메뉴 건너뛰기




Volumn 62, Issue 5, 2013, Pages 738-749

Glutathione and thioredoxin dependent systems in neurodegenerative disease: What can be learned from reverse genetics in mice

Author keywords

Glutathione; Knockout; Neurodegeneration; Oxidative stress; Thiols; Thioredoxin

Indexed keywords

ACYLTRANSFERASE; ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; AMINE OXIDASE (FLAVIN CONTAINING); ANTIINFECTIVE AGENT; APOPTOSIS SIGNAL REGULATING KINASE 1; CASPASE; CASPASE 3; CASPASE 8; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROXYL RADICAL; NITRIC OXIDE; PEROXIREDOXIN; PHOSPHATASE; PROTEIN TYROSINE KINASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; SUPEROXIDE DISMUTASE; TAU PROTEIN; THIOREDOXIN; THIOREDOXIN REDUCTASE; XANTHINE OXIDASE;

EID: 84875708705     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2013.01.010     Document Type: Review
Times cited : (32)

References (164)
  • 1
    • 0021318441 scopus 로고
    • Catalase in vitro
    • H. Aebi Catalase in vitro Methods Enzymol. 105 1984 121 126
    • (1984) Methods Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 2
    • 84859517209 scopus 로고    scopus 로고
    • Glutathione S-transferase omega genes in Alzheimer and Parkinson disease risk, age-at-diagnosis and brain gene expression: An association study with mechanistic implications
    • M. Allen, F. Zou, H.S. Chai, C.S. Younkin, R. Miles, A.A. Nair, J.E. Crook, V.S. Pankratz, M.M. Carrasquillo, and C.N. Rowley Glutathione S-transferase omega genes in Alzheimer and Parkinson disease risk, age-at-diagnosis and brain gene expression: an association study with mechanistic implications Mol. Neurodegener. 7 2012 13
    • (2012) Mol. Neurodegener. , vol.7 , pp. 13
    • Allen, M.1    Zou, F.2    Chai, H.S.3    Younkin, C.S.4    Miles, R.5    Nair, A.A.6    Crook, J.E.7    Pankratz, V.S.8    Carrasquillo, M.M.9    Rowley, C.N.10
  • 4
    • 29444459269 scopus 로고    scopus 로고
    • Neuronal glutathione deficiency and age-dependent neurodegeneration in the EAAC1 deficient mouse
    • K. Aoyama, S.W. Suh, A.M. Hamby, J. Liu, W.Y. Chan, Y. Chen, and R.A. Swanson Neuronal glutathione deficiency and age-dependent neurodegeneration in the EAAC1 deficient mouse Nat. Neurosci. 9 2006 119 126
    • (2006) Nat. Neurosci. , vol.9 , pp. 119-126
    • Aoyama, K.1    Suh, S.W.2    Hamby, A.M.3    Liu, J.4    Chan, W.Y.5    Chen, Y.6    Swanson, R.A.7
  • 6
    • 0021348393 scopus 로고
    • Induction of cystine and glutamate transport activity in human fibroblasts by diethyl maleate and other electrophilic agents
    • S. Bannai Induction of cystine and glutamate transport activity in human fibroblasts by diethyl maleate and other electrophilic agents J. Biol. Chem. 259 1984 2435 2440
    • (1984) J. Biol. Chem. , vol.259 , pp. 2435-2440
    • Bannai, S.1
  • 7
    • 0021215013 scopus 로고
    • Transport of cystine and cysteine in mammalian cells
    • S. Bannai Transport of cystine and cysteine in mammalian cells Biochim. Biophys. Acta 779 1984 289 306
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 289-306
    • Bannai, S.1
  • 8
    • 33847746679 scopus 로고    scopus 로고
    • Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: Implications for diseases in the cardiovascular system
    • C. Berndt, C.H. Lillig, and A. Holmgren Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system Am. J. Physiol. Heart Circ. Physiol. 292 2007 H1227 H1236
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 11
    • 84856217140 scopus 로고    scopus 로고
    • Mercury and selenium interaction in vivo: Effects on thioredoxin reductase and glutathione peroxidase
    • V. Branco, J. Canario, J. Lu, A. Holmgren, and C. Carvalho Mercury and selenium interaction in vivo: effects on thioredoxin reductase and glutathione peroxidase Free Radic. Biol. Med. 52 2012 781 793
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 781-793
    • Branco, V.1    Canario, J.2    Lu, J.3    Holmgren, A.4    Carvalho, C.5
  • 13
    • 84875697554 scopus 로고    scopus 로고
    • Glutathione peroxidases
    • 10.1016/j.bbagen.2012.11.020 (Epub ahead of print)
    • R. Brigelius-Flohe, and M. Maiorino Glutathione peroxidases Biochim. Biophys. Acta 2012 10.1016/j.bbagen.2012.11.020 (Epub ahead of print)
    • (2012) Biochim. Biophys. Acta
    • Brigelius-Flohe, R.1    Maiorino, M.2
  • 14
    • 0029064709 scopus 로고
    • Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia
    • L.M. Carlsson, J. Jonsson, T. Edlund, and S.L. Marklund Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia Proc. Natl. Acad. Sci. USA 92 1995 6264 6268
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6264-6268
    • Carlsson, L.M.1    Jonsson, J.2    Edlund, T.3    Marklund, S.L.4
  • 16
    • 84864003121 scopus 로고    scopus 로고
    • Necrostatin-1 attenuates mitochondrial dysfunction in neurons and astrocytes following neonatal hypoxia-ischemia
    • R. Chavez-Valdez, L.J. Martin, D.L. Flock, and F.J. Northington Necrostatin-1 attenuates mitochondrial dysfunction in neurons and astrocytes following neonatal hypoxia-ischemia Neuroscience 219 2012 192 203
    • (2012) Neuroscience , vol.219 , pp. 192-203
    • Chavez-Valdez, R.1    Martin, L.J.2    Flock, D.L.3    Northington, F.J.4
  • 17
    • 79251577061 scopus 로고    scopus 로고
    • The regulation of autophagy-unanswered questions
    • Y. Chen, and D.J. Klionsky The regulation of autophagy-unanswered questions J. Cell Sci. 124 2011 161 170
    • (2011) J. Cell Sci. , vol.124 , pp. 161-170
    • Chen, Y.1    Klionsky, D.J.2
  • 18
    • 0021276089 scopus 로고
    • Metabolism of the neurotoxic tertiary amine, MPTP, by brain monoamine oxidase
    • K. Chiba, A. Trevor, and N. Castagnoli Jr. Metabolism of the neurotoxic tertiary amine, MPTP, by brain monoamine oxidase Biochem. Biophys. Res. Commun. 120 1984 574 578
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 574-578
    • Chiba, K.1    Trevor, A.2    Castagnoli, Jr.N.3
  • 19
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • H. Choi, S. Kim, P. Mukhopadhyay, S. Cho, J. Woo, G. Storz, and S.E. Ryu Structural basis of the redox switch in the OxyR transcription factor Cell 105 2001 103 113
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5    Storz, G.6    Ryu, S.E.7
  • 20
    • 72649107570 scopus 로고    scopus 로고
    • Transgenic mouse models for the vital selenoenzymes cytosolic thioredoxin reductase, mitochondrial thioredoxin reductase and glutathione peroxidase 4
    • M. Conrad Transgenic mouse models for the vital selenoenzymes cytosolic thioredoxin reductase, mitochondrial thioredoxin reductase and glutathione peroxidase 4 Biochim. Biophys. Acta 1790 2009 1575 1585
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1575-1585
    • Conrad, M.1
  • 23
    • 84859031263 scopus 로고    scopus 로고
    • The oxidative stress-inducible cystine/glutamate antiporter, system x (c) (-): Cystine supplier and beyond
    • M. Conrad, and H. Sato The oxidative stress-inducible cystine/glutamate antiporter, system x (c) (-): cystine supplier and beyond Amino Acids 42 2012 231 246
    • (2012) Amino Acids , vol.42 , pp. 231-246
    • Conrad, M.1    Sato, H.2
  • 24
    • 77649267654 scopus 로고    scopus 로고
    • Unveiling the molecular mechanisms behind selenium-related diseases through knockout mouse studies
    • M. Conrad, and U. Schweizer Unveiling the molecular mechanisms behind selenium-related diseases through knockout mouse studies Antioxid. Redox Signal. 12 2010 851 865
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 851-865
    • Conrad, M.1    Schweizer, U.2
  • 25
    • 33646369421 scopus 로고    scopus 로고
    • Lack of glutathione peroxidase-1 exacerbates Abeta-mediated neurotoxicity in cortical neurons
    • P.J. Crack, K. Cimdins, U. Ali, P.J. Hertzog, and R.C. Iannello Lack of glutathione peroxidase-1 exacerbates Abeta-mediated neurotoxicity in cortical neurons J. Neural. Transm. 113 2006 645 657
    • (2006) J. Neural. Transm. , vol.113 , pp. 645-657
    • Crack, P.J.1    Cimdins, K.2    Ali, U.3    Hertzog, P.J.4    Iannello, R.C.5
  • 26
    • 0034801462 scopus 로고    scopus 로고
    • Increased infarct size and exacerbated apoptosis in the glutathione peroxidase-1 (Gpx-1) knockout mouse brain in response to ischemia/reperfusion injury
    • P.J. Crack, J.M. Taylor, N.J. Flentjar, J. de Haan, P. Hertzog, R.C. Iannello, and I. Kola Increased infarct size and exacerbated apoptosis in the glutathione peroxidase-1 (Gpx-1) knockout mouse brain in response to ischemia/reperfusion injury J. Neurochem. 78 2001 1389 1399
    • (2001) J. Neurochem. , vol.78 , pp. 1389-1399
    • Crack, P.J.1    Taylor, J.M.2    Flentjar, N.J.3    De Haan, J.4    Hertzog, P.5    Iannello, R.C.6    Kola, I.7
  • 27
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • B. D'Autreaux, and M.B. Toledano ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis Nat. Rev. Mol. Cell Biol. 8 2007 813 824
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 28
    • 79955824241 scopus 로고    scopus 로고
    • The "dying-back" phenomenon of motor neurons in ALS
    • M. Dadon-Nachum, E. Melamed, and D. Offen The "dying-back" phenomenon of motor neurons in ALS J. Mol. Neurosci. MN 43 2011 470 477
    • (2011) J. Mol. Neurosci. MN , vol.43 , pp. 470-477
    • Dadon-Nachum, M.1    Melamed, E.2    Offen, D.3
  • 30
    • 79955759157 scopus 로고    scopus 로고
    • Loss of system x(c)- does not induce oxidative stress but decreases extracellular glutamate in hippocampus and influences spatial working memory and limbic seizure susceptibility
    • D. De Bundel, A. Schallier, E. Loyens, R. Fernando, H. Miyashita, J. Van Liefferinge, K. Vermoesen, S. Bannai, H. Sato, and Y. Michotte Loss of system x(c)- does not induce oxidative stress but decreases extracellular glutamate in hippocampus and influences spatial working memory and limbic seizure susceptibility J. Neurosci. 31 2011 5792 5803
    • (2011) J. Neurosci. , vol.31 , pp. 5792-5803
    • De Bundel, D.1    Schallier, A.2    Loyens, E.3    Fernando, R.4    Miyashita, H.5    Van Liefferinge, J.6    Vermoesen, K.7    Bannai, S.8    Sato, H.9    Michotte, Y.10
  • 33
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • B.C. Dickinson, and C.J. Chang Chemistry and biology of reactive oxygen species in signaling or stress responses Nat. Chem. Biol. 7 2011 504 511
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 36
    • 0033859495 scopus 로고    scopus 로고
    • Low glutathione peroxidase activity in Gpx1 knockout mice protects jejunum crypts from gamma-irradiation damage
    • R.S. Esworthy, J.R. Mann, M. Sam, and F.F. Chu Low glutathione peroxidase activity in Gpx1 knockout mice protects jejunum crypts from gamma-irradiation damage Am. J. Physiol. Gastrointest. Liver Physiol. 279 2000 G426 G436
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.279
    • Esworthy, R.S.1    Mann, J.R.2    Sam, M.3    Chu, F.F.4
  • 37
    • 64749101531 scopus 로고    scopus 로고
    • Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
    • G. Ferrer-Sueta, and R. Radi Chemical biology of peroxynitrite: kinetics, diffusion, and radicals ACS Chem. Biol. 4 2009 161 177
    • (2009) ACS Chem. Biol. , vol.4 , pp. 161-177
    • Ferrer-Sueta, G.1    Radi, R.2
  • 38
    • 0033597885 scopus 로고    scopus 로고
    • Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase
    • A.B. Fisher, C. Dodia, Y. Manevich, J.W. Chen, and S.I. Feinstein Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase J. Biol. Chem. 274 1999 21326 21334
    • (1999) J. Biol. Chem. , vol.274 , pp. 21326-21334
    • Fisher, A.B.1    Dodia, C.2    Manevich, Y.3    Chen, J.W.4    Feinstein, S.I.5
  • 40
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • I. Fridovich Superoxide radical and superoxide dismutases Annu. Rev. Biochem. 64 1995 97 112
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 41
    • 0032820359 scopus 로고    scopus 로고
    • Knockout of cellular glutathione peroxidase gene renders mice susceptible to diquat-induced oxidative stress
    • Y. Fu, W.H. Cheng, J.M. Porres, D.A. Ross, and X.G. Lei Knockout of cellular glutathione peroxidase gene renders mice susceptible to diquat-induced oxidative stress Free Radic. Biol. Med. 27 1999 605 611
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 605-611
    • Fu, Y.1    Cheng, W.H.2    Porres, J.M.3    Ross, D.A.4    Lei, X.G.5
  • 45
    • 84857058225 scopus 로고    scopus 로고
    • Control of autophagy as a therapy for neurodegenerative disease
    • H. Harris, and D.C. Rubinsztein Control of autophagy as a therapy for neurodegenerative disease Nat. Rev. Neurol. 8 2012 108 117
    • (2012) Nat. Rev. Neurol. , vol.8 , pp. 108-117
    • Harris, H.1    Rubinsztein, D.C.2
  • 47
    • 0025904916 scopus 로고
    • Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate
    • H.C. Hawkins, E.C. Blackburn, and R.B. Freedman Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate Biochem. J. 275 Pt 2 1991 349 353
    • (1991) Biochem. J. , vol.275 , Issue.PART 2 , pp. 349-353
    • Hawkins, H.C.1    Blackburn, E.C.2    Freedman, R.B.3
  • 48
    • 84857833776 scopus 로고    scopus 로고
    • Cell signalling by reactive lipid species: New concepts and molecular mechanisms
    • A. Higdon, A.R. Diers, J.Y. Oh, A. Landar, and V.M. Darley-Usmar Cell signalling by reactive lipid species: new concepts and molecular mechanisms Biochem. J. 442 2012 453 464
    • (2012) Biochem. J. , vol.442 , pp. 453-464
    • Higdon, A.1    Diers, A.R.2    Oh, J.Y.3    Landar, A.4    Darley-Usmar, V.M.5
  • 50
    • 0030971057 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
    • Y.S. Ho, J.L. Magnenat, R.T. Bronson, J. Cao, M. Gargano, M. Sugawara, and C.D. Funk Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia J. Biol. Chem. 272 1997 16644 16651
    • (1997) J. Biol. Chem. , vol.272 , pp. 16644-16651
    • Ho, Y.S.1    Magnenat, J.L.2    Bronson, R.T.3    Cao, J.4    Gargano, M.5    Sugawara, M.6    Funk, C.D.7
  • 51
    • 34548844721 scopus 로고    scopus 로고
    • Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia
    • Y.S. Ho, Y. Xiong, D.S. Ho, J. Gao, B.H. Chua, H. Pai, and J.J. Mieyal Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia Free Radic. Biol. Med. 43 2007 1299 1312
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1299-1312
    • Ho, Y.S.1    Xiong, Y.2    Ho, D.S.3    Gao, J.4    Chua, B.H.5    Pai, H.6    Mieyal, J.J.7
  • 52
    • 3543040601 scopus 로고    scopus 로고
    • Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury
    • Y.S. Ho, Y. Xiong, W. Ma, A. Spector, and D.S. Ho Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury J. Biol. Chem. 279 2004 32804 32812
    • (2004) J. Biol. Chem. , vol.279 , pp. 32804-32812
    • Ho, Y.S.1    Xiong, Y.2    Ma, W.3    Spector, A.4    Ho, D.S.5
  • 53
    • 77952311188 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
    • A. Holmgren, and J. Lu Thioredoxin and thioredoxin reductase: current research with special reference to human disease Biochem. Biophys. Res. Commun. 396 2010 120 124
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 120-124
    • Holmgren, A.1    Lu, J.2
  • 54
    • 77953363542 scopus 로고    scopus 로고
    • DJ-1 protects against oxidative damage by regulating the thioredoxin/ASK1 complex
    • J.Y. Im, K.W. Lee, E. Junn, and M.M. Mouradian DJ-1 protects against oxidative damage by regulating the thioredoxin/ASK1 complex Neurosci. Res. 67 2010 203 208
    • (2010) Neurosci. Res. , vol.67 , pp. 203-208
    • Im, J.Y.1    Lee, K.W.2    Junn, E.3    Mouradian, M.M.4
  • 55
    • 84863518914 scopus 로고    scopus 로고
    • DJ-1 induces thioredoxin 1 expression through the Nrf2 pathway
    • J.Y. Im, K.W. Lee, J.M. Woo, E. Junn, and M.M. Mouradian DJ-1 induces thioredoxin 1 expression through the Nrf2 pathway Hum. Mol. Genet. 21 2012 3013 3024
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 3013-3024
    • Im, J.Y.1    Lee, K.W.2    Woo, J.M.3    Junn, E.4    Mouradian, M.M.5
  • 56
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • J.A. Imlay Cellular defenses against superoxide and hydrogen peroxide Annu. Rev. Biochem. 77 2008 755 776
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 58
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • C. Johansson, C.H. Lillig, and A. Holmgren Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase J. Biol. Chem. 279 2004 7537 7543
    • (2004) J. Biol. Chem. , vol.279 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 59
    • 36549008295 scopus 로고    scopus 로고
    • Constitutive expression and functional characterization of mitochondrial glutaredoxin (Grx2) in mouse and human brain
    • S. Karunakaran, U. Saeed, S. Ramakrishnan, R.C. Koumar, and V. Ravindranath Constitutive expression and functional characterization of mitochondrial glutaredoxin (Grx2) in mouse and human brain Brain Res. 1185 2007 8 17
    • (2007) Brain Res. , vol.1185 , pp. 8-17
    • Karunakaran, S.1    Saeed, U.2    Ramakrishnan, S.3    Koumar, R.C.4    Ravindranath, V.5
  • 60
    • 84863137295 scopus 로고    scopus 로고
    • Glutathione s-transferase omega 1 activity is sufficient to suppress neurodegeneration in a Drosophila model of Parkinson disease
    • K. Kim, S.H. Kim, J. Kim, H. Kim, and J. Yim Glutathione s-transferase omega 1 activity is sufficient to suppress neurodegeneration in a Drosophila model of Parkinson disease J. Biol. Chem. 287 2012 6628 6641
    • (2012) J. Biol. Chem. , vol.287 , pp. 6628-6641
    • Kim, K.1    Kim, S.H.2    Kim, J.3    Kim, H.4    Yim, J.5
  • 62
    • 78650723904 scopus 로고    scopus 로고
    • Inducible dopaminergic glutathione depletion in an alpha-synuclein transgenic mouse model results in age-related olfactory dysfunction
    • Y.H. Kim, S. Lussier, A. Rane, S.W. Choi, and J.K. Andersen Inducible dopaminergic glutathione depletion in an alpha-synuclein transgenic mouse model results in age-related olfactory dysfunction Neuroscience 172 2011 379 386
    • (2011) Neuroscience , vol.172 , pp. 379-386
    • Kim, Y.H.1    Lussier, S.2    Rane, A.3    Choi, S.W.4    Andersen, J.K.5
  • 64
  • 71
    • 67649644885 scopus 로고    scopus 로고
    • Peroxiredoxin III-deficiency sensitizes macrophages to oxidative stress
    • L. Li, T. Kaifu, M. Obinata, and T. Takai Peroxiredoxin III-deficiency sensitizes macrophages to oxidative stress J. Biochem. 145 2009 425 427
    • (2009) J. Biochem. , vol.145 , pp. 425-427
    • Li, L.1    Kaifu, T.2    Obinata, M.3    Takai, T.4
  • 74
    • 0030867994 scopus 로고    scopus 로고
    • A role for 12-lipoxygenase in nerve cell death caused by glutathione depletion
    • Y. Li, P. Maher, and D. Schubert A role for 12-lipoxygenase in nerve cell death caused by glutathione depletion Neuron 19 1997 453 463
    • (1997) Neuron , vol.19 , pp. 453-463
    • Li, Y.1    Maher, P.2    Schubert, D.3
  • 75
    • 71449113005 scopus 로고    scopus 로고
    • Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions
    • H. Liang, S.E. Yoo, R. Na, C.A. Walter, A. Richardson, and Q. Ran Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions J. Biol. Chem. 284 2009 30836 30844
    • (2009) J. Biol. Chem. , vol.284 , pp. 30836-30844
    • Liang, H.1    Yoo, S.E.2    Na, R.3    Walter, C.A.4    Richardson, A.5    Ran, Q.6
  • 77
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • M.T. Lin, and M.F. Beal Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases Nature 443 2006 787 795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 79
    • 53449095486 scopus 로고    scopus 로고
    • Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse
    • S. Lofgren, M.R. Fernando, K.Y. Xing, Y. Wang, C.A. Kuszynski, Y.S. Ho, and M.F. Lou Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse Invest. Ophthalmol. Vis. Sci. 49 2008 4497 4505
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 4497-4505
    • Lofgren, S.1    Fernando, M.R.2    Xing, K.Y.3    Wang, Y.4    Kuszynski, C.A.5    Ho, Y.S.6    Lou, M.F.7
  • 80
    • 50249108403 scopus 로고    scopus 로고
    • Membrane redox state and apoptosis: Death by peroxide
    • J. Loscalzo Membrane redox state and apoptosis: death by peroxide Cell Metab. 8 2008 182 183
    • (2008) Cell Metab. , vol.8 , pp. 182-183
    • Loscalzo, J.1
  • 81
    • 0019350010 scopus 로고
    • Coupling of dopamine oxidation (monoamine oxidase activity) to glutathione oxidation via the generation of hydrogen peroxide in rat brain homogenates
    • H.S. Maker, C. Weiss, D.J. Silides, and G. Cohen Coupling of dopamine oxidation (monoamine oxidase activity) to glutathione oxidation via the generation of hydrogen peroxide in rat brain homogenates J. Neurochem. 36 1981 589 593
    • (1981) J. Neurochem. , vol.36 , pp. 589-593
    • Maker, H.S.1    Weiss, C.2    Silides, D.J.3    Cohen, G.4
  • 84
    • 0029443151 scopus 로고
    • The chemistry of lipid alkoxyl radicals and their role in metal-amplified lipid peroxidation
    • L.J. Marnett, and A.L. Wilcox The chemistry of lipid alkoxyl radicals and their role in metal-amplified lipid peroxidation Biochem. Soc. Symp. 61 1995 65 72
    • (1995) Biochem. Soc. Symp. , vol.61 , pp. 65-72
    • Marnett, L.J.1    Wilcox, A.L.2
  • 86
    • 2042470971 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene
    • M. Matsui, M. Oshima, H. Oshima, K. Takaku, T. Maruyama, J. Yodoi, and M.M. Taketo Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene Dev. Biol. 178 1996 179 185
    • (1996) Dev. Biol. , vol.178 , pp. 179-185
    • Matsui, M.1    Oshima, M.2    Oshima, H.3    Takaku, K.4    Maruyama, T.5    Yodoi, J.6    Taketo, M.M.7
  • 88
    • 0031760436 scopus 로고    scopus 로고
    • Ovarian function in superoxide dismutase 1 and 2 knockout mice
    • M.M. Matzuk, L. Dionne, Q. Guo, T.R. Kumar, and R.M. Lebovitz Ovarian function in superoxide dismutase 1 and 2 knockout mice Endocrinology 139 1998 4008 4011
    • (1998) Endocrinology , vol.139 , pp. 4008-4011
    • Matzuk, M.M.1    Dionne, L.2    Guo, Q.3    Kumar, T.R.4    Lebovitz, R.M.5
  • 91
    • 33745154155 scopus 로고    scopus 로고
    • Conditional knockout of Mn superoxide dismutase in postnatal motor neurons reveals resistance to mitochondrial generated superoxide radicals
    • H. Misawa, K. Nakata, J. Matsuura, Y. Moriwaki, K. Kawashima, T. Shimizu, T. Shirasawa, and R. Takahashi Conditional knockout of Mn superoxide dismutase in postnatal motor neurons reveals resistance to mitochondrial generated superoxide radicals Neurobiol. Dis. 23 2006 169 177
    • (2006) Neurobiol. Dis. , vol.23 , pp. 169-177
    • Misawa, H.1    Nakata, K.2    Matsuura, J.3    Moriwaki, Y.4    Kawashima, K.5    Shimizu, T.6    Shirasawa, T.7    Takahashi, R.8
  • 92
    • 0026975771 scopus 로고
    • Reactive oxygen-reducing and protein-refolding activities of adult T cell leukemia-derived factor/human thioredoxin
    • A. Mitsui, T. Hirakawa, and J. Yodoi Reactive oxygen-reducing and protein-refolding activities of adult T cell leukemia-derived factor/human thioredoxin Biochem. Biophys. Res. Commun. 186 1992 1220 1226
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1220-1226
    • Mitsui, A.1    Hirakawa, T.2    Yodoi, J.3
  • 93
    • 31044456412 scopus 로고    scopus 로고
    • Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen
    • S. Miyamoto, G.R. Martinez, D. Rettori, O. Augusto, M.H. Medeiros, and P. Di Mascio Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen Proc. Natl. Acad. Sci. USA 103 2006 293 298
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 293-298
    • Miyamoto, S.1    Martinez, G.R.2    Rettori, D.3    Augusto, O.4    Medeiros, M.H.5    Di Mascio, P.6
  • 94
    • 77955035878 scopus 로고    scopus 로고
    • Reactive oxygen species in TNFalpha-induced signaling and cell death
    • M.J. Morgan, and Z.G. Liu Reactive oxygen species in TNFalpha-induced signaling and cell death Mol. Cells 30 2010 1 12
    • (2010) Mol. Cells , vol.30 , pp. 1-12
    • Morgan, M.J.1    Liu, Z.G.2
  • 95
    • 0031974368 scopus 로고    scopus 로고
    • Mitochondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency
    • K. Murakami, T. Kondo, M. Kawase, Y. Li, S. Sato, S.F. Chen, and P.H. Chan Mitochondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency J. Neurosci. 18 1998 205 213
    • (1998) J. Neurosci. , vol.18 , pp. 205-213
    • Murakami, K.1    Kondo, T.2    Kawase, M.3    Li, Y.4    Sato, S.5    Chen, S.F.6    Chan, P.H.7
  • 96
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 100
    • 0037305881 scopus 로고    scopus 로고
    • The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice
    • L. Nonn, R.R. Williams, R.P. Erickson, and G. Powis The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice Mol. Cell. Biol. 23 2003 916 922
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 916-922
    • Nonn, L.1    Williams, R.R.2    Erickson, R.P.3    Powis, G.4
  • 102
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria
    • A. Okado-Matsumoto, and I. Fridovich Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria J. Biol. Chem. 276 2001 38388 38393
    • (2001) J. Biol. Chem. , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 105
    • 80053513183 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatases by reversible oxidation
    • A. Ostman, J. Frijhoff, A. Sandin, and F.D. Bohmer Regulation of protein tyrosine phosphatases by reversible oxidation J. Biochem. 150 2011 345 356
    • (2011) J. Biochem. , vol.150 , pp. 345-356
    • Ostman, A.1    Frijhoff, J.2    Sandin, A.3    Bohmer, F.D.4
  • 107
    • 33747885659 scopus 로고    scopus 로고
    • Cyclooxygenases, lipoxygenases, and epoxygenases in CNS: Their role and involvement in neurological disorders
    • J.W. Phillis, L.A. Horrocks, and A.A. Farooqui Cyclooxygenases, lipoxygenases, and epoxygenases in CNS: their role and involvement in neurological disorders Brain Res. Rev. 52 2006 201 243
    • (2006) Brain Res. Rev. , vol.52 , pp. 201-243
    • Phillis, J.W.1    Horrocks, L.A.2    Farooqui, A.A.3
  • 108
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • P.J. Pomposiello, and B. Demple Redox-operated genetic switches: the SoxR and OxyR transcription factors Trends Biotechnol. 19 2001 109 114
    • (2001) Trends Biotechnol. , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 115
    • 0024999558 scopus 로고
    • Reactions of Fe(II)-ATP and Fe(II)-citrate complexes with t-butyl hydroperoxide and cumyl hydroperoxide
    • J.D. Rush, and W.H. Koppenol Reactions of Fe(II)-ATP and Fe(II)-citrate complexes with t-butyl hydroperoxide and cumyl hydroperoxide FEBS Lett. 275 1990 114 116
    • (1990) FEBS Lett. , vol.275 , pp. 114-116
    • Rush, J.D.1    Koppenol, W.H.2
  • 120
    • 0037337666 scopus 로고    scopus 로고
    • Gene disruption discloses role of selenoprotein P in selenium delivery to target tissues
    • L. Schomburg, U. Schweizer, B. Holtmann, L. Flohe, M. Sendtner, and J. Kohrle Gene disruption discloses role of selenoprotein P in selenium delivery to target tissues Biochem. J. 370 2003 397 402
    • (2003) Biochem. J. , vol.370 , pp. 397-402
    • Schomburg, L.1    Schweizer, U.2    Holtmann, B.3    Flohe, L.4    Sendtner, M.5    Kohrle, J.6
  • 122
    • 0032227107 scopus 로고    scopus 로고
    • Characterization, regulation of the expression and putative roles of two glutathione peroxidase proteins found in the mouse epididymis
    • V. Schwaab, J.J. Lareyre, P. Vernet, E. Pons, J. Faure, J.P. Dufaure, and J.R. Drevet Characterization, regulation of the expression and putative roles of two glutathione peroxidase proteins found in the mouse epididymis J. Reprod. Fertil. Suppl. 53 1998 157 162
    • (1998) J. Reprod. Fertil. Suppl. , vol.53 , pp. 157-162
    • Schwaab, V.1    Lareyre, J.J.2    Vernet, P.3    Pons, E.4    Faure, J.5    Dufaure, J.P.6    Drevet, J.R.7
  • 124
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • M.S. Seo, S.W. Kang, K. Kim, I.C. Baines, T.H. Lee, and S.G. Rhee Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate J. Biol. Chem. 275 2000 20346 20354
    • (2000) J. Biol. Chem. , vol.275 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 125
    • 0033515794 scopus 로고    scopus 로고
    • Differential effects of l-buthionine sulfoximine and ethacrynic acid on glutathione levels and mitochondrial function in PC12 cells
    • J. Seyfried, F. Soldner, J.B. Schulz, T. Klockgether, K.A. Kovar, and U. Wullner Differential effects of l-buthionine sulfoximine and ethacrynic acid on glutathione levels and mitochondrial function in PC12 cells Neurosci. Lett. 264 1999 1 4
    • (1999) Neurosci. Lett. , vol.264 , pp. 1-4
    • Seyfried, J.1    Soldner, F.2    Schulz, J.B.3    Klockgether, T.4    Kovar, K.A.5    Wullner, U.6
  • 126
  • 131
    • 0030834975 scopus 로고    scopus 로고
    • Glutathione peroxidase protects against peroxynitrite-mediated oxidations. A new function for selenoproteins as peroxynitrite reductase
    • H. Sies, V.S. Sharov, L.O. Klotz, and K. Briviba Glutathione peroxidase protects against peroxynitrite-mediated oxidations. A new function for selenoproteins as peroxynitrite reductase J. Biol. Chem. 272 1997 27812 27817
    • (1997) J. Biol. Chem. , vol.272 , pp. 27812-27817
    • Sies, H.1    Sharov, V.S.2    Klotz, L.O.3    Briviba, K.4
  • 133
    • 0345724066 scopus 로고
    • Dopamine turnover and glutathione oxidation: Implications for Parkinson disease
    • M.B. Spina, and G. Cohen Dopamine turnover and glutathione oxidation: implications for Parkinson disease Proc. Natl. Acad. Sci. USA 86 1989 1398 1400
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1398-1400
    • Spina, M.B.1    Cohen, G.2
  • 135
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • L. Sun, H. Wang, Z. Wang, S. He, S. Chen, D. Liao, L. Wang, J. Yan, W. Liu, and X. Lei Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase Cell 148 2012 213 227
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1    Wang, H.2    Wang, Z.3    He, S.4    Chen, S.5    Liao, D.6    Wang, L.7    Yan, J.8    Liu, W.9    Lei, X.10
  • 137
    • 79959313038 scopus 로고    scopus 로고
    • Role of apoptosis inducing factor (AIF) for hippocampal neuronal cell death following global cerebral ischemia in mice
    • S.E. Thal, C. Zhu, S.C. Thal, K. Blomgren, and N. Plesnila Role of apoptosis inducing factor (AIF) for hippocampal neuronal cell death following global cerebral ischemia in mice Neurosci. Lett. 499 2011 1 3
    • (2011) Neurosci. Lett. , vol.499 , pp. 1-3
    • Thal, S.E.1    Zhu, C.2    Thal, S.C.3    Blomgren, K.4    Plesnila, N.5
  • 138
    • 0031025924 scopus 로고    scopus 로고
    • Glutathione depletion in rat brain does not cause nigrostriatal pathway degeneration
    • S. Toffa, G.M. Kunikowska, B.Y. Zeng, P. Jenner, and C.D. Marsden Glutathione depletion in rat brain does not cause nigrostriatal pathway degeneration J. Neural. Transm. 104 1997 67 75
    • (1997) J. Neural. Transm. , vol.104 , pp. 67-75
    • Toffa, S.1    Kunikowska, G.M.2    Zeng, B.Y.3    Jenner, P.4    Marsden, C.D.5
  • 139
    • 0028023175 scopus 로고
    • Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: A mechanism for differential promoter selection
    • M.B. Toledano, I. Kullik, F. Trinh, P.T. Baird, T.D. Schneider, and G. Storz Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection Cell 78 1994 897 909
    • (1994) Cell , vol.78 , pp. 897-909
    • Toledano, M.B.1    Kullik, I.2    Trinh, F.3    Baird, P.T.4    Schneider, T.D.5    Storz, G.6
  • 140
    • 84861321238 scopus 로고    scopus 로고
    • Connecting the chemical and biological properties of nitric oxide
    • J.C. Toledo Jr., and O. Augusto Connecting the chemical and biological properties of nitric oxide Chem. Res. Toxicol. 25 2012 975 989
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 975-989
    • Toledo, Jr.J.C.1    Augusto, O.2
  • 142
    • 0031225515 scopus 로고    scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase (PHGPx): More than an antioxidant enzyme?
    • F. Ursini, M. Maiorino, and A. Roveri Phospholipid hydroperoxide glutathione peroxidase (PHGPx): more than an antioxidant enzyme? Biomed. Environ. Sci. 10 1997 327 332
    • (1997) Biomed. Environ. Sci. , vol.10 , pp. 327-332
    • Ursini, F.1    Maiorino, M.2    Roveri, A.3
  • 144
    • 33845442015 scopus 로고    scopus 로고
    • Baicalein and 12/15-lipoxygenase in the ischemic brain
    • K. van Leyen, H.Y. Kim, S.R. Lee, G. Jin, K. Arai, and E.H. Lo Baicalein and 12/15-lipoxygenase in the ischemic brain Stroke 37 2006 3014 3018
    • (2006) Stroke , vol.37 , pp. 3014-3018
    • Van Leyen, K.1    Kim, H.Y.2    Lee, S.R.3    Jin, G.4    Arai, K.5    Lo, E.H.6
  • 146
    • 84857977037 scopus 로고    scopus 로고
    • Alzheimer's disease: Redox dysregulation as a common denominator for diverse pathogenic mechanisms
    • R. von Bernhardi, and J. Eugenin Alzheimer's disease: redox dysregulation as a common denominator for diverse pathogenic mechanisms Antioxid. Redox Signal. 16 2012 974 1031
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 974-1031
    • Von Bernhardi, R.1    Eugenin, J.2
  • 147
    • 33644662758 scopus 로고    scopus 로고
    • Peroxiredoxin 6 gene-targeted mice show increased lung injury with paraquat-induced oxidative stress
    • Y. Wang, S.I. Feinstein, Y. Manevich, Y.S. Ho, and A.B. Fisher Peroxiredoxin 6 gene-targeted mice show increased lung injury with paraquat-induced oxidative stress Antioxid. Redox Signal. 8 2006 229 237
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 229-237
    • Wang, Y.1    Feinstein, S.I.2    Manevich, Y.3    Ho, Y.S.4    Fisher, A.B.5
  • 149
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Z. Wang, H. Jiang, S. Chen, F. Du, and X. Wang The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways Cell 148 2012 228 243
    • (2012) Cell , vol.148 , pp. 228-243
    • Wang, Z.1    Jiang, H.2    Chen, S.3    Du, F.4    Wang, X.5
  • 151
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • C.C. Winterbourn Reconciling the chemistry and biology of reactive oxygen species Nat. Chem. Biol. 4 2008 278 286
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 152
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • C.C. Winterbourn, and M.B. Hampton Thiol chemistry and specificity in redox signaling Free Radic. Biol. Med. 45 2008 549 561
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 154
    • 51849083386 scopus 로고    scopus 로고
    • Absence of glutathione peroxidase-1 exacerbates cerebral ischemia-reperfusion injury by reducing post-ischemic microvascular perfusion
    • C.H. Wong, S. Bozinovski, P.J. Hertzog, M.J. Hickey, and P.J. Crack Absence of glutathione peroxidase-1 exacerbates cerebral ischemia-reperfusion injury by reducing post-ischemic microvascular perfusion J. Neurochem. 107 2008 241 252
    • (2008) J. Neurochem. , vol.107 , pp. 241-252
    • Wong, C.H.1    Bozinovski, S.2    Hertzog, P.J.3    Hickey, M.J.4    Crack, P.J.5
  • 155
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 2003 650 653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 157
    • 80255140367 scopus 로고    scopus 로고
    • Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells
    • H. Wu, L. Lin, F. Giblin, Y.S. Ho, and M.F. Lou Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells Free Radic. Biol. Med. 51 2011 2108 2117
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 2108-2117
    • Wu, H.1    Lin, L.2    Giblin, F.3    Ho, Y.S.4    Lou, M.F.5
  • 160
    • 80054089650 scopus 로고    scopus 로고
    • Free radical lipid peroxidation: Mechanisms and analysis
    • H. Yin, L. Xu, and N.A. Porter Free radical lipid peroxidation: mechanisms and analysis Chem. Rev. 111 2011 5944 5972
    • (2011) Chem. Rev. , vol.111 , pp. 5944-5972
    • Yin, H.1    Xu, L.2    Porter, N.A.3
  • 161
    • 84859060800 scopus 로고    scopus 로고
    • Gpx4 ablation in adult mice results in a lethal phenotype accompanied by neuronal loss in brain
    • S.E. Yoo, L. Chen, R. Na, Y. Liu, C. Rios, H. Van Remmen, A. Richardson, and Q. Ran Gpx4 ablation in adult mice results in a lethal phenotype accompanied by neuronal loss in brain Free Radic. Biol. Med. 52 9 2012 1820 1827
    • (2012) Free Radic. Biol. Med. , vol.52 , Issue.9 , pp. 1820-1827
    • Yoo, S.E.1    Chen, L.2    Na, R.3    Liu, Y.4    Rios, C.5    Van Remmen, H.6    Richardson, A.7    Ran, Q.8
  • 163
    • 2942696470 scopus 로고    scopus 로고
    • Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner
    • R. Zhang, R. Al-Lamki, L. Bai, J.W. Streb, J.M. Miano, J. Bradley, and W. Min Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner Circ. Res. 94 2004 1483 1491
    • (2004) Circ. Res. , vol.94 , pp. 1483-1491
    • Zhang, R.1    Al-Lamki, R.2    Bai, L.3    Streb, J.W.4    Miano, J.M.5    Bradley, J.6    Min, W.7
  • 164
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • M. Zheng, F. Aslund, and G. Storz Activation of the OxyR transcription factor by reversible disulfide bond formation Science 279 1998 1718 1721
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.