PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33872411-5	2021	Our studies show that PRMT5 or MEP50 loss reduces H4R3me2s formation and that this is associated with reduced cancer cell spheroid formation, invasion, and migration.	h4r3me2s	50-58	protein arginine methyltransferase 5	Homo sapiens	22-27	
20495075-2	2010	We have previously demonstrated that symmetric methylation of histone H4 Arginine 3 (H4R3me2s) by the protein arginine methyltransferase PRMT5 is required for recruitment of the DNA methyltransferase DNMT3A to the gamma-promoter, and subsequent DNA methylation and gene silencing.	h4r3me2s	85-93	protein arginine methyltransferase 5	Homo sapiens	137-142	
19234465-2	2009	Using the human beta-globin locus as a model, we demonstrate that symmetric methylation of histone H4 arginine 3 (H4R3me2s) by the protein arginine methyltransferase PRMT5 is required for subsequent DNA methylation.	h4r3me2s	114-122	protein arginine methyltransferase 5	Homo sapiens	166-171	
32739156-5	2020	Intracellular H4R3me2s was significantly increased after treatment with the DNA oxidant reagent H2O2, and this increase was regulated by OGG1, which could directly interact with the specific arginine methyltransferase, PRMT5.	h4r3me2s	14-22	protein arginine methyltransferase 5	Homo sapiens	219-224	
32739429-5	2020	Prmt5 silencing or its inhibitor EPZ, or knockdown of cooperator of Prmt5 (Copr5) to disrupt H4R3me2s, facilitated cardiomyocyte hypertrophy, whereas overexpression of wild type Prmt5 rather than the inactive mutant protected cardiomyocytes against hypertrophy; 3.	h4r3me2s	93-101	protein arginine methyltransferase 5	Homo sapiens	68-73	
32739429-8	2020	CONCLUSIONS: the present study reveals that Prmt5-induced H4R3me2s ameliorates cardiomyocyte hypertrophy by transcriptional upregulation of Filip1L and subsequent enhancement of beta-catenin degradation.	h4r3me2s	58-66	protein arginine methyltransferase 5	Homo sapiens	44-49	
32739429-9	2020	Deficiency of Prmt5 and the resulting suppression of H4R3me2s might facilitate the development of pathological cardiac hypertrophy.	h4r3me2s	53-61	protein arginine methyltransferase 5	Homo sapiens	14-19	
30189247-2	2018	PRMT5 mediates symmetric di-methylation (sDMA) of arginine 2 (H3R2me2s) and arginine 8 on histone 3 (H3R8me2s), arginine 3 on histones 2A and 4 (H2A/H4R3me2s) as well as several non-histone substrates like Sm proteins.	h4r3me2s	149-157	protein arginine methyltransferase 5	Homo sapiens	0-5	
30858358-7	2019	Intriguingly, we found that NAA40 knockdown and loss of N-acH4 reduce the levels of symmetric dimethylation of histone H4 (H4R3me2s) through transcriptional downregulation of protein arginine methyltransferase 5 (PRMT5).	h4r3me2s	123-131	protein arginine methyltransferase 5	Homo sapiens	175-211	
30858358-7	2019	Intriguingly, we found that NAA40 knockdown and loss of N-acH4 reduce the levels of symmetric dimethylation of histone H4 (H4R3me2s) through transcriptional downregulation of protein arginine methyltransferase 5 (PRMT5).	h4r3me2s	123-131	protein arginine methyltransferase 5	Homo sapiens	213-218	
30930442-8	2019	Besides, Western blot assay results showed that 4 could reduce the H4R3me2s level in a dose-dependent manner, indicating that it could inhibit the activity of PRMT5 in cellular context.	h4r3me2s	67-75	protein arginine methyltransferase 5	Homo sapiens	159-164	
30257864-1	2018	Protein arginine methyltransferase 5 (PRMT5) is a member of the arginine methyltransferase protein family that critically mediates the symmetric dimethylation of Arg-3 at histone H4 (H4R3me2s) and is involved in many key cellular processes, including hematopoiesis.	h4r3me2s	183-191	protein arginine methyltransferase 5	Homo sapiens	0-36	
30257864-1	2018	Protein arginine methyltransferase 5 (PRMT5) is a member of the arginine methyltransferase protein family that critically mediates the symmetric dimethylation of Arg-3 at histone H4 (H4R3me2s) and is involved in many key cellular processes, including hematopoiesis.	h4r3me2s	183-191	protein arginine methyltransferase 5	Homo sapiens	38-43	
28854561-3	2017	We show that knockdown of PRMT5 or MEP50 results in reduced H4R3me2s formation, and reduced cell proliferation, invasion, migration and tumor formation.	h4r3me2s	60-68	protein arginine methyltransferase 5	Homo sapiens	26-31	
23749998-4	2013	These experiments revealed that two Mediator CDKs, CDK8 and CDK19, individually interact with PRMT5 and WDR77, and their interactions with PRMT5 cause transcriptional repression of C/EBPbeta target genes by regulating symmetric dimethylation of histone H4 arginine 3 (H4R3me2s) in the promoter regions of those genes.	h4r3me2s	268-276	protein arginine methyltransferase 5	Homo sapiens	94-99	
23749998-4	2013	These experiments revealed that two Mediator CDKs, CDK8 and CDK19, individually interact with PRMT5 and WDR77, and their interactions with PRMT5 cause transcriptional repression of C/EBPbeta target genes by regulating symmetric dimethylation of histone H4 arginine 3 (H4R3me2s) in the promoter regions of those genes.	h4r3me2s	268-276	protein arginine methyltransferase 5	Homo sapiens	139-144	
23048031-3	2012	We discovered that SC1 recruits the chromatin modifier PRMT5, an arginine methyltransferase that catalyzes symmetric dimethylation of histone H4 arginine 3 (H4R3me2s) and that this modification is preferentially associated with undifferentiated cortical NSCs.	h4r3me2s	157-165	protein arginine methyltransferase 5	Homo sapiens	55-60