PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
16369774-0	2006	Elevations of plasma methylarginines in obesity and ageing are related to insulin sensitivity and rates of protein turnover.	methylarginines	21-36	insulin	Homo sapiens	74-81
15312771-1	2004	In mammals, the enzyme dimethylarginine dimethylaminohydrolase (DDAH) is implicated in the regulation of the cellular levels of asymmetric methylarginines, small molecule metabolites that themselves represent a family of endogenous inhibitors of nitric oxide synthase (NOS).	methylarginines	139-154	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	64-68
15574418-1	2005	The endogenous methylarginines asymmetric dimethylarginine (ADMA) and N(G)-monomethyl-L-arginine (L-NMMA) regulate nitric oxide (NO) production from neuronal NO synthase (nNOS).	methylarginines	15-30	nitric oxide synthase 1	Homo sapiens	171-175
16000003-1	2005	The enzyme DDAH metabolizes methylarginines that are inhibitors of nitric oxide synthase (NOS).	methylarginines	28-43	nitric oxide synthase 2	Homo sapiens	67-88
12523648-5	2002	Finally, amino acid analyses revealed that the modification of recombinant murine fibrillarin forms methylarginines, mostly as dimethylarginines.	methylarginines	100-115	fibrillarin	Mus musculus	82-93
10493931-2	1999	Cellular concentrations of methylarginines are determined in part by the activity of dimethylarginine dimethylaminohydrolase (DDAH; EC 3.5.3.	methylarginines	27-42	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	85-124
10691782-1	2000	Methylarginines are endogenous inhibitors of nitric oxide synthase (NOS) and have been implicated in the regulation of the nitric oxide pathway in health and disease.	methylarginines	0-15	nitric oxide synthase 2	Homo sapiens	45-66
10691782-2	2000	Cellular concentrations of free methylarginines are determined in part by the activity of dimethylarginine dimethylaminohydrolase (DDAH).	methylarginines	32-47	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	90-129
10691782-2	2000	Cellular concentrations of free methylarginines are determined in part by the activity of dimethylarginine dimethylaminohydrolase (DDAH).	methylarginines	32-47	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	131-135
10691782-6	2000	These data suggest that the key role for DDAH may be to ensure that under normal conditions the levels of methylarginines are kept low throughout the whole cell.	methylarginines	106-121	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	41-45
10493931-2	1999	Cellular concentrations of methylarginines are determined in part by the activity of dimethylarginine dimethylaminohydrolase (DDAH; EC 3.5.3.	methylarginines	27-42	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	126-130
29501774-5	2018	The Eno-1R50me was confirmed by its interaction with the tudor domain (TD) from TD-containing 3 (TDRD3) protein recognizing methylarginines.	methylarginines	124-139	tudor domain containing 3	Homo sapiens	97-102
34822417-2	2021	Methylarginines are biomarkers of cardiometabolic risk, liver steatosis, and insulin resistance.	methylarginines	0-15	insulin	Homo sapiens	77-84
31533264-5	2019	ADMA, MMA and symmetric dimethylarginine (SDMA) are also metabolized by alanine: glyoxylate aminotransferase 2 (AGXT2), however, in addition to methylarginines, this enzyme also has several cardiovascular protective substrates, so the net effect of possible therapeutic targeting of AGXT2 is currently unclear.	methylarginines	144-159	alanine--glyoxylate aminotransferase 2	Homo sapiens	72-110
31533264-5	2019	ADMA, MMA and symmetric dimethylarginine (SDMA) are also metabolized by alanine: glyoxylate aminotransferase 2 (AGXT2), however, in addition to methylarginines, this enzyme also has several cardiovascular protective substrates, so the net effect of possible therapeutic targeting of AGXT2 is currently unclear.	methylarginines	144-159	alanine--glyoxylate aminotransferase 2	Homo sapiens	112-117
28167521-13	2017	Our results show that the transcriptional regulator DdaR (PA1196) and the sigma factor RpoN positively regulate expression of dimethylarginine dimethylaminohydrolases (DDAHs) in response to exogenous methylarginines.	methylarginines	200-215	transcriptional regulator	Pseudomonas aeruginosa PAO1	58-64
23023372-0	2012	Alanine-glyoxylate aminotransferase-2 metabolizes endogenous methylarginines, regulates NO, and controls blood pressure.	methylarginines	61-76	alanine-glyoxylate aminotransferase 2	Mus musculus	0-37
28167521-0	2017	DdaR (PA1196) Regulates Expression of Dimethylarginine Dimethylaminohydrolase for the Metabolism of Methylarginines in Pseudomonas aeruginosa PAO1.	methylarginines	100-115	transcriptional regulator	Pseudomonas aeruginosa PAO1	6-12
28167521-8	2017	Both PA1196 and RpoN were essential for the expression of the ddaH gene in response to methylarginines.	methylarginines	87-102	transcriptional regulator	Pseudomonas aeruginosa PAO1	5-11
27979648-0	2017	Methylarginines within the RGG-Motif Region of hnRNP A1 Affect Its IRES Trans-Acting Factor Activity and Are Required for hnRNP A1 Stress Granule Localization and Formation.	methylarginines	0-15	heterogeneous nuclear ribonucleoprotein A1	Homo sapiens	47-55
27979648-0	2017	Methylarginines within the RGG-Motif Region of hnRNP A1 Affect Its IRES Trans-Acting Factor Activity and Are Required for hnRNP A1 Stress Granule Localization and Formation.	methylarginines	0-15	heterogeneous nuclear ribonucleoprotein A1	Homo sapiens	122-130
27752141-0	2016	Diabetes-linked transcription factor HNF4alpha regulates metabolism of endogenous methylarginines and beta-aminoisobutyric acid by controlling expression of alanine-glyoxylate aminotransferase 2.	methylarginines	82-97	hepatocyte nuclear factor 4 alpha	Homo sapiens	37-46
27752141-0	2016	Diabetes-linked transcription factor HNF4alpha regulates metabolism of endogenous methylarginines and beta-aminoisobutyric acid by controlling expression of alanine-glyoxylate aminotransferase 2.	methylarginines	82-97	alanine--glyoxylate aminotransferase 2	Homo sapiens	157-194
24586340-2	2014	Both methylarginines are substrates of alanine-glyoxylate aminotransferase 2 (AGXT2).	methylarginines	5-20	alanine--glyoxylate aminotransferase 2	Homo sapiens	39-76
24586340-2	2014	Both methylarginines are substrates of alanine-glyoxylate aminotransferase 2 (AGXT2).	methylarginines	5-20	alanine--glyoxylate aminotransferase 2	Homo sapiens	78-83
24586340-3	2014	It was the aim of the present study to simultaneously investigate the functional relevance and relative contributions of common AGXT2 single nucleotide polymorphisms (SNPs) to plasma and urinary concentrations of methylarginines as well as beta-aminoisobutyrate (BAIB), a prototypic substrate of AGXT2.	methylarginines	213-228	alanine--glyoxylate aminotransferase 2	Homo sapiens	128-133
23642268-7	2013	Three identified proteins: splicing factor, proline- and glutamine-rich (SFPQ), heterogeneous nuclear ribonucleoprotein D-like (hnRNP DL) and cellular nucleic acid binding protein (CNBP) are known to contain methylarginines in their glycine and arginine rich (GAR) sequences.	methylarginines	208-223	splicing factor proline and glutamine rich	Homo sapiens	27-71
23642268-7	2013	Three identified proteins: splicing factor, proline- and glutamine-rich (SFPQ), heterogeneous nuclear ribonucleoprotein D-like (hnRNP DL) and cellular nucleic acid binding protein (CNBP) are known to contain methylarginines in their glycine and arginine rich (GAR) sequences.	methylarginines	208-223	heterogeneous nuclear ribonucleoprotein D like	Homo sapiens	80-126
23642268-7	2013	Three identified proteins: splicing factor, proline- and glutamine-rich (SFPQ), heterogeneous nuclear ribonucleoprotein D-like (hnRNP DL) and cellular nucleic acid binding protein (CNBP) are known to contain methylarginines in their glycine and arginine rich (GAR) sequences.	methylarginines	208-223	heterogeneous nuclear ribonucleoprotein D like	Homo sapiens	128-136
23642268-7	2013	Three identified proteins: splicing factor, proline- and glutamine-rich (SFPQ), heterogeneous nuclear ribonucleoprotein D-like (hnRNP DL) and cellular nucleic acid binding protein (CNBP) are known to contain methylarginines in their glycine and arginine rich (GAR) sequences.	methylarginines	208-223	CCHC-type zinc finger nucleic acid binding protein	Homo sapiens	142-179
23642268-7	2013	Three identified proteins: splicing factor, proline- and glutamine-rich (SFPQ), heterogeneous nuclear ribonucleoprotein D-like (hnRNP DL) and cellular nucleic acid binding protein (CNBP) are known to contain methylarginines in their glycine and arginine rich (GAR) sequences.	methylarginines	208-223	CCHC-type zinc finger nucleic acid binding protein	Homo sapiens	181-185
23023372-9	2012	CONCLUSIONS: Although the effect of variation at rs37369 needs further study, these findings suggest that AGXT2 is an important regulator of methylarginines and represents a novel mechanism through which the kidney regulates blood pressure.	methylarginines	141-156	alanine-glyoxylate aminotransferase 2	Mus musculus	106-111
21777201-1	2012	Methylarginines have been shown to interfere with NO (nitric oxide) formation by inhibiting NOS (NO synthase)-ADMA (asymmetric dimethylarginine) and cellular L-arginine uptake into the cell [ADMA and SDMA (symmetric dimethylarginine)].	methylarginines	0-15	nitric oxide synthase 2	Homo sapiens	97-108
22997150-6	2012	To determine whether the identified Hmt1-interactors had the potential to act as an Hmt1 substrate, we used published bioinformatics algorithms that predict the presence and location of potential methylarginines for each identified interactor.	methylarginines	196-211	protein-arginine omega-N methyltransferase HMT1	Saccharomyces cerevisiae S288C	36-40
22997150-6	2012	To determine whether the identified Hmt1-interactors had the potential to act as an Hmt1 substrate, we used published bioinformatics algorithms that predict the presence and location of potential methylarginines for each identified interactor.	methylarginines	196-211	protein-arginine omega-N methyltransferase HMT1	Saccharomyces cerevisiae S288C	84-88
19820234-5	2009	The current study investigated the effects of both DDAH-1 and DDAH-2 in the regulation of methylarginines and endothelial NO generation.	methylarginines	90-105	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	51-57
21851090-4	2011	As a result of this interaction, PRMT2 stimulated PRMT1 activity, affecting its apparent V(max) and K(M) values in vitro and increasing the production of methylarginines in cells.	methylarginines	154-169	protein arginine methyltransferase 2	Homo sapiens	33-38
21851090-4	2011	As a result of this interaction, PRMT2 stimulated PRMT1 activity, affecting its apparent V(max) and K(M) values in vitro and increasing the production of methylarginines in cells.	methylarginines	154-169	protein arginine methyltransferase 1	Homo sapiens	50-55
19820234-3	2009	Decreased DDAH expression/activity is evident in disease states associated with endothelial dysfunction and is believed to be the mechanism responsible for increased methylarginines and subsequent ADMA-mediated endothelial nitric-oxide synthase impairment.	methylarginines	166-181	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	10-14
19820234-5	2009	The current study investigated the effects of both DDAH-1 and DDAH-2 in the regulation of methylarginines and endothelial NO generation.	methylarginines	90-105	dimethylarginine dimethylaminohydrolase 2	Homo sapiens	62-68
19917889-2	2009	Dimethylarginine dimethylaminohydrolase 1 (DDAH1) degrades asymmetrical methylarginines.	methylarginines	72-87	dimethylarginine dimethylaminohydrolase 1	Mus musculus	0-41
19917889-2	2009	Dimethylarginine dimethylaminohydrolase 1 (DDAH1) degrades asymmetrical methylarginines.	methylarginines	72-87	dimethylarginine dimethylaminohydrolase 1	Mus musculus	43-48
19917889-11	2009	In the context that asymmetric methylarginines are broadly produced by many type of cells, the strong DDAH1 expression in vascular endothelium demonstrates for the first time that vascular endothelium can be an important site to actively dispose of toxic biochemical molecules produced by other types of cells.	methylarginines	31-46	dimethylarginine dimethylaminohydrolase 1	Mus musculus	102-107
19682581-8	2009	Decreased DDAH expression/activity is evident in disease states associated with endothelial dysfunction and is believed to be the mechanism responsible for increased methylarginines and subsequent ADMA mediated eNOS impairment.	methylarginines	166-181	dimethylarginine dimethylaminohydrolase 1	Homo sapiens	10-14