PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7526387-0	1994	Formation of free nitric oxide from l-arginine by nitric oxide synthase: direct enhancement of generation by superoxide dismutase.	Arginine	36-46	superoxide dismutase 1	Homo sapiens	109-129	
7526387-7	1994	SOD appears to elicit a novel biological action, perhaps accelerating the conversion of an intermediate in the L-arginine-NO pathway such as nitroxyl (HNO) to NO.	Arginine	111-121	superoxide dismutase 1	Homo sapiens	0-3	
8066083-0	1994	The role of arginine 143 in the electrostatics and mechanism of Cu,Zn superoxide dismutase: computational and experimental evaluation by mutational analysis.	Arginine	12-20	superoxide dismutase 1	Homo sapiens	64-90	
8066083-14	1994	Results from this joint analysis establish that, aside from the Cu ligands, Arg-143 is the single most important residue in Cu,Zn superoxide dismutase both electrostatically and mechanistically, and provide an explanation for the evolutionary selection of arginine at position 143.	Arginine	76-79	superoxide dismutase 1	Homo sapiens	124-150	
2492791-20	1989	It appears that the positive charge of arginine-143 plays a role in the binding of HO2- at the active site of human Cu,ZnSOD, and that replacement of the arginine by lysine gives an enzyme with a similar affinity mechanism of inactivation, but with a greatly reduced affinity for HO2-.	Arginine	154-162	superoxide dismutase 1	Homo sapiens	116-124	
24369116-4	2014	Our results show considerable differences in H43R compared to WT and W32F mutated SOD1, such as increasing distances between the critical residues results in open conformation at the active site, strong fluctuations in the important loops (Zinc and electrostatic loops) and weakening of important hydrogen bonds especially between N (His 43/Arg 43) and carbonyl oxygen (His 120) in agreement with the experimental report.	Arginine	341-344	superoxide dismutase 1	Homo sapiens	82-86	
2492791-1	1989	Site-specific mutants of human Cu,Zn superoxide dismutase (Cu,ZnSOD) have been prepared in which the active-site arginine at position 143 (i.e., SODR143) has been replaced by either lysine (SODK143) or isoleucine (SODI143).	Arginine	113-121	superoxide dismutase 1	Homo sapiens	31-57	
2492791-1	1989	Site-specific mutants of human Cu,Zn superoxide dismutase (Cu,ZnSOD) have been prepared in which the active-site arginine at position 143 (i.e., SODR143) has been replaced by either lysine (SODK143) or isoleucine (SODI143).	Arginine	113-121	superoxide dismutase 1	Homo sapiens	59-67	
2492791-20	1989	It appears that the positive charge of arginine-143 plays a role in the binding of HO2- at the active site of human Cu,ZnSOD, and that replacement of the arginine by lysine gives an enzyme with a similar affinity mechanism of inactivation, but with a greatly reduced affinity for HO2-.	Arginine	39-47	superoxide dismutase 1	Homo sapiens	116-124	
32955857-3	2020	Mechanistic studies show that the catalysis consists of a three-step reaction: the oxidation of NADPH to produce O2- via oxidase-like activity, the subsequent dismutation of O2- to H2O2 via SOD-like activity, followed by H2O2-mediated oxidation of L-arginine to produce NO via a non-enzymatic pathway.	Arginine	248-258	superoxide dismutase 1	Homo sapiens	190-193	
30175262-8	2018	Compared with the DT group, the DT + Arg and DT + NCG groups manifested improved anti-hydroxyl radical, catalase, and total superoxide dismutase (T-SOD) activities, increased glutathione content (P < 0.05), and decreased malondialdehyde content (P < 0.05).	Arginine	37-40	superoxide dismutase 1	Homo sapiens	124-144	
30175262-9	2018	Moreover, compared with the DT group, the DT + Arg and DT + NCG groups enhanced mRNA expression of superoxide dismutase (SOD), glutathione peroxidase 1 (GPx1), glutathione reductase (GR), nuclear factor erythroid 2-related factor 2 (Nrf2), Kelch-like ECH-associated protein 1(Keap-1), and mammalian target of rapamycin (mTOR) (P < 0.05).	Arginine	47-50	superoxide dismutase 1	Homo sapiens	99-119	
30175262-9	2018	Moreover, compared with the DT group, the DT + Arg and DT + NCG groups enhanced mRNA expression of superoxide dismutase (SOD), glutathione peroxidase 1 (GPx1), glutathione reductase (GR), nuclear factor erythroid 2-related factor 2 (Nrf2), Kelch-like ECH-associated protein 1(Keap-1), and mammalian target of rapamycin (mTOR) (P < 0.05).	Arginine	47-50	superoxide dismutase 1	Homo sapiens	121-124	
25478411-4	2014	RESULTS: The cord serum NO levels (mumol/lt) showed a significant increase & SOD (U/ml) & GSH (U/lt) values were increased in newborns to mothers diagnosed with IUGR after treatment with L-arginine.	Arginine	195-205	superoxide dismutase 1	Homo sapiens	81-84	
3112154-1	1987	The active site arginine-143 of human Cu,Zn superoxide dismutase has been replaced by lysine or by isoleucine.	Arginine	16-24	superoxide dismutase 1	Homo sapiens	38-64	
3024961-1	1986	Quantum mechanical simulations of the mechanism of action of superoxide dismutase (SOD) indicate that the presence of Arg-141 in the active site of the enzyme is responsible for the formation of an intermediate complex between superoxide and the enzyme in which the copper is not reduced.	Arginine	118-121	superoxide dismutase 1	Homo sapiens	61-81	
3024961-1	1986	Quantum mechanical simulations of the mechanism of action of superoxide dismutase (SOD) indicate that the presence of Arg-141 in the active site of the enzyme is responsible for the formation of an intermediate complex between superoxide and the enzyme in which the copper is not reduced.	Arginine	118-121	superoxide dismutase 1	Homo sapiens	83-86	
32945480-7	2020	The results showed that, miR-30a-5p mimic reduced the production of ROS in HK-2 cells treated with H/R, but increased the activity of SOD, CAT and GPx.	Arginine	27-28	superoxide dismutase 1	Homo sapiens	134-137	
28705740-5	2017	Especially, the glutamine metabolic process related molecules, GPX1, GPX3, SMS, GGCT, GSTK1, NFkappaB, GSTT2, SOD1 and GCLM, are involved in the switching process from oxidized glutathione (GSSG) conversion to the reduced glutathione (GSH) by glutathione, mercapturic acid and arginine metabolism process.	Arginine	277-285	superoxide dismutase 1	Homo sapiens	110-114	
28035186-6	2016	Sequencing of the SOD1 gene by PCR revealed a missense mutation of G to C (c.37G>C) in exon 1, and amino acid substitution of glycine by arginine (p.Gly13Arg).	Arginine	140-148	superoxide dismutase 1	Homo sapiens	18-22	
27867347-12	2016	Furthermore, seeding the aggregation of DTT/EDTA-treated SOD1G37R with preformed SOD1G93A fibrils elicited minimal aggregation response, suggesting that the arginine substitution at position-37 blocks the templating of SOD1 onto preformed fibrils.	Arginine	157-165	superoxide dismutase 1	Homo sapiens	57-61	
19071212-3	2009	Albumin, fetal cord serum ultrafiltrate, and L-arginine triggered capacitation and ROS generation (NO* and O(2)(*)(-)) and superoxide dismutase (SOD) and NOS inhibitors prevented all these effects.	Arginine	45-55	superoxide dismutase 1	Homo sapiens	145-148	
24152914-6	2013	When Cu,Zn-SOD that has been exposed to acrolein was subsequently analyzed by amino acid analysis, serine, histidine, arginine, threonine and lysine residues were particularly sensitive.	Arginine	118-126	superoxide dismutase 1	Homo sapiens	11-14	
22264771-9	2012	Among the metabolites that contributed most to the CSF signature were arginine, lysine, ornithine, serine, threonine and pyroglutamic acid, all found to be reduced in patients carrying a D90A SOD1 mutation.	Arginine	70-78	superoxide dismutase 1	Homo sapiens	192-196	
22508683-4	2012	The CCS mutation, p.Arg163Trp, predicts substitution of a highly conserved arginine residue at position 163, with tryptophan in domain II of CCS, which interacts directly with superoxide dismutase 1 (SOD1).	Arginine	75-83	superoxide dismutase 1	Homo sapiens	176-198	
22508683-4	2012	The CCS mutation, p.Arg163Trp, predicts substitution of a highly conserved arginine residue at position 163, with tryptophan in domain II of CCS, which interacts directly with superoxide dismutase 1 (SOD1).	Arginine	75-83	superoxide dismutase 1	Homo sapiens	200-204	
20716909-0	2009	Oral administration of L-arginine in patients with angina or following myocardial infarction may be protective by increasing plasma superoxide dismutase and total thiols with reduction in serum cholesterol and xanthine oxidase.	Arginine	23-33	superoxide dismutase 1	Homo sapiens	132-152	
20716909-6	2009	We have observed that L-arginine administration (three grams per day for 15 days) resulted in increased activity of free radical scavenging enzyme superoxide dismutase (SOD) and increase in the levels of total thiols (T-SH) and ascorbic acid with concomitant decrease in lipid per-oxidation, carbonyl content, serum cholesterol and the activity of proxidant enzyme, xanthine oxidase (XO).	Arginine	22-32	superoxide dismutase 1	Homo sapiens	147-167	
20716909-6	2009	We have observed that L-arginine administration (three grams per day for 15 days) resulted in increased activity of free radical scavenging enzyme superoxide dismutase (SOD) and increase in the levels of total thiols (T-SH) and ascorbic acid with concomitant decrease in lipid per-oxidation, carbonyl content, serum cholesterol and the activity of proxidant enzyme, xanthine oxidase (XO).	Arginine	22-32	superoxide dismutase 1	Homo sapiens	169-172	
19243126-9	2009	In agreement, peroxymonocarbonate was docked into the hSod1 active site, where it interacted with the conserved Arg(143).	Arginine	112-115	superoxide dismutase 1	Homo sapiens	54-59	
19000626-5	2009	Direct sequencing of SOD1 gene revealed a heterozygous mutation in codon 22 substituting a highly conserved amino acid, from glutamine to arginine (Q22R).	Arginine	138-146	superoxide dismutase 1	Homo sapiens	21-25	
15096035-8	2004	The catalytic and structural role of His41 is consistent with the observation that the mutation of His43 in human SOD (equivalent to His41 in bovine SOD) to Arg largely reduces the dismutase activity and the protein structural stability.	Arginine	157-160	superoxide dismutase 1	Homo sapiens	114-117	
17042490-5	2006	The chelators also protected the SOD activity against inhibition by the arginine-specific reagent, phenylglyoxal.	Arginine	72-80	superoxide dismutase 1	Homo sapiens	33-36	
15096035-8	2004	The catalytic and structural role of His41 is consistent with the observation that the mutation of His43 in human SOD (equivalent to His41 in bovine SOD) to Arg largely reduces the dismutase activity and the protein structural stability.	Arginine	157-160	superoxide dismutase 1	Homo sapiens	149-152	
10912770-1	2000	Cardiovascular responses to L-arginine and nitric oxide (NO) are augmented in the rostral ventrolateral medulla (RVLM) of spontaneously hypertensive rats (SHR), and the intravenous injection of superoxide dismutase (SOD) mimetic decreases the arterial pressure in these rats.	Arginine	28-38	superoxide dismutase 1	Homo sapiens	216-219	
10912770-3	2000	For this purpose, we administered L-arginine (SHR-Arg: 13.2 micromol/day, n=6), a stable membrane-permeable SOD mimetic, 4-hydroxy-2, 2,6,6-tetramethyl piperidine-1-oxyl (tempol) (SHR-Temp: 13.2 micromol/day, n=6), or vehicle (SHR-C: n=6) into the lateral ventricle of 12-week-old SHR for 2 weeks.	Arginine	34-44	superoxide dismutase 1	Homo sapiens	108-111	
8962079-8	1996	SOD lowered the NADPH:Cit stoichiometry to 0.8-1.1, suggesting either that additional reducing equivalents besides NADPH are required to explain Arg oxidation to .NO or that .NO was not primarily formed.	Arginine	145-148	superoxide dismutase 1	Homo sapiens	0-3	
14658402-1	2003	We report the clinical and neuropathological features of a Japanese family with familial amyotrophic lateral sclerosis (FALS), whose members have an amino acid substitution of histidine by arginine in Cu/Zn superoxide dismutase.	Arginine	189-197	superoxide dismutase 1	Homo sapiens	201-227	
11036505-6	2000	Significantly higher CuZn superoxide dismutase (CuZn-SOD) activity was observed in the L-arginine + L-NAME group compared to arginine.	Arginine	87-97	superoxide dismutase 1	Homo sapiens	21-46	
11036505-6	2000	Significantly higher CuZn superoxide dismutase (CuZn-SOD) activity was observed in the L-arginine + L-NAME group compared to arginine.	Arginine	87-97	superoxide dismutase 1	Homo sapiens	48-56	
11036505-6	2000	Significantly higher CuZn superoxide dismutase (CuZn-SOD) activity was observed in the L-arginine + L-NAME group compared to arginine.	Arginine	89-97	superoxide dismutase 1	Homo sapiens	21-46	
11036505-6	2000	Significantly higher CuZn superoxide dismutase (CuZn-SOD) activity was observed in the L-arginine + L-NAME group compared to arginine.	Arginine	89-97	superoxide dismutase 1	Homo sapiens	48-56