BRENDA - Enzyme Database show
show all sequences of 1.8.98.2

Characterization of plant sulfiredoxin and role of sulphinic form of 2-Cys peroxiredoxin

Iglesias-Baena, I.; Barranco-Medina, S.; Lazaro-Payo, A.; Lopez-Jaramillo, F.J.; Sevilla, F.; Lazaro, J.J.; J. Exp. Bot. 61, 1509-1521 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression of N-terminally His6-tagged wild-type Srx and mutants in Escherichia coli strain BL21(DE3)
Arabidopsis thaliana
Engineering
Amino acid exchange
Commentary
Organism
C72S
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
Arabidopsis thaliana
E76A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Arabidopsis thaliana
K40Q
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
Arabidopsis thaliana
additional information
construction of a Srx knockout mutant, phenotype, overview
Arabidopsis thaliana
R28Q
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
Arabidopsis thaliana
R28Q/E76A
site-directed mutagenesis, inactive mutant
Arabidopsis thaliana
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic analysis, overview
Arabidopsis thaliana
0.029
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH 7.5, 30°C, saturating ATP, 0.03 mM Srx, 0.04 mM substrate
Arabidopsis thaliana
0.079
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH 7.5, 30°C, 1 mM ATP, 0.03 mM Srx, saturating substrate concentration
Arabidopsis thaliana
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
Srx possesses a chloroplast transit peptide in the N-terminus
Arabidopsis thaliana
9507
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Arabidopsis thaliana
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
11546
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
Arabidopsis thaliana
13914
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
Arabidopsis thaliana
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
-
-
-
Arabidopsis thaliana Columbia
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type Srx and mutants to homogeneity from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
Arabidopsis thaliana
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
-
Arabidopsis thaliana
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
assay conditions optimization, overview
712607
Arabidopsis thaliana
?
-
-
-
-
additional information
assay conditions optimization, overview
712607
Arabidopsis thaliana Columbia
?
-
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
-
712607
Arabidopsis thaliana
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
-
712607
Arabidopsis thaliana Columbia
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
-
712607
Arabidopsis thaliana
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
-
712607
Arabidopsis thaliana Columbia
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
-
712607
Arabidopsis thaliana
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
-
712607
Arabidopsis thaliana Columbia
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
Arabidopsis thaliana
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Arabidopsis thaliana
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00042
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH 7.5, 30°C, saturating ATP, 0.03 mM Srx, 0.04 mM substrate
Arabidopsis thaliana
0.011
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH 7.5, 30°C, 1 mM ATP, 0.03 mM Srx, saturating substrate concentration
Arabidopsis thaliana
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
-
Arabidopsis thaliana
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Arabidopsis thaliana
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Arabidopsis thaliana
mature enzyme, sequence calculation
-
9.86
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression of N-terminally His6-tagged wild-type Srx and mutants in Escherichia coli strain BL21(DE3)
Arabidopsis thaliana
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Arabidopsis thaliana
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C72S
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
Arabidopsis thaliana
E76A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Arabidopsis thaliana
K40Q
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
Arabidopsis thaliana
additional information
construction of a Srx knockout mutant, phenotype, overview
Arabidopsis thaliana
R28Q
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
Arabidopsis thaliana
R28Q/E76A
site-directed mutagenesis, inactive mutant
Arabidopsis thaliana
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic analysis, overview
Arabidopsis thaliana
0.029
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH 7.5, 30°C, saturating ATP, 0.03 mM Srx, 0.04 mM substrate
Arabidopsis thaliana
0.079
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH 7.5, 30°C, 1 mM ATP, 0.03 mM Srx, saturating substrate concentration
Arabidopsis thaliana
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
Srx possesses a chloroplast transit peptide in the N-terminus
Arabidopsis thaliana
9507
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Arabidopsis thaliana
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
11546
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
Arabidopsis thaliana
13914
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
Arabidopsis thaliana
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type Srx and mutants to homogeneity from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
Arabidopsis thaliana
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Arabidopsis thaliana
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
assay conditions optimization, overview
712607
Arabidopsis thaliana
?
-
-
-
-
additional information
assay conditions optimization, overview
712607
Arabidopsis thaliana Columbia
?
-
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
-
712607
Arabidopsis thaliana
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
-
712607
Arabidopsis thaliana Columbia
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
-
712607
Arabidopsis thaliana
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
-
712607
Arabidopsis thaliana Columbia
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
-
712607
Arabidopsis thaliana
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
-
712607
Arabidopsis thaliana Columbia
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
Arabidopsis thaliana
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Arabidopsis thaliana
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00042
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH 7.5, 30°C, saturating ATP, 0.03 mM Srx, 0.04 mM substrate
Arabidopsis thaliana
0.011
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH 7.5, 30°C, 1 mM ATP, 0.03 mM Srx, saturating substrate concentration
Arabidopsis thaliana
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
-
Arabidopsis thaliana
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Arabidopsis thaliana
mature enzyme, sequence calculation
-
9.86
General Information
General Information
Commentary
Organism
physiological function
the antioxidant function of 2-Cys peroxiredoxin, Prx, EC 1.11.1.15, involves the oxidation of its conserved peroxidatic cysteine to sulfinic acid that is recycled by a reductor agent. Sulfiredoxin reduces the sulfinic 2-Cys Prx, Prx-SO2H. The activity of sulfiredoxin is dependent on the concentration of the sulfinic form of Prx and the conserved Srx is capable of regenerating the functionality of both pea and Arabidopsis Prx-SO2H
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the antioxidant function of 2-Cys peroxiredoxin, Prx, EC 1.11.1.15, involves the oxidation of its conserved peroxidatic cysteine to sulfinic acid that is recycled by a reductor agent. Sulfiredoxin reduces the sulfinic 2-Cys Prx, Prx-SO2H. The activity of sulfiredoxin is dependent on the concentration of the sulfinic form of Prx and the conserved Srx is capable of regenerating the functionality of both pea and Arabidopsis Prx-SO2H
Arabidopsis thaliana
Other publictions for EC 1.8.98.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742457
Shi
Sulfiredoxin involved in the ...
Rattus norvegicus
Exp. Cell Res.
352
273-280
2017
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2
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1
1
1
1
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742601
Calderon
Glutathionylation of pea chlo ...
Pisum sativum
Front. Plant Sci.
8
118
2017
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1
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2
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742566
Rhee
Mitochondrial H2O2 signaling ...
Mus musculus
Free Radic. Biol. Med.
99
120-127
2016
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1
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1
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3
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2
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1
1
-
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742996
Sevilla
The thioredoxin/peroxiredoxin ...
Arabidopsis thaliana
J. Exp. Bot.
66
2945-2955
2015
-
-
-
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2
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1
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2
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1
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1
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1
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724192
Moon
Reversal of 2-Cys peroxiredoxi ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
432
291-295
2013
-
-
1
-
1
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2
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1
1
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743135
Li
Sulfiredoxin-1 protects PC12 ...
Rattus norvegicus
J. Neurosci. Res.
91
861-870
2013
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1
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1
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1
1
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743228
Kil
Study of the signaling functi ...
Mus musculus
Methods Enzymol.
527
169-181
2013
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3
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1
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1
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1
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1
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725015
Chi
Dual functions of Arabidopsis ...
Arabidopsis thaliana
FEBS Lett.
586
3493-3499
2012
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1
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1
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1
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2
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1
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725510
Baek
Sulfiredoxin protein is critic ...
Mus musculus
J. Biol. Chem.
287
81-89
2012
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725010
Roussel
The rate-limiting step of sulf ...
Saccharomyces cerevisiae
FEBS Lett.
585
574-578
2011
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2
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726220
Iglesias-Baena
The dual-targeted plant sulfir ...
Arabidopsis thaliana, Pisum sativum
Plant Physiol.
155
944-955
2011
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5
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6
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5
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712607
Iglesias-Baena
Characterization of plant sulf ...
Arabidopsis thaliana, Arabidopsis thaliana Columbia
J. Exp. Bot.
61
1509-1521
2010
-
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1
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6
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3
1
1
2
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11
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1
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1
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8
1
1
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2
1
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1
-
1
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1
1
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6
-
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3
1
1
2
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1
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1
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8
1
1
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2
1
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1
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1
1
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-
695553
Kim
A colorimetric assay for sulfi ...
Homo sapiens
Anal. Biochem.
393
36-40
2009
-
1
1
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1
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1
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1
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1
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2
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1
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1
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2
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1
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3
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1
1
3
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1
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1
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1
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1
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1
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1
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2
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1
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-
698052
Singh
Nrf2-dependent sulfiredoxin-1 ...
Homo sapiens, Mus musculus
Free Radic. Biol. Med.
46
376-386
2009
-
2
1
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-
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2
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2
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4
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4
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2
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2
1
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2
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2
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4
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1
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689157
Joensson
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700520
Lei
Protein cysteine sulfinic acid ...
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1
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Mutagenesis and modeling of th ...
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668161
Findlay
A novel role for human sulfire ...
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1
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2
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Molecular mechanism of the red ...
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8
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8
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658132
Jönsson
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Homo sapiens
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2
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658255
Findlay
Sulfiredoxin: a potential ther ...
Homo sapiens
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374-379
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659491
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Reduction of cysteine sulfinic ...
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Characterization of mammalian ...
Homo sapiens, Mus musculus, Rattus norvegicus
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9
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3
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6
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9
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659998
Biteau
ATP-dependent reduction of cys ...
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Nature
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