메뉴 건너뛰기




Volumn 218, Issue 12, 2015, Pages 1867-1879

Proteomic responses to environmentally induced oxidative stress

Author keywords

Endoplasmic reticulum; Environmental proteomics; Glutathione; Mitochondria; NAD(H); NADP(H); Peroxiredoxin; Peroxisome; Reactive oxygen species; Thioredoxin

Indexed keywords

PROTEOME; REACTIVE OXYGEN METABOLITE;

EID: 84946218551     PISSN: 00220949     EISSN: 14779145     Source Type: Journal    
DOI: 10.1242/jeb.116475     Document Type: Review
Times cited : (117)

References (98)
  • 1
    • 4644242217 scopus 로고    scopus 로고
    • Formation of reactive species and induction of antioxidant defence systems in polar and temperate marine invertebrates and fish
    • Abele, D. and Puntarulo, S. (2004). Formation of reactive species and induction of antioxidant defence systems in polar and temperate marine invertebrates and fish. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 138, 405-415.
    • (2004) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.138 , pp. 405-415
    • Abele, D.1    Puntarulo, S.2
  • 2
    • 0036022026 scopus 로고    scopus 로고
    • Temperaturedependence of mitochondrial function and production of reactive oxygen species in the intertidal mud clam Mya arenaria
    • Abele, D., Heise, K., Pörtner, H. O. and Puntarulo, S. (2002). Temperaturedependence of mitochondrial function and production of reactive oxygen species in the intertidal mud clam Mya arenaria. J. Exp. Biol. 205, 1831-1841.
    • (2002) J. Exp. Biol. , vol.205 , pp. 1831-1841
    • Abele, D.1    Heise, K.2    Pörtner, H.O.3    Puntarulo, S.4
  • 4
    • 84875719244 scopus 로고    scopus 로고
    • The role of mitochondrial dehydrogenases in the generation of oxidative stress
    • Adam-Vizi, V. and Tretter, L. (2013). The role of mitochondrial dehydrogenases in the generation of oxidative stress. Neurochem. Int. 62, 757-763.
    • (2013) Neurochem. Int. , vol.62 , pp. 757-763
    • Adam-Vizi, V.1    Tretter, L.2
  • 5
    • 25444469412 scopus 로고    scopus 로고
    • Mitochondrial metabolism of reactive oxygen species
    • Andreyev, A. Y., Kushnareva, Y. E. and Starkov, A. A. (2005). Mitochondrial metabolism of reactive oxygen species. Biochemistry 70, 200-214.
    • (2005) Biochemistry , vol.70 , pp. 200-214
    • Andreyev, A.Y.1    Kushnareva, Y.E.2    Starkov, A.A.3
  • 6
    • 79952808113 scopus 로고    scopus 로고
    • Glutathione- And non-glutathione-based oxidant control in the endoplasmic reticulum
    • Appenzeller-Herzog, C. (2011). Glutathione- And non-glutathione-based oxidant control in the endoplasmic reticulum. J. Cell Sci. 124, 847-855.
    • (2011) J. Cell Sci. , vol.124 , pp. 847-855
    • Appenzeller-Herzog, C.1
  • 7
    • 71549116049 scopus 로고    scopus 로고
    • Peroxisomal proteomics: Biomonitoring in mussels after the Prestige's oil spill
    • Apraiz, I., Cajaraville, M. P. and Cristobal, S. (2009). Peroxisomal proteomics: Biomonitoring in mussels after the Prestige's oil spill. Mar. Pollut. Bull. 58, 1815-1826.
    • (2009) Mar. Pollut. Bull. , vol.58 , pp. 1815-1826
    • Apraiz, I.1    Cajaraville, M.P.2    Cristobal, S.3
  • 8
    • 84867804213 scopus 로고    scopus 로고
    • Protein folding and quality control in the ER
    • (ed. R. I. Morimoto, D. J. Selkoe and J. W. Kelley), New York: Cold Spring Harbor Press
    • Araki, K. and Nagata, K. (2012). Protein folding and quality control in the ER. In Protein Homeostasis (ed. R. I. Morimoto, D. J. Selkoe and J. W. Kelley), pp. 121-145. New York: Cold Spring Harbor Press.
    • (2012) Protein Homeostasis , pp. 121-145
    • Araki, K.1    Nagata, K.2
  • 9
    • 84897112203 scopus 로고    scopus 로고
    • Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide
    • Bienert, G. P. and Chaumont, F. (2014). Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide. Biochim. Biophys. Acta 1840, 1596-1604.
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 1596-1604
    • Bienert, G.P.1    Chaumont, F.2
  • 10
    • 0040816232 scopus 로고
    • Shell ultrastructure in two subspecies of the ribbed mussel, Geukensia demissa (Dillwyn, 1817)
    • Blackwell, J. F., Gainey, L. F. and Greenberg, M. J. (1977). Shell ultrastructure in two subspecies of the ribbed mussel, Geukensia demissa (Dillwyn, 1817). Biol. Bull. 152, 1-11.
    • (1977) Biol. Bull. , vol.152 , pp. 1-11
    • Blackwell, J.F.1    Gainey, L.F.2    Greenberg, M.J.3
  • 11
    • 70449715463 scopus 로고    scopus 로고
    • Reactive oxygen species and peroxisomes: Struggling for balance
    • Bonekamp, N. A., Völkl, A., Fahimi, H. D. and Schrader, M. (2009). Reactive oxygen species and peroxisomes: Struggling for balance. Biofactors 35, 346-355.
    • (2009) Biofactors , vol.35 , pp. 346-355
    • Bonekamp, N.A.1    Völkl, A.2    Fahimi, H.D.3    Schrader, M.4
  • 12
    • 17044399794 scopus 로고    scopus 로고
    • Protein expression patterns in zebrafish skeletal muscle: Initial characterization and the effects of hypoxic exposure
    • Bosworth, C. A., IV, Chou, C.-W., Cole, R. B. and Rees, B. B. (2005). Protein expression patterns in zebrafish skeletal muscle: Initial characterization and the effects of hypoxic exposure. Proteomics 5, 1362-1371.
    • (2005) Proteomics , vol.5 , pp. 1362-1371
    • Bosworth, C.A.1    Chou, C.-W.2    Cole, R.B.3    Rees, B.B.4
  • 13
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman, I. and Bulleid, N. J. (2011). Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem. 80, 71-99.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 14
    • 84946210789 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum
    • (ed. S. Ferro-Novick, T. A. Rapoport and R. Schekman), Cold Spring Harbor: Cold Spring Harbor Press
    • Braakman, I. and Hebert, D. N. (2013). Protein folding in the endoplasmic reticulum. In The Endoplasmic Reticulum (ed. S. Ferro-Novick, T. A. Rapoport and R. Schekman), pp. 63-79. Cold Spring Harbor: Cold Spring Harbor Press.
    • (2013) The Endoplasmic Reticulum , pp. 63-79
    • Braakman, I.1    Hebert, D.N.2
  • 15
    • 85005965995 scopus 로고    scopus 로고
    • Disulfide bond formation in the mammalian endoplasmic reticulum
    • (ed. S. Ferro-Novick, T. A. Rapoport and R. Schekman), Cold Spring Harbor: Cold Spring Harbor Press
    • Bulleid, N. J. (2013). Disulfide bond formation in the mammalian endoplasmic reticulum. In The Endoplasmic Reticulum (ed. S. Ferro-Novick, T. A. Rapoport and R. Schekman), pp. 81-92. Cold Spring Harbor: Cold Spring Harbor Press.
    • (2013) The Endoplasmic Reticulum , pp. 81-92
    • Bulleid, N.J.1
  • 16
    • 80052372197 scopus 로고    scopus 로고
    • Multiple ways to make disulfides
    • Bulleid, N. J. and Ellgaard, L. (2011). Multiple ways to make disulfides. Trends Biochem. Sci. 36, 485-492.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 485-492
    • Bulleid, N.J.1    Ellgaard, L.2
  • 17
    • 0037352050 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase complexes in redox regulation. Role of the lipoate residues and thioredoxin
    • Bunik, V. I. (2003). 2-Oxo acid dehydrogenase complexes in redox regulation. Role of the lipoate residues and thioredoxin. Eur. J. Biochem. 270, 1036-1042.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1036-1042
    • Bunik, V.I.1
  • 20
    • 0029667844 scopus 로고    scopus 로고
    • Respiratory responses of the salt marsh animals, Fundulus heteroclitus, Leiostomus xanthurus, and Palaemonetes pugio to environmental hypoxia and hypercapnia and to the organophosphate pesticide, azinphosmethyl
    • Cochran, R. E. and Burnett, L. E. (1996). Respiratory responses of the salt marsh animals, Fundulus heteroclitus, Leiostomus xanthurus, and Palaemonetes pugio to environmental hypoxia and hypercapnia and to the organophosphate pesticide, azinphosmethyl. J. Exp. Mar. Biol. Ecol. 195, 125-144.
    • (1996) J. Exp. Mar. Biol. Ecol. , vol.195 , pp. 125-144
    • Cochran, R.E.1    Burnett, L.E.2
  • 22
    • 73849144014 scopus 로고    scopus 로고
    • Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling
    • Cox, A. G., Winterbourn, C. C. and Hampton, M. B. (2010). Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling. Biochem. J. 425, 313-325.
    • (2010) Biochem. J. , vol.425 , pp. 313-325
    • Cox, A.G.1    Winterbourn, C.C.2    Hampton, M.B.3
  • 25
    • 0030703154 scopus 로고    scopus 로고
    • Pyruvate protects neurons against hydrogen peroxide-induced toxicity
    • Desagher, S., Glowinski, J. and Premont, J. (1997). Pyruvate protects neurons against hydrogen peroxide-induced toxicity. J. Neurosci. 17, 9060-9067.
    • (1997) J. Neurosci. , vol.17 , pp. 9060-9067
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 26
    • 84863870893 scopus 로고    scopus 로고
    • Exploring the limit of metazoan thermal tolerance via comparative proteomics: Thermally induced changes in protein abundance by two hydrothermal vent polychaetes
    • Dilly, G. F., Young, C. R., Lane, W. S., Pangilinan, J. and Girguis, P. R. (2012). Exploring the limit of metazoan thermal tolerance via comparative proteomics: Thermally induced changes in protein abundance by two hydrothermal vent polychaetes. Proc. R. Soc. B Biol. Sci. 279, 3347-3356.
    • (2012) Proc. R. Soc. B Biol. Sci. , vol.279 , pp. 3347-3356
    • Dilly, G.F.1    Young, C.R.2    Lane, W.S.3    Pangilinan, J.4    Girguis, P.R.5
  • 29
    • 84860161263 scopus 로고    scopus 로고
    • Ocean salinities reveal strong global water cycle intensification during 1950 to 2000
    • Durack, P. J., Wijffels, S. E. and Matear, R. J. (2012). Ocean salinities reveal strong global water cycle intensification during 1950 to 2000. Science 336, 455-458.
    • (2012) Science , vol.336 , pp. 455-458
    • Durack, P.J.1    Wijffels, S.E.2    Matear, R.J.3
  • 31
    • 0036065181 scopus 로고    scopus 로고
    • Lipid radical generation in polar (Laternula elliptica) and temperate (Mya arenaria) bivalves
    • Estevez, M. S., Abele, D. and Puntarulo, S. (2002). Lipid radical generation in polar (Laternula elliptica) and temperate (Mya arenaria) bivalves. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 132, 729-737.
    • (2002) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.132 , pp. 729-737
    • Estevez, M.S.1    Abele, D.2    Puntarulo, S.3
  • 32
    • 84867812390 scopus 로고    scopus 로고
    • Latitudinal variation in protein expression after heat stress in the salt marsh mussel Geukensia demissa
    • Fields, P. A., Cox, K. M. and Karch, K. R. (2012a). Latitudinal variation in protein expression after heat stress in the salt marsh mussel Geukensia demissa. Integr. Comp. Biol. 52, 636-647.
    • (2012) Integr. Comp. Biol. , vol.52 , pp. 636-647
    • Fields, P.A.1    Cox, K.M.2    Karch, K.R.3
  • 33
    • 84858629618 scopus 로고    scopus 로고
    • Proteomic responses of blue mussel (Mytilus) congeners to temperature acclimation
    • Fields, P. A., Zuzow, M. J. and Tomanek, L. (2012b). Proteomic responses of blue mussel (Mytilus) congeners to temperature acclimation. J. Exp. Biol. 215, 1106-1116.
    • (2012) J. Exp. Biol. , vol.215 , pp. 1106-1116
    • Fields, P.A.1    Zuzow, M.J.2    Tomanek, L.3
  • 34
    • 84910001778 scopus 로고    scopus 로고
    • Changes in protein expression in the salt marsh mussel Geukensia demissa: Evidence for a shift from anaerobic to aerobic metabolism during prolonged aerial exposure
    • Fields, P. A., Eurich, C., Gao, W. L. and Cela, B. (2014). Changes in protein expression in the salt marsh mussel Geukensia demissa: Evidence for a shift from anaerobic to aerobic metabolism during prolonged aerial exposure. J. Exp. Biol. 217, 1601-1612.
    • (2014) J. Exp. Biol. , vol.217 , pp. 1601-1612
    • Fields, P.A.1    Eurich, C.2    Gao, W.L.3    Cela, B.4
  • 35
    • 84922233989 scopus 로고    scopus 로고
    • Biology of ferritin in mammals: An update on iron storage, oxidative damage and neurodegeneration
    • Finazzi, D. and Arosio, P. (2014). Biology of ferritin in mammals: An update on iron storage, oxidative damage and neurodegeneration. Arch. Toxicol. 88, 1787-1802.
    • (2014) Arch. Toxicol. , vol.88 , pp. 1787-1802
    • Finazzi, D.1    Arosio, P.2
  • 36
    • 79953249112 scopus 로고    scopus 로고
    • Peroxiredoxin 6: A bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
    • Fisher, A. B. (2011). Peroxiredoxin 6: A bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. Antioxid. Redox Signal. 15, 831-844.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 831-844
    • Fisher, A.B.1
  • 38
    • 0032053161 scopus 로고    scopus 로고
    • Oxygen toxicity: A radical explanation
    • Fridovich, I. (1998). Oxygen toxicity: A radical explanation. J. Exp. Biol. 201, 1203-1209.
    • (1998) J. Exp. Biol. , vol.201 , pp. 1203-1209
    • Fridovich, I.1
  • 39
    • 0038529613 scopus 로고    scopus 로고
    • The ALD6 gene product is indispensable for providing NADPH in yeast cells lacking glucose-6-phosphate dehydrogenase activity
    • Grabowska, D. and Chelstowska, A. (2003). The ALD6 gene product is indispensable for providing NADPH in yeast cells lacking glucose-6-phosphate dehydrogenase activity. J. Biol. Chem. 278, 13984-13988.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13984-13988
    • Grabowska, D.1    Chelstowska, A.2
  • 40
    • 84900453863 scopus 로고    scopus 로고
    • Mitochondrial production of reactive oxygen species
    • Grivennikova, V. G. and Vinogradov, A. D. (2013). Mitochondrial production of reactive oxygen species. Biochemistry 78, 1490-1511.
    • (2013) Biochemistry , vol.78 , pp. 1490-1511
    • Grivennikova, V.G.1    Vinogradov, A.D.2
  • 42
    • 0346034910 scopus 로고    scopus 로고
    • Production of reactive oxygen species by isolated mitochondria of the Antarctic bivalve Laternula elliptica (King and Broderip) under heat stress
    • Heise, K., Puntarulo, S., Pörtner, H. O. and Abele, D. (2003). Production of reactive oxygen species by isolated mitochondria of the Antarctic bivalve Laternula elliptica (King and Broderip) under heat stress. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 134, 79-90.
    • (2003) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.134 , pp. 79-90
    • Heise, K.1    Puntarulo, S.2    Pörtner, H.O.3    Abele, D.4
  • 43
    • 34548166529 scopus 로고    scopus 로고
    • Rat liver peroxisomes after fibrate treatment: A survey using quantitative mass spectrometry
    • Islinger, M., Luers, G. H., Li, K. W., Loos, M. and Volkl, A. (2007). Rat liver peroxisomes after fibrate treatment: A survey using quantitative mass spectrometry. J. Biol. Chem. 282, 23055-23069.
    • (2007) J. Biol. Chem. , vol.282 , pp. 23055-23069
    • Islinger, M.1    Luers, G.H.2    Li, K.W.3    Loos, M.4    Volkl, A.5
  • 44
    • 0035844289 scopus 로고    scopus 로고
    • Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+- dependent isocitrate dehydrogenase
    • Jo, S.-H., Son, M.-K., Koh, H.-J., Lee, S.-M., Song, I.-H., Kim, Y.-O., Lee, Y.-S., Jeong, K.-S., Kim,W. B., Park, J.-W. et al. (2001). Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+- dependent isocitrate dehydrogenase. J. Biol. Chem. 276, 16168-16176.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16168-16176
    • Jo, S.-H.1    Son, M.-K.2    Koh, H.-J.3    Lee, S.-M.4    Song, I.-H.5    Kim, Y.-O.6    Lee, Y.-S.7    Jeong, K.-S.8    Kim, W.B.9    Park, J.-W.10
  • 45
    • 3543017979 scopus 로고    scopus 로고
    • Seasonality of energetic functioning and production of reactive oxygen species by lugworm (Arenicola marina) mitochondria exposed to acute temperature changes
    • Keller, M., Sommer, A. M., Pörtner, H. O. and Abele, D. (2004). Seasonality of energetic functioning and production of reactive oxygen species by lugworm (Arenicola marina) mitochondria exposed to acute temperature changes. J. Exp. Biol. 207, 2529-2538.
    • (2004) J. Exp. Biol. , vol.207 , pp. 2529-2538
    • Keller, M.1    Sommer, A.M.2    Pörtner, O.3    Abele, D.4
  • 46
    • 0345791524 scopus 로고    scopus 로고
    • Proteomic analysis of rat liver peroxisome: Presence of peroxisomespecific isozyme of Lon protease
    • Kikuchi, M., Hatano, N., Yokota, S., Shimozawa, N., Imanaka, T. and Taniguchi, H. (2004). Proteomic analysis of rat liver peroxisome: Presence of peroxisomespecific isozyme of Lon protease. J. Biol. Chem. 279, 421-428.
    • (2004) J. Biol. Chem. , vol.279 , pp. 421-428
    • Kikuchi, M.1    Hatano, N.2    Yokota, S.3    Shimozawa, N.4    Imanaka, T.5    Taniguchi, H.6
  • 47
    • 15544377794 scopus 로고    scopus 로고
    • Molecular and evolutionary basis of the cellular stress response
    • Kültz, D. (2005). Molecular and evolutionary basis of the cellular stress response. Annu. Rev. Physiol. 67, 225-257.
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 225-257
    • Kültz, D.1
  • 48
    • 0019433557 scopus 로고
    • Regulation of protein synthesis during heat shock
    • Lindquist, S. (1981). Regulation of protein synthesis during heat shock. Nature 293, 311-314.
    • (1981) Nature , vol.293 , pp. 311-314
    • Lindquist, S.1
  • 49
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist, S. (1986). The heat-shock response. Annu. Rev. Biochem. 55, 1151-1191.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 51
    • 84888133598 scopus 로고    scopus 로고
    • Unearthing the secrets of mitochondrial ROS and glutathione in bioenergetics
    • Mailloux, R. J., McBride, S. L. and Harper, M.-E. (2013). Unearthing the secrets of mitochondrial ROS and glutathione in bioenergetics. Trends Biochem. Sci. 38, 592-602.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 592-602
    • Mailloux, R.J.1    McBride, S.L.2    Harper, M.-E.3
  • 52
    • 39749173200 scopus 로고    scopus 로고
    • Isocitrate dehydrogenase: A NADPHgenerating enzyme in the lumen of the endoplasmic reticulum
    • Margittai, E. and Bánhegyi, G. (2008). Isocitrate dehydrogenase: A NADPHgenerating enzyme in the lumen of the endoplasmic reticulum. Arch. Biochem. Biophys. 471, 184-190.
    • (2008) Arch. Biochem. Biophys. , vol.471 , pp. 184-190
    • Margittai, E.1    Bánhegyi, G.2
  • 53
    • 73349133007 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins: Unifying elements in redox biology
    • Meyer, Y., Buchanan, B. B., Vignols, F. and Reichheld, J.-P. (2009). Thioredoxins and glutaredoxins: Unifying elements in redox biology. Annu. Rev. Genet. 43, 335-367.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 335-367
    • Meyer, Y.1    Buchanan, B.B.2    Vignols, F.3    Reichheld, J.-P.4
  • 56
    • 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
  • 57
    • 84856729192 scopus 로고    scopus 로고
    • Mitochondrial thiols in antioxidant protection and redox signaling: Distinct roles for glutathionylation and other thiol modifications
    • Murphy, M. P. (2012). Mitochondrial thiols in antioxidant protection and redox signaling: Distinct roles for glutathionylation and other thiol modifications. Antioxid. Redox Signal. 16, 476-495.
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 476-495
    • Murphy, M.P.1
  • 60
    • 84895098727 scopus 로고    scopus 로고
    • Peroxisomal metabolism and oxidative stress
    • Nordgren, M. and Fransen, M. (2014). Peroxisomal metabolism and oxidative stress. Biochimie 98, 56-62.
    • (2014) Biochimie , vol.98 , pp. 56-62
    • Nordgren, M.1    Fransen, M.2
  • 61
    • 33846838600 scopus 로고    scopus 로고
    • Detection of hypoxia-related proteins in medaka (Oryzias latipes) brain tissue by difference gel electrophoresis and de novo sequencing of 4-sulfophenyl isothiocyanate-derivatized peptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Oehlers, L. P., Perez, A. N. and Walter, R. B. (2007). Detection of hypoxia-related proteins in medaka (Oryzias latipes) brain tissue by difference gel electrophoresis and de novo sequencing of 4-sulfophenyl isothiocyanate-derivatized peptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 145, 120-133.
    • (2007) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.145 , pp. 120-133
    • Oehlers, L.P.1    Perez, A.N.2    Walter, R.B.3
  • 62
    • 77953024704 scopus 로고    scopus 로고
    • Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum
    • Pearse, B. R. and Hebert, D. N. (2010). Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum. Biochim. Biophys. Acta 1803, 684-693.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 684-693
    • Pearse, B.R.1    Hebert, D.N.2
  • 63
    • 43549094212 scopus 로고    scopus 로고
    • Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins
    • Petrak, J., Ivanek, R., Toman, O., Cmejla, R., Cmejlova, J., Vyoral, D., Zivny, J. and Vulpe, C. D. (2008). Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins. Proteomics 8, 1744-1749.
    • (2008) Proteomics , vol.8 , pp. 1744-1749
    • Petrak, J.1    Ivanek, R.2    Toman, O.3    Cmejla, R.4    Cmejlova, J.5    Vyoral, D.6    Zivny, J.7    Vulpe, C.D.8
  • 64
    • 84946210878 scopus 로고    scopus 로고
    • Physiological strategies during animal diapause: Lessons from brine shrimp and annual killifish
    • Podrabsky, J. E. and Hand, S. C. (2015). Physiological strategies during animal diapause: Lessons from brine shrimp and annual killifish. J. Exp. Biol. 218, 1897-1906.
    • (2015) J. Exp. Biol. , vol.218 , pp. 1897-1906
    • Podrabsky, J.E.1    Hand, S.C.2
  • 65
    • 33847711060 scopus 로고    scopus 로고
    • The power to reduce: Pyridine nucleotides - small molecules with a multitude of functions
    • Pollak, N., Dölle, C. and Ziegler, M. (2007). The power to reduce: Pyridine nucleotides - small molecules with a multitude of functions. Biochem. J. 402, 205-218.
    • (2007) Biochem. J. , vol.402 , pp. 205-218
    • Pollak, N.1    Dölle, C.2    Ziegler, M.3
  • 66
    • 0036772306 scopus 로고    scopus 로고
    • Water quality variation and clam growth: Is pH really a non-issue in estuaries?
    • Ringwood, A. H. and Keppler, C. J. (2002). Water quality variation and clam growth: Is pH really a non-issue in estuaries? Estuaries 25, 901-907.
    • (2002) Estuaries , vol.25 , pp. 901-907
    • Ringwood, A.H.1    Keppler, C.J.2
  • 68
    • 33745635338 scopus 로고    scopus 로고
    • Mitochondrial NADPH, transhydrogenase and disease
    • Rydström, J. (2006). Mitochondrial NADPH, transhydrogenase and disease. Biochim. Biophys. Acta 1757, 721-726.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 721-726
    • Rydström, J.1
  • 69
    • 46449087496 scopus 로고    scopus 로고
    • Fatty acids as modulators of the cellular production of reactive oxygen species
    • Schönfeld, P. and Wojtczak, L. (2008). Fatty acids as modulators of the cellular production of reactive oxygen species. Free Radic. Biol. Med. 45, 231-241.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 231-241
    • Schönfeld, P.1    Wojtczak, L.2
  • 70
    • 77953809888 scopus 로고    scopus 로고
    • Mitochondrial fatty acid oxidation and oxidative stress: Lack of reverse electron transfer-associated production of reactive oxygen species
    • Schönfeld, P., Wie?ckowski, M. R., Lebiedzińska, M. and Wojtczak, L. (2010). Mitochondrial fatty acid oxidation and oxidative stress: Lack of reverse electron transfer-associated production of reactive oxygen species. Biochim. Biophys. Acta 1797, 929-938.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 929-938
    • Schönfeld, P.1    Wieckowski, M.R.2    Lebiedzińska, M.3    Wojtczak, L.4
  • 71
    • 33845292901 scopus 로고    scopus 로고
    • Peroxisomes and oxidative stress
    • Schrader, M. and Fahimi, H. D. (2006). Peroxisomes and oxidative stress. Biochim. Biophys. Acta 1763, 1755-1766.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1755-1766
    • Schrader, M.1    Fahimi, H.D.2
  • 73
    • 65349148426 scopus 로고    scopus 로고
    • Proteomic changes in the crucian carp brain during exposure to anoxia
    • Smith, R. W., Cash, P., Ellefsen, S. and Nilsson, G. E. (2009). Proteomic changes in the crucian carp brain during exposure to anoxia. Proteomics 9, 2217-2229.
    • (2009) Proteomics , vol.9 , pp. 2217-2229
    • Smith, R.W.1    Cash, P.2    Ellefsen, S.3    Nilsson, G.E.4
  • 74
    • 84875670814 scopus 로고    scopus 로고
    • An update on the role of mitochondrial alpha-ketoglutarate dehydrogenase in oxidative stress
    • Starkov, A. A. (2013). An update on the role of mitochondrial alpha-ketoglutarate dehydrogenase in oxidative stress. Mol. Cell. Neurosci. 55, 13-16.
    • (2013) Mol. Cell. Neurosci. , vol.55 , pp. 13-16
    • Starkov, A.A.1
  • 76
    • 63349087445 scopus 로고    scopus 로고
    • Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation
    • Tahara, E. B., Navarete, F. D. T. and Kowaltowski, A. J. (2009). Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation. Free Radic. Biol. Med. 46, 1283-1297.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1283-1297
    • Tahara, E.B.1    Navarete, F.D.T.2    Kowaltowski, A.J.3
  • 77
    • 78650270477 scopus 로고    scopus 로고
    • Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
    • Tavender, T. J., Springate, J. J. and Bulleid, N. J. (2010). Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J. 29, 4185-4197.
    • (2010) EMBO J. , vol.29 , pp. 4185-4197
    • Tavender, T.J.1    Springate, J.J.2    Bulleid, N.J.3
  • 78
    • 84867733514 scopus 로고    scopus 로고
    • Glutathione-S-transferases as determinants of cell survival and death
    • Tew, K. D. and Townsend, D. M. (2012). Glutathione-S-transferases as determinants of cell survival and death. Antioxid. Redox Signal. 17, 1728-1737.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1728-1737
    • Tew, K.D.1    Townsend, D.M.2
  • 79
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas, J. A., Poland, B. and Honzatko, R. (1995). Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch. Biochem. Biophys. 319, 1-9.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 80
    • 55549094419 scopus 로고    scopus 로고
    • The importance of physiological limits in determining biogeographical range shifts due to global climate change: The heat-shock response
    • Tomanek, L. (2008). The importance of physiological limits in determining biogeographical range shifts due to global climate change: The heat-shock response. Physiol. Biochem. Zool. 81, 709-717.
    • (2008) Physiol. Biochem. Zool. , vol.81 , pp. 709-717
    • Tomanek, L.1
  • 81
    • 77649211464 scopus 로고    scopus 로고
    • Variation in the heat shock response and its implication for predicting the effect of global climate change on species' biogeographical distribution ranges and metabolic costs
    • Tomanek, L. (2010). Variation in the heat shock response and its implication for predicting the effect of global climate change on species' biogeographical distribution ranges and metabolic costs. J. Exp. Biol. 213, 971-979.
    • (2010) J. Exp. Biol. , vol.213 , pp. 971-979
    • Tomanek, L.1
  • 82
    • 78751584111 scopus 로고    scopus 로고
    • Environmental proteomics: Changes in the proteome of marine organisms in response to environmental stress, pollutants, infection, symbiosis, and development
    • Tomanek, L. (2011). Environmental proteomics: Changes in the proteome of marine organisms in response to environmental stress, pollutants, infection, symbiosis, and development. Annu. Rev. Mar. Sci. 3, 373-399.
    • (2011) Annu. Rev. Mar. Sci. , vol.3 , pp. 373-399
    • Tomanek, L.1
  • 83
    • 84867787191 scopus 로고    scopus 로고
    • Environmental proteomics of the mussel Mytilus: Implications for tolerance to stress and change in limits of biogeographic ranges in response to climate change
    • Tomanek, L. (2012). Environmental proteomics of the mussel Mytilus: Implications for tolerance to stress and change in limits of biogeographic ranges in response to climate change. Integr. Comp. Biol. 52, 648-664.
    • (2012) Integr. Comp. Biol. , vol.52 , pp. 648-664
    • Tomanek, L.1
  • 84
    • 84901843464 scopus 로고    scopus 로고
    • Proteomics to study adaptations in marine organisms to environmental stress
    • Tomanek, L. (2014). Proteomics to study adaptations in marine organisms to environmental stress. J. Proteomics 105, 92-106.
    • (2014) J. Proteomics , vol.105 , pp. 92-106
    • Tomanek, L.1
  • 85
    • 0034094164 scopus 로고    scopus 로고
    • Time course and magnitude of synthesis of heat-shock proteins in congeneric marine snails (genus Tegula) from different tidal heights
    • Tomanek, L. and Somero,G. N. (2000). Time course and magnitude of synthesis of heat-shock proteins in congeneric marine snails (genus Tegula) from different tidal heights. Physiol. Biochem. Zool. 73, 249-256.
    • (2000) Physiol. Biochem. Zool. , vol.73 , pp. 249-256
    • Tomanek, L.1    Somero, G.N.2
  • 86
    • 77954932614 scopus 로고    scopus 로고
    • The proteomic response of the mussel congeners Mytilus galloprovincialis and M. trossulus to acute heat stress: Implications for thermal tolerance limits and metabolic costs of thermal stress
    • Tomanek, L. and Zuzow, M. J. (2010). The proteomic response of the mussel congeners Mytilus galloprovincialis and M. trossulus to acute heat stress: Implications for thermal tolerance limits and metabolic costs of thermal stress. J. Exp. Biol. 213, 3559-3574.
    • (2010) J. Exp. Biol. , vol.213 , pp. 3559-3574
    • Tomanek, L.1    Zuzow, M.J.2
  • 88
    • 84867749042 scopus 로고    scopus 로고
    • Proteomics of hyposaline stress in blue mussel congeners (genus Mytilus): Implications for biogeographic range limits in response to climate change
    • Tomanek, L., Zuzow, M. J., Hitt, L., Serafini, L. and Valenzuela, J. J. (2012). Proteomics of hyposaline stress in blue mussel congeners (genus Mytilus): Implications for biogeographic range limits in response to climate change. J. Exp. Biol. 215, 3905-3916.
    • (2012) J. Exp. Biol. , vol.215 , pp. 3905-3916
    • Tomanek, L.1    Zuzow, M.J.2    Hitt, L.3    Serafini, L.4    Valenzuela, J.J.5
  • 89
    • 58649100268 scopus 로고    scopus 로고
    • Novel role for glutathione S-transferase pi. Regulator of protein S-glutathionylation following oxidative and nitrosative stress
    • Townsend, D. M., Manevich, Y., He, L., Hutchens, S., Pazoles, C. J. and Tew, K. D. (2009). Novel role for glutathione S-transferase pi. Regulator of protein S-glutathionylation following oxidative and nitrosative stress. J. Biol. Chem. 284, 436-445.
    • (2009) J. Biol. Chem. , vol.284 , pp. 436-445
    • Townsend, D.M.1    Manevich, Y.2    He, L.3    Hutchens, S.4    Pazoles, C.J.5    Tew, K.D.6
  • 90
    • 46449115525 scopus 로고    scopus 로고
    • Peroxynitrite detoxification and its biologic implications
    • Trujillo, M., Ferrer-Sueta, G. and Radi, R. (2008). Peroxynitrite detoxification and its biologic implications. Antioxid. Redox Signal. 10, 1607-1620.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1607-1620
    • Trujillo, M.1    Ferrer-Sueta, G.2    Radi, R.3
  • 92
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • Walsh, C. T., Garneau-Tsodikova, S. and Gatto, G. J.Jr. (2005). Protein posttranslational modifications: The chemistry of proteome diversifications. Angew. Chem. Int. Ed. Engl. 44, 7342-7372.
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto, G.J.3
  • 93
    • 67649184787 scopus 로고    scopus 로고
    • Generally detected proteins in comparative proteomics - A matter of cellular stress response?
    • Wang, P., Bouwman, F. G. and Mariman, E. C. M. (2009). Generally detected proteins in comparative proteomics - A matter of cellular stress response? Proteomics 9, 2955-2966.
    • (2009) Proteomics , vol.9 , pp. 2955-2966
    • Wang, P.1    Bouwman, F.G.2    Mariman, E.C.M.3
  • 94
    • 33847019963 scopus 로고    scopus 로고
    • Hexose 6-phosphate dehydrogenase (H6PD) and corticosteroid metabolism
    • White, P. C., Rogoff, D., McMillan, D. R. and Lavery, G. G. (2007). Hexose 6-phosphate dehydrogenase (H6PD) and corticosteroid metabolism. Mol. Cell. Endocrinol. 265-266, 89-92.
    • (2007) Mol. Cell. Endocrinol. , vol.265-266 , pp. 89-92
    • White, P.C.1    Rogoff, D.2    McMillan, D.R.3    Lavery, G.G.4
  • 96
    • 0034867911 scopus 로고    scopus 로고
    • Localization of cytosolic NADP-dependent isocitrate dehydrogenase in the peroxisomes of rat liver cells: Biochemical and immunocytochemical studies
    • Yoshihara, T., Hamamoto, T., Munakata, R., Tajiri, R., Ohsumi, M. and Yokota, S. (2001). Localization of cytosolic NADP-dependent isocitrate dehydrogenase in the peroxisomes of rat liver cells: Biochemical and immunocytochemical studies. J. Histochem. Cytochem. 49, 1123-1131.
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 1123-1131
    • Yoshihara, T.1    Hamamoto, T.2    Munakata, R.3    Tajiri, R.4    Ohsumi, M.5    Yokota, S.6
  • 97
    • 84859951790 scopus 로고    scopus 로고
    • SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
    • Yu, W., Dittenhafer-Reed, K. E. and Denu, J. M. (2012). SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status. J. Biol. Chem. 287, 14078-14086.
    • (2012) J. Biol. Chem. , vol.287 , pp. 14078-14086
    • Yu, W.1    Dittenhafer-Reed, K.E.2    Denu, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.