PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
34041522-8	2021	Our results demonstrated that PRMT7 mRNA and protein levels in arrested embryos were significantly increased compared with those in control embryos; meanwhile, the methylation levels of H4R3me2s in arrested embryos were also increased significantly.	h4r3me2s	186-194	protein arginine methyltransferase 7	Homo sapiens	30-35
34911774-4	2022	Mechanistically, T cell deficiency of PRMT5 activated Prdm1 by decreasing H4R3me2s and H3R8me2s deposition on its loci, which promoted the differentiation of Klrg1+CD8+ T cells.	h4r3me2s	74-82	protein arginine N-methyltransferase 5	Mus musculus	38-43
34911774-4	2022	Mechanistically, T cell deficiency of PRMT5 activated Prdm1 by decreasing H4R3me2s and H3R8me2s deposition on its loci, which promoted the differentiation of Klrg1+CD8+ T cells.	h4r3me2s	74-82	PR domain containing 1, with ZNF domain	Mus musculus	54-59
34911774-4	2022	Mechanistically, T cell deficiency of PRMT5 activated Prdm1 by decreasing H4R3me2s and H3R8me2s deposition on its loci, which promoted the differentiation of Klrg1+CD8+ T cells.	h4r3me2s	74-82	killer cell lectin-like receptor subfamily G, member 1	Mus musculus	158-163
35500745-7	2022	Thus, our results indicate that PRMT5 mediated symmetric dimethylation at histone H4 arginine 3 (H4R3me2s) is crucial for preventing pathological polyploidization, liver cirrhosis and tumorigenesis in mouse liver.	h4r3me2s	97-105	protein arginine N-methyltransferase 5	Mus musculus	32-37
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	8-oxoguanine DNA glycosylase	Homo sapiens	137-141
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	coordinator of PRMT5 and differentiation stimulator	Homo sapiens	75-80
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
32739429-8	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	filamin A interacting protein 1 like	Homo sapiens	140-147
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	catenin beta 1	Homo sapiens	178-190
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
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
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	WD repeat domain 77	Homo sapiens	31-36
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
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	N-alpha-acetyltransferase 40, NatD catalytic subunit	Homo sapiens	28-33
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	H4 clustered histone 9	Homo sapiens	111-121
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
30660775-7	2019	Our results suggest that H4R3me2s generation by the type II PRMT Hsl7 is required for transcriptional repression, possibly in cooperation with histone deacetylation by Rpd3.	h4r3me2s	25-33	histone deacetylase RPD3	Saccharomyces cerevisiae S288C	168-172
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
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
26763441-4	2016	This protein interacts with a cofactor, methylosome protein 50 (MEP50), and symmetrically dimethylates arginine eight of histone 3 (H3R8me2s) and arginine three of histone 4 (H4R3me2s) to silence gene expression.	h4r3me2s	175-183	WD repeat domain 77	Homo sapiens	40-62
29409673-4	2018	First, to study the effects of OGG1 on histone modification, the protein levels of symmetric dimethylation of histone H4 arginine-3 (H4R3me2s) were determined by western blot analysis following the knockdown or overexpression of OGG1.	h4r3me2s	133-141	LOC102641229	Mus musculus	110-120
29409673-7	2018	We found that OGG1 affects PRMT5 binding on histone H4 and the formation of H4R3me2s via PRMT5.	h4r3me2s	76-84	8-oxoguanine DNA-glycosylase 1	Mus musculus	14-18
29409673-7	2018	We found that OGG1 affects PRMT5 binding on histone H4 and the formation of H4R3me2s via PRMT5.	h4r3me2s	76-84	protein arginine N-methyltransferase 5	Mus musculus	89-94
29409673-9	2018	Knockdown of OGG1 by siRNA led to a decrease in H4R3me2s, while overexpression of OGG1 increased the level of H4R3me2s.	h4r3me2s	48-56	8-oxoguanine DNA-glycosylase 1	Mus musculus	13-17
29409673-9	2018	Knockdown of OGG1 by siRNA led to a decrease in H4R3me2s, while overexpression of OGG1 increased the level of H4R3me2s.	h4r3me2s	110-118	8-oxoguanine DNA-glycosylase 1	Mus musculus	82-86
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
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	WD repeat domain 77	Homo sapiens	35-40
26763441-4	2016	This protein interacts with a cofactor, methylosome protein 50 (MEP50), and symmetrically dimethylates arginine eight of histone 3 (H3R8me2s) and arginine three of histone 4 (H4R3me2s) to silence gene expression.	h4r3me2s	175-183	WD repeat domain 77	Homo sapiens	64-69
26563484-5	2015	We show that both Myc and Omomyc stimulate histone H4 symmetric dimethylation of arginine (R) 3 (H4R3me2s), in human glioblastoma and HEK293T cells.	h4r3me2s	97-105	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	18-21
26072710-10	2015	Further study revealed that H4R3me2s was virtually absent in germ cells after Prmt5 inactivation.	h4r3me2s	28-36	protein arginine N-methyltransferase 5	Mus musculus	78-83
25810472-8	2015	Further study revealed that H4R3me2s was completely absent after Prmt5 inactivation, whereas the level of H3R2me2s was not changed in Prmt5-deficient germ cells.	h4r3me2s	28-36	protein arginine N-methyltransferase 5	Mus musculus	65-70
24097435-2	2014	Here, we show that the type-II protein arginine methyltransferase PRMT5 controls H4R3me2s in mouse embryonic fibroblasts (MEFs).	h4r3me2s	81-89	protein arginine N-methyltransferase 5	Mus musculus	66-71
24097435-10	2014	Furthermore, comparative bioinformatics analyses suggest a putative role of PRMT5-mediated H4R3me2s in chromatin configuration in the nucleus.	h4r3me2s	91-99	protein arginine N-methyltransferase 5	Mus musculus	76-81
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	cyclin dependent kinase 8	Homo sapiens	45-49
23249737-7	2012	The protein arginine methyltransferase 7 (PRMT7), but not PRMT5, represses MLL4 target genes by up-regulating H4R3me2s levels and antagonizes MLL4-mediated differentiation.	h4r3me2s	110-118	protein arginine methyltransferase 7	Homo sapiens	4-40
23249737-7	2012	The protein arginine methyltransferase 7 (PRMT7), but not PRMT5, represses MLL4 target genes by up-regulating H4R3me2s levels and antagonizes MLL4-mediated differentiation.	h4r3me2s	110-118	protein arginine methyltransferase 7	Homo sapiens	42-47
23249737-7	2012	The protein arginine methyltransferase 7 (PRMT7), but not PRMT5, represses MLL4 target genes by up-regulating H4R3me2s levels and antagonizes MLL4-mediated differentiation.	h4r3me2s	110-118	lysine methyltransferase 2B	Homo sapiens	75-79
23249737-9	2012	During differentiation, decreased H4R3me2s levels are associated with increased H3K4me3 levels at a cohort of genes, including many HOXA and HOXB genes.	h4r3me2s	34-42	homeobox A cluster	Homo sapiens	132-136
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
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	DNA methyltransferase 3 alpha	Homo sapiens	200-206
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
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	cyclin dependent kinase 8	Homo sapiens	51-55
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	cyclin dependent kinase 19	Homo sapiens	60-65
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	WD repeat domain 77	Homo sapiens	104-109
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
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	CCAAT enhancer binding protein beta	Homo sapiens	181-190
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	transcription factor 19	Homo sapiens	19-22
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