메뉴 건너뛰기




Volumn 396, Issue 5, 2015, Pages 465-482

Thiol switches in mitochondria: Operation and physiological relevance

Author keywords

glutathione; hydrogen peroxide; mitochondria; NADPH; reactive oxygen species; redox regulation; ROS; signaling; thiol switch

Indexed keywords

ACETYL COENZYME A ACETYLTRANSFERASE; ACONITATE HYDRATASE; ALDEHYDE DEHYDROGENASE; BRANCHED CHAIN AMINO ACID; CREATINE KINASE; CYSTEINE; HYDROGEN PEROXIDE; MITOCHONDRIAL ENZYME; MITOCHONDRIAL PROTEIN; REACTIVE OXYGEN METABOLITE; THIOL;

EID: 84927939726     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2014-0293     Document Type: Review
Times cited : (50)

References (167)
  • 1
    • 82955227412 scopus 로고    scopus 로고
    • In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis
    • Albrecht, S.C., Barata, A.G., Grosshans, J., Teleman, A.A., and Dick, T.P. (2011). In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis. Cell Metab. 14, 819-829.
    • (2011) Cell Metab. , vol.14 , pp. 819-829
    • Albrecht, S.C.1    Barata, A.G.2    Grosshans, J.3    Teleman, A.A.4    Dick, T.P.5
  • 2
    • 27144438677 scopus 로고    scopus 로고
    • Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c
    • Allen, S., Balabanidou, V., Sideris, D.P., Lisowsky, T., and Tokatlidis, K. (2005). Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. J. Mol. Biol. 353, 937-944.
    • (2005) J. Mol. Biol. , vol.353 , pp. 937-944
    • Allen, S.1    Balabanidou, V.2    Sideris, D.P.3    Lisowsky, T.4    Tokatlidis, K.5
  • 3
    • 84901841671 scopus 로고    scopus 로고
    • Characterisation of the active/de-active transition of mitochondrial complex I
    • Babot, M., Birch, A., Labarbuta, P., and Galkin, A. (2014). Characterisation of the active/de-active transition of mitochondrial complex I. Biochim. Biophys. Acta 1837, 1083-1092.
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 1083-1092
    • Babot, M.1    Birch, A.2    Labarbuta, P.3    Galkin, A.4
  • 5
    • 18444411338 scopus 로고    scopus 로고
    • Up-regulation of the mitochondrial alternative oxidase pathway enhances photosynthetic electron transport under drought conditions
    • Bartoli, C.G., Gomez, F., Gergoff, G., Guiamet, J.J., and Puntarulo, S. (2005). Up-regulation of the mitochondrial alternative oxidase pathway enhances photosynthetic electron transport under drought conditions. J. Exp. Bot. 56, 1269-1276.
    • (2005) J. Exp. Bot. , vol.56 , pp. 1269-1276
    • Bartoli, C.G.1    Gomez, F.2    Gergoff, G.3    Guiamet, J.J.4    Puntarulo, S.5
  • 6
    • 77149120128 scopus 로고    scopus 로고
    • Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proof read by glutathione
    • Bien, M., Longen, S., Wagener, N., Chwalla, I., Herrmann, J.M., and Riemer, J. (2010). Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proof read by glutathione. Mol. Cell 37, 516-528.
    • (2010) Mol. Cell , vol.37 , pp. 516-528
    • Bien, M.1    Longen, S.2    Wagener, N.3    Chwalla, I.4    Herrmann, J.M.5    Riemer, J.6
  • 7
    • 35948991049 scopus 로고    scopus 로고
    • The disulfide relay system of mitochondria is connected to the respiratory chain
    • Bihlmaier, K., Mesecke, N., Terzyiska, N., Bien, M., Hell, K., and Herrmann, J.M. (2007). The disulfide relay system of mitochondria is connected to the respiratory chain. J. Cell Biol. 179, 389-395.
    • (2007) J. Cell Biol. , vol.179 , pp. 389-395
    • Bihlmaier, K.1    Mesecke, N.2    Terzyiska, N.3    Bien, M.4    Hell, K.5    Herrmann, J.M.6
  • 9
    • 82355181555 scopus 로고    scopus 로고
    • Using quantitative redox proteomics to dissect the yeast redoxome
    • Brandes, N., Reichmann, D., Tienson, H., Leichert, L.I., and Jakob, U. (2011). Using quantitative redox proteomics to dissect the yeast redoxome. J. Biol. Chem. 286, 41893-41903.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41893-41903
    • Brandes, N.1    Reichmann, D.2    Tienson, H.3    Leichert, L.I.4    Jakob, U.5
  • 10
    • 17844393112 scopus 로고    scopus 로고
    • Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion
    • Bulteau, A.L., Lundberg, K.C., Ikeda-Saito, M., Isaya, G., and Szweda, L.I. (2005). Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion. Proc. Natl. Acad. Sci. USA 102, 5987-5991.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5987-5991
    • Bulteau, A.L.1    Lundberg, K.C.2    Ikeda-Saito, M.3    Isaya, G.4    Szweda, L.I.5
  • 11
    • 20444468821 scopus 로고    scopus 로고
    • The inner mitochondrial membrane has aquaporin-8 water channels and is highly permeable to water
    • Calamita, G., Ferri, D., Gena, P., Liquori, G.E., Cavalier, A., Thomas, D., and Svelto, M. (2005). The inner mitochondrial membrane has aquaporin-8 water channels and is highly permeable to water. J. Biol. Chem. 280, 17149-17153.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17149-17153
    • Calamita, G.1    Ferri, D.2    Gena, P.3    Liquori, G.E.4    Cavalier, A.5    Thomas, D.6    Svelto, M.7
  • 14
    • 0031012252 scopus 로고    scopus 로고
    • Alcoholism and alcoholic organ damage and genetic polymorphisms of alcohol metabolizing enzymes in Chinese patients
    • Chao, Y.C., Young, T.H., Tang, H.S., and Hsu, C.T. (1997). Alcoholism and alcoholic organ damage and genetic polymorphisms of alcohol metabolizing enzymes in Chinese patients. Hepatology 25, 112-117.
    • (1997) Hepatology , vol.25 , pp. 112-117
    • Chao, Y.C.1    Young, T.H.2    Tang, H.S.3    Hsu, C.T.4
  • 15
    • 77956565655 scopus 로고    scopus 로고
    • Mitochondrial aldehyde dehydrogenase and cardiac diseases
    • Chen, C.H., Sun, L., and Mochly-Rosen, D. (2010). Mitochondrial aldehyde dehydrogenase and cardiac diseases. Cardiovasc. Res. 88, 51-57.
    • (2010) Cardiovasc. Res. , vol.88 , pp. 51-57
    • Chen, C.H.1    Sun, L.2    Mochly-Rosen, D.3
  • 16
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • Chew, O., Whelan, J., and Millar, A.H. (2003). Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J. Biol. Chem. 278, 46869-46877.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 17
    • 0035981218 scopus 로고    scopus 로고
    • Creatine kinase B is a target molecule of reactive oxygen species in cervical cancer
    • Choi, H., Park, C.S., Kim, B.G., Cho, J.W., Park, J.B., Bae, Y.S., and Bae, D.S. (2001). Creatine kinase B is a target molecule of reactive oxygen species in cervical cancer. Mol. Cells 12, 412-417.
    • (2001) Mol. Cells , vol.12 , pp. 412-417
    • Choi, H.1    Park, C.S.2    Kim, B.G.3    Cho, J.W.4    Park, J.B.5    Bae, Y.S.6    Bae, D.S.7
  • 21
    • 59249105149 scopus 로고    scopus 로고
    • S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation
    • Coles, S.J., Easton, P., Sharrod, H., Hutson, S.M., Hancock, J., Patel, V.B., and Conway, M.E. (2009). S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation. Biochemistry 48, 645-656.
    • (2009) Biochemistry , vol.48 , pp. 645-656
    • Coles, S.J.1    Easton, P.2    Sharrod, H.3    Hutson, S.M.4    Hancock, J.5    Patel, V.B.6    Conway, M.E.7
  • 23
    • 0037162427 scopus 로고    scopus 로고
    • Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase
    • Conway, M.E., Yennawar, N., Wallin, R., Poole, L.B., and Hutson, S.M. (2002). Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase. Biochemistry 41, 9070-9078.
    • (2002) Biochemistry , vol.41 , pp. 9070-9078
    • Conway, M.E.1    Yennawar, N.2    Wallin, R.3    Poole, L.B.4    Hutson, S.M.5
  • 24
    • 1242341233 scopus 로고    scopus 로고
    • Human mitochondrial branched chain aminotransferase: Structural basis for substrate specificity and role of redox active cysteines
    • Conway, M.E., Yennawar, N., Wallin, R., Poole, L.B., and Hutson, S.M. (2003). Human mitochondrial branched chain aminotransferase: structural basis for substrate specificity and role of redox active cysteines. Biochim. Biophys. Acta 1647, 61-65.
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 61-65
    • Conway, M.E.1    Yennawar, N.2    Wallin, R.3    Poole, L.B.4    Hutson, S.M.5
  • 25
    • 2942616628 scopus 로고    scopus 로고
    • Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme
    • Conway, M.E., Poole, L.B., and Hutson, S.M. (2004). Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme. Biochemistry 43, 7356-7364.
    • (2004) Biochemistry , vol.43 , pp. 7356-7364
    • Conway, M.E.1    Poole, L.B.2    Hutson, S.M.3
  • 27
    • 33646369421 scopus 로고    scopus 로고
    • Lack of glutathione peroxidase-1 exacerbates Aβ-mediated neurotoxicity in cortical neurons
    • Crack, P.J., Cimdins, K., Ali, U., Hertzog, P.J., and Iannello, R.C. (2006). Lack of glutathione peroxidase-1 exacerbates Aβ-mediated neurotoxicity in cortical neurons. J. Neural. Transm. 113, 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
  • 28
    • 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
    • Crack, P.J., Taylor, J.M., Flentjar, N.J., de Haan, J., Hertzog, P., Iannello, R.C., and Kola, I. (2001). 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, 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
  • 29
    • 84884344280 scopus 로고    scopus 로고
    • Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria
    • Daum, B., Walter, A., Horst, A., Osiewacz, H.D., and Kuhlbrandt, W. (2013). Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria. Proc. Natl. Acad. Sci. USA 110, 15301-15306.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 15301-15306
    • Daum, B.1    Walter, A.2    Horst, A.3    Osiewacz, H.D.4    Kuhlbrandt, W.5
  • 32
    • 84902242573 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation
    • Dröse, S., Brandt, U., and Wittig, I. (2014). Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation. Biochim. Biophys. Acta 1844, 1344-1354.
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1344-1354
    • Dröse, S.1    Brandt, U.2    Wittig, I.3
  • 35
    • 84902332213 scopus 로고    scopus 로고
    • Quantitative flux analysis reveals folate-dependent NADPH production
    • Fan, J., Ye, J., Kamphorst, J.J., Shlomi, T., Thompson, C.B., and Rabinowitz, J.D. (2014). Quantitative flux analysis reveals folate-dependent NADPH production. Nature 510, 298-302.
    • (2014) Nature , vol.510 , pp. 298-302
    • Fan, J.1    Ye, J.2    Kamphorst, J.J.3    Shlomi, T.4    Thompson, C.B.5    Rabinowitz, J.D.6
  • 37
    • 84884908350 scopus 로고    scopus 로고
    • SOD2 in mitochondrial dysfunction and neurodegeneration
    • Flynn, J.M. and Melov, S. (2013). SOD2 in mitochondrial dysfunction and neurodegeneration. Free Radic. Biol. Med. 62, 4-12.
    • (2013) Free Radic. Biol. Med. , vol.62 , pp. 4-12
    • Flynn, J.M.1    Melov, S.2
  • 39
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • Frey, T.G. and Mannella, C.A. (2000). The internal structure of mitochondria. Trends Biochem. Sci 25, 319-324.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 41
    • 51049093616 scopus 로고    scopus 로고
    • Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I
    • Galkin, A., Meyer, B., Wittig, I., Karas, M., Schagger, H., Vinogradov, A., and Brandt, U. (2008). Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I. J. Biol. Chem. 283, 20907-20913.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20907-20913
    • Galkin, A.1    Meyer, B.2    Wittig, I.3    Karas, M.4    Schagger, H.5    Vinogradov, A.6    Brandt, U.7
  • 42
    • 78650068036 scopus 로고    scopus 로고
    • Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates
    • Garcia, J., Han, D., Sancheti, H., Yap, L.P., Kaplowitz, N., and Cadenas, E. (2010). Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates. J. Biol. Chem. 285, 39646-39654.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39646-39654
    • Garcia, J.1    Han, D.2    Sancheti, H.3    Yap, L.P.4    Kaplowitz, N.5    Cadenas, E.6
  • 43
    • 84901819602 scopus 로고    scopus 로고
    • Superoxide dismutase deficiency impairs olfactory sexual signaling and alters bioenergetic function in mice
    • Garratt, M., Pichaud, N., Glaros, E.N., Kee, A.J., and Brooks, R.C. (2014). Superoxide dismutase deficiency impairs olfactory sexual signaling and alters bioenergetic function in mice. Proc. Natl. Acad. Sci. USA 111, 8119-8124.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 8119-8124
    • Garratt, M.1    Pichaud, N.2    Glaros, E.N.3    Kee, A.J.4    Brooks, R.C.5
  • 44
    • 62549115324 scopus 로고    scopus 로고
    • Hunting for plant nitric oxide synthase provides new evidence of a central role for plastids in nitric oxide metabolism
    • Gas, E., Flores-Perez, U., Sauret-Gueto, S., and Rodriguez-Concepcion, M. (2009). Hunting for plant nitric oxide synthase provides new evidence of a central role for plastids in nitric oxide metabolism. Plant Cell 21, 18-23.
    • (2009) Plant Cell , vol.21 , pp. 18-23
    • Gas, E.1    Flores-Perez, U.2    Sauret-Gueto, S.3    Rodriguez-Concepcion, M.4
  • 46
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi, C., Poderoso, J.J., and Boveris, A. (1998). Production of nitric oxide by mitochondria. J. Biol. Chem. 273, 11038-11043.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 47
    • 84892915705 scopus 로고    scopus 로고
    • The free radical theory of aging is dead. Long live the damage theory!
    • Gladyshev, V.N. (2014). The free radical theory of aging is dead. Long live the damage theory! Antioxid. Redox. Signal. 20, 727-731.
    • (2014) Antioxid. Redox. Signal. , vol.20 , pp. 727-731
    • Gladyshev, V.N.1
  • 48
    • 84920520304 scopus 로고    scopus 로고
    • Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise
    • Goncalves, R.L., Quinlan, C.L., Perevoshchikova, I.V., Hey- Mogensen, M., and Brand, M.D. (2015). Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise. J. Biol. Chem. 290, 209-227.
    • (2015) J. Biol. Chem. , vol.290 , pp. 209-227
    • Goncalves, R.L.1    Quinlan, C.L.2    Perevoshchikova, I.V.3    Hey-Mogensen, M.4    Brand, M.D.5
  • 49
    • 0035131144 scopus 로고    scopus 로고
    • Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions
    • Grant, C.M. (2001). Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol. Microbiol. 39, 533-541.
    • (2001) Mol. Microbiol. , vol.39 , pp. 533-541
    • Grant, C.M.1
  • 50
    • 0023022429 scopus 로고
    • Decreased rate of ketone-body oxidation and decreased activity of D-3-hydroxybutyrate dehydrogenase and succinyl-CoA:3-oxo-acid CoA-transferase in heart mitochondria of diabetic rats
    • Grinblat, L., Pacheco Bolanos, L.F. and Stoppani, A.O. (1986). Decreased rate of ketone-body oxidation and decreased activity of D-3-hydroxybutyrate dehydrogenase and succinyl-CoA:3-oxo-acid CoA-transferase in heart mitochondria of diabetic rats. Biochem. J. 240, 49-56.
    • (1986) Biochem. J. , vol.240 , pp. 49-56
    • Grinblat, L.1    Pacheco Bolanos, L.F.2    Stoppani, A.O.3
  • 52
    • 84885084776 scopus 로고    scopus 로고
    • Creatine kinase-overexpression improves myocardial energetics, contractile dysfunction and survival in murine doxorubicin cardiotoxicity
    • Gupta, A., Rohlfsen, C., Leppo, M.K., Chacko, V.P., Wang, Y., Steenbergen, C., and Weiss, R.G. (2013). Creatine kinase-overexpression improves myocardial energetics, contractile dysfunction and survival in murine doxorubicin cardiotoxicity. PLoS One 8, e74675.
    • (2013) PLoS One , vol.8 , pp. e74675
    • Gupta, A.1    Rohlfsen, C.2    Leppo, M.K.3    Chacko, V.P.4    Wang, Y.5    Steenbergen, C.6    Weiss, R.G.7
  • 53
    • 30944439111 scopus 로고    scopus 로고
    • The thiolase superfamily: Condensing enzymes with diverse reaction specificities
    • Haapalainen, A.M., Merilainen, G., and Wierenga, R.K. (2006). The thiolase superfamily: condensing enzymes with diverse reaction specificities. Trends Biochem. Sci. 31, 64-71.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 64-71
    • Haapalainen, A.M.1    Merilainen, G.2    Wierenga, R.K.3
  • 54
    • 58849148335 scopus 로고    scopus 로고
    • Quantifying the global cellular thiol-disulfide status
    • Hansen, R.E., Roth, D., and Winther, J.R. (2009). Quantifying the global cellular thiol-disulfide status. Proc. Natl. Acad. Sci. USA 106, 422-427.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 422-427
    • Hansen, R.E.1    Roth, D.2    Winther, J.R.3
  • 56
    • 77957060561 scopus 로고    scopus 로고
    • The intermembrane space of mitochondria
    • Herrmann, J.M. and Riemer, J. (2010). The intermembrane space of mitochondria. Antioxid. Redox. Signal. 13, 1341-1358.
    • (2010) Antioxid. Redox. Signal. , vol.13 , pp. 1341-1358
    • Herrmann, J.M.1    Riemer, J.2
  • 59
    • 57649183232 scopus 로고    scopus 로고
    • The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix
    • Hu, J., Dong, L., and Outten, C.E. (2008). The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix. J. Biol. Chem. 283, 29126-29134.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29126-29134
    • Hu, J.1    Dong, L.2    Outten, C.E.3
  • 61
    • 84863082820 scopus 로고    scopus 로고
    • Copper chaperone-dependent and -independent activation of three copper-zinc superoxide dismutase homologs localized in different cellular compartments in Arabidopsis
    • Huang, C.H., Kuo, W.Y., Weiss, C., and Jinn, T.L. (2012). Copper chaperone-dependent and -independent activation of three copper-zinc superoxide dismutase homologs localized in different cellular compartments in Arabidopsis. Plant Physiol. 158, 737-746.
    • (2012) Plant Physiol. , vol.158 , pp. 737-746
    • Huang, C.H.1    Kuo, W.Y.2    Weiss, C.3    Jinn, T.L.4
  • 62
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex I
    • Hunte, C., Zickermann, V., and Brandt, U. (2010). Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 329, 448-451.
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 63
    • 34347213728 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity: Implications for mitochondrial energy metabolism and apoptosis
    • Inarrea, P., Moini, H., Han, D., Rettori, D., Aguilo, I., Alava, M.A., Iturralde, M., and Cadenas, E. (2007). Mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity: implications for mitochondrial energy metabolism and apoptosis. Biochem. J. 405, 173-179.
    • (2007) Biochem. J. , vol.405 , pp. 173-179
    • Inarrea, P.1    Moini, H.2    Han, D.3    Rettori, D.4    Aguilo, I.5    Alava, M.A.6    Iturralde, M.7    Cadenas, E.8
  • 65
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jimenez, A., Hernandez, J.A., Del Rio, L.A., and Sevilla, F. (1997). Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol. 114, 275-284.
    • (1997) Plant Physiol. , vol.114 , pp. 275-284
    • Jimenez, A.1    Hernandez, J.A.2    Del Rio, L.A.3    Sevilla, F.4
  • 66
    • 70149113002 scopus 로고    scopus 로고
    • Structural basis of yeast Tim40/Mia40 as an oxidative translocator in the mitochondrial intermembrane space
    • Kawano, S., Yamano, K., Naoe, M., Momose, T., Terao, K., Nishikawa, S., Watanabe, N., and Endo, T. (2009). Structural basis of yeast Tim40/Mia40 as an oxidative translocator in the mitochondrial intermembrane space. Proc. Natl. Acad. Sci. USA 106, 14403-14407.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14403-14407
    • Kawano, S.1    Yamano, K.2    Naoe, M.3    Momose, T.4    Terao, K.5    Nishikawa, S.6    Watanabe, N.7    Endo, T.8
  • 68
    • 0036913740 scopus 로고    scopus 로고
    • Burning fat: The structural basis of fatty acid beta-oxidation
    • Kim, J.J. and Battaile, K.P. (2002). Burning fat: the structural basis of fatty acid beta-oxidation. Curr. Opin. Struct. Biol. 12, 721-728.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 721-728
    • Kim, J.J.1    Battaile, K.P.2
  • 69
    • 79960017554 scopus 로고    scopus 로고
    • Peroxiredoxin 5: Structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin
    • Knoops, B., Goemaere, J., Van der Eecken, V., and Declercq, J.P. (2011). Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin. Antioxid. Redox. Signal. 15, 817-829.
    • (2011) Antioxid. Redox. Signal. , vol.15 , pp. 817-829
    • Knoops, B.1    Goemaere, J.2    Van Der Eecken, V.3    Declercq, J.P.4
  • 70
    • 84892184637 scopus 로고    scopus 로고
    • Mia40 targets cysteines in a hydrophobic environment to direct oxidative protein folding in the mitochondria
    • Koch, J.R. and Schmid, F.X. (2014). Mia40 targets cysteines in a hydrophobic environment to direct oxidative protein folding in the mitochondria. Nat. Commun. 5, 3041.
    • (2014) Nat. Commun. , vol.5 , pp. 3041
    • Koch, J.R.1    Schmid, F.X.2
  • 71
    • 84864119697 scopus 로고    scopus 로고
    • Glutathione redox potential in the mitochondrial intermembrane space is linked to the cytosol and impacts the Mia40 redox state
    • Kojer, K., Bien, M., Gangel, H., Morgan, B., Dick, T.P., and Riemer, J. (2012). Glutathione redox potential in the mitochondrial intermembrane space is linked to the cytosol and impacts the Mia40 redox state. EMBO J. 31, 3169-3182.
    • (2012) EMBO J. , vol.31 , pp. 3169-3182
    • Kojer, K.1    Bien, M.2    Gangel, H.3    Morgan, B.4    Dick, T.P.5    Riemer, J.6
  • 72
    • 84920982875 scopus 로고    scopus 로고
    • Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space
    • Kojer, K., Peleh, V., Calabrese, G., Herrmann, J.M., and Riemer, J. (2015). Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space. Mol. Biol. Cell. 26, 195-204.
    • (2015) Mol. Biol. Cell. , vol.26 , pp. 195-204
    • Kojer, K.1    Peleh, V.2    Calabrese, G.3    Herrmann, J.M.4    Riemer, J.5
  • 81
    • 67649644885 scopus 로고    scopus 로고
    • Peroxiredoxin III-deficiency sensitizes macrophages to oxidative stress
    • Li, L., Kaifu, T., Obinata, M., and Takai, T. (2009). Peroxiredoxin III-deficiency sensitizes macrophages to oxidative stress. J. Biochem. 145, 425-427.
    • (2009) J. Biochem. , vol.145 , pp. 425-427
    • Li, L.1    Kaifu, T.2    Obinata, M.3    Takai, T.4
  • 82
    • 71449113005 scopus 로고    scopus 로고
    • Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions
    • Liang, H., Yoo, S.E., Na, R., Walter, C.A., Richardson, A., and Ran, Q. (2009). Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions. J. Biol. Chem. 284, 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
  • 84
    • 0024391195 scopus 로고
    • Reaction between sheep liver mitochondrial aldehyde dehydrogenase and various thiolmodifying reagents
    • Loomes, K.M. and Kitson, T.M. (1989). Reaction between sheep liver mitochondrial aldehyde dehydrogenase and various thiolmodifying reagents. Biochem. J. 261, 281-284.
    • (1989) Biochem. J. , vol.261 , pp. 281-284
    • Loomes, K.M.1    Kitson, T.M.2
  • 85
    • 84891867173 scopus 로고    scopus 로고
    • Aconitase post-translational modification as a key in linkage between Krebs cycle, iron homeostasis, redox signaling, and metabolism of reactive oxygen species
    • Lushchak, O.V., Piroddi, M., Galli, F., and Lushchak, V.I. (2014). Aconitase post-translational modification as a key in linkage between Krebs cycle, iron homeostasis, redox signaling, and metabolism of reactive oxygen species. Redox. Rep. 19, 8-15.
    • (2014) Redox. Rep. , vol.19 , pp. 8-15
    • Lushchak, O.V.1    Piroddi, M.2    Galli, F.3    Lushchak, V.I.4
  • 86
    • 84875439431 scopus 로고    scopus 로고
    • Glutaredoxin-2 is required to control proton leak through uncoupling protein-3
    • Mailloux, R.J., Xuan, J.Y., Beauchamp, B., Jui, L.D., Lou, M., and Harper, M.E. (2013). Glutaredoxin-2 is required to control proton leak through uncoupling protein-3. J. Biol. Chem. 288, 8365-8379.
    • (2013) J. Biol. Chem. , vol.288 , pp. 8365-8379
    • Mailloux, R.J.1    Xuan, J.Y.2    Beauchamp, B.3    Jui, L.D.4    Lou, M.5    Harper, M.E.6
  • 88
    • 84866873131 scopus 로고    scopus 로고
    • Mitochondrial aquaporin-8 knockdown in human hepatoma HepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability
    • Marchissio, M.J., Frances, D.E., Carnovale, C.E. and Marinelli, R.A. (2012). Mitochondrial aquaporin-8 knockdown in human hepatoma HepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability. Toxicol. Appl. Pharmacol. 264, 246-254.
    • (2012) Toxicol. Appl. Pharmacol. , vol.264 , pp. 246-254
    • Marchissio, M.J.1    Frances, D.E.2    Carnovale, C.E.3    Marinelli, R.A.4
  • 90
    • 52649083174 scopus 로고    scopus 로고
    • Aconitate hydratase of mammals under oxidative stress
    • Matasova, L.V. and Popova, T.N. (2008). Aconitate hydratase of mammals under oxidative stress. Biochemistry (Mosc) 73, 957-964.
    • (2008) Biochemistry (Mosc) , vol.73 , pp. 957-964
    • Matasova, L.V.1    Popova, T.N.2
  • 91
    • 0029977161 scopus 로고    scopus 로고
    • Creatine kinase is the main target of reactive oxygen species in cardiac myofibrils
    • Mekhfi, H., Veksler, V., Mateo, P., Maupoil, V., Rochette, L., and Ventura-Clapier, R. (1996). Creatine kinase is the main target of reactive oxygen species in cardiac myofibrils. Circ. Res. 78, 1016-1027.
    • (1996) Circ. Res. , vol.78 , pp. 1016-1027
    • Mekhfi, H.1    Veksler, V.2    Mateo, P.3    Maupoil, V.4    Rochette, L.5    Ventura-Clapier, R.6
  • 92
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., and Herrmann, J.M. (2005). A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121, 1059-1069.
    • (2005) Cell , vol.121 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 94
    • 0027264668 scopus 로고
    • Organic acid activation of the alternative oxidase of plant mitochondria
    • Millar, A.H., Wiskich, J.T., Whelan, J., and Day, D.A. (1993). Organic acid activation of the alternative oxidase of plant mitochondria. FEBS Lett. 329, 259-262.
    • (1993) FEBS Lett. , vol.329 , pp. 259-262
    • Millar, A.H.1    Wiskich, J.T.2    Whelan, J.3    Day, D.A.4
  • 96
    • 0033569705 scopus 로고    scopus 로고
    • A biosynthetic thiolase in complex with a reaction intermediate: The crystal structure provides new insights into the catalytic mechanism
    • Modis, Y. and Wierenga, R.K. (1999). A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism. Structure 7, 1279-1290.
    • (1999) Structure , vol.7 , pp. 1279-1290
    • Modis, Y.1    Wierenga, R.K.2
  • 97
    • 27544510276 scopus 로고    scopus 로고
    • Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide-mediated S-nitrosylation
    • Moon, K.H., Kim, B.J., and Song, B.J. (2005). Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide-mediated S-nitrosylation. FEBS Lett. 579, 6115-6120.
    • (2005) FEBS Lett. , vol.579 , pp. 6115-6120
    • Moon, K.H.1    Kim, B.J.2    Song, B.J.3
  • 98
    • 33751003258 scopus 로고    scopus 로고
    • Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats
    • Moon, K.H., Hood, B.L., Kim, B.J., Hardwick, J.P., Conrads, T.P., Veenstra, T.D., and Song, B.J. (2006). Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats. Hepatology 44, 1218-1230.
    • (2006) Hepatology , vol.44 , pp. 1218-1230
    • Moon, K.H.1    Hood, B.L.2    Kim, B.J.3    Hardwick, J.P.4    Conrads, T.P.5    Veenstra, T.D.6    Song, B.J.7
  • 101
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M.P. (2009). How mitochondria produce reactive oxygen species. Biochem. J. 417, 1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 103
    • 9144273327 scopus 로고    scopus 로고
    • Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space
    • Naoe, M., Ohwa, Y., Ishikawa, D., Ohshima, C., Nishikawa, S., Yamamoto, H., and Endo, T. (2004). Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space. J. Biol. Chem. 279, 47815-47821.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47815-47821
    • Naoe, M.1    Ohwa, Y.2    Ishikawa, D.3    Ohshima, C.4    Nishikawa, S.5    Yamamoto, H.6    Endo, T.7
  • 105
    • 0037305881 scopus 로고    scopus 로고
    • The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice
    • Nonn, L., Williams, R.R., Erickson, R.P., and Powis, G. (2003). The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice. Mol. Cell. Biol. 23, 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
  • 107
    • 0037881908 scopus 로고    scopus 로고
    • A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae
    • Outten, C.E. and Culotta, V.C. (2003). A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae. EMBO J. 22, 2015-2024.
    • (2003) EMBO J. , vol.22 , pp. 2015-2024
    • Outten, C.E.1    Culotta, V.C.2
  • 108
    • 35448993279 scopus 로고    scopus 로고
    • What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?
    • Pai, H.V., Starke, D.W., Lesnefsky, E.J., Hoppel, C.L., and Mieyal, J.J. (2007). What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria? Antioxid. Redox. Signal. 9, 2027-2033.
    • (2007) Antioxid. Redox. Signal. , vol.9 , pp. 2027-2033
    • Pai, H.V.1    Starke, D.W.2    Lesnefsky, E.J.3    Hoppel, C.L.4    Mieyal, J.J.5
  • 109
    • 40849136587 scopus 로고    scopus 로고
    • Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin
    • Parsonage, D., Karplus, P.A., and Poole, L.B. (2008). Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin. Proc. Natl. Acad. Sci. USA 105, 8209-8214.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8209-8214
    • Parsonage, D.1    Karplus, P.A.2    Poole, L.B.3
  • 111
    • 0037866381 scopus 로고    scopus 로고
    • Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase
    • Perez-Miller, S.J. and Hurley, T.D. (2003). Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase. Biochemistry 42, 7100-7109.
    • (2003) Biochemistry , vol.42 , pp. 7100-7109
    • Perez-Miller, S.J.1    Hurley, T.D.2
  • 114
    • 79960027526 scopus 로고    scopus 로고
    • Hydrogen peroxide acts on sensitive mitochondrial proteins to induce death of a fungal pathogen revealed by proteomic analysis
    • Qin, G., Liu, J., Cao, B., Li, B., and Tian, S. (2011). Hydrogen peroxide acts on sensitive mitochondrial proteins to induce death of a fungal pathogen revealed by proteomic analysis. PLoS One 6, e21945.
    • (2011) PLoS One , vol.6 , pp. e21945
    • Qin, G.1    Liu, J.2    Cao, B.3    Li, B.4    Tian, S.5
  • 115
    • 84896935583 scopus 로고    scopus 로고
    • The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I
    • Quinlan, C.L., Goncalves, R.L., Hey-Mogensen, M., Yadava, N., Bunik, V.I., and Brand, M.D. (2014). The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I. J. Biol. Chem. 289, 8312-8325.
    • (2014) J. Biol. Chem. , vol.289 , pp. 8312-8325
    • Quinlan, C.L.1    Goncalves, R.L.2    Hey-Mogensen, M.3    Yadava, N.4    Bunik, V.I.5    Brand, M.D.6
  • 116
    • 2542486403 scopus 로고    scopus 로고
    • Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue
    • Reddy, S., Jones, A.D., Cross, C.E., Wong, P.S., and Van Der Vliet, A. (2000). Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. Biochem. J. 347, 821-827.
    • (2000) Biochem. J. , vol.347 , pp. 821-827
    • Reddy, S.1    Jones, A.D.2    Cross, C.E.3    Wong, P.S.4    Van Der Vliet, A.5
  • 118
    • 0032514922 scopus 로고    scopus 로고
    • Regulation of the cyanide-resistant alternative oxidase of plant mitochondria. Identification of the cysteine residue involved in α-keto acid stimulation and intersubunit disulfide bond formation
    • Rhoads, D.M., Umbach, A.L., Sweet, C.R., Lennon, A.M., Rauch, G.S., and Siedow, J.N. (1998). Regulation of the cyanide-resistant alternative oxidase of plant mitochondria. Identification of the cysteine residue involved in α-keto acid stimulation and intersubunit disulfide bond formation. J. Biol. Chem. 273, 30750-30756.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30750-30756
    • Rhoads, D.M.1    Umbach, A.L.2    Sweet, C.R.3    Lennon, A.M.4    Rauch, G.S.5    Siedow, J.N.6
  • 120
    • 35649001933 scopus 로고    scopus 로고
    • Impairment of mitochondrial acetoacetyl CoA thiolase activity in the colonic mucosa of patients with ulcerative colitis
    • Santhanam, S., Venkatraman, A., and Ramakrishna, B.S. (2007). Impairment of mitochondrial acetoacetyl CoA thiolase activity in the colonic mucosa of patients with ulcerative colitis. Gut 56, 1543-1549.
    • (2007) Gut , vol.56 , pp. 1543-1549
    • Santhanam, S.1    Venkatraman, A.2    Ramakrishna, B.S.3
  • 123
  • 124
  • 125
    • 84879414710 scopus 로고    scopus 로고
    • Targeted disruption of glutathione peroxidase 4 in mouse skin epithelial cells impairs postnatal hair follicle morphogenesis that is partially rescued through inhibition of COX-2
    • Sengupta, A., Lichti, U.F., Carlson, B.A., Cataisson, C., Ryscavage, A.O., Mikulec, C., Conrad, M., Fischer, S.M., Hatfield, D.L., and Yuspa, S.H. (2013). Targeted disruption of glutathione peroxidase 4 in mouse skin epithelial cells impairs postnatal hair follicle morphogenesis that is partially rescued through inhibition of COX-2. J. Invest. Dermatol. 133, 1731-1741.
    • (2013) J. Invest. Dermatol. , vol.133 , pp. 1731-1741
    • Sengupta, A.1    Lichti, U.F.2    Carlson, B.A.3    Cataisson, C.4    Ryscavage, A.O.5    Mikulec, C.6    Conrad, M.7    Fischer, S.M.8    Hatfield, D.L.9    Yuspa, S.H.10
  • 127
    • 0027209389 scopus 로고
    • Strategies of antioxidant defense
    • Sies, H. (1993). Strategies of antioxidant defense. Eur. J. Biochem. 215, 213-219.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 213-219
    • Sies, H.1
  • 128
    • 84897444272 scopus 로고    scopus 로고
    • Role of metabolic H2O2 generation: Redox signaling and oxidative stress
    • Sies, H. (2014). Role of metabolic H2O2 generation: redox signaling and oxidative stress. J. Biol. Chem. 289, 8735-8741.
    • (2014) J. Biol. Chem. , vol.289 , pp. 8735-8741
    • Sies, H.1
  • 131
    • 84899813575 scopus 로고    scopus 로고
    • Quantitative proteomics of synaptic and nonsynaptic mitochondria: Insights for synaptic mitochondrial vulnerability
    • Stauch, K.L., Purnell, P.R., and Fox, H.S. (2014). Quantitative proteomics of synaptic and nonsynaptic mitochondria: insights for synaptic mitochondrial vulnerability. J. Proteome Res. 13, 2620-2636.
    • (2014) J. Proteome Res. , vol.13 , pp. 2620-2636
    • Stauch, K.L.1    Purnell, P.R.2    Fox, H.S.3
  • 132
    • 84897000909 scopus 로고    scopus 로고
    • Mitochondrial iron-sulfur protein biogenesis and human disease
    • Stehling, O., Wilbrecht, C., and Lill, R. (2014). Mitochondrial iron-sulfur protein biogenesis and human disease. Biochimie 100, 61-77.
    • (2014) Biochimie , vol.100 , pp. 61-77
    • Stehling, O.1    Wilbrecht, C.2    Lill, R.3
  • 133
    • 84862527999 scopus 로고    scopus 로고
    • The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates
    • Stoldt, S., Wenzel, D., Hildenbeutel, M., Wurm, C.A., Herrmann, J.M., and Jakobs, S. (2012). The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates. Mol. Biol. Cell. 23, 2292-2301.
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 2292-2301
    • Stoldt, S.1    Wenzel, D.2    Hildenbeutel, M.3    Wurm, C.A.4    Herrmann, J.M.5    Jakobs, S.6
  • 134
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz, L.A., Diekert, K., Jensen, L.T., Lill, R., and Culotta, V.C. (2001). A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J. Biol. Chem. 276, 38084-38089.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 135
    • 0026436761 scopus 로고
    • Inactivation of rabbit muscle creatine kinase by hydrogen peroxide
    • Suzuki, Y.J., Edmondson, J.D., and Ford, G.D. (1992). Inactivation of rabbit muscle creatine kinase by hydrogen peroxide. Free Radic. Res. Commun. 16, 131-136.
    • (1992) Free Radic. Res. Commun. , vol.16 , pp. 131-136
    • Suzuki, Y.J.1    Edmondson, J.D.2    Ford, G.D.3
  • 136
    • 0028000309 scopus 로고
    • Free radical inactivation of rabbit muscle creatinine kinase: Catalysis by physiological and hydrolyzed ICRF-187 (ICRF-198) iron chelates
    • Thomas, C., Carr, A.C., and Winterbourn, C.C. (1994). Free radical inactivation of rabbit muscle creatinine kinase: catalysis by physiological and hydrolyzed ICRF-187 (ICRF-198) iron chelates. Free Radic. Res. 21, 387-397.
    • (1994) Free Radic. Res. , vol.21 , pp. 387-397
    • Thomas, C.1    Carr, A.C.2    Winterbourn, C.C.3
  • 137
    • 84875740128 scopus 로고    scopus 로고
    • Functions and cellular compartmentation of the thioredoxin and glutathione pathways in yeast
    • Toledano, M.B., Delaunay-Moisan, A., Outten, C.E., and Igbaria, A. (2013). Functions and cellular compartmentation of the thioredoxin and glutathione pathways in yeast. Antioxid. Redox. Signal. 18, 1699-1711.
    • (2013) Antioxid. Redox. Signal. , vol.18 , pp. 1699-1711
    • Toledano, M.B.1    Delaunay-Moisan, A.2    Outten, C.E.3    Igbaria, A.4
  • 138
    • 13844313006 scopus 로고    scopus 로고
    • Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae
    • Trotter, E.W. and Grant, C.M. (2005). Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae. Eukaryot. Cell 4, 392-400.
    • (2005) Eukaryot. Cell , vol.4 , pp. 392-400
    • Trotter, E.W.1    Grant, C.M.2
  • 139
    • 84875214011 scopus 로고    scopus 로고
    • The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1
    • Tsybovsky, Y., Malakhau, Y., Strickland, K.C., and Krupenko, S.A. (2013). The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1. Chem. Biol. Interact. 202, 62-69.
    • (2013) Chem. Biol. Interact. , vol.202 , pp. 62-69
    • Tsybovsky, Y.1    Malakhau, Y.2    Strickland, K.C.3    Krupenko, S.A.4
  • 140
    • 0027140930 scopus 로고
    • Covalent and noncovalent dimers of the cyanide-resistant alternative oxidase protein in higher plant mitochondria and their relationship to enzyme activity
    • Umbach, A.L. and Siedow, J.N. (1993). Covalent and noncovalent dimers of the cyanide-resistant alternative oxidase protein in higher plant mitochondria and their relationship to enzyme activity. Plant Physiol. 103, 845-854.
    • (1993) Plant Physiol. , vol.103 , pp. 845-854
    • Umbach, A.L.1    Siedow, J.N.2
  • 141
    • 0028226147 scopus 로고
    • Regulation of alternative oxidase kinetics by pyruvate and intermolecular disulfide bond redox status in soybean seedling mitochondria
    • Umbach, A.L., Wiskich, J.T., and Siedow, J.N. (1994). Regulation of alternative oxidase kinetics by pyruvate and intermolecular disulfide bond redox status in soybean seedling mitochondria. FEBS Lett. 348, 181-184.
    • (1994) FEBS Lett. , vol.348 , pp. 181-184
    • Umbach, A.L.1    Wiskich, J.T.2    Siedow, J.N.3
  • 142
    • 0037156868 scopus 로고    scopus 로고
    • Activation of the plant mitochondrial alternative oxidase: Insights from site-directed mutagenesis
    • Umbach, A.L., Gonzalez-Meler, M.A., Sweet, C.R., and Siedow, J.N. (2002). Activation of the plant mitochondrial alternative oxidase: insights from site-directed mutagenesis. Biochim. Biophys. Acta 1554, 118-128.
    • (2002) Biochim. Biophys. Acta , vol.1554 , pp. 118-128
    • Umbach, A.L.1    Gonzalez-Meler, M.A.2    Sweet, C.R.3    Siedow, J.N.4
  • 143
    • 33645011305 scopus 로고    scopus 로고
    • Characterization of transformed Arabidopsis with altered alternative oxidase levels and analysis of effects on reactive oxygen species in tissue
    • Umbach, A.L., Fiorani, F., and Siedow, J.N. (2005). Characterization of transformed Arabidopsis with altered alternative oxidase levels and analysis of effects on reactive oxygen species in tissue. Plant Physiol. 139, 1806-1820.
    • (2005) Plant Physiol. , vol.139 , pp. 1806-1820
    • Umbach, A.L.1    Fiorani, F.2    Siedow, J.N.3
  • 144
    • 0039174315 scopus 로고    scopus 로고
    • Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation
    • Vasquez-Vivar, J., Kalyanaraman, B., and Kennedy, M.C. (2000). Mitochondrial aconitase is a source of hydroxyl radical. An electron spin resonance investigation. J. Biol. Chem. 275, 14064-14069.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14064-14069
    • Vasquez-Vivar, J.1    Kalyanaraman, B.2    Kennedy, M.C.3
  • 145
    • 84915761829 scopus 로고    scopus 로고
    • Architecture of mammalian respiratory complex I
    • Vinothkumar, K.R., Zhu, J., and Hirst, J. (2014). Architecture of mammalian respiratory complex I. Nature 515, 80-84.
    • (2014) Nature , vol.515 , pp. 80-84
    • Vinothkumar, K.R.1    Zhu, J.2    Hirst, J.3
  • 146
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • Vogel, F., Bornhovd, C., Neupert, W., and Reichert, A.S. (2006). Dynamic subcompartmentalization of the mitochondrial inner membrane. J. Cell Biol. 175, 237-247.
    • (2006) J. Cell Biol. , vol.175 , pp. 237-247
    • Vogel, F.1    Bornhovd, C.2    Neupert, W.3    Reichert, A.S.4
  • 150
    • 0035797915 scopus 로고    scopus 로고
    • An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase
    • Wang, P.F., McLeish, M.J., Kneen, M.M., Lee, G., and Kenyon, G.L. (2001). An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase. Biochemistry 40, 11698-11705.
    • (2001) Biochemistry , vol.40 , pp. 11698-11705
    • Wang, P.F.1    McLeish, M.J.2    Kneen, M.M.3    Lee, G.4    Kenyon, G.L.5
  • 152
    • 79952860374 scopus 로고    scopus 로고
    • Inhibition of aldehyde dehydrogenase 2 by oxidative stress is associated with cardiac dysfunction in diabetic rats
    • Wang, J., Wang, H., Hao, P., Xue, L., Wei, S., Zhang, Y., and Chen, Y. (2011). Inhibition of aldehyde dehydrogenase 2 by oxidative stress is associated with cardiac dysfunction in diabetic rats. Mol. Med. 17, 172-179.
    • (2011) Mol. Med. , vol.17 , pp. 172-179
    • Wang, J.1    Wang, H.2    Hao, P.3    Xue, L.4    Wei, S.5    Zhang, Y.6    Chen, Y.7
  • 154
    • 33846969562 scopus 로고    scopus 로고
    • Role of reduced lipoic acid in the redox regulation of mitochondrial aldehyde dehydrogenase (ALDH-2) activity. Implications for mitochondrial oxidative stress and nitrate tolerance
    • Wenzel, P., Hink, U., Oelze, M., Schuppan, S., Schaeuble, K., Schildknecht, S., Ho, K.K., Weiner, H., Bachschmid, M., Munzel, T. et al. (2007). Role of reduced lipoic acid in the redox regulation of mitochondrial aldehyde dehydrogenase (ALDH-2) activity. Implications for mitochondrial oxidative stress and nitrate tolerance. J. Biol. Chem. 282, 792-799.
    • (2007) J. Biol. Chem. , vol.282 , pp. 792-799
    • Wenzel, P.1    Hink, U.2    Oelze, M.3    Schuppan, S.4    Schaeuble, K.5    Schildknecht, S.6    Ho, K.K.7    Weiner, H.8    Bachschmid, M.9    Munzel, T.10
  • 155
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn, C.C. and Hampton, M.B. (2008). Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med. 45, 549-561.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 157
    • 51849083386 scopus 로고    scopus 로고
    • Absence of glutathione peroxidase-1 exacerbates cerebral ischemia-reperfusion injury by reducing post-ischemic microvascular perfusion
    • Wong, C.H., Bozinovski, S., Hertzog, P.J., Hickey, M.J., and Crack, P.J. (2008). Absence of glutathione peroxidase-1 exacerbates cerebral ischemia-reperfusion injury by reducing post-ischemic microvascular perfusion. J. Neurochem. 107, 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
  • 158
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood, Z.A., Poole, L.B., and Karplus, P.A. (2003). Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653.
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 160
    • 80255140367 scopus 로고    scopus 로고
    • Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells
    • Wu, H., Lin, L., Giblin, F., Ho, Y.S., and Lou, M.F. (2011). Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells. Free Radic. Biol. Med. 51, 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
  • 161
    • 33749352547 scopus 로고    scopus 로고
    • Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast
    • Wurm, C.A. and Jakobs, S. (2006). Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast. FEBS Lett. 580, 5628-5634.
    • (2006) FEBS Lett. , vol.580 , pp. 5628-5634
    • Wurm, C.A.1    Jakobs, S.2
  • 163
    • 84900299463 scopus 로고    scopus 로고
    • The intrinsic apoptosis pathway mediates the pro-longevity response to mitochondrial ROS in C. elegans
    • Yee, C., Yang, W., and Hekimi, S. (2014). The intrinsic apoptosis pathway mediates the pro-longevity response to mitochondrial ROS in C. elegans. Cell 157, 897-909.
    • (2014) Cell , vol.157 , pp. 897-909
    • Yee, C.1    Yang, W.2    Hekimi, S.3
  • 164
    • 34548746306 scopus 로고    scopus 로고
    • Myocardial reperfusion injury
    • Yellon, D.M. and Hausenloy, D.J. (2007). Myocardial reperfusion injury. N. Engl. J. Med. 357, 1121-1135.
    • (2007) N. Engl. J. Med. , vol.357 , pp. 1121-1135
    • Yellon, D.M.1    Hausenloy, D.J.2
  • 165
    • 84964701402 scopus 로고    scopus 로고
    • Mitochondrial isocitrate dehydrogenase is inactivated upon oxidation and reactivated by thioredoxin-dependent reduction in Arabidopsis
    • Yoshida, K. and Hisabori, T. (2014). Mitochondrial isocitrate dehydrogenase is inactivated upon oxidation and reactivated by thioredoxin-dependent reduction in Arabidopsis. Front. Environm. Sci. 2, Article 38, 1-7.
    • (2014) Front. Environm. Sci. , vol.2 , pp. 1-7
    • Yoshida, K.1    Hisabori, T.2
  • 166
    • 84878846165 scopus 로고    scopus 로고
    • Systematic exploration of thioredoxin target proteins in plant mitochondria
    • Yoshida, K., Noguchi, K., Motohashi, K., and Hisabori, T. (2013). Systematic exploration of thioredoxin target proteins in plant mitochondria. Plant Cell. Physiol. 54, 875-892.
    • (2013) Plant Cell. Physiol. , vol.54 , pp. 875-892
    • Yoshida, K.1    Noguchi, K.2    Motohashi, K.3    Hisabori, T.4
  • 167
    • 84859475161 scopus 로고    scopus 로고
    • Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolism to induce a transient ROS signal
    • Zarse, K., Schmeisser, S., Groth, M., Priebe, S., Beuster, G., Kuhlow, D., Guthke, R., Platzer, M., Kahn, C.R., and Ristow, M. (2012). Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolism to induce a transient ROS signal. Cell Metab. 15, 451-465.
    • (2012) Cell Metab. , vol.15 , pp. 451-465
    • Zarse, K.1    Schmeisser, S.2    Groth, M.3    Priebe, S.4    Beuster, G.5    Kuhlow, D.6    Guthke, R.7    Platzer, M.8    Kahn, C.R.9    Ristow, M.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.