References

Methyltransferases: Functions and Applications

10.1002/cbic.202200212 · ExternalCitation · doi-reference

Modulation of I(Ks) channel-PIP(2) interaction by PRMT1 plays a critical role in the control of cardiac repolarization

10.1002/jcp.30775 · ExternalCitation · doi-reference

Geometry of guanidinium groups in arginines

10.1002/pro.2970 · ExternalCitation · doi-reference

Protein arginine methyltransferases: Insights into the enzyme structure and mechanism at the atomic level

10.1007/s00018-019-03145-x · ExternalCitation · doi-reference

PRMT7 ablation in cardiomyocytes causes cardiac hypertrophy and fibrosis through β-catenin dysregulation

10.1007/s00018-021-04097-x · ExternalCitation · doi-reference

Physiological and unappreciated roles of CaMKII in the heart

10.1007/s00395-018-0688-8 · ExternalCitation · doi-reference

Protein Arginine Methyltransferases in Cardiovascular and Neuronal Function

10.1007/s12035-019-01850-z · ExternalCitation · doi-reference

The emerging role of CARM1 in cancer

10.1007/s13402-024-00943-9 · ExternalCitation · doi-reference

PRMT7 as a unique member of the protein arginine methyltransferase family: A review

10.1016/j.abb.2019.02.014 · ExternalCitation · doi-reference

Diversity of the reaction mechanisms of SAM-dependent enzymes

10.1016/j.apsb.2020.08.011 · ExternalCitation · doi-reference

Prmt1 upregulated by Hdc deficiency aggravates acute myocardial infarction via NETosis

10.1016/j.apsb.2021.10.016 · ExternalCitation · doi-reference

Inhibition of PRMT3 activity reduces hepatic steatosis without altering atherosclerosis susceptibility in apoE knockout mice

10.1016/j.bbadis.2019.02.012 · ExternalCitation · doi-reference

PRMT4 overexpression aggravates cardiac remodeling following myocardial infarction by promoting cardiomyocyte apoptosis

10.1016/j.bbrc.2019.10.085 · ExternalCitation · doi-reference

PRMT2 inhibits the formation of foam cell induced by ox-LDL in RAW 264.7 macrophage involving ABCA1 mediated cholesterol efflux

10.1016/j.bbrc.2020.01.040 · ExternalCitation · doi-reference

Protein arginine methyltransferase 3: A crucial regulator in metabolic reprogramming and gene expression in cancers

10.1016/j.canlet.2022.216008 · ExternalCitation · doi-reference

Increased β-catenin accumulation and nuclear translocation are associated with concentric hypertrophy in cardiomyocytes

10.1016/j.carpath.2017.07.003 · ExternalCitation · doi-reference

PRMT1 suppresses doxorubicin-induced cardiotoxicity by inhibiting endoplasmic reticulum stress

10.1016/j.cellsig.2022.110412 · ExternalCitation · doi-reference

Genomic Location of PRMT6-Dependent H3R2 Methylation Is Linked to the Transcriptional Outcome of Associated Genes

10.1016/j.celrep.2018.08.052 · ExternalCitation · doi-reference

Role of O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins in diabetic cardiovascular complications

10.1016/j.coph.2020.08.005 · ExternalCitation · doi-reference

Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl

10.1016/j.devcel.2018.03.007 · ExternalCitation · doi-reference

Modulating the modulators: Regulation of protein arginine methyltransferases by post-translational modifications

10.1016/j.drudis.2020.06.031 · ExternalCitation · doi-reference

Promising role of protein arginine methyltransferases in overcoming anti-cancer drug resistance

10.1016/j.drup.2023.101016 · ExternalCitation · doi-reference

Overview of the development of protein arginine methyltransferase modulators: Achievements and future directions

10.1016/j.ejmech.2024.116212 · ExternalCitation · doi-reference

Novel alternative splice variants of the human protein arginine methyltransferase 1 (PRMT1) gene, discovered using next-generation sequencing

10.1016/j.gene.2019.02.072 · ExternalCitation · doi-reference

Protein arginine methyltransferase 6 mediates cardiac hypertrophy by differential regulation of histone H3 arginine methylation

10.1016/j.heliyon.2020.e03864 · ExternalCitation · doi-reference

Macrophage polarisation and inflammatory mechanisms in atherosclerosis: Implications for prevention and treatment

10.1016/j.heliyon.2024.e32073 · ExternalCitation · doi-reference

Tropomyosin-troponin complex in inherited cardiomyopathies

10.1016/j.hrthm.2024.02.034 · ExternalCitation · doi-reference

The inhibitory subunit of cardiac troponin (cTnI) is modified by arginine methylation in the human heart

10.1016/j.ijcard.2019.01.102 · ExternalCitation · doi-reference

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

10.1016/j.intimp.2023.110529 · ExternalCitation · doi-reference

Macrophages after myocardial infarction: Mechanisms for repairing and potential as therapeutic approaches

10.1016/j.intimp.2024.113562 · ExternalCitation · doi-reference

PRMT1 Deficiency in Mouse Juvenile Heart Induces Dilated Cardiomyopathy and Reveals Cryptic Alternative Splicing Products

10.1016/j.isci.2018.09.023 · ExternalCitation · doi-reference

Independent transcriptomic and proteomic regulation by type I and II protein arginine methyltransferases

10.1016/j.isci.2021.102971 · ExternalCitation · doi-reference

PRMT4-mediated arginine methylation promotes tyrosine phosphorylation of VEGFR-2 and regulates filopodia protrusions

10.1016/j.isci.2022.104736 · ExternalCitation · doi-reference

TAK1 Activation by NLRP3 Deficiency Confers Cardioprotection Against Pressure Overload-Induced Cardiomyocyte Pyroptosis and Hypertrophy

10.1016/j.jacbts.2023.05.008 · ExternalCitation · doi-reference

The Global Burden of Cardiovascular Diseases and Risk A Compass for Future Health

10.1016/j.jacc.2022.11.005 · ExternalCitation · doi-reference

Oligomerization of protein arginine methyltransferase 1 and its functional impact on substrate arginine methylation

10.1016/j.jbc.2024.107947 · ExternalCitation · doi-reference

Biomedical effects of protein arginine methyltransferase inhibitors

10.1016/j.jbc.2025.108201 · ExternalCitation · doi-reference

Novel insights into histone lysine methyltransferases in cancer therapy: From epigenetic regulation to selective drugs

10.1016/j.jpha.2022.11.009 · ExternalCitation · doi-reference

Arginine Methylation: The Coming of Age

10.1016/j.molcel.2016.11.003 · ExternalCitation · doi-reference

Lysine Methylation Regulators Moonlighting Outside the Epigenome

10.1016/j.molcel.2019.08.026 · ExternalCitation · doi-reference

Cellular pathways influenced by protein arginine methylation: Implications for cancer

10.1016/j.molcel.2021.09.011 · ExternalCitation · doi-reference

Productive mRNA chromatin escape is promoted by PRMT5 activity

10.1016/j.molcel.2025.09.021 · ExternalCitation · doi-reference

Insights into S-adenosyl-L-methionine (SAM)-dependent methyltransferase related diseases and genetic polymorphisms

10.1016/j.mrrev.2021.108396 · ExternalCitation · doi-reference

Histone H4R3 symmetric di-methylation by Prmt5 protects against cardiac hypertrophy via regulation of Filip1L/β-catenin

10.1016/j.phrs.2020.105104 · ExternalCitation · doi-reference

RNA methylation and cancer treatment

10.1016/j.phrs.2021.105937 · ExternalCitation · doi-reference

Methylation modification of non-histone proteins in breast cancer: An emerging targeted therapeutic strategy

10.1016/j.phrs.2024.107354 · ExternalCitation · doi-reference

The role of protein arginine N-methyltransferases in inflammation

10.1016/j.semcdb.2022.08.005 · ExternalCitation · doi-reference

To incise or not and where: SET-domain methyltransferases know

10.1016/j.tibs.2022.10.003 · ExternalCitation · doi-reference

PRMT5 up-regulation improves myocardial hypertrophy by mediating E2F-1/NF-κB/NLRP3 pathway

10.1016/j.ypmed.2023.107553 · ExternalCitation · doi-reference

The Lancet Commission on rethinking coronary artery disease: Moving from ischaemia to atheroma

10.1016/s0140-6736(25)00055-8 · ExternalCitation · doi-reference

S-Adenosylmethionine

10.1016/s1357-2725(99)00139-9 · ExternalCitation · doi-reference

Mechanism of Radical Initiation in the Radical S-Adenosyl-l-methionine Superfamily

10.1021/acs.accounts.8b00356 · ExternalCitation · doi-reference

A Family Divided: Distinct Structural and Mechanistic Features of the SpoU-TrmD (SPOUT) Methyltransferase Superfamily

10.1021/acs.biochem.8b01047 · ExternalCitation · doi-reference

Inhibitors of Protein Methyltransferases and Demethylases

10.1021/acs.chemrev.6b00801 · ExternalCitation · doi-reference

Chemical and Biochemical Perspectives of Protein Lysine Methylation

10.1021/acs.chemrev.8b00008 · ExternalCitation · doi-reference

Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor

10.1021/acs.jmedchem.3c01030 · ExternalCitation · doi-reference

Non-Histone Protein Methylation: Biological Significance and Bioengineering Potential

10.1021/acschembio.0c00771 · ExternalCitation · doi-reference

Pdcd4 deficiency enhances macrophage lipoautophagy and attenuates foam cell formation and atherosclerosis in mice

10.1038/cddis.2015.416 · ExternalCitation · doi-reference

Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition

10.1038/ncomms15571 · ExternalCitation · doi-reference

PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145

10.1038/ncomms7428 · ExternalCitation · doi-reference

SREBP-regulated lipid metabolism: Convergent physiology—Divergent pathophysiology

10.1038/nrendo.2017.91 · ExternalCitation · doi-reference

The DNA methyltransferase family: A versatile toolkit for epigenetic regulation

10.1038/nrg.2017.80 · ExternalCitation · doi-reference

Protein arginine methyltransferases: Promising targets for cancer therapy

10.1038/s12276-021-00613-y · ExternalCitation · doi-reference

Inducible Prmt1 ablation in adult vascular smooth muscle leads to contractile dysfunction and aortic dissection

10.1038/s12276-021-00684-x · ExternalCitation · doi-reference

Prmt7 regulates the JAK/STAT/Socs3 signaling pathway in postmenopausal cardiomyopathy

10.1038/s12276-024-01193-3 · ExternalCitation · doi-reference

Endothelial PRMT7 prevents dysfunction, promotes revascularization and enhances cardiac recovery post-myocardial infarction

10.1038/s12276-025-01517-x · ExternalCitation · doi-reference

Protein arginine methyltransferases coordinate mitochondrial stress adaptation and neuromuscular function

10.1038/s12276-026-01762-8 · ExternalCitation · doi-reference

The role of histone methylation in the development of digestive cancers: A potential direction for cancer management

10.1038/s41392-020-00252-1 · ExternalCitation · doi-reference

Methylation across the central dogma in health and diseases: New therapeutic strategies

10.1038/s41392-023-01528-y · ExternalCitation · doi-reference

Adriamycin induces cardiac fibrosis in mice via PRMT5-mediated cardiac fibroblast activation

10.1038/s41401-022-00963-x · ExternalCitation · doi-reference

Prmt7 promotes myoblast differentiation via methylation of p38MAPK on arginine residue 70

10.1038/s41418-019-0373-y · ExternalCitation · doi-reference

Programmed cell death 4 modulates lysosomal function by inhibiting TFEB translation

10.1038/s41418-020-00646-2 · ExternalCitation · doi-reference

PRMT4 promotes ferroptosis to aggravate doxorubicin-induced cardiomyopathy via inhibition of the Nrf2/GPX4 pathway

10.1038/s41418-022-00990-5 · ExternalCitation · doi-reference

PRMT5 critically mediates TMAO-induced inflammatory response in vascular smooth muscle cells

10.1038/s41419-022-04719-7 · ExternalCitation · doi-reference

Cardiac specific PRMT1 ablation causes heart failure through CaMKII dysregulation

10.1038/s41467-018-07606-y · ExternalCitation · doi-reference

Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site

10.1038/s41467-020-14722-1 · ExternalCitation · doi-reference

Protein context shapes the specificity of SH3 domain-mediated interactions in vivo

10.1038/s41467-021-21873-2 · ExternalCitation · doi-reference

Fibroblast-specific PRMT5 deficiency suppresses cardiac fibrosis and left ventricular dysfunction in male mice

10.1038/s41467-024-46711-z · ExternalCitation · doi-reference

Loss-of-function mutation in PRMT9 causes abnormal synapse development by dysregulation of RNA alternative splicing

10.1038/s41467-024-47107-9 · ExternalCitation · doi-reference

AtPRMT3-RPS2B promotes ribosome biogenesis and coordinates growth and cold adaptation trade-off

10.1038/s41467-024-52945-8 · ExternalCitation · doi-reference

Vitamin B12 produced by gut bacteria modulates cholinergic signalling

10.1038/s41556-023-01299-2 · ExternalCitation · doi-reference

Mechanisms of physiological and pathological cardiac hypertrophy

10.1038/s41569-018-0007-y · ExternalCitation · doi-reference

Epigenetics and beyond: Targeting writers of protein lysine methylation to treat disease

10.1038/s41573-020-00108-x · ExternalCitation · doi-reference

Protein arginine methylation: From enigmatic functions to therapeutic targeting

10.1038/s41573-021-00159-8 · ExternalCitation · doi-reference

RNA modification systems as therapeutic targets

10.1038/s41573-025-01280-8 · ExternalCitation · doi-reference

The regulation, functions and clinical relevance of arginine methylation

10.1038/s41580-019-0155-x · ExternalCitation · doi-reference

Loss of PRMT2 in myeloid cells in normoglycemic mice phenocopies impaired regression of atherosclerosis in diabetic mice

10.1038/s41598-022-15349-6 · ExternalCitation · doi-reference

PP2A-B55alpha controls keratinocyte adhesion through dephosphorylation of the Desmoplakin C-terminus

10.1038/s41598-023-37874-8 · ExternalCitation · doi-reference

S-adenosylhomocysteine as a methyl transfer catalyst in biocatalytic methylation reactions

10.1038/s41929-019-0300-0 · ExternalCitation · doi-reference

PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting retinoic acid signaling

10.1038/s42003-020-01644-3 · ExternalCitation · doi-reference

Molecular determinants of arginine versus lysine cation–π interactions in biomolecular condensates

10.1038/s42004-026-02075-7 · ExternalCitation · doi-reference

Protein arginine methyltransferase 1 (PRMT1) represses MHC II transcription in macrophages by methylating CIITA

10.1038/srep40531 · ExternalCitation · doi-reference

S-Adenosylmethionine: More than just a methyl donor

10.1039/d2np00086e · ExternalCitation · doi-reference

10.1039/d6np00006a

10.1039/d6np00006a · ExternalCitation · doi-reference

Effectors and effects of arginine methylation

10.1042/bst20221147 · ExternalCitation · doi-reference

SDMA as a marker and mediator in cerebrovascular disease

10.1042/cs20241021 · ExternalCitation · doi-reference

Tumor necrosis factor (TNF)-α induction of CXCL10 in endothelial cells requires protein arginine methyltransferase 5 (PRMT5)-mediated nuclear factor (NF)-κB p65 methylation

10.1074/jbc.m114.547349 · ExternalCitation · doi-reference

Histone H2A and H4 N-Terminal Tails Are Positioned by the MEP50 WD Repeat Protein for Efficient Methylation by the PRMT5 Arginine Methyltransferase

10.1074/jbc.m115.636894 · ExternalCitation · doi-reference

Protein Arginine Methyltransferase Product Specificity Is Mediated by Distinct Active-Site Architectures

10.1074/jbc.m116.740399 · ExternalCitation · doi-reference

MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase

10.1074/jbc.ra120.012934 · ExternalCitation · doi-reference

GSK3- and PRMT-1-dependent modifications of desmoplakin control desmoplakin-cytoskeleton dynamics

10.1083/jcb.201406020 · ExternalCitation · doi-reference

Cross-talk between Arg methylation and Ser phosphorylation modulates apoptosis signal-regulating kinase 1 activation in endothelial cells

10.1091/mbc.e15-10-0738 · ExternalCitation · doi-reference

Protein arginine methyltransferase 5-mediated arginine methylation stabilizes Kruppel-like factor 4 to accelerate neointimal formation

10.1093/cvr/cvad080 · ExternalCitation · doi-reference

Epigenetic regulation of vascular smooth muscle cell phenotypic switch and neointimal formation by PRMT5

10.1093/cvr/cvad110 · ExternalCitation · doi-reference

Vinculin phosphorylation impairs vascular endothelial junctions promoting atherosclerosis

10.1093/eurheartj/ehac647 · ExternalCitation · doi-reference

Staying true to yourself: Mechanisms of DNA methylation maintenance in mammals

10.1093/nar/gkaa1154 · ExternalCitation · doi-reference

The PRMT5/WDR77 complex regulates alternative splicing through ZNF326 in breast cancer

10.1093/nar/gkx727 · ExternalCitation · doi-reference

SCN5A channelopathy: Arrhythmia, cardiomyopathy, epilepsy and beyond

10.1098/rstb.2022.0164 · ExternalCitation · doi-reference

10.1101/2024.05.24.595777

10.1101/2024.05.24.595777 · ExternalCitation · doi-reference

S-adenosylmethionine: A metabolite critical to the regulation of autophagy

10.1111/cpr.12891 · ExternalCitation · doi-reference

Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors

10.1111/febs.13953 · ExternalCitation · doi-reference

Matrifibrocytes Redefine Cardiac Fibrosis: From Terminal Differentiation to Translational Modulation

10.1111/jcmm.71174 · ExternalCitation · doi-reference

Protein arginine methyltransferase 1, a major regulator of biological processes

10.1139/bcb-2023-0212 · ExternalCitation · doi-reference

The Role of Protein Arginine Methyltransferases in Inflammatory Responses

10.1155/2016/4028353 · ExternalCitation · doi-reference

Arginine Methylation of SREBP1a via PRMT5 Promotes De Novo Lipogenesis and Tumor Growth

10.1158/0008-5472.can-15-1766 · ExternalCitation · doi-reference

Admixture Mapping of Subclinical Atherosclerosis and Subsequent Clinical Events Among African Americans in 2 Large Cohort Studies

10.1161/circgenetics.116.001569 · ExternalCitation · doi-reference

Cardiac Nonmyocytes in the Hub of Cardiac Hypertrophy

10.1161/circresaha.117.305349 · ExternalCitation · doi-reference

PRMT5 Prevents Dilated Cardiomyopathy via Suppression of Protein O-GlcNAcylation

10.1161/circresaha.121.319456 · ExternalCitation · doi-reference

Kindlin-2 Phase Separation in Response to Flow Controls Vascular Stability

10.1161/circresaha.124.324773 · ExternalCitation · doi-reference

Epigenetic Regulation of Cardiomyocyte Maturation by Arginine Methyltransferase CARM1

10.1161/circulationaha.121.055738 · ExternalCitation · doi-reference

Immunomodulatory Therapy for Ischemic Heart Disease

10.1161/circulationaha.124.070368 · ExternalCitation · doi-reference

Macrophage PRMT9 Ameliorates Acute Myocardial Infarction by Promoting Symmetric Dimethylation and Degradation of STAT1

10.1161/circulationaha.125.076101 · ExternalCitation · doi-reference

Endothelial PRMT5 plays a crucial role in angiogenesis after acute ischemic injury

10.1172/jci.insight.152481 · ExternalCitation · doi-reference

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

10.1186/s12933-017-0569-8 · ExternalCitation · doi-reference

Asymmetric dimethylarginine (ADMA), symmetric dimethylarginine (SDMA) and homoarginine (hArg): The ADMA, SDMA and hArg paradoxes

10.1186/s12933-017-0656-x · ExternalCitation · doi-reference

TGF-β and WNT signaling pathways in cardiac fibrosis: Non-coding RNAs come into focus

10.1186/s12964-020-00555-4 · ExternalCitation · doi-reference

Intrafamily heterooligomerization as an emerging mechanism of methyltransferase regulation

10.1186/s13072-024-00530-0 · ExternalCitation · doi-reference

Crosstalk between metabolism and epigenetics during macrophage polarization

10.1186/s13072-025-00575-9 · ExternalCitation · doi-reference

Update of the Methyltransferase Gene Family: Classification, Evolution and Biological Functions

10.1186/s40246-026-00949-4 · ExternalCitation · doi-reference

Arginine methylation in cancer: Mechanisms and therapeutic implications

10.1186/s40364-025-00860-5 · ExternalCitation · doi-reference

10.1371/journal.pgen.1009641

10.1371/journal.pgen.1009641 · ExternalCitation · doi-reference

10.1371/journal.pone.0148905

10.1371/journal.pone.0148905 · ExternalCitation · doi-reference

10.1371/journal.pone.0193205

10.1371/journal.pone.0193205 · ExternalCitation · doi-reference

10.20944/preprints202409.1669.v1

10.20944/preprints202409.1669.v1 · ExternalCitation · doi-reference

Using Yeast to Define the Regulatory Role of Protein Lysine Methylation

10.2174/1389203720666191023150727 · ExternalCitation · doi-reference

Hypertensive Heart Disease: Mechanisms, Diagnosis and Treatment

10.31083/j.rcm2503093 · ExternalCitation · doi-reference

10.3389/fimmu.2020.584303

10.3389/fimmu.2020.584303 · ExternalCitation · doi-reference

10.3389/fimmu.2025.1663258

10.3389/fimmu.2025.1663258 · ExternalCitation · doi-reference

10.3389/fmolb.2024.1455415

10.3389/fmolb.2024.1455415 · ExternalCitation · doi-reference

10.3389/fonc.2022.841381

10.3389/fonc.2022.841381 · ExternalCitation · doi-reference

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10.3389/fphar.2020.600627 · ExternalCitation · doi-reference

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10.3389/fphar.2023.1264216 · ExternalCitation · doi-reference

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10.3389/fphys.2020.609733 · ExternalCitation · doi-reference

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10.3389/freae.2023.1245832 · ExternalCitation · doi-reference

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10.3390/cells10051079 · ExternalCitation · doi-reference

10.3390/cells11244060

10.3390/cells11244060 · ExternalCitation · doi-reference

10.3390/cells14110796

10.3390/cells14110796 · ExternalCitation · doi-reference

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10.3390/ijms20153668 · ExternalCitation · doi-reference

10.3390/ijms21218118

10.3390/ijms21218118 · ExternalCitation · doi-reference

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10.3390/ijms26167907 · ExternalCitation · doi-reference

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10.3390/ijms262210855 · ExternalCitation · doi-reference

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10.3390/life11080768 · ExternalCitation · doi-reference

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10.3390/life11090951 · ExternalCitation · doi-reference

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10.3390/life11111147 · ExternalCitation · doi-reference

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10.3390/life12030405 · ExternalCitation · doi-reference

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