kim, B. Y. Ahn, T. T. V. Tran, J. H. Pyun, J. S. Kang, and Y. E. Leem, “PRMT1 Suppresses Doxorubicin-Induced Cardiotoxicity by Inhibiting Endoplasmic Reticulum Stress,” Cell Signalling 98 (2022): 110412.

[156]

S. Zhao, P. Sun, C. Wang, et al., “LncRNA 91234.1 Targets PRMT1/ASCL4/GPX4 Axis to Regulate Formaldehyde-Induced Cardiomyocyte Ferroptosis and Congenital Heart Disease,” Journal of Molecular and Cellular Cardiology 206 (2025): 76–90.

[157]

A. Caturano, E. Vetrano, R. Galiero, et al., “Cardiac Hypertrophy: From Pathophysiological Mechanisms to Heart Failure Development,” Reviews in Cardiovascular Medicine 23, no. 5 (2022): 165.

[158]

S. Zheng, C. Zeng, A. Huang, et al., “Relationship Between Protein Arginine Methyltransferase and Cardiovascular Disease (Review),” Biomedical Reports 17, no. 5 (2022): 90.

[159]

Z. Yan, W. Zhao, N. Zhao, et al., “PRMT1 Alleviates Isoprenaline-Induced Myocardial Hypertrophy by Methylating SRSF1,” Acta Biochimica et Biophysica Sinica (Shanghai) 57, no. 8 (2024): 1338–1349.

[160]

O. Jackson-Weaver, N. Ungvijanpunya, Y. Yuan, et al., “PRMT1-p53 Pathway Controls Epicardial EMT and Invasion,” Cell Reports 31, no. 10 (2020): 107739.

[161]

Z. Feng, “p53 Regulation of the IGF-1/AKT/mTOR Pathways and the Endosomal Compartment,” Cold Spring Harbor Perspectives in Biology 2, no. 2 (2010): a001057.

[162]

J. Kim, K. P. Lee, B. S. Kim, S. J. Lee, B. S. Moon, and S. Baek, “Heat Shock Protein 90 Inhibitor AUY922 Attenuates Platelet-Derived Growth Factor-BB-Induced Migration and Proliferation of Vascular Smooth Muscle Cells,” Korean Journal of Physiology & Pharmacology 24, no. 3 (2020): 241–248.

[163]

J. H. Pyun, B. Y. Ahn, T. A. Vuong, et al., “Inducible Prmt1 Ablation in Adult Vascular Smooth Muscle Leads to Contractile Dysfunction and Aortic Dissection,” Experimental & Molecular Medicine 53, no. 10 (2021): 1569–1579.

[164]

C. Penna and P. Pagliaro, “Endothelial Dysfunction: Redox Imbalance, NLRP3 Inflammasome, and Inflammatory Responses in Cardiovascular Diseases,” Antioxidants (Basel) 14, no. 3 (2025): 256.

[165]

M. F. McCarty, “Asymmetric Dimethylarginine Is a Well Established Mediating Risk Factor for Cardiovascular Morbidity and Mortality-Should Patients With Elevated Levels Be Supplemented With Citrulline?,” Healthcare (Basel) 4, no. 3 (2016): 40.

[166]

R. H. Böger, K. Sydow, J. Borlak, et al., “LDL Cholesterol Upregulates Synthesis of Asymmetrical Dimethylarginine in Human Endothelial Cells: Involvement of S-Adenosylmethionine-Dependent Methyltransferases,” Circulation Research 87, no. 2 (2000): 99–105.

[167]

Y. Morales, D. V. Nitzel, O. M. Price, et al., “Redox Control of Protein Arginine Methyltransferase 1 (PRMT1) Activity,” Journal of Biological Chemistry 290, no. 24 (2015): 14915–14926.

[168]

A. Łuczak, M. Madej, A. Kasprzyk, and A. Doroszko, “Role of the eNOS Uncoupling and the Nitric Oxide Metabolic Pathway in the Pathogenesis of Autoimmune Rheumatic Diseases,” Oxidative Medicine and Cellular Longevity 2020 (2020): 1417981.

[169]

V. Raj, S. Natarajan, M. C, et al., “Cholecalciferol and Metformin Protect Against Lipopolysaccharide-Induced Endothelial Dysfunction and Senescence by Modulating Sirtuin-1 and Protein Arginine Methyltransferase-1,” European Journal of Pharmacology 912 (2021): 174531.

[170]

Y. Zhang, S. Wei, E. J. Jin, et al., “Protein Arginine Methyltransferases: Emerging Targets in Cardiovascular and Metabolic Disease,” Diabetes & Metabolism Journal 48, no. 4 (2024): 487–502.

[171]

M. Krzystek-Korpacka, M. G. Fleszar, I. Bednarz-Misa, et al., “Transcriptional and Metabolomic Analysis of L-Arginine/Nitric Oxide Pathway in Inflammatory Bowel Disease and Its Association With Local Inflammatory and Angiogenic Response: Preliminary Findings,” International Journal of Molecular Sciences 21, no. 5 (2020): 1641.

[172]

X. Quan, W. Yue, Y. Luo, et al., “The Protein Arginine Methyltransferase PRMT5 Regulates Abeta-Induced Toxicity in Human Cells and Caenorhabditis Elegans Models of Alzheimer's Disease,” Journal of Neurochemistry 134, no. 5 (2015): 969–977.

[173]

M. Tibshirani, M. L. Tradewell, K. R. Mattina, et al., “Cytoplasmic Sequestration of FUS/TLS Associated With ALS Alters Histone Marks Through Loss of Nuclear Protein Arginine Methyltransferase 1,” Human Molecular Genetics 24, no. 3 (2015): 773–786.

[174]

T. Ratovitski, N. Arbez, J. C. Stewart, E. Chighladze, and C. A. Ross, “PRMT5- Mediated Symmetric Arginine Dimethylation is Attenuated by Mutant Huntingtin and is Impaired in Huntington's Disease (HD),” Cell Cycle 14, no. 11 (2015): 1716–1729.

[175]

G. Plascencia-Villa and G. Perry, “Neuropathologic Changes Provide Insights Into Key Mechanisms of Alzheimer Disease and Related Dementia,” American Journal of Pathology 192, no. 10 (2022): 1340–1346.

[176]

F. Zhang, A. Rakhimbekova, T. Lashley, and T. Madl, “Brain Regions Show Different Metabolic and Protein Arginine Methylation Phenotypes in Frontotemporal Dementias and Alzheimer's Disease,” Progress in Neurobiology 221 (2023): 102400.

[177]

E. Angelopoulou, E. S. Pyrgelis, C. Ahire, P. Suman, A. Mishra, and C. Piperi, “Functional Implications of Protein Arginine Methyltransferases (PRMTs) in Neurodegenerative Diseases,” Biology (Basel) 12, no. 9 (2023).

[178]

Y. L. Tsai, Y. C. Mu, and J. L. Manley, “Nuclear RNA Transcript Levels Modulate Nucleocytoplasmic Distribution of ALS/FTD-Associated Protein FUS,” Scientific Reports 12, no. 1 (2022): 8180.

[179]

D. M. Baron, L. J. Kaushansky, C. L. Ward, et al., “Amyotrophic Lateral Sclerosis-Linked FUS/TLS Alters Stress Granule Assembly and Dynamics,” Molecular Neurodegeneration 8 (2013): 30.

[180]

C. Scaramuzzino, J. Monaghan, C. Milioto, et al., “Protein Arginine Methyltransferase 1 and 8 Interact With FUS to Modify its Sub-Cellular Distribution and Toxicity In Vitro and In Vivo,” PLoS ONE 8, no. 4 (2013): e61576.

[181]

T. L. Dane, A. L. Gill, F. G. Vieira, and K. R. Denton, “Reduced C9orf72 Expression Exacerbates polyGR Toxicity in Patient iPSC-Derived Motor Neurons and a Type I Protein Arginine Methyltransferase Inhibitor Reduces that Toxicity,” Frontiers in Cellular Neuroscience 17 (2023): 1134090.

[182]

M. Aikio, H. M. Odeh, H. J. Wobst, et al., “Opposing Roles of p38α-Mediated Phosphorylation and PRMT1-Mediated Arginine Methylation in Driving TDP-43 Proteinopathy,” Cell Reports 44, no. 1 (2025): 115205.

[183]

M.-H. Jun, H.-H. Ryu, Y.-W. Jun, et al., “Sequestration of PRMT1 and Nd1-L mRNA Into ALS-linked FUS Mutant R521C-Positive Aggregates Contributes to Neurite Degeneration Upon Oxidative Stress,” Scientific Reports 7, no. 1 (2017): 40474.

[184]

L. Phan, D. Miller, A. Gopinath, et al., “Parkinson's Paradox: Alpha-Synuclein's Selective Strike on SNc Dopamine Neurons Over VTA,” NPJ Parkinson's Disease 11, no. 1 (2025): 207.

[185]

M. A. Burguillos, N. Hajji, E. Englund, et al., “Apoptosis-Inducing Factor Mediates Dopaminergic Cell Death in Response to LPS-Induced Inflammatory Stimulus: Evidence in Parkinson's Disease Patients,” Neurobiology of Disease 41, no. 1 (2011): 177–188.

[186]

J. H. Cho, M. K. Lee, K. W. Yoon, J. Lee, S. G. Cho, and E. J. Choi, “Arginine Methylation-Dependent Regulation of ASK1 Signaling by PRMT1,” Cell Death and Differentiation 19, no. 5 (2012): 859–870.

[187]

. and 左方 , “PRMT1介导的EZH2甲基化通过靶向抑制SOCS3促进帕金森病发生和发展.[J],” 临床神经外科杂志 22, no. 1 (2025): 61–68.

[188]

“A Novel Gene Containing a Trinucleotide Repeat that is Expanded and Unstable on Huntington's Disease Chromosomes. The Huntington's Disease Collaborative Research Group,” Cell 72, no. 6 (1993): 971–983.

[189]

T. Ratovitski, E. Chighladze, N. Arbez, et al., “Huntingtin Protein Interactions Altered by Polyglutamine Expansion as Determined by Quantitative Proteomic Analysis,” Cell Cycle 11, no. 10 (2012): 2006–2021.

[190]

C. Chamontin, G. Bossis, S. Nisole, N. J. Arhel, and G. Maarifi, “Regulation of Viral Restriction by Post-Translational Modifications,” Viruses 13, no. 11 (2021): 2197.

[191]

M. T. Bedford and S. Richard, “Arginine Methylation an Emerging Regulator of Protein Function,” Molecular Cell 18, no. 3 (2005): 263–272.

[192]

K. Bonham, S. Hemmers, Y. H. Lim, D. M. Hill, M. G. Finn, and K. A. Mowen, “Effects of a Novel Arginine Methyltransferase Inhibitor on T-Helper Cell Cytokine Production,” Febs Journal 277, no. 9 (2010): 2096–2108.

[193]

N. Srour, S. Khan, and S. Richard, “The Influence of Arginine Methylation in Immunity and Inflammation,” Journal of Inflammation Research 15 (2022): 2939–2958.

[194]

E. Dolezal, S. Infantino, F. Drepper, et al., “The BTG2-PRMT1 Module Limits Pre-B Cell Expansion by Regulating the CDK4-Cyclin-D3 Complex,” Nature Immunology 18, no. 8 (2017): 911–920.

[195]

J. Zhao, M. O'Neil, A. Vittal, S. A. Weinman, and I. Tikhanovich, “PRMT1-Dependent Macrophage IL-6 Production Is Required for Alcohol-Induced HCC Progression,” Gene Expression 19, no. 2 (2019): 137–150.

[196]

Z. Fan, J. Li, P. Li, et al., “Protein Arginine Methyltransferase 1 (PRMT1) Represses MHC II Transcription in Macrophages by Methylating CIITA,” Scientific Reports 7 (2017): 40531.

[197]

P. Brown, A. G. Pratt, and K. L. Hyrich, “Therapeutic Advances in Rheumatoid Arthritis,” Bmj 384 (2024): e070856.

[198]

J. Liu, Y. Li, Z. Jiang, Y. Liu, and Z. Wei, “Protein Arginine Methyltransferase 1 Upregulates Matrix Metalloproteinase-2/9 Expression Via Zeste Homolog 2 to Promote Human Rheumatoid Arthritis Fibroblast-Like Synovial Cell Survival and Metastasis,” International Journal of Rheumatic Diseases 26, no. 1 (2023): 88–98.

[199]

E. Kim, J. Jang, J. G. Park, et al., “Protein Arginine Methyltransferase 1 (PRMT1) Selective Inhibitor, TC-E 5003, Has Anti-Inflammatory Properties in TLR4 Signaling,” International Journal of Molecular Sciences 21, no. 9 (2020): 3058.

[200]

E. D. Kaan, T. E. Brunekreef, J. Drylewicz, et al., “Association of Autoantibodies With the IFN Signature and NETosis in Patients With Systemic Lupus Erythematosus,” Journal of Translational Autoimmunity 9 (2024): 100246.

[201]

E. Navarro Quiroz, V. Chavez-Estrada, K. Macias-Ochoa, et al., “Epigenetic Mechanisms and Posttranslational Modifications in Systemic Lupus Erythematosus,” International Journal of Molecular Sciences 20, no. 22 (2019): 5679.

[202]

M. Ramaswamy, R. Tummala, K. Streicher, A. Nogueira da Costa, and P. Z. Brohawn, “The Pathogenesis, Molecular Mechanisms, and Therapeutic Potential of the Interferon Pathway in Systemic Lupus Erythematosus and Other Autoimmune Diseases,” International Journal of Molecular Sciences 22, no. 20 (2021): 11286.

[203]

P. Bradding, C. Porsbjerg, A. Côté, S. E. Dahlén, T. S. Hallstrand, and C. E. Brightling, “Airway Hyperresponsiveness in Asthma: The role of the Epithelium,” Journal of Allergy and Clinical Immunology 153, no. 5 (2024): 1181–1193.

[204]

W. Zhai, H. Sun, Z. Li, et al., “PRMT1 Modulates Processing of Asthma-Related Primary MicroRNAs (Pri-miRNAs) Into Mature miRNAs in Lung Epithelial Cells,” Journal of Immunology 206, no. 1 (2021): 11–22.

[205]

J. Y. Park, J. H. Choi, S. N. Lee, et al., “Protein Arginine Methyltransferase 1 Contributes to the Development of Allergic Rhinitis by Promoting the Production of Epithelial-Derived Cytokines,” Journal of Allergy and Clinical Immunology 147, no. 5 (2021): 1720–1731.

[206]

J. H. Kim, B. C. Yoo, W. S. Yang, E. Kim, S. Hong, and J. Y. Cho, “The Role of Protein Arginine Methyltransferases in Inflammatory Responses,” Mediators of Inflammation 2016 (2016): 4028353.

[207]

E. Strattan and G. C. Hildebrandt, “Mast Cell Involvement in Fibrosis in Chronic Graft-Versus-Host Disease,” International Journal of Molecular Sciences 22, no. 5 (2021): 2385.

[208]

X. Zhao, Y. Sun, Z. Xu, L. Cai, Y. Hu, and H. Wang, “Targeting PRMT1 Prevents Acute and Chronic Graft-Versus-Host Disease,” Molecular Therapy 31, no. 11 (2023): 3259–3276.

[209]

D. Cheng, N. Yadav, R. W. King, M. S. Swanson, E. J. Weinstein, and M. T. Bedford, “Small Molecule Regulators of Protein Arginine Methyltransferases,” Journal of Biological Chemistry 279, no. 23 (2004): 23892–23899.

[210]

F. Chen and D. J. Fulton, “An Inhibitor of Protein Arginine Methyltransferases, 7,7'-Carbonylbis(Azanediyl)Bis(4-Hydroxynaphthalene-2-Sulfonic Acid) (AMI-1), is a Potent Scavenger of NADPH-Oxidase-Derived Superoxide,” Molecular Pharmacology 77, no. 2 (2010): 280–287.

[211]

M. S. Eram, Y. Shen, M. Szewczyk, et al., “A Potent, Selective, and Cell-Active Inhibitor of Human Type I Protein Arginine Methyltransferases,” American Chemical Society Chemical Biology 11, no. 3 (2016): 772–781.

[212]

Y. Zhu, X. He, Y. C. Lin, et al., “Targeting PRMT1-Mediated FLT3 Methylation Disrupts Maintenance of MLL-Rearranged Acute Lymphoblastic Leukemia,” Blood 134, no. 15 (2019): 1257–1268.

[213]

Z. Zhao, J. Zhang, Y. Ren, et al., “Discovery of 2,4-Diphenyl-Substituted Thiazole Derivatives as PRMT1 Inhibitors and Investigation of Their Anti-Cervical Cancer Effects,” Bioorganic & Medicinal Chemistry 92 (2023): 117436.

[214]

E. M. Bissinger, R. Heinke, A. Spannhoff, et al., “Acyl Derivatives of p-Aminosulfonamides and Dapsone as New Inhibitors of the Arginine Methyltransferase hPRMT1,” Bioorganic & Medicinal Chemistry 19, no. 12 (2011): 3717–3731.

[215]

P. Zhang, H. Tao, L. Yu, L. Zhou, and C. Zhu, “Developing Protein Arginine Methyltransferase 1 (PRMT1) Inhibitor TC-E-5003 as an Antitumor Drug Using INEI Drug Delivery Systems,” Drug Delivery 27, no. 1 (2020): 491–501.

[216]

Y. Xie, R. Zhou, F. Lian, et al., “Virtual Screening and Biological Evaluation of Novel Small Molecular Inhibitors Against Protein Arginine Methyltransferase 1 (PRMT1),” Organic & Biomolecular Chemistry 12, no. 47 (2014): 9665–9673.

[217]

L. Yan, C. Yan, K. Qian, et al., “Diamidine Compounds for Selective Inhibition of Protein Arginine Methyltransferase 1,” Journal of Medicinal Chemistry 57, no. 6 (2014): 2611–2622.

[218]

B. Sergi, N. Yuksel-Catal, S. C. Ozcan, et al., “Epidrug Screening Identifies Type I PRMT Inhibitors as Modulators of Lysosomal Exocytosis and Drug Sensitivity in Cancers,” Cell Death & Disease 16, no. 1 (2025): 600.

[219]

H. Shi, Y. Han, X. Fu, et al., “Abstract 4224: The Pharmacological Intervention of Protein Arginine Methyltransferase 1 (PRMT1) Leads to Metastatic Castration-Resistant Prostate Cancer (mCRPC) Repression Through Unique and Significant Androgen Receptor (AR) Downregulation and Epigenetic Modulation,” Cancer Research 85, no. 8_Supplement_1 (2025): 4224.

[220]

A. Fedoriw, S. R. Rajapurkar, S. O'Brien, et al., “Anti-tumor Activity of the Type I PRMT Inhibitor, GSK3368715, Synergizes With PRMT5 Inhibition Through MTAP Loss,” Cancer Cell 36, no. 1 (2019): 100–114.e25.

[221]

A. B. El-Khoueiry, J. Clarke, T. Neff, et al., “Phase 1 Study of GSK3368715, a Type I PRMT Inhibitor, in Patients With Advanced Solid Tumors,” British Journal of Cancer 129, no. 2 (2023): 309–317.

[222]

L. Zhou, X. Jia, Y. Shang, et al., “PRMT1 Inhibition Promotes Ferroptosis Sensitivity Via ACSL1 Upregulation in Acute Myeloid Leukemia,” Molecular Carcinogenesis 62, no. 8 (2023): 1119–1135.

[223]

I. D. Iyamu, A. A. Al-Hamashi, and R. Huang, “A Pan-Inhibitor for Protein Arginine Methyltransferase Family Enzymes,” Biomolecules 11, no. 6 (2021): 854.

[224]

J. Wu, D. Li, and L. Wang, “Overview of PRMT1 Modulators: Inhibitors and Degraders,” European Journal of Medicinal Chemistry 279 (2024): 116887.

[225]

S. Jiang, H. Li, L. Zhang, et al., “Generic Diagramming Platform (GDP): A Comprehensive Database of High-Quality Biomedical Graphics,” Nucleic Acids Research 53, no. D1 (2025): D1670–D1676.

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