PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
22657153-5	2013	Concentrations of homocysteine and H(2)S in the plasma of control MsrA(-/-) mice were significantly lower than those in control MsrA(+/+) mice.	Homocysteine	18-30	methionine sulfoxide reductase A	Mus musculus	66-70
22657153-5	2013	Concentrations of homocysteine and H(2)S in the plasma of control MsrA(-/-) mice were significantly lower than those in control MsrA(+/+) mice.	Hydrogen Sulfide	35-40	methionine sulfoxide reductase A	Mus musculus	66-70
22657153-6	2013	I/R reduced the levels of homocysteine and H(2)S in both MsrA(+/+) and MsrA(-/-) mice, and these reductions were significantly more profound in MsrA(-/-) than in MsrA(+/+) mice.	Homocysteine	26-38	methionine sulfoxide reductase A	Mus musculus	57-61
22657153-6	2013	I/R reduced the levels of homocysteine and H(2)S in both MsrA(+/+) and MsrA(-/-) mice, and these reductions were significantly more profound in MsrA(-/-) than in MsrA(+/+) mice.	Homocysteine	26-38	methionine sulfoxide reductase A	Mus musculus	71-75
22657153-6	2013	I/R reduced the levels of homocysteine and H(2)S in both MsrA(+/+) and MsrA(-/-) mice, and these reductions were significantly more profound in MsrA(-/-) than in MsrA(+/+) mice.	Homocysteine	26-38	methionine sulfoxide reductase A	Mus musculus	71-75
22657153-6	2013	I/R reduced the levels of homocysteine and H(2)S in both MsrA(+/+) and MsrA(-/-) mice, and these reductions were significantly more profound in MsrA(-/-) than in MsrA(+/+) mice.	Homocysteine	26-38	methionine sulfoxide reductase A	Mus musculus	71-75
22657153-6	2013	I/R reduced the levels of homocysteine and H(2)S in both MsrA(+/+) and MsrA(-/-) mice, and these reductions were significantly more profound in MsrA(-/-) than in MsrA(+/+) mice.	Hydrogen Sulfide	43-48	methionine sulfoxide reductase A	Mus musculus	57-61
22657153-6	2013	I/R reduced the levels of homocysteine and H(2)S in both MsrA(+/+) and MsrA(-/-) mice, and these reductions were significantly more profound in MsrA(-/-) than in MsrA(+/+) mice.	Hydrogen Sulfide	43-48	methionine sulfoxide reductase A	Mus musculus	71-75
22657153-6	2013	I/R reduced the levels of homocysteine and H(2)S in both MsrA(+/+) and MsrA(-/-) mice, and these reductions were significantly more profound in MsrA(-/-) than in MsrA(+/+) mice.	Hydrogen Sulfide	43-48	methionine sulfoxide reductase A	Mus musculus	71-75
22657153-6	2013	I/R reduced the levels of homocysteine and H(2)S in both MsrA(+/+) and MsrA(-/-) mice, and these reductions were significantly more profound in MsrA(-/-) than in MsrA(+/+) mice.	Hydrogen Sulfide	43-48	methionine sulfoxide reductase A	Mus musculus	71-75
22657153-9	2013	INNOVATION: The data provided herein constitute the first in vivo evidence for the involvement of MsrA in regulating methionine metabolism and the trans-sulfuration pathway under normal and I/R conditions.	Methionine	117-127	methionine sulfoxide reductase A	Mus musculus	98-102
22657153-11	2013	The data indicate that MsrA regulates H(2)S production during I/R by modulating the expression and activity of the CBS and CSE enzymes.	Hydrogen Sulfide	38-43	methionine sulfoxide reductase A	Mus musculus	23-27
22740506-0	2012	Protective effects of taurine against oxidative stress in the heart of MsrA knockout mice.	Taurine	22-29	methionine sulfoxide reductase A	Mus musculus	71-75
22740506-6	2012	However, the dysfunction was corrected in MsrA(-/-) mice treated with taurine supplement in the diet for 5 months.	Taurine	70-77	methionine sulfoxide reductase A	Mus musculus	42-46
22740506-8	2012	Our data indicated that cardiac myocytes from MsrA(-/-) mice treated with taurine exhibited an improved cell contraction and could tolerate oxidative stress better.	Taurine	74-81	methionine sulfoxide reductase A	Mus musculus	46-50
22740506-9	2012	Furthermore, taurine treatment reduced significantly the protein oxidation levels in mitochondria of MsrA(-/-) hearts, suggesting an anti-oxidant effect of taurine in cardiac mitochondria.	Taurine	13-20	methionine sulfoxide reductase A	Mus musculus	101-105
22740506-9	2012	Furthermore, taurine treatment reduced significantly the protein oxidation levels in mitochondria of MsrA(-/-) hearts, suggesting an anti-oxidant effect of taurine in cardiac mitochondria.	Taurine	156-163	methionine sulfoxide reductase A	Mus musculus	101-105
22081025-5	2011	Myocardial CaMKII inhibition, overexpression of methionine sulfoxide reductase A (an enzyme that reduces oxidized CaMKII) or NADPH oxidase deficiency prevented aldosterone-enhanced cardiac rupture after myocardial infarction.	Aldosterone	160-171	methionine sulfoxide reductase A	Mus musculus	48-80
22661718-1	2012	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	Reactive Oxygen Species	98-121	methionine sulfoxide reductase A	Mus musculus	0-32
22661718-1	2012	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	Methionine	164-174	methionine sulfoxide reductase A	Mus musculus	0-32
22661718-1	2012	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	methionine sulfoxide	179-199	methionine sulfoxide reductase A	Mus musculus	0-32
22661719-0	2012	A low pKa cysteine at the active site of mouse methionine sulfoxide reductase A.	Cysteine	10-18	methionine sulfoxide reductase A	Mus musculus	47-79
22661719-1	2012	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	Reactive Oxygen Species	98-121	methionine sulfoxide reductase A	Mus musculus	0-32
22661719-1	2012	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	Methionine	164-174	methionine sulfoxide reductase A	Mus musculus	0-32
22661719-1	2012	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	methionine sulfoxide	179-199	methionine sulfoxide reductase A	Mus musculus	0-32
20971073-1	2010	Methionine sulfoxide reductase A (MsrA) is an enzyme that reverses oxidation of methionine in proteins.	Methionine	80-90	methionine sulfoxide reductase A	Mus musculus	0-32
21841012-1	2011	Methionine sulfoxide reductase A (MsrA) catalytically scavenges reactive oxygen species and also repairs oxidized methionines in proteins.	Reactive Oxygen Species	64-87	methionine sulfoxide reductase A	Mus musculus	0-32
21841012-1	2011	Methionine sulfoxide reductase A (MsrA) catalytically scavenges reactive oxygen species and also repairs oxidized methionines in proteins.	Reactive Oxygen Species	64-87	methionine sulfoxide reductase A	Mus musculus	34-38
21841012-1	2011	Methionine sulfoxide reductase A (MsrA) catalytically scavenges reactive oxygen species and also repairs oxidized methionines in proteins.	Methionine	114-125	methionine sulfoxide reductase A	Mus musculus	0-32
21841012-1	2011	Methionine sulfoxide reductase A (MsrA) catalytically scavenges reactive oxygen species and also repairs oxidized methionines in proteins.	Methionine	114-125	methionine sulfoxide reductase A	Mus musculus	34-38
21841012-3	2011	A single gene encodes MsrA of which ~25% is targeted to the mitochondria, a major site of reactive oxygen species production.	Reactive Oxygen Species	90-113	methionine sulfoxide reductase A	Mus musculus	22-26
21696616-3	2011	MsrA, the only enzyme in the Msr gene family that can reduce the S-form epimers of methionine sulfoxide, has been located in different cellular compartments including mitochondria, cytosol and nuclei of various cell lines.	methionine sulfoxide	83-103	methionine sulfoxide reductase A	Mus musculus	0-4
21696616-7	2011	CONCLUSION: One possibility for the existence of a truncated form of the MsrA transcripts could be that with a smaller protein size, yet retaining a GCWFG action site, this protein might have easier access to oxidize methionine residues on proteins than the longer form of the MsrA protein, thus having an evolutionary selection advantage.	Methionine	217-227	methionine sulfoxide reductase A	Mus musculus	73-77
21696616-7	2011	CONCLUSION: One possibility for the existence of a truncated form of the MsrA transcripts could be that with a smaller protein size, yet retaining a GCWFG action site, this protein might have easier access to oxidize methionine residues on proteins than the longer form of the MsrA protein, thus having an evolutionary selection advantage.	Methionine	217-227	methionine sulfoxide reductase A	Mus musculus	277-281
21362417-2	2011	The results showed that the contents of methionine sulfoxide (MetO), protein carbonyl (PC) and Malondialdehyde (MDA) in the lenses of STZ-induced diabetic mice after 14 days were significantly higher than that in the normal control, level of total sulfhydryl groups (TSH) was 60% of normal control, and mRNA expressing levels of the MsrA and MsrBs were significantly decreased compared with normal group, as was the expression of MsrB1 protein.	Streptozocin	134-137	methionine sulfoxide reductase A	Mus musculus	333-337
21219974-0	2011	Quantification of reserve pool dopamine in methionine sulfoxide reductase A null mice.	Dopamine	31-39	methionine sulfoxide reductase A	Mus musculus	43-75
21219974-1	2011	Methionine sulfoxide reductase A knockout (MsrA-/-) mice, which serve as a potential model for neurodegeneration, suffer from increased oxidative stress and have previously been found to have chronically elevated brain dopamine (DA) content levels relative to control mice.	Dopamine	219-227	methionine sulfoxide reductase A	Mus musculus	0-32
22332004-1	2011	Previously, we have showed that overexpression of methionine-oxidized alpha-synuclein in methionine sulfoxide reductase A (MsrA) null mutant yeast cells inhibits alpha-synuclein phosphorylation and increases protein fibrillation.	Methionine	50-60	methionine sulfoxide reductase A	Mus musculus	89-121
22332004-2	2011	The current studies show that ablation of mouse MsrA gene caused enhanced methionine oxidation of alpha-synuclein while reducing its own phophorylation levels, especially in the hydrophobic cell-extracted fraction.	Methionine	74-84	methionine sulfoxide reductase A	Mus musculus	48-52
21219974-1	2011	Methionine sulfoxide reductase A knockout (MsrA-/-) mice, which serve as a potential model for neurodegeneration, suffer from increased oxidative stress and have previously been found to have chronically elevated brain dopamine (DA) content levels relative to control mice.	Dopamine	219-227	methionine sulfoxide reductase A	Mus musculus	43-51
21219974-1	2011	Methionine sulfoxide reductase A knockout (MsrA-/-) mice, which serve as a potential model for neurodegeneration, suffer from increased oxidative stress and have previously been found to have chronically elevated brain dopamine (DA) content levels relative to control mice.	Dopamine	229-231	methionine sulfoxide reductase A	Mus musculus	0-32
21219974-1	2011	Methionine sulfoxide reductase A knockout (MsrA-/-) mice, which serve as a potential model for neurodegeneration, suffer from increased oxidative stress and have previously been found to have chronically elevated brain dopamine (DA) content levels relative to control mice.	Dopamine	229-231	methionine sulfoxide reductase A	Mus musculus	43-51
20971073-1	2010	Methionine sulfoxide reductase A (MsrA) is an enzyme that reverses oxidation of methionine in proteins.	Methionine	80-90	methionine sulfoxide reductase A	Mus musculus	34-38
20971073-4	2010	However, the cellular contractility, when stressed using a higher stimulation frequency (2Hz), is significantly reduced in MsrA(-/-) cardiac myocytes.	(2z)-3-(3'-Nitrobiphenyl-3-Yl)prop-2-Enoic Acid	89-92	methionine sulfoxide reductase A	Mus musculus	123-127
20971073-6	2010	Corresponding changes in Ca(2+) transients are observed in MsrA(-/-) cardiomyocytes treated with 2Hz stimulation or with H(2)O(2).	(2z)-3-(3'-Nitrobiphenyl-3-Yl)prop-2-Enoic Acid	97-100	methionine sulfoxide reductase A	Mus musculus	59-63
20971073-6	2010	Corresponding changes in Ca(2+) transients are observed in MsrA(-/-) cardiomyocytes treated with 2Hz stimulation or with H(2)O(2).	Water	121-126	methionine sulfoxide reductase A	Mus musculus	59-63
20368336-1	2010	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system, which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	Reactive Oxygen Species	99-122	methionine sulfoxide reductase A	Mus musculus	0-32
20506347-1	2010	Methionine sulfoxide reductase A (MsrA), a member of the Msr gene family, can reduce methionine sulfoxide residues in proteins formed by oxidation of methionine by reactive oxygen species (ROS).	Reactive Oxygen Species	164-187	methionine sulfoxide reductase A	Mus musculus	0-32
20506347-1	2010	Methionine sulfoxide reductase A (MsrA), a member of the Msr gene family, can reduce methionine sulfoxide residues in proteins formed by oxidation of methionine by reactive oxygen species (ROS).	Reactive Oxygen Species	164-187	methionine sulfoxide reductase A	Mus musculus	34-38
20506347-1	2010	Methionine sulfoxide reductase A (MsrA), a member of the Msr gene family, can reduce methionine sulfoxide residues in proteins formed by oxidation of methionine by reactive oxygen species (ROS).	Reactive Oxygen Species	189-192	methionine sulfoxide reductase A	Mus musculus	0-32
20506347-1	2010	Methionine sulfoxide reductase A (MsrA), a member of the Msr gene family, can reduce methionine sulfoxide residues in proteins formed by oxidation of methionine by reactive oxygen species (ROS).	Reactive Oxygen Species	189-192	methionine sulfoxide reductase A	Mus musculus	34-38
20506347-5	2010	To confirm the protective function of MsrA in ESCs against oxidative stress, a siRNA approach has been used to knockdown MsrA expression in ES cells which showed less resistance than control cells to hydrogen peroxide treatment.	Hydrogen Peroxide	200-217	methionine sulfoxide reductase A	Mus musculus	121-125
20506347-6	2010	Overexpression of MsrA gene products in ES cells showed improved survivability of these cells to hydrogen peroxide treatment.	Hydrogen Peroxide	97-114	methionine sulfoxide reductase A	Mus musculus	18-22
20506347-0	2010	Methionine sulfoxide reductase A (MsrA) protects cultured mouse embryonic stem cells from H2O2-mediated oxidative stress.	Hydrogen Peroxide	90-94	methionine sulfoxide reductase A	Mus musculus	0-32
20506347-0	2010	Methionine sulfoxide reductase A (MsrA) protects cultured mouse embryonic stem cells from H2O2-mediated oxidative stress.	Hydrogen Peroxide	90-94	methionine sulfoxide reductase A	Mus musculus	34-38
20506347-1	2010	Methionine sulfoxide reductase A (MsrA), a member of the Msr gene family, can reduce methionine sulfoxide residues in proteins formed by oxidation of methionine by reactive oxygen species (ROS).	methionine sulfoxide	85-105	methionine sulfoxide reductase A	Mus musculus	0-32
20506347-1	2010	Methionine sulfoxide reductase A (MsrA), a member of the Msr gene family, can reduce methionine sulfoxide residues in proteins formed by oxidation of methionine by reactive oxygen species (ROS).	methionine sulfoxide	85-105	methionine sulfoxide reductase A	Mus musculus	34-38
20506347-1	2010	Methionine sulfoxide reductase A (MsrA), a member of the Msr gene family, can reduce methionine sulfoxide residues in proteins formed by oxidation of methionine by reactive oxygen species (ROS).	Methionine	85-95	methionine sulfoxide reductase A	Mus musculus	0-32
20506347-1	2010	Methionine sulfoxide reductase A (MsrA), a member of the Msr gene family, can reduce methionine sulfoxide residues in proteins formed by oxidation of methionine by reactive oxygen species (ROS).	Methionine	85-95	methionine sulfoxide reductase A	Mus musculus	34-38
20510353-3	2010	Methionine sulfoxide reductase A acts on the S-epimer of methionine sulfoxide, and it is known that altering its cellular level by genetic ablation or overexpression has notable effects on resistance to oxidative stress and on life span in species from microorganisms to animals.	methionine sulfoxide	57-77	methionine sulfoxide reductase A	Mus musculus	0-32
20368336-1	2010	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system, which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	Methionine	165-175	methionine sulfoxide reductase A	Mus musculus	0-32
20368336-1	2010	Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system, which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide.	methionine sulfoxide	180-200	methionine sulfoxide reductase A	Mus musculus	0-32
19487311-1	2009	Methionine sulfoxide reductase A (MsrA) repairs oxidized methionine residues within proteins and may also function as a general antioxidant.	Methionine	57-67	methionine sulfoxide reductase A	Mus musculus	0-32
19733220-0	2009	Methionine sulfoxide reductase A (MsrA) restores alpha-crystallin chaperone activity lost upon methionine oxidation.	Methionine	95-105	methionine sulfoxide reductase A	Mus musculus	0-32
19733220-0	2009	Methionine sulfoxide reductase A (MsrA) restores alpha-crystallin chaperone activity lost upon methionine oxidation.	Methionine	95-105	methionine sulfoxide reductase A	Mus musculus	34-38
19733220-2	2009	Two proteins that cause cataract when deleted from the lens are methionine sulfoxide reductase A (MsrA) that repairs protein methionine sulfoxide (PMSO) oxidized proteins and alpha-crystallin which is a two-subunit (alphaA and alphaB) chaperone.	methionine sulfoxide	64-84	methionine sulfoxide reductase A	Mus musculus	98-102
19733220-2	2009	Two proteins that cause cataract when deleted from the lens are methionine sulfoxide reductase A (MsrA) that repairs protein methionine sulfoxide (PMSO) oxidized proteins and alpha-crystallin which is a two-subunit (alphaA and alphaB) chaperone.	pmso	147-151	methionine sulfoxide reductase A	Mus musculus	64-96
19733220-2	2009	Two proteins that cause cataract when deleted from the lens are methionine sulfoxide reductase A (MsrA) that repairs protein methionine sulfoxide (PMSO) oxidized proteins and alpha-crystallin which is a two-subunit (alphaA and alphaB) chaperone.	pmso	147-151	methionine sulfoxide reductase A	Mus musculus	98-102
19733220-9	2009	MsrA treatment of PMSO-alpha-crystallin repaired its chaperone activity through reduction of PMSO.	pmso	18-22	methionine sulfoxide reductase A	Mus musculus	0-4
19733220-11	2009	CONCLUSIONS: Methionine oxidation damages alpha-crystallin chaperone function and MsrA can repair PMSO-alpha-crystallin restoring its chaperone function.	pmso-alpha-crystallin	98-119	methionine sulfoxide reductase A	Mus musculus	82-86
19733220-12	2009	MsrA is required for maintaining the reduced state of alpha-crystallin methionines in the lens.	Methionine	71-82	methionine sulfoxide reductase A	Mus musculus	0-4
19769460-1	2010	Methionine residues are susceptible to oxidation, but this damage may be reversed by methionine sulfoxide reductases MsrA and MsrB.	Methionine	0-10	methionine sulfoxide reductase A	Mus musculus	117-121
19854239-4	2010	Previously, we have shown that MsrA(-/-) mice exhibit altered locomotor activity and brain dopamine levels as function of age.	Dopamine	91-99	methionine sulfoxide reductase A	Mus musculus	31-35
19854239-10	2010	This differs from the abnormal dopamine levels previously observed in MsrA(-/-) mice fed ad-libitum.	Dopamine	31-39	methionine sulfoxide reductase A	Mus musculus	70-74
19487311-4	2009	We show here that MsrA(-/-) mice are more susceptible to oxidative stress induced by paraquat.	Paraquat	85-93	methionine sulfoxide reductase A	Mus musculus	18-22
19487311-1	2009	Methionine sulfoxide reductase A (MsrA) repairs oxidized methionine residues within proteins and may also function as a general antioxidant.	Methionine	57-67	methionine sulfoxide reductase A	Mus musculus	34-38
19633607-2	2009	The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which reduce the R- and the S- forms of MetO, respectively.	methionine sulfoxide	4-24	methionine sulfoxide reductase A	Mus musculus	170-174
19633607-2	2009	The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which reduce the R- and the S- forms of MetO, respectively.	methionine sulfoxide	83-87	methionine sulfoxide reductase A	Mus musculus	170-174
19633607-2	2009	The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which reduce the R- and the S- forms of MetO, respectively.	Methionine	4-14	methionine sulfoxide reductase A	Mus musculus	170-174
19633607-4	2009	Additionally, new data about the levels of selenium in brain, liver, and kidneys of WT and MsrA(-)/(-) mice are presented and discussed.	Selenium	43-51	methionine sulfoxide reductase A	Mus musculus	91-95
18697736-0	2008	Mammals reduce methionine-S-sulfoxide with MsrA and are unable to reduce methionine-R-sulfoxide, and this function can be restored with a yeast reductase.	L-Methionine (S)-S-oxide	15-37	methionine sulfoxide reductase A	Mus musculus	43-47
18990697-2	2009	Methionine residues are particularly susceptible to oxidation, but the resulting mixture of methionine R-sulfoxide (Met-RO) and methionine S-sulfoxide (Met-SO) can be repaired by thioredoxin-dependent enzymes MsrB and MsrA, respectively.	Methionine	0-10	methionine sulfoxide reductase A	Mus musculus	218-222
18697736-6	2008	Only methionine-R-sulfoxide was detected in the plasma of wild type mice, but both sulfoxides were in the plasma of MsrA knock-out mice.	Sulfoxides	83-93	methionine sulfoxide reductase A	Mus musculus	116-120
18697736-7	2008	These results show that mammals can support methionine metabolism by reduction of methionine-S-sulfoxide, that this process is dependent on MsrA, that mammals are inherently deficient in the reduction of methionine-R-sulfoxide, and that expression of yeast free methionine-R-sulfoxide reductase can fully compensate for this deficiency.	Methionine	44-54	methionine sulfoxide reductase A	Mus musculus	140-144
19461988-7	2009	Methionine-specific CNBr cleavage was used to differentiate oxidized and un-oxidized methionines in cyt c in vitro and the ability of MsrA to restore the activity of oxidized cyt c was evaluated.	Methionine	0-10	methionine sulfoxide reductase A	Mus musculus	134-138
19461988-11	2009	In vitro analysis of oxidized cyt c revealed the presence of two oxidized methionines (met 65 and met 80) that were repairable by MsrA.	Methionine	74-85	methionine sulfoxide reductase A	Mus musculus	130-134
18990697-2	2009	Methionine residues are particularly susceptible to oxidation, but the resulting mixture of methionine R-sulfoxide (Met-RO) and methionine S-sulfoxide (Met-SO) can be repaired by thioredoxin-dependent enzymes MsrB and MsrA, respectively.	methionine r-sulfoxide	92-114	methionine sulfoxide reductase A	Mus musculus	218-222
18990697-2	2009	Methionine residues are particularly susceptible to oxidation, but the resulting mixture of methionine R-sulfoxide (Met-RO) and methionine S-sulfoxide (Met-SO) can be repaired by thioredoxin-dependent enzymes MsrB and MsrA, respectively.	met-ro	116-122	methionine sulfoxide reductase A	Mus musculus	218-222
18990697-2	2009	Methionine residues are particularly susceptible to oxidation, but the resulting mixture of methionine R-sulfoxide (Met-RO) and methionine S-sulfoxide (Met-SO) can be repaired by thioredoxin-dependent enzymes MsrB and MsrA, respectively.	methionine s-sulfoxide	128-150	methionine sulfoxide reductase A	Mus musculus	218-222
18990697-2	2009	Methionine residues are particularly susceptible to oxidation, but the resulting mixture of methionine R-sulfoxide (Met-RO) and methionine S-sulfoxide (Met-SO) can be repaired by thioredoxin-dependent enzymes MsrB and MsrA, respectively.	methionine sulfoxide	152-158	methionine sulfoxide reductase A	Mus musculus	218-222
17364942-0	2007	Prolonged selenium-deficient diet in MsrA knockout mice causes enhanced oxidative modification to proteins and affects the levels of antioxidant enzymes in a tissue-specific manner.	Selenium	10-18	methionine sulfoxide reductase A	Mus musculus	37-41
18466776-0	2008	MsrA knockout mouse exhibits abnormal behavior and brain dopamine levels.	Dopamine	57-65	methionine sulfoxide reductase A	Mus musculus	0-4
18466776-6	2008	Furthermore, MsrA(-/-) mice were less responsive to amphetamine treatment.	Amphetamine	52-63	methionine sulfoxide reductase A	Mus musculus	13-17
18466776-8	2008	Surprisingly, relative to wild-type mice, MsrA(-/-) brains contained significantly higher levels of dopamine up to 12 months of age, while lower levels of dopamine were observed at 16 months of age.	Dopamine	100-108	methionine sulfoxide reductase A	Mus musculus	42-46
18466776-9	2008	Moreover, striatal regions of MsrA(-/-) mice showed an increase of dopamine release parallel to observed dopamine levels.	Dopamine	67-75	methionine sulfoxide reductase A	Mus musculus	30-34
18466776-9	2008	Moreover, striatal regions of MsrA(-/-) mice showed an increase of dopamine release parallel to observed dopamine levels.	Dopamine	105-113	methionine sulfoxide reductase A	Mus musculus	30-34
18466776-11	2008	Thus, it is suggested that dopamine regulation and signaling pathways are impaired in MsrA(-/-) mice, which may contribute to their abnormal behavior.	Dopamine	27-35	methionine sulfoxide reductase A	Mus musculus	86-90
17333008-6	2007	Also, a comparison between cultured brain slices of the hippocampal region of both mouse strains showed more sensitivity of the MsrA ( -/- ) cultured cells to H(2)O(2) treatment.	h(2)o	159-164	methionine sulfoxide reductase A	Mus musculus	128-132
17333008-7	2007	It is suggested that a deficiency in MsrA activity fosters oxidative-stress that is manifested by the accumulation of faulty proteins (via methionine oxidation), deposition of aggregated proteins, and premature brain cell death.	Methionine	139-149	methionine sulfoxide reductase A	Mus musculus	37-41
17625247-2	2007	MetO is reduced back to methionine by the methionine sulfoxide reductases MsrA and MsrB.	Methionine	24-34	methionine sulfoxide reductase A	Mus musculus	74-78
17364942-1	2007	The methionine sulfoxide reductase (Msr) system (comprised of MsrA and MsrB) is responsible for reducing methionine sulfoxide (MetO) to methionine.	methionine sulfoxide	4-24	methionine sulfoxide reductase A	Mus musculus	62-66
17364942-1	2007	The methionine sulfoxide reductase (Msr) system (comprised of MsrA and MsrB) is responsible for reducing methionine sulfoxide (MetO) to methionine.	methionine sulfoxide	127-131	methionine sulfoxide reductase A	Mus musculus	62-66
17364942-1	2007	The methionine sulfoxide reductase (Msr) system (comprised of MsrA and MsrB) is responsible for reducing methionine sulfoxide (MetO) to methionine.	Methionine	4-14	methionine sulfoxide reductase A	Mus musculus	62-66
17364942-3	2007	Following prolonged selenium deficient diet (SD), through F2 generation, the MsrA -/- mice exhibited higher protein-MetO and carbonyl levels relative to their wild-type (WT) control in most organs.	Selenium	20-28	methionine sulfoxide reductase A	Mus musculus	77-81
17364942-7	2007	In summary, it is suggested that the lack of the MsrA gene in conjunction with prolonged SD diet causes decreased antioxidant capability and enhanced protein oxidation.	SD 0006	89-91	methionine sulfoxide reductase A	Mus musculus	49-53
17105189-5	2006	We also generated a selenoprotein form of mouse MsrA and found that the presence of Sec increased the activity of this enzyme when a resolving Cys was mutated in the protein.	Cysteine	143-146	methionine sulfoxide reductase A	Mus musculus	48-52
15924425-1	2005	Oxidized forms of methionine residues in proteins can be repaired by methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide reductase (MsrB).	Methionine	18-28	methionine sulfoxide reductase A	Mus musculus	69-101
17105189-4	2006	We characterized the selenocysteine (Sec)-containing Chlamydomonas MsrA and found that this protein exhibited 10-50-fold higher activity than either its cysteine (Cys) mutant form or the natural mouse Cys-containing MsrA, making this selenoenzyme the most efficient MsrA known.	Selenocysteine	21-35	methionine sulfoxide reductase A	Mus musculus	67-71
17105189-4	2006	We characterized the selenocysteine (Sec)-containing Chlamydomonas MsrA and found that this protein exhibited 10-50-fold higher activity than either its cysteine (Cys) mutant form or the natural mouse Cys-containing MsrA, making this selenoenzyme the most efficient MsrA known.	Selenocysteine	21-35	methionine sulfoxide reductase A	Mus musculus	216-220
17105189-4	2006	We characterized the selenocysteine (Sec)-containing Chlamydomonas MsrA and found that this protein exhibited 10-50-fold higher activity than either its cysteine (Cys) mutant form or the natural mouse Cys-containing MsrA, making this selenoenzyme the most efficient MsrA known.	Selenocysteine	21-35	methionine sulfoxide reductase A	Mus musculus	216-220
17105189-4	2006	We characterized the selenocysteine (Sec)-containing Chlamydomonas MsrA and found that this protein exhibited 10-50-fold higher activity than either its cysteine (Cys) mutant form or the natural mouse Cys-containing MsrA, making this selenoenzyme the most efficient MsrA known.	Cysteine	27-35	methionine sulfoxide reductase A	Mus musculus	67-71
17105189-4	2006	We characterized the selenocysteine (Sec)-containing Chlamydomonas MsrA and found that this protein exhibited 10-50-fold higher activity than either its cysteine (Cys) mutant form or the natural mouse Cys-containing MsrA, making this selenoenzyme the most efficient MsrA known.	Cysteine	27-35	methionine sulfoxide reductase A	Mus musculus	216-220
17105189-4	2006	We characterized the selenocysteine (Sec)-containing Chlamydomonas MsrA and found that this protein exhibited 10-50-fold higher activity than either its cysteine (Cys) mutant form or the natural mouse Cys-containing MsrA, making this selenoenzyme the most efficient MsrA known.	Cysteine	27-35	methionine sulfoxide reductase A	Mus musculus	216-220
17105189-4	2006	We characterized the selenocysteine (Sec)-containing Chlamydomonas MsrA and found that this protein exhibited 10-50-fold higher activity than either its cysteine (Cys) mutant form or the natural mouse Cys-containing MsrA, making this selenoenzyme the most efficient MsrA known.	Cysteine	163-166	methionine sulfoxide reductase A	Mus musculus	67-71
17105189-4	2006	We characterized the selenocysteine (Sec)-containing Chlamydomonas MsrA and found that this protein exhibited 10-50-fold higher activity than either its cysteine (Cys) mutant form or the natural mouse Cys-containing MsrA, making this selenoenzyme the most efficient MsrA known.	Cysteine	201-204	methionine sulfoxide reductase A	Mus musculus	67-71
15924425-1	2005	Oxidized forms of methionine residues in proteins can be repaired by methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide reductase (MsrB).	Methionine	18-28	methionine sulfoxide reductase A	Mus musculus	103-107
12792026-1	2003	Mammals contain two methionine sulfoxide (MetO) reductases, MsrA and MsrB, that catalyze the thioredoxin-dependent reduction of the S-MetO and R-MetO derivatives, respectively, to methionine.	Methionine	20-30	methionine sulfoxide reductase A	Mus musculus	60-64
15043713-12	2004	We also show in a knockout mouse for methionine sulfoxide reductase (MsrA), the enzyme responsible for reducing methionine sulfoxide back to methionine, and a regulator of cellular antioxidant defence, that following hyperoxia brain PrPc in the null mutant is elevated relative to PrPc content in the parent strain.	methionine sulfoxide	37-57	methionine sulfoxide reductase A	Mus musculus	69-73
15043713-12	2004	We also show in a knockout mouse for methionine sulfoxide reductase (MsrA), the enzyme responsible for reducing methionine sulfoxide back to methionine, and a regulator of cellular antioxidant defence, that following hyperoxia brain PrPc in the null mutant is elevated relative to PrPc content in the parent strain.	Methionine	37-47	methionine sulfoxide reductase A	Mus musculus	69-73
12792026-4	2003	Moreover, mice that were grown on a selenium-deficient (SD) diet showed a substantial decrease in the levels of MsrB-catalytic activity, MsrB protein, and MsrB mRNA in liver and kidney tissues of both WT and MsrA-/- mouse strains.	Selenium	36-44	methionine sulfoxide reductase A	Mus musculus	208-212
11338182-2	2001	On average, there was a 60% reduction in the uptake of Cy3-fA beta in microglia from the MSR-A-/- mice.	cy3-fa beta	55-66	methionine sulfoxide reductase A	Mus musculus	89-94
11779133-1	2002	Many organisms have been shown to possess a methionine sulfoxide reductase (MsrA), exhibiting high specificity for reduction the S form of free and protein-bound methionine sulfoxide to methionine.	methionine sulfoxide	44-64	methionine sulfoxide reductase A	Mus musculus	76-80
11779133-1	2002	Many organisms have been shown to possess a methionine sulfoxide reductase (MsrA), exhibiting high specificity for reduction the S form of free and protein-bound methionine sulfoxide to methionine.	Methionine	44-54	methionine sulfoxide reductase A	Mus musculus	76-80
11606777-2	2001	Although free and protein-bound methionine residues are particularly sensitive to oxidation to methionine sulfoxide derivatives, these oxidations are readily repaired by the action of methionine sulfoxide reductase (MsrA).	Methionine	32-42	methionine sulfoxide reductase A	Mus musculus	216-220
11606777-2	2001	Although free and protein-bound methionine residues are particularly sensitive to oxidation to methionine sulfoxide derivatives, these oxidations are readily repaired by the action of methionine sulfoxide reductase (MsrA).	methionine sulfoxide	95-115	methionine sulfoxide reductase A	Mus musculus	216-220
11338182-3	2001	Cy3-fA beta uptake in the MSR-A-/- mice was still competable by scavenger receptor ligands, including acetylated low-density lipoprotein (Ac-LDL) and fucoidan.	cy3-fa	0-6	methionine sulfoxide reductase A	Mus musculus	26-31
11016456-9	2000	However, GA-BSA, but not MG-BSA or GO-BSA, underwent receptor-mediated endocytosis by the macrophage-derived cell line RAW 264.7, which was effectively inhibited by glucose-derived AGE-BSA, acetylated LDL, and oxidized LDL, which are well-known ligands for the macrophage type I and type II class A scavenger receptors (MSR-A).	Glucose	165-172	methionine sulfoxide reductase A	Mus musculus	320-325
11062078-6	2000	Furthermore, formaldehyde-treated serum albumin (f-Alb), a ligand known to undergo scavenger-receptor-mediated endocytosis by LECs, was effectively taken up by MSR-A knock-out LECs at a capacity that did not differ from that of wild-type LECs.	Formaldehyde	13-25	methionine sulfoxide reductase A	Mus musculus	160-165
11016456-11	2000	Our results suggest that GA serves as an important intermediate for the generation of AGE structure(s) responsible for recognition by MSR-A.	glycolaldehyde	25-27	methionine sulfoxide reductase A	Mus musculus	134-139
11004705-2	2000	MSR-A recognizes a broad range of polyanionic ligands such as chemically modified lipoproteins, LPS of Gram-negative bacteria, and lipoteichoic acid of Gram-positive bacteria, suggesting a role in host defence.	lipoteichoic acid	131-148	methionine sulfoxide reductase A	Mus musculus	0-5
10223745-3	1999	The administration of LPS, zymosan, BCG, or L. monocytogenes to mice resulted in marked and transient MARCO expression and in the upregulation of MSR-A expression in the liver and spleen.	Zymosan	27-34	methionine sulfoxide reductase A	Mus musculus	146-151
34397279-0	2021	Inhibition of HDACs (Histone Deacetylases) Ameliorates High-Fat Diet-Induced Hypertension Through Restoration of the MsrA (Methionine Sulfoxide Reductase A)/Hydrogen Sulfide Axis.	Hydrogen Sulfide	157-173	methionine sulfoxide reductase A	Mus musculus	117-121
9069289-1	1997	Macrophage type-I and type-II class-A scavenger receptors (MSR-A) are implicated in the pathological deposition of cholesterol during atherogenesis as a result of receptor-mediated uptake of modified low-density lipoproteins (mLDL).	Cholesterol	115-126	methionine sulfoxide reductase A	Mus musculus	59-64
34397279-0	2021	Inhibition of HDACs (Histone Deacetylases) Ameliorates High-Fat Diet-Induced Hypertension Through Restoration of the MsrA (Methionine Sulfoxide Reductase A)/Hydrogen Sulfide Axis.	Hydrogen Sulfide	157-173	methionine sulfoxide reductase A	Mus musculus	123-155
34397279-2	2021	MsrA (methionine sulfoxide reductase A) enables the metabolism of homocysteine by reducing methionine sulfoxide to methionine.	Homocysteine	66-78	methionine sulfoxide reductase A	Mus musculus	0-4
34397279-2	2021	MsrA (methionine sulfoxide reductase A) enables the metabolism of homocysteine by reducing methionine sulfoxide to methionine.	Homocysteine	66-78	methionine sulfoxide reductase A	Mus musculus	6-38
34397279-2	2021	MsrA (methionine sulfoxide reductase A) enables the metabolism of homocysteine by reducing methionine sulfoxide to methionine.	methionine sulfoxide	91-111	methionine sulfoxide reductase A	Mus musculus	0-4
34397279-2	2021	MsrA (methionine sulfoxide reductase A) enables the metabolism of homocysteine by reducing methionine sulfoxide to methionine.	methionine sulfoxide	91-111	methionine sulfoxide reductase A	Mus musculus	6-38
34397279-2	2021	MsrA (methionine sulfoxide reductase A) enables the metabolism of homocysteine by reducing methionine sulfoxide to methionine.	Methionine	115-125	methionine sulfoxide reductase A	Mus musculus	0-4
34397279-2	2021	MsrA (methionine sulfoxide reductase A) enables the metabolism of homocysteine by reducing methionine sulfoxide to methionine.	Methionine	115-125	methionine sulfoxide reductase A	Mus musculus	6-38
34397279-10	2021	CG200745 increased acetylation of histone H3 and MsrA levels in the mesenteric arteries while downregulating oxidative stress, inflammation, and vasocontractile proteins.	N1-(3-(dimethylamino)propyl)-N8-hydroxy-2-((naphthalene-1-loxy)methyl)oct-2-enediamide	0-8	methionine sulfoxide reductase A	Mus musculus	49-53
34397279-13	2021	Collectively, HFD-induced downregulation of MsrA plays a pivotal role in HFD-induced hypertension by reducing H2S levels.	Deuterium	110-113	methionine sulfoxide reductase A	Mus musculus	44-48
34397279-14	2021	MsrA expression is epigenetically regulated by HDAC inhibitors, providing HDAC inhibitors as a therapeutic option and MsrA and H2S as novel therapeutic targets.	Deuterium	127-130	methionine sulfoxide reductase A	Mus musculus	0-4
35332198-5	2022	We tested the functional role of the ubiquitously expressed methionine repair enzyme methionine sulfoxide reductase A (MsrA) on the metabolic benefits of MR in mice.	Methionine	60-70	methionine sulfoxide reductase A	Mus musculus	85-117
35332198-5	2022	We tested the functional role of the ubiquitously expressed methionine repair enzyme methionine sulfoxide reductase A (MsrA) on the metabolic benefits of MR in mice.	Methionine	60-70	methionine sulfoxide reductase A	Mus musculus	119-123
35332198-6	2022	MsrA catalytically reduces both free and protein-bound oxidized methionine, thus playing a key role in its redox state.	Methionine	64-74	methionine sulfoxide reductase A	Mus musculus	0-4
35279645-10	2021	In mice, depletion of the gut microbiota by administration of antibiotics resulted in a 31% decrease in the AUC ratio of sulindac sulfide to sulindac, indicating that the contribution of tissue MsrA to sulindac activation is expected to be 69% in the body.	sulindac sulfide	121-137	methionine sulfoxide reductase A	Mus musculus	194-198
35279645-10	2021	In mice, depletion of the gut microbiota by administration of antibiotics resulted in a 31% decrease in the AUC ratio of sulindac sulfide to sulindac, indicating that the contribution of tissue MsrA to sulindac activation is expected to be 69% in the body.	Sulindac	141-149	methionine sulfoxide reductase A	Mus musculus	194-198
35279645-10	2021	In mice, depletion of the gut microbiota by administration of antibiotics resulted in a 31% decrease in the AUC ratio of sulindac sulfide to sulindac, indicating that the contribution of tissue MsrA to sulindac activation is expected to be 69% in the body.	Sulindac	202-210	methionine sulfoxide reductase A	Mus musculus	194-198
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	1,3-dipropyl-8-cyclopentylxanthine	84-89	methionine sulfoxide reductase A	Mus musculus	40-44
33617903-9	2021	Adora1, Msra, Nrf2 and Tfam genes may be involved in mediating the antioxidant effect of the combined treatment with fluoxetine and Mito - TEMPO.	Fluoxetine	117-127	methionine sulfoxide reductase A	Mus musculus	8-12
33617903-9	2021	Adora1, Msra, Nrf2 and Tfam genes may be involved in mediating the antioxidant effect of the combined treatment with fluoxetine and Mito - TEMPO.	MitoTEMPO	132-144	methionine sulfoxide reductase A	Mus musculus	8-12
33806413-4	2021	MsrA can reduce free or protein-containing L-Met-O (S), whereas MsrBs can only function on the L-Met-O (R) epimer in proteins.	Methionine	44-48	methionine sulfoxide reductase A	Mus musculus	0-4
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	1,3-dipropyl-8-cyclopentylxanthine	72-77	methionine sulfoxide reductase A	Mus musculus	40-44
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	Zinc	90-94	methionine sulfoxide reductase A	Mus musculus	40-44
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	magnesium ion	78-82	methionine sulfoxide reductase A	Mus musculus	40-44
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	istradefylline	96-110	methionine sulfoxide reductase A	Mus musculus	40-44
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	magnesium ion	111-115	methionine sulfoxide reductase A	Mus musculus	40-44
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	istradefylline	120-134	methionine sulfoxide reductase A	Mus musculus	40-44
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	1,3-dipropyl-8-cyclopentylxanthine	84-89	methionine sulfoxide reductase A	Mus musculus	40-44
33673282-7	2021	Moreover, the changes obtained in Ogg1, MsrA, Nrf2 expression show that DPCPX-Mg2+, DPCPX-Zn2+, istradefylline-Mg2+ and istradefylline-Zn2+ co-treatment may have greater antioxidant capacity benefits than administration of DPCPX and istradefylline alone.	istradefylline	120-134	methionine sulfoxide reductase A	Mus musculus	40-44
31975555-6	2020	High-level hepatic MsrA significantly reduced the plasma free cholesterol contents, improved HDL functional proteins apolipoprotein A-I (apoAI), apoE, paraoxonase1 (PON1), and lecithin:cholesterol acyltransferase (LCAT), while decreased the pro-inflammatory property of dysfunctional HDL, contributing to reduced atherosclerosis and hepatic steatosis in Western diet-fed mice.	Cholesterol	62-73	methionine sulfoxide reductase A	Mus musculus	19-23
31473893-8	2020	Levels of MsrB2 mRNA and MsrA protein were significantly increased by ATO treatment, except in the highest dose group.	Arsenic Trioxide	70-73	methionine sulfoxide reductase A	Mus musculus	25-29
33241629-9	2021	Moreover, 3 mumol/L acacetin clearly decreased ROS levels and enhanced reductase protein expression through MsrA and Nrf2 pathway through phosphorylation of Nrf2 and degradation of Keap1.	acacetin	20-28	methionine sulfoxide reductase A	Mus musculus	108-112
31975555-7	2020	Furthermore, the study revealed that hepatic MsrA altered the expression of several genes controlling HDL biogenesis, cholesterol esterification, cholesterol uptake mediated by low-density lipoprotein receptor (LDLR) and biliary excretion, as well as suppressed nuclear factor kappaB (NF-kappaB) signaling pathway, which largely relied on liver X receptor alpha (LXRalpha)-upregulation.	Cholesterol	118-129	methionine sulfoxide reductase A	Mus musculus	45-49
31975555-7	2020	Furthermore, the study revealed that hepatic MsrA altered the expression of several genes controlling HDL biogenesis, cholesterol esterification, cholesterol uptake mediated by low-density lipoprotein receptor (LDLR) and biliary excretion, as well as suppressed nuclear factor kappaB (NF-kappaB) signaling pathway, which largely relied on liver X receptor alpha (LXRalpha)-upregulation.	Cholesterol	146-157	methionine sulfoxide reductase A	Mus musculus	45-49
26210777-1	2015	Methionine sulfoxide reductase A (MsrA), which stereospecifically catalyzes the reduction of methionine-S-sulfoxide, is an important reactive oxygen species (ROS) scavenger.	L-Methionine (S)-S-oxide	93-115	methionine sulfoxide reductase A	Mus musculus	0-32
33829213-5	2020	Results: Surprisingly, in the samples from mice with mitochondrial-targeted MsrA overexpression, we found dramatically increased free radical production though no specific defect in respiration, ATP production, or membrane potential.	Adenosine Triphosphate	195-198	methionine sulfoxide reductase A	Mus musculus	76-80
30322141-14	2018	We conclude that reversible oxidation of methionine 77 in calmodulin by MSRA has the potential to regulate cellular function.	Methionine	41-51	methionine sulfoxide reductase A	Mus musculus	72-76
29929200-1	2018	Methionine sulfoxide reductases (MsrA and MsrB) protect the biological activity of proteins from oxidative modifications to methionine residues and are important for protecting against the pathological effects of neurodegenerative diseases.	Methionine	124-134	methionine sulfoxide reductase A	Mus musculus	33-37
28803836-1	2017	Methionine sulfoxide reductase A (MsrA) is a major antioxidant enzyme that specifically catalyzes the reduction of methionine S-sulfoxide.	methionine s-sulfoxide	115-137	methionine sulfoxide reductase A	Mus musculus	0-32
28803836-1	2017	Methionine sulfoxide reductase A (MsrA) is a major antioxidant enzyme that specifically catalyzes the reduction of methionine S-sulfoxide.	methionine s-sulfoxide	115-137	methionine sulfoxide reductase A	Mus musculus	34-38
28803836-6	2017	Basal and LPS-induced reactive oxygen species (ROS) levels were higher in MsrA-/- than in MsrA+/+ BMDMs.	Reactive Oxygen Species	22-45	methionine sulfoxide reductase A	Mus musculus	74-78
28803836-6	2017	Basal and LPS-induced reactive oxygen species (ROS) levels were higher in MsrA-/- than in MsrA+/+ BMDMs.	Reactive Oxygen Species	22-45	methionine sulfoxide reductase A	Mus musculus	90-94
28803836-6	2017	Basal and LPS-induced reactive oxygen species (ROS) levels were higher in MsrA-/- than in MsrA+/+ BMDMs.	Reactive Oxygen Species	47-50	methionine sulfoxide reductase A	Mus musculus	74-78
28803836-6	2017	Basal and LPS-induced reactive oxygen species (ROS) levels were higher in MsrA-/- than in MsrA+/+ BMDMs.	Reactive Oxygen Species	47-50	methionine sulfoxide reductase A	Mus musculus	90-94
28803836-9	2017	Taken together, our results suggest that MsrA protects against LPS-induced septic shock, and negatively regulates proinflammatory responses via inhibition of the ROS-MAPK-NF-kappaB signaling pathways.	Reactive Oxygen Species	162-165	methionine sulfoxide reductase A	Mus musculus	41-45
27259041-0	2016	A Methionine Residue Promotes Hyperoxidation of the Catalytic Cysteine of Mouse Methionine Sulfoxide Reductase A.	Methionine	2-12	methionine sulfoxide reductase A	Mus musculus	80-112
27259041-0	2016	A Methionine Residue Promotes Hyperoxidation of the Catalytic Cysteine of Mouse Methionine Sulfoxide Reductase A.	Cysteine	62-70	methionine sulfoxide reductase A	Mus musculus	80-112
27259041-1	2016	Methionine sulfoxide reductase A (msrA) reduces methionine sulfoxide in proteins back to methionine.	methionine sulfoxide	48-68	methionine sulfoxide reductase A	Mus musculus	0-32
27259041-1	2016	Methionine sulfoxide reductase A (msrA) reduces methionine sulfoxide in proteins back to methionine.	methionine sulfoxide	48-68	methionine sulfoxide reductase A	Mus musculus	34-38
27259041-1	2016	Methionine sulfoxide reductase A (msrA) reduces methionine sulfoxide in proteins back to methionine.	Methionine	48-58	methionine sulfoxide reductase A	Mus musculus	0-32
27259041-1	2016	Methionine sulfoxide reductase A (msrA) reduces methionine sulfoxide in proteins back to methionine.	Methionine	48-58	methionine sulfoxide reductase A	Mus musculus	34-38
27259041-4	2016	However, the sulfenic acid is vulnerable to "irreversible" oxidation to cysteine sulfinic acid that inactivates msrA (hyperoxidation).	Sulfenic Acids	13-26	methionine sulfoxide reductase A	Mus musculus	112-116
27259041-4	2016	However, the sulfenic acid is vulnerable to "irreversible" oxidation to cysteine sulfinic acid that inactivates msrA (hyperoxidation).	cysteine sulfinic acid	72-94	methionine sulfoxide reductase A	Mus musculus	112-116
27259041-5	2016	We observed that human msrA is resistant to hyperoxidation while mouse msrA is readily hyperoxidized by micromolar concentrations of hydrogen peroxide.	Hydrogen Peroxide	133-150	methionine sulfoxide reductase A	Mus musculus	71-75
27259041-10	2016	The carboxyl domain of msrA is known to be flexible and to have access to the active site, and Met residues are known to form stable, noncovalent bonds with aromatic residues through interaction of the sulfur atom with the aromatic ring.	Sulfur	202-208	methionine sulfoxide reductase A	Mus musculus	23-27
27294204-3	2016	We found that overexpression of methionine sulfoxide reductase A (MsrA), an antioxidant enzyme that reverses protein methionine oxidation, attenuated ROS-augmented NF-kappaB activation in endothelial cells, in part, by protecting against the oxidation of methionine residues in the regulatory domain of calcium/calmodulin-dependent protein kinase II (CaMKII).	Methionine	32-42	methionine sulfoxide reductase A	Mus musculus	66-70
27294204-3	2016	We found that overexpression of methionine sulfoxide reductase A (MsrA), an antioxidant enzyme that reverses protein methionine oxidation, attenuated ROS-augmented NF-kappaB activation in endothelial cells, in part, by protecting against the oxidation of methionine residues in the regulatory domain of calcium/calmodulin-dependent protein kinase II (CaMKII).	ros	150-153	methionine sulfoxide reductase A	Mus musculus	32-64
27294204-3	2016	We found that overexpression of methionine sulfoxide reductase A (MsrA), an antioxidant enzyme that reverses protein methionine oxidation, attenuated ROS-augmented NF-kappaB activation in endothelial cells, in part, by protecting against the oxidation of methionine residues in the regulatory domain of calcium/calmodulin-dependent protein kinase II (CaMKII).	ros	150-153	methionine sulfoxide reductase A	Mus musculus	66-70
27294204-3	2016	We found that overexpression of methionine sulfoxide reductase A (MsrA), an antioxidant enzyme that reverses protein methionine oxidation, attenuated ROS-augmented NF-kappaB activation in endothelial cells, in part, by protecting against the oxidation of methionine residues in the regulatory domain of calcium/calmodulin-dependent protein kinase II (CaMKII).	Methionine	117-127	methionine sulfoxide reductase A	Mus musculus	32-64
27294204-3	2016	We found that overexpression of methionine sulfoxide reductase A (MsrA), an antioxidant enzyme that reverses protein methionine oxidation, attenuated ROS-augmented NF-kappaB activation in endothelial cells, in part, by protecting against the oxidation of methionine residues in the regulatory domain of calcium/calmodulin-dependent protein kinase II (CaMKII).	Methionine	117-127	methionine sulfoxide reductase A	Mus musculus	66-70
33829213-2	2020	Methionine sulfoxide reductase A (MsrA) is a ubiquitous protein oxidation repair enzyme that specifically and catalytically reduces a specific epimer of oxidized methionine: methionine sulfoxide.	Methionine	162-172	methionine sulfoxide reductase A	Mus musculus	0-32
33829213-2	2020	Methionine sulfoxide reductase A (MsrA) is a ubiquitous protein oxidation repair enzyme that specifically and catalytically reduces a specific epimer of oxidized methionine: methionine sulfoxide.	Methionine	162-172	methionine sulfoxide reductase A	Mus musculus	34-38
33829213-2	2020	Methionine sulfoxide reductase A (MsrA) is a ubiquitous protein oxidation repair enzyme that specifically and catalytically reduces a specific epimer of oxidized methionine: methionine sulfoxide.	methionine sulfoxide	174-194	methionine sulfoxide reductase A	Mus musculus	0-32
33829213-2	2020	Methionine sulfoxide reductase A (MsrA) is a ubiquitous protein oxidation repair enzyme that specifically and catalytically reduces a specific epimer of oxidized methionine: methionine sulfoxide.	methionine sulfoxide	174-194	methionine sulfoxide reductase A	Mus musculus	34-38
30787927-3	2019	Gonococcal MsrA/B has previously been shown to reduce methionine sulfoxide [Met(O)] to methionine (Met) in oxidized proteins and protect against oxidative stress.	methionine sulfoxide	54-74	methionine sulfoxide reductase A	Mus musculus	11-15
30787927-3	2019	Gonococcal MsrA/B has previously been shown to reduce methionine sulfoxide [Met(O)] to methionine (Met) in oxidized proteins and protect against oxidative stress.	methionine sulfoxide	76-82	methionine sulfoxide reductase A	Mus musculus	11-15
30787927-3	2019	Gonococcal MsrA/B has previously been shown to reduce methionine sulfoxide [Met(O)] to methionine (Met) in oxidized proteins and protect against oxidative stress.	Methionine	54-64	methionine sulfoxide reductase A	Mus musculus	11-15
30787927-3	2019	Gonococcal MsrA/B has previously been shown to reduce methionine sulfoxide [Met(O)] to methionine (Met) in oxidized proteins and protect against oxidative stress.	Methionine	76-79	methionine sulfoxide reductase A	Mus musculus	11-15
30096435-6	2018	Based on our previous observations showing that MsrA knockout mice have elevated expression levels of dopamine and 14-3-3 zeta and our current data, we propose that MsrA-dependent 14-3-3 zeta ubiquitination affects the regulation of alpha synuclein degradation and dopamine synthesis in the brain.	Dopamine	102-110	methionine sulfoxide reductase A	Mus musculus	48-52
30096435-6	2018	Based on our previous observations showing that MsrA knockout mice have elevated expression levels of dopamine and 14-3-3 zeta and our current data, we propose that MsrA-dependent 14-3-3 zeta ubiquitination affects the regulation of alpha synuclein degradation and dopamine synthesis in the brain.	Dopamine	102-110	methionine sulfoxide reductase A	Mus musculus	165-169
30096435-6	2018	Based on our previous observations showing that MsrA knockout mice have elevated expression levels of dopamine and 14-3-3 zeta and our current data, we propose that MsrA-dependent 14-3-3 zeta ubiquitination affects the regulation of alpha synuclein degradation and dopamine synthesis in the brain.	Dopamine	265-273	methionine sulfoxide reductase A	Mus musculus	48-52
30096435-6	2018	Based on our previous observations showing that MsrA knockout mice have elevated expression levels of dopamine and 14-3-3 zeta and our current data, we propose that MsrA-dependent 14-3-3 zeta ubiquitination affects the regulation of alpha synuclein degradation and dopamine synthesis in the brain.	Dopamine	265-273	methionine sulfoxide reductase A	Mus musculus	165-169
28158949-1	2017	AIMS: Methionine sulfoxide reductase A (MsrA), which is abundantly localized in the mitochondria, reduces methionine-S-sulfoxide, scavenging reactive oxygen species (ROS).	L-Methionine (S)-S-oxide	106-128	methionine sulfoxide reductase A	Mus musculus	6-38
28158949-1	2017	AIMS: Methionine sulfoxide reductase A (MsrA), which is abundantly localized in the mitochondria, reduces methionine-S-sulfoxide, scavenging reactive oxygen species (ROS).	L-Methionine (S)-S-oxide	106-128	methionine sulfoxide reductase A	Mus musculus	40-44
28158949-1	2017	AIMS: Methionine sulfoxide reductase A (MsrA), which is abundantly localized in the mitochondria, reduces methionine-S-sulfoxide, scavenging reactive oxygen species (ROS).	Reactive Oxygen Species	141-164	methionine sulfoxide reductase A	Mus musculus	6-38
28158949-1	2017	AIMS: Methionine sulfoxide reductase A (MsrA), which is abundantly localized in the mitochondria, reduces methionine-S-sulfoxide, scavenging reactive oxygen species (ROS).	Reactive Oxygen Species	141-164	methionine sulfoxide reductase A	Mus musculus	40-44
28158949-1	2017	AIMS: Methionine sulfoxide reductase A (MsrA), which is abundantly localized in the mitochondria, reduces methionine-S-sulfoxide, scavenging reactive oxygen species (ROS).	Reactive Oxygen Species	166-169	methionine sulfoxide reductase A	Mus musculus	6-38
28158949-1	2017	AIMS: Methionine sulfoxide reductase A (MsrA), which is abundantly localized in the mitochondria, reduces methionine-S-sulfoxide, scavenging reactive oxygen species (ROS).	Reactive Oxygen Species	166-169	methionine sulfoxide reductase A	Mus musculus	40-44
28158949-6	2017	MsrA gene deletion exacerbated cisplatin-induced reductions in the expression and activity of MsrA and MsrBs, and the expression of thioredoxin 1, glutathione peroxidase 1 and 4, mitochondrial superoxide dismutase, cystathionine-beta-synthase, and cystathionine-gamma-lyase.	Cisplatin	31-40	methionine sulfoxide reductase A	Mus musculus	0-4
28158949-6	2017	MsrA gene deletion exacerbated cisplatin-induced reductions in the expression and activity of MsrA and MsrBs, and the expression of thioredoxin 1, glutathione peroxidase 1 and 4, mitochondrial superoxide dismutase, cystathionine-beta-synthase, and cystathionine-gamma-lyase.	Cisplatin	31-40	methionine sulfoxide reductase A	Mus musculus	94-98
28158949-7	2017	Cisplatin induced swelling, cristae loss, and fragmentation of mitochondria with increased lipid peroxidation, more so in MsrA-/- than in MsrA+/+ kidneys.	Cisplatin	0-9	methionine sulfoxide reductase A	Mus musculus	122-126
28158949-7	2017	Cisplatin induced swelling, cristae loss, and fragmentation of mitochondria with increased lipid peroxidation, more so in MsrA-/- than in MsrA+/+ kidneys.	Cisplatin	0-9	methionine sulfoxide reductase A	Mus musculus	138-142
28158949-9	2017	MsrA deletion exacerbated cisplatin-induced increases in Bax to Bcl-2 ratio, cleaved caspase-3 level, and apoptosis, whereas MsrA overexpression attenuated cisplatin-induced oxidative stress and apoptosis.	Cisplatin	26-35	methionine sulfoxide reductase A	Mus musculus	0-4
28158949-9	2017	MsrA deletion exacerbated cisplatin-induced increases in Bax to Bcl-2 ratio, cleaved caspase-3 level, and apoptosis, whereas MsrA overexpression attenuated cisplatin-induced oxidative stress and apoptosis.	Cisplatin	156-165	methionine sulfoxide reductase A	Mus musculus	0-4
28158949-9	2017	MsrA deletion exacerbated cisplatin-induced increases in Bax to Bcl-2 ratio, cleaved caspase-3 level, and apoptosis, whereas MsrA overexpression attenuated cisplatin-induced oxidative stress and apoptosis.	Cisplatin	156-165	methionine sulfoxide reductase A	Mus musculus	125-129
28158949-10	2017	INNOVATION: MsrA gene deletion in mice exacerbates cisplatin-induced renal injury through increases of mitochondrial susceptibility, whereas MsrA overexpression protects cells against cisplatin.	Cisplatin	51-60	methionine sulfoxide reductase A	Mus musculus	12-16
28158949-10	2017	INNOVATION: MsrA gene deletion in mice exacerbates cisplatin-induced renal injury through increases of mitochondrial susceptibility, whereas MsrA overexpression protects cells against cisplatin.	Cisplatin	184-193	methionine sulfoxide reductase A	Mus musculus	141-145
28158949-11	2017	CONCLUSION: This study demonstrates that MsrA protects kidney cells against cisplatin-induced methionine oxidation, oxidative stress, mitochondrial damage, and apoptosis, suggesting that MsrA could be a useful target protein for the treatment of cisplatin-induced nephrotoxicity.	Cisplatin	76-85	methionine sulfoxide reductase A	Mus musculus	41-45
28158949-11	2017	CONCLUSION: This study demonstrates that MsrA protects kidney cells against cisplatin-induced methionine oxidation, oxidative stress, mitochondrial damage, and apoptosis, suggesting that MsrA could be a useful target protein for the treatment of cisplatin-induced nephrotoxicity.	Cisplatin	76-85	methionine sulfoxide reductase A	Mus musculus	187-191
28158949-11	2017	CONCLUSION: This study demonstrates that MsrA protects kidney cells against cisplatin-induced methionine oxidation, oxidative stress, mitochondrial damage, and apoptosis, suggesting that MsrA could be a useful target protein for the treatment of cisplatin-induced nephrotoxicity.	Methionine	94-104	methionine sulfoxide reductase A	Mus musculus	41-45
28158949-11	2017	CONCLUSION: This study demonstrates that MsrA protects kidney cells against cisplatin-induced methionine oxidation, oxidative stress, mitochondrial damage, and apoptosis, suggesting that MsrA could be a useful target protein for the treatment of cisplatin-induced nephrotoxicity.	Cisplatin	246-255	methionine sulfoxide reductase A	Mus musculus	41-45
28158949-11	2017	CONCLUSION: This study demonstrates that MsrA protects kidney cells against cisplatin-induced methionine oxidation, oxidative stress, mitochondrial damage, and apoptosis, suggesting that MsrA could be a useful target protein for the treatment of cisplatin-induced nephrotoxicity.	Cisplatin	246-255	methionine sulfoxide reductase A	Mus musculus	187-191
28104395-2	2017	Methionine sulfoxide reductase A (MsrA) acts as a reactive oxygen species scavenger by catalyzing the cyclic reduction of methionine-S-sulfoxide.	Reactive Oxygen Species	50-73	methionine sulfoxide reductase A	Mus musculus	0-32
28104395-2	2017	Methionine sulfoxide reductase A (MsrA) acts as a reactive oxygen species scavenger by catalyzing the cyclic reduction of methionine-S-sulfoxide.	Reactive Oxygen Species	50-73	methionine sulfoxide reductase A	Mus musculus	34-38
28104395-2	2017	Methionine sulfoxide reductase A (MsrA) acts as a reactive oxygen species scavenger by catalyzing the cyclic reduction of methionine-S-sulfoxide.	L-Methionine (S)-S-oxide	122-144	methionine sulfoxide reductase A	Mus musculus	0-32
28104395-2	2017	Methionine sulfoxide reductase A (MsrA) acts as a reactive oxygen species scavenger by catalyzing the cyclic reduction of methionine-S-sulfoxide.	L-Methionine (S)-S-oxide	122-144	methionine sulfoxide reductase A	Mus musculus	34-38
28104395-4	2017	We found that MsrA-/- mice were more susceptible to APAP-induced acute liver injury than wild-type mice (MsrA+/+).	Acetaminophen	52-56	methionine sulfoxide reductase A	Mus musculus	14-18
28104395-6	2017	Serum alanine transaminase, aspartate transaminase, and lactate dehydrogenase levels were significantly higher in MsrA-/- than in MsrA+/+ mice after APAP challenge.	Acetaminophen	149-153	methionine sulfoxide reductase A	Mus musculus	114-118
28104395-7	2017	Deletion of MsrA enhanced APAP-induced hepatic GSH depletion and oxidative stress, leading to increased susceptibility to APAP-induced liver injury in MsrA-deficient mice.	Acetaminophen	26-30	methionine sulfoxide reductase A	Mus musculus	12-16
28104395-7	2017	Deletion of MsrA enhanced APAP-induced hepatic GSH depletion and oxidative stress, leading to increased susceptibility to APAP-induced liver injury in MsrA-deficient mice.	Glutathione	47-50	methionine sulfoxide reductase A	Mus musculus	12-16
28104395-7	2017	Deletion of MsrA enhanced APAP-induced hepatic GSH depletion and oxidative stress, leading to increased susceptibility to APAP-induced liver injury in MsrA-deficient mice.	Acetaminophen	122-126	methionine sulfoxide reductase A	Mus musculus	12-16
28104395-8	2017	APAP challenge increased Nrf2 activation more profoundly in MsrA-/- than in MsrA+/+ livers.	Acetaminophen	0-4	methionine sulfoxide reductase A	Mus musculus	60-64
28104395-8	2017	APAP challenge increased Nrf2 activation more profoundly in MsrA-/- than in MsrA+/+ livers.	Acetaminophen	0-4	methionine sulfoxide reductase A	Mus musculus	76-80
28104395-10	2017	Taken together, our results demonstrate that MsrA protects the liver from APAP-induced toxicity.	Acetaminophen	74-78	methionine sulfoxide reductase A	Mus musculus	45-49
27821326-3	2016	Methionine sulfoxide reductase A (MsrA) repairs oxidation of free- and protein-bound methionine residues through enzymatic reduction and is found in both the cytosol and the mitochondria.	Methionine	85-95	methionine sulfoxide reductase A	Mus musculus	0-32
27821326-3	2016	Methionine sulfoxide reductase A (MsrA) repairs oxidation of free- and protein-bound methionine residues through enzymatic reduction and is found in both the cytosol and the mitochondria.	Methionine	85-95	methionine sulfoxide reductase A	Mus musculus	34-38
26786779-2	2016	The current studies determine the effect of an in vivo methionine sulfoxidation of Abeta through ablation of the methionine sulfoxide reductase A (MsrA) in a mouse model of AD, a mouse that overexpresses amyloid precursor protein (APP) and Abeta in neurons.	Methionine	55-65	methionine sulfoxide reductase A	Mus musculus	147-151
26786779-3	2016	Lack of MsrA fosters the formation of methionine sulfoxide in proteins, and thus its ablation in the AD-mouse model will increase the formation of methionine sulfoxide in Abeta.	methionine sulfoxide	38-58	methionine sulfoxide reductase A	Mus musculus	8-12
26786779-3	2016	Lack of MsrA fosters the formation of methionine sulfoxide in proteins, and thus its ablation in the AD-mouse model will increase the formation of methionine sulfoxide in Abeta.	methionine sulfoxide	147-167	methionine sulfoxide reductase A	Mus musculus	8-12
26210777-1	2015	Methionine sulfoxide reductase A (MsrA), which stereospecifically catalyzes the reduction of methionine-S-sulfoxide, is an important reactive oxygen species (ROS) scavenger.	L-Methionine (S)-S-oxide	93-115	methionine sulfoxide reductase A	Mus musculus	34-38
26210777-1	2015	Methionine sulfoxide reductase A (MsrA), which stereospecifically catalyzes the reduction of methionine-S-sulfoxide, is an important reactive oxygen species (ROS) scavenger.	Reactive Oxygen Species	133-156	methionine sulfoxide reductase A	Mus musculus	0-32
26210777-1	2015	Methionine sulfoxide reductase A (MsrA), which stereospecifically catalyzes the reduction of methionine-S-sulfoxide, is an important reactive oxygen species (ROS) scavenger.	Reactive Oxygen Species	133-156	methionine sulfoxide reductase A	Mus musculus	34-38
26210777-1	2015	Methionine sulfoxide reductase A (MsrA), which stereospecifically catalyzes the reduction of methionine-S-sulfoxide, is an important reactive oxygen species (ROS) scavenger.	Reactive Oxygen Species	158-161	methionine sulfoxide reductase A	Mus musculus	0-32
26210777-1	2015	Methionine sulfoxide reductase A (MsrA), which stereospecifically catalyzes the reduction of methionine-S-sulfoxide, is an important reactive oxygen species (ROS) scavenger.	Reactive Oxygen Species	158-161	methionine sulfoxide reductase A	Mus musculus	34-38
26318157-1	2015	Methionine sulfoxide reductase A (MsrA), a specific enzyme that converts methionine-S-sulfoxide to methionine, plays an important role in the regulation of protein function and the maintenance of redox homeostasis.	L-Methionine (S)-S-oxide	73-95	methionine sulfoxide reductase A	Mus musculus	0-32
26318157-1	2015	Methionine sulfoxide reductase A (MsrA), a specific enzyme that converts methionine-S-sulfoxide to methionine, plays an important role in the regulation of protein function and the maintenance of redox homeostasis.	L-Methionine (S)-S-oxide	73-95	methionine sulfoxide reductase A	Mus musculus	34-38
26318157-1	2015	Methionine sulfoxide reductase A (MsrA), a specific enzyme that converts methionine-S-sulfoxide to methionine, plays an important role in the regulation of protein function and the maintenance of redox homeostasis.	Methionine	73-83	methionine sulfoxide reductase A	Mus musculus	0-32
26318157-1	2015	Methionine sulfoxide reductase A (MsrA), a specific enzyme that converts methionine-S-sulfoxide to methionine, plays an important role in the regulation of protein function and the maintenance of redox homeostasis.	Methionine	73-83	methionine sulfoxide reductase A	Mus musculus	34-38
24632144-1	2014	The mouse methionine sulfoxide reductase A (MsrA) belongs to the subclass of MsrAs with one catalytic and two recycling Cys corresponding to Cys51, Cys198 and Cys206 in Escherichia coli MsrA, respectively.	Cysteine	120-123	methionine sulfoxide reductase A	Mus musculus	10-42
24632144-1	2014	The mouse methionine sulfoxide reductase A (MsrA) belongs to the subclass of MsrAs with one catalytic and two recycling Cys corresponding to Cys51, Cys198 and Cys206 in Escherichia coli MsrA, respectively.	Cysteine	120-123	methionine sulfoxide reductase A	Mus musculus	44-48
24632144-1	2014	The mouse methionine sulfoxide reductase A (MsrA) belongs to the subclass of MsrAs with one catalytic and two recycling Cys corresponding to Cys51, Cys198 and Cys206 in Escherichia coli MsrA, respectively.	Cysteine	120-123	methionine sulfoxide reductase A	Mus musculus	77-81
24632144-3	2014	In the present study carried out with E. coli MsrA, kinetic evidence are presented which show that formation of the second mol of Ac-L-Met-NHMe is rate-limiting in the absence of thioredoxin.	ac-l-met-nhme	130-143	methionine sulfoxide reductase A	Mus musculus	46-50
24632144-5	2014	Kinetic arguments are presented which support the accumulation of the E. coli MsrA under Cys51 sulfenic acid state in the presence of Trx.	cys51 sulfenic acid	89-108	methionine sulfoxide reductase A	Mus musculus	78-82
26410585-10	2015	RESULTS: PEP-1-MsrA could penetrate the cells and significantly reduced intracellular ROS levels and apoptosis in H2O2-treated macrophages.	Reactive Oxygen Species	86-89	methionine sulfoxide reductase A	Mus musculus	15-19
26410585-10	2015	RESULTS: PEP-1-MsrA could penetrate the cells and significantly reduced intracellular ROS levels and apoptosis in H2O2-treated macrophages.	Hydrogen Peroxide	114-118	methionine sulfoxide reductase A	Mus musculus	15-19
25341044-1	2014	Methionine sulfoxide reductase A (MSRA) protects proteins from oxidation, and also helps remove reactive oxygen species (ROS) by recovering antioxidant enzymes inactivated by oxidation.	Reactive Oxygen Species	96-119	methionine sulfoxide reductase A	Mus musculus	0-32
25341044-1	2014	Methionine sulfoxide reductase A (MSRA) protects proteins from oxidation, and also helps remove reactive oxygen species (ROS) by recovering antioxidant enzymes inactivated by oxidation.	Reactive Oxygen Species	96-119	methionine sulfoxide reductase A	Mus musculus	34-38
25341044-1	2014	Methionine sulfoxide reductase A (MSRA) protects proteins from oxidation, and also helps remove reactive oxygen species (ROS) by recovering antioxidant enzymes inactivated by oxidation.	Reactive Oxygen Species	121-124	methionine sulfoxide reductase A	Mus musculus	0-32
25341044-1	2014	Methionine sulfoxide reductase A (MSRA) protects proteins from oxidation, and also helps remove reactive oxygen species (ROS) by recovering antioxidant enzymes inactivated by oxidation.	Reactive Oxygen Species	121-124	methionine sulfoxide reductase A	Mus musculus	34-38