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2-Cys peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
2-Cys peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
-
-
-
-
?
overoxidized human peroxiredoxin V + reduced thioredoxin
? + oxidized thioredoxin
Arabidopsis enzyme is able to reduce overoxidized human Prx V
-
-
?
peroxiredoxin IIF-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin IIF-(S-hydroxycysteine) + ADP + phosphate + GSSG
-
-
-
-
?
peroxiredoxin III-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin III-(S-hydroxycysteine) + ADP + phosphate + GSSG
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + dADP + phosphate + R-S-S-R
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dGTP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dGTP + R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
-
formation of a covalent thiosulfinate peroxiredoxin-sulfiredoxin species as an intermediate on the catalytic pathway
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + gamma-S-ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + thiophosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + GTP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
sulfinic form of peroxiredoxin IIF + oxidized thioredoxin
? + reduced thioredoxin
in mitochondria, sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical peroxiredoxin IIF using thioredoxin as reducing agent
-
-
?
sulfinic form of peroxiredoxin IIF + reduced thioredoxin
? + oxidized thioredoxin
in mitochondria, sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical peroxiredoxin IIF using thioredoxin as reducing agent
-
-
?
additional information
?
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
Srx is largely responsible for reduction of the Cys-SO2H of peroxiredoxin in A549 human cells
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
the ATP molecule is cleaved between the beta- and gamma-phosphate groups
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
reduction of Cys-SO2H by Srx is specific to 2-Cys peroxiredoxin isoforms. For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process that causes protein damage
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
the rate-limiting step of the reaction is associated with the chemical process of transfer of the gamma-phosphate of ATP to the sulfinic acid. Two pKapp values of 6.2 and 7.5 of the bell-shaped pH-rate profile correspond to the gamma-phosphate of ATP, and to an acid-base catalyst, respectively
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
-
-
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
-
identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
additional information

?
-
-
assay conditions optimization, overview
-
-
-
additional information
?
-
-
enzyme is able to act as a redox-dependent sulfinic acid reductase and as a redox-independent nuclease enzyme. Sulfiredoxin functions as a nuclease enzyme that can use single-stranded and double-stranded DNAs as substrates. The active site of the reductase function of sulfiredoxin is not involved in its nuclease function
-
-
-
additional information
?
-
-
assay conditions optimization, overview
-
-
-
additional information
?
-
-
no activity with CTP, UTP, dCTP, or dTTP
-
-
-
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
additional information
?
-
-
catalyzes the deglutathionylation of actin
-
-
-
additional information
?
-
-
promotes the reversal of cysteine modified PTP1B to its reduced and enzymatically active form
-
-
-
additional information
?
-
-
reduction of cysteine sulfinic acid to sulfenic acid in proteins subject to oxidative stress
-
-
-
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
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peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
additional information
?
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
Q9BYN0
repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
Srx is largely responsible for reduction of the Cys-SO2H of peroxiredoxin in A549 human cells
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
reduction of Cys-SO2H by Srx is specific to 2-Cys peroxiredoxin isoforms. For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process that causes protein damage
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH

peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
Q8GY89
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
additional information

?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
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Adenocarcinoma
Nuclear Nrf2 expression is related to a poor survival in pancreatic adenocarcinoma.
Brain Injuries
Sulfiredoxin-1 Attenuates Oxidative Stress via Nrf2/ARE Pathway and 2-Cys Prdxs After Oxygen-Glucose Deprivation in Astrocytes.
Brain Ischemia
Neuroprotective effects of sulfiredoxin-1 during cerebral ischemia/reperfusion oxidative stress injury in rats.
Brain Ischemia
Sulfiredoxin-1 exerts anti-apoptotic and neuroprotective effects against oxidative stress-induced injury in rat cortical astrocytes following exposure to oxygen-glucose deprivation and hydrogen peroxide.
Breast Neoplasms
Correction: Genetic Polymorphisms and Protein Expression of NRF2 and Sulfiredoxin Predict Survival Outcomes in Breast Cancer.
Breast Neoplasms
Genetic polymorphisms and protein expression of NRF2 and sulfiredoxin predict survival outcomes in breast cancer.
Breast Neoplasms
Maesopsin 4-O-beta-D-glucoside, a natural compound isolated from the leaves of Artocarpus tonkinensis, inhibits proliferation and up-regulates HMOX1, SRXN1 and BCAS3 in acute myeloid leukemia.
Carcinogenesis
Loss of sulfiredoxin renders mice resistant to azoxymethane/dextran sulfate sodium-induced colon carcinogenesis.
Carcinogenesis
Sulfiredoxin-Peroxiredoxin IV axis promotes human lung cancer progression through modulation of specific phosphokinase signaling.
Carcinogenesis
Tumor promoter-induced sulfiredoxin is required for mouse skin tumorigenesis.
Carcinoma
Nuclear factor erythroid-derived 2-like 2 (Nrf2) and DJ1 are prognostic factors in lung cancer.
Carcinoma
Sulfiredoxin may promote metastasis and invasion of cervical squamous cell carcinoma by epithelial-mesenchymal transition.
Carcinoma
[Highly expressed sulfiredoxin and ?-catenin are associated with malignancy of cervical squamous cell carcinoma].
Carcinoma, Squamous Cell
Sulfiredoxin may promote metastasis and invasion of cervical squamous cell carcinoma by epithelial-mesenchymal transition.
Carcinoma, Squamous Cell
[Highly expressed sulfiredoxin and ?-catenin are associated with malignancy of cervical squamous cell carcinoma].
Cerebral Infarction
Neuroprotective effects of sulfiredoxin-1 during cerebral ischemia/reperfusion oxidative stress injury in rats.
Cerebrovascular Disorders
Genetic Polymorphisms of Transcription Factor NRF2 and of its Host Gene Sulfiredoxin (SRXN1) are Associated with Cerebrovascular Disease in a Finnish Cohort, the TAMRISK Study.
Colorectal Neoplasms
Sulfiredoxin Promotes Colorectal Cancer Cell Invasion and Metastasis through a Novel Mechanism of Enhancing EGFR Signaling.
Hypersensitivity
Role of sulfiredoxin as a peroxiredoxin-2 denitrosylase in human iPSC-derived dopaminergic neurons.
Hypertension
Genetic Polymorphisms of Transcription Factor NRF2 and of its Host Gene Sulfiredoxin (SRXN1) are Associated with Cerebrovascular Disease in a Finnish Cohort, the TAMRISK Study.
Idiopathic Pulmonary Fibrosis
Cell-specific elevation of NRF2 and sulfiredoxin-1 as markers of oxidative stress in the lungs of idiopathic pulmonary fibrosis and non-specific interstitial pneumonia.
Infarction, Middle Cerebral Artery
Neuroprotective effects of sulfiredoxin-1 during cerebral ischemia/reperfusion oxidative stress injury in rats.
Leukemia, Myeloid, Acute
Maesopsin 4-O-beta-D-glucoside, a natural compound isolated from the leaves of Artocarpus tonkinensis, inhibits proliferation and up-regulates HMOX1, SRXN1 and BCAS3 in acute myeloid leukemia.
Lung Diseases, Interstitial
Cell-specific elevation of NRF2 and sulfiredoxin-1 as markers of oxidative stress in the lungs of idiopathic pulmonary fibrosis and non-specific interstitial pneumonia.
Lung Neoplasms
Nuclear factor E2-related factor 2 dependent overexpression of sulfiredoxin and peroxiredoxin III in human lung cancer.
Lung Neoplasms
Nuclear factor erythroid-derived 2-like 2 (Nrf2) and DJ1 are prognostic factors in lung cancer.
Meningoencephalitis
Sulfiredoxin plays peroxiredoxin-dependent and -independent roles via the HOG signaling pathway in Cryptococcus neoformans and contributes to fungal virulence.
Neoplasm Metastasis
Sulfiredoxin May Promote Cervical Cancer Metastasis via Wnt/?-Catenin Signaling Pathway.
Neoplasm Metastasis
Sulfiredoxin may promote metastasis and invasion of cervical squamous cell carcinoma by epithelial-mesenchymal transition.
Neoplasm Metastasis
Sulfiredoxin Promotes Colorectal Cancer Cell Invasion and Metastasis through a Novel Mechanism of Enhancing EGFR Signaling.
Neoplasms
Effective killing of cancer cells and regression of tumor growth by K27 targeting sulfiredoxin.
Neoplasms
Identification and characterization of human leukocyte antigen class I ligands in renal cell carcinoma cells.
Neoplasms
NRF2, DJ1 and SNRX1 and their prognostic impact in astrocytic gliomas.
Neoplasms
Nuclear factor erythroid-derived 2-like 2 (Nrf2) and DJ1 are prognostic factors in lung cancer.
Neoplasms
Sulfiredoxin inhibitor induces preferential death of cancer cells through reactive oxygen species-mediated mitochondrial damage.
Neoplasms
Sulfiredoxin is an AP-1 target gene that is required for transformation and shows elevated expression in human skin malignancies.
Neoplasms
Sulfiredoxin May Promote Cervical Cancer Metastasis via Wnt/?-Catenin Signaling Pathway.
Neoplasms
Sulfiredoxin may promote metastasis and invasion of cervical squamous cell carcinoma by epithelial-mesenchymal transition.
Neoplasms
Sulfiredoxin redox-sensitive interaction with S100A4 and non-muscle myosin IIA regulates cancer cell motility.
Neoplasms
Sulfiredoxin-Peroxiredoxin IV axis promotes human lung cancer progression through modulation of specific phosphokinase signaling.
Neoplasms
The cinnamon-derived Michael acceptor cinnamic aldehyde impairs melanoma cell proliferation, invasiveness, and tumor growth.
Neoplasms
Thioredoxin system-mediated regulation of mutant Kras associated pancreatic neoplasia and cancer.
Neoplasms
Tumor promoter-induced sulfiredoxin is required for mouse skin tumorigenesis.
Neoplasms
[Highly expressed sulfiredoxin and ?-catenin are associated with malignancy of cervical squamous cell carcinoma].
Neurodegenerative Diseases
Role of sulfiredoxin as a peroxiredoxin-2 denitrosylase in human iPSC-derived dopaminergic neurons.
Neurodegenerative Diseases
Sulfiredoxin-1 protects primary cultured astrocytes from ischemia-induced damage.
Pancreatic Neoplasms
Nuclear Nrf2 expression is related to a poor survival in pancreatic adenocarcinoma.
Prostatic Neoplasms
Increased Peroxiredoxin 6 Expression Predicts Biochemical Recurrence in Prostate Cancer Patients After Radical Prostatectomy.
Pulmonary Disease, Chronic Obstructive
The aryl hydrocarbon receptor suppresses cigarette-smoke-induced oxidative stress in association with dioxin response element (DRE)-independent regulation of sulfiredoxin 1.
Shock, Septic
Sulfiredoxin Protects Mice from Lipopolysaccharide-Induced Endotoxic Shock.
Skin Neoplasms
Tumor promoter-induced sulfiredoxin is required for mouse skin tumorigenesis.
Stroke
Neuroprotective effects of sulfiredoxin-1 during cerebral ischemia/reperfusion oxidative stress injury in rats.
Stroke
Sulfiredoxin-1 protects primary cultured astrocytes from ischemia-induced damage.
Uterine Cervical Neoplasms
Sulfiredoxin May Promote Cervical Cancer Metastasis via Wnt/?-Catenin Signaling Pathway.
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Jönsson, T.J.; Murray, M.S.; Johnson, L.C.; Poole, L.B.; Lowther, W.T.
Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin
Biochemistry
44
8634-8642
2005
Homo sapiens, Homo sapiens (Q9BYN0)
brenda
Findlay, V.J.; Tapiero, H.; Townsend, D.M.
Sulfiredoxin: a potential therapeutic agent?
Biomed. Pharmacother.
59
374-379
2005
Homo sapiens
brenda
Chang, T.S.; Jeong, W.; Woo, H.A.; Lee, S.M.; Park, S.; Rhee, S.G.
Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
J. Biol. Chem.
279
50994-51001
2004
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Woo, H.A.; Jeong, W.; Chang, T.S.; Park, K.J.; Park, S.J.; Yang, J.S.; Rhee, S.G.
Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins
J. Biol. Chem.
280
3125-3128
2005
Rattus norvegicus
brenda
Biteau, B.; Labarre, J.; Toledano, M.B.
ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
Nature
425
980-984
2003
Saccharomyces cerevisiae
brenda
Lee, D.Y.; Park, S.J.; Jeong, W.; Sung, H.J.; Oho, T.; Wu, X.; Rhee, S.G.; Gruschus, J.M.
Mutagenesis and modeling of the peroxiredoxin (Prx) complex with the NMR structure of ATP-bound human sulfiredoxin implicate aspartate 187 of Prx I as the catalytic residue in ATP hydrolysis
Biochemistry
45
15301-15309
2006
Homo sapiens, Homo sapiens (Q9BYN0)
brenda
Findlay, V.J.; Townsend, D.M.; Morris, T.E.; Fraser, J.P.; He, L.; Tew, K.D.
A novel role for human sulfiredoxin in the reversal of glutathionylation
Cancer Res.
66
6800-6806
2006
Homo sapiens, Homo sapiens (Q9BYN0)
brenda
Liu, X.P.; Liu, X.Y.; Zhang, J.; Xia, Z.L.; Liu, X.; Qin, H.J.; Wang, D.W.
Molecular and functional characterization of sulfiredoxin homologs from higher plants
Cell Res.
16
287-296
2006
Arabidopsis thaliana (Q8GY89), Oryza sativa
brenda
Jeong, W.; Park, S.J.; Chang, T.S.; Lee, D.Y.; Rhee, S.G.
Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin
J. Biol. Chem.
281
14400-14407
2006
Homo sapiens
brenda
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Homo sapiens, Saccharomyces cerevisiae
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Arabidopsis thaliana, Arabidopsis thaliana (Q8GY89)
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Saccharomyces cerevisiae
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Homo sapiens, Homo sapiens (Q9BYN0)
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Rattus norvegicus
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Joensson, T.J.; Johnson, L.C.; Lowther, W.T.
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Nature
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2008
Homo sapiens, Homo sapiens (Q9BYN0)
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Homo sapiens
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Homo sapiens, Mus musculus
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Park, J.W.; Mieyal, J.J.; Rhee, S.G.; Chock, P.B.
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Homo sapiens
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Roussel, X.; Kriznik, A.; Richard, C.; Rahuel-Clermont, S.; Branlant, G.
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Saccharomyces cerevisiae
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Homo sapiens
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Lei, K.; Townsend, D.M.; Tew, K.D.
Protein cysteine sulfinic acid reductase (sulfiredoxin) as a regulator of cell proliferation and drug response
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Homo sapiens
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Iglesias-Baena, I.; Barranco-Medina, S.; Lazaro-Payo, A.; Lopez-Jaramillo, F.J.; Sevilla, F.; Lazaro, J.J.
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Arabidopsis thaliana, Arabidopsis thaliana Columbia
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Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Arabidopsis thaliana
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Mus musculus, Mus musculus (Q9D975)
brenda
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Arabidopsis thaliana (Q8GY89), Pisum sativum (D2KKL9), Pisum sativum
brenda
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Sulfiredoxin involved in the protection of peroxiredoxins against hyperoxidation in the early hyperglycaemia
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Rattus norvegicus
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Rhee, S.G.; Kil, I.S.
Mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin Linking mitochondrial function to circadian rhythm
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2016
Mus musculus
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Calderon, A.; Lazaro-Payo, A.; Iglesias-Baena, I.; Camejo, D.; Lazaro, J.J.; Sevilla, F.; Jimenez, A.
Glutathionylation of pea chloroplast 2-Cys Prx and mitochondrial Prx IIF affects their structure and peroxidase activity and sulfiredoxin deglutathionylates only the 2-Cys Prx
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Pisum sativum
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Sevilla, F.; Camejo, D.; Ortiz-Espin, A.; Calderon, A.; Lazaro, J.J.; Jimenez, A.
The thioredoxin/peroxiredoxin/sulfiredoxin system current overview on its redox function in plants and regulation by reactive oxygen and nitrogen species
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2015
Arabidopsis thaliana
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Li, Q.; Yu, S.; Wu, J.; Zou, Y.; Zhao, Y.
Sulfiredoxin-1 protects PC12 cells against oxidative stress induced by hydrogen peroxide
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Rattus norvegicus
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Kil, I.S.; Bae, S.H.; Rhee, S.G.
Study of the signaling function of sulfiredoxin and peroxiredoxin III in isolated adrenal gland unsuitability of clonal and primary adrenocortical cells
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Mus musculus
brenda