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Volumn 50, Issue 4, 2011, Pages 495-509

Cysteine/cystine redox signaling in cardiovascular disease

Author keywords

Atherosclerosis; Endothelial cells; Free radicals; Inflammatory mechanism; Monocytes; Plasma redox state; Thiol disulfide

Indexed keywords

ACETYLCYSTEINE; ACTIN; ARYLDIALKYLPHOSPHATASE; CELL SURFACE PROTEIN; CERULOPLASMIN; CYSTEINE; CYSTINE; CYTOSKELETON PROTEIN; DISULFIDE; EPIDERMAL GROWTH FACTOR RECEPTOR; FIBRONECTIN; GLUTATHIONE DISULFIDE; GLUTATHIONE SYNTHASE; HOMOCYSTEINE; HYDROGEN PEROXIDE; HYDROGEN SULFIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; METALLOTHIONEIN; METHIONINE; MITOGEN ACTIVATED PROTEIN KINASE; MYELOPEROXIDASE; NITRIC OXIDE; PARACETAMOL; SULFUR AMINO ACID; THIOCTIC ACID; THIOL DERIVATIVE; THIOL OXIDASE; TUMOR NECROSIS FACTOR ALPHA; ZINC;

EID: 79251614656     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.11.029     Document Type: Review
Times cited : (340)

References (138)
  • 1
    • 70349280209 scopus 로고    scopus 로고
    • Chronic antioxidant therapy fails to ameliorate hypertension: Potential mechanisms behind
    • O. Pechanova, and F. Simko Chronic antioxidant therapy fails to ameliorate hypertension: potential mechanisms behind J. Hypertens. 27 Suppl. 6 2009 S32 S36
    • (2009) J. Hypertens. , vol.27 , Issue.SUPPL. 6
    • Pechanova, O.1    Simko, F.2
  • 3
    • 43049180323 scopus 로고    scopus 로고
    • Why have antioxidants failed in clinical trials?
    • S.R. Steinhubl Why have antioxidants failed in clinical trials? Am. J. Cardiol. 101 2008 14D 19D
    • (2008) Am. J. Cardiol. , vol.101
    • Steinhubl, S.R.1
  • 4
    • 33847378451 scopus 로고    scopus 로고
    • Mortality in randomized trials of antioxidant supplements for primary and secondary prevention: Systematic review and meta-analysis
    • G. Bjelakovic, D. Nikolova, L.L. Gluud, R.G. Simonetti, and C. Gluud Mortality in randomized trials of antioxidant supplements for primary and secondary prevention: systematic review and meta-analysis JAMA 297 2007 842 857
    • (2007) JAMA , vol.297 , pp. 842-857
    • Bjelakovic, G.1    Nikolova, D.2    Gluud, L.L.3    Simonetti, R.G.4    Gluud, C.5
  • 5
    • 0025663252 scopus 로고
    • Oxidatively stressed lymphocytes remain in G0/G1a on mitogenic stimulation
    • D.D. Duncan, and D.A. Lawrence Oxidatively stressed lymphocytes remain in G0/G1a on mitogenic stimulation J. Biochem. Toxicol. 5 1990 229 235
    • (1990) J. Biochem. Toxicol. , vol.5 , pp. 229-235
    • Duncan, D.D.1    Lawrence, D.A.2
  • 6
    • 0029826005 scopus 로고    scopus 로고
    • Surface thiols of human lymphocytes and their changes after in vitro and in vivo activation
    • D.A. Lawrence, R. Song, and P. Weber Surface thiols of human lymphocytes and their changes after in vitro and in vivo activation J. Leukocyte Biol. 60 1996 611 618
    • (1996) J. Leukocyte Biol. , vol.60 , pp. 611-618
    • Lawrence, D.A.1    Song, R.2    Weber, P.3
  • 9
    • 4644310560 scopus 로고    scopus 로고
    • Role of oxidative modifications in atherosclerosis
    • R. Stocker, and J.F. Keaney Jr. Role of oxidative modifications in atherosclerosis Physiol. Rev. 84 2004 1381 1478
    • (2004) Physiol. Rev. , vol.84 , pp. 1381-1478
    • Stocker, R.1    Keaney, Jr.J.F.2
  • 10
    • 0025900662 scopus 로고
    • Postirradiation sensitization of mammalian cells by the thiol-depleting agent dimethyl fumarate
    • K.D. Held, E.R. Epp, S. Awad, and J.E. Biaglow Postirradiation sensitization of mammalian cells by the thiol-depleting agent dimethyl fumarate Radiat. Res. 127 1991 75 80
    • (1991) Radiat. Res. , vol.127 , pp. 75-80
    • Held, K.D.1    Epp, E.R.2    Awad, S.3    Biaglow, J.E.4
  • 12
    • 0029939676 scopus 로고    scopus 로고
    • Homocysteine and vascular disease
    • K.S. McCully Homocysteine and vascular disease Nat. Med. 2 1996 386 389
    • (1996) Nat. Med. , vol.2 , pp. 386-389
    • McCully, K.S.1
  • 13
    • 0036545912 scopus 로고    scopus 로고
    • The plasma redox state and ageing
    • W. Droge The plasma redox state and ageing Ageing Res. Rev. 1 2002 257 278
    • (2002) Ageing Res. Rev. , vol.1 , pp. 257-278
    • Droge, W.1
  • 14
    • 0032125750 scopus 로고    scopus 로고
    • The redox state as a correlate of senescence and wasting and as a target for therapeutic intervention
    • V. Hack, R. Breitkreutz, R. Kinscherf, H. Rohrer, P. Bartsch, F. Taut, A. Benner, and W. Droge The redox state as a correlate of senescence and wasting and as a target for therapeutic intervention Blood 92 1998 59 67
    • (1998) Blood , vol.92 , pp. 59-67
    • Hack, V.1    Breitkreutz, R.2    Kinscherf, R.3    Rohrer, H.4    Bartsch, P.5    Taut, F.6    Benner, A.7    Droge, W.8
  • 15
    • 0028901371 scopus 로고
    • Redox status and protein binding of plasma homocysteine and other aminothiols in patients with early-onset peripheral vascular disease: Homocysteine and peripheral vascular disease
    • M.A. Mansoor, C. Bergmark, A.M. Svardal, P.E. Lonning, and P.M. Ueland Redox status and protein binding of plasma homocysteine and other aminothiols in patients with early-onset peripheral vascular disease: homocysteine and peripheral vascular disease Arterioscler. Thromb. Vasc. Biol. 15 1995 232 240
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 232-240
    • Mansoor, M.A.1    Bergmark, C.2    Svardal, A.M.3    Lonning, P.E.4    Ueland, P.M.5
  • 16
    • 0034682644 scopus 로고    scopus 로고
    • Nontraditional risk factors for coronary heart disease incidence among persons with diabetes: The Atherosclerosis Risk in Communities (ARIC) Study
    • I. Saito, A.R. Folsom, F.L. Brancati, B.B. Duncan, L.E. Chambless, and P.G. McGovern Nontraditional risk factors for coronary heart disease incidence among persons with diabetes: the Atherosclerosis Risk in Communities (ARIC) Study Ann. Int. Med. 133 2000 81 91
    • (2000) Ann. Int. Med. , vol.133 , pp. 81-91
    • Saito, I.1    Folsom, A.R.2    Brancati, F.L.3    Duncan, B.B.4    Chambless, L.E.5    McGovern, P.G.6
  • 18
    • 4043155719 scopus 로고    scopus 로고
    • High dietary methionine plus cholesterol exacerbates atherosclerosis formation in the left main coronary artery of rabbits
    • A. Zulli, D.L. Hare, B.F. Buxton, and M.J. Black High dietary methionine plus cholesterol exacerbates atherosclerosis formation in the left main coronary artery of rabbits Atherosclerosis 176 2004 83 89
    • (2004) Atherosclerosis , vol.176 , pp. 83-89
    • Zulli, A.1    Hare, D.L.2    Buxton, B.F.3    Black, M.J.4
  • 19
    • 0032779052 scopus 로고    scopus 로고
    • Lifestyle and cardiovascular disease risk factors as determinants of total cysteine in plasma: The Hordaland Homocysteine Study
    • L. El-Khairy, P.M. Ueland, O. Nygard, H. Refsum, and S.E. Vollset Lifestyle and cardiovascular disease risk factors as determinants of total cysteine in plasma: the Hordaland Homocysteine Study Am. J. Clin. Nutr. 70 1999 1016 1024
    • (1999) Am. J. Clin. Nutr. , vol.70 , pp. 1016-1024
    • El-Khairy, L.1    Ueland, P.M.2    Nygard, O.3    Refsum, H.4    Vollset, S.E.5
  • 20
    • 0035967497 scopus 로고    scopus 로고
    • Plasma total cysteine as a risk factor for vascular disease: The European Concerted Action Project
    • L. El-Khairy, P.M. Ueland, H. Refsum, I.M. Graham, and S.E. Vollset Plasma total cysteine as a risk factor for vascular disease: the European Concerted Action Project Circulation 103 2001 2544 2549
    • (2001) Circulation , vol.103 , pp. 2544-2549
    • El-Khairy, L.1    Ueland, P.M.2    Refsum, H.3    Graham, I.M.4    Vollset, S.E.5
  • 22
    • 0036126402 scopus 로고    scopus 로고
    • Plasma total homocysteine and cysteine levels as cardiovascular risk factors in coronary heart disease
    • Y. Ozkan, E. Ozkan, and B. Simsek Plasma total homocysteine and cysteine levels as cardiovascular risk factors in coronary heart disease Int. J. Cardiol. 82 2002 269 277
    • (2002) Int. J. Cardiol. , vol.82 , pp. 269-277
    • Ozkan, Y.1    Ozkan, E.2    Simsek, B.3
  • 23
    • 0036829579 scopus 로고    scopus 로고
    • Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses
    • D.P. Jones, V.C. Mody Jr., J.L. Carlson, M.J. Lynn, and P. Sternberg Jr. Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses Free Radic. Biol. Med. 33 2002 1290 1300
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1290-1300
    • Jones, D.P.1    Mody, Jr.V.C.2    Carlson, J.L.3    Lynn, M.J.4    Sternberg, Jr.P.5
  • 24
    • 74949087000 scopus 로고    scopus 로고
    • Gene and protein responses of human monocytes to extracellular cysteine redox potential
    • Y.M. Go, S.E. Craige, M. Orr, K.M. Gernert, and D.P. Jones Gene and protein responses of human monocytes to extracellular cysteine redox potential Toxicol. Sci. 112 2009 354 362
    • (2009) Toxicol. Sci. , vol.112 , pp. 354-362
    • Go, Y.M.1    Craige, S.E.2    Orr, M.3    Gernert, K.M.4    Jones, D.P.5
  • 25
    • 20444499841 scopus 로고    scopus 로고
    • Intracellular proatherogenic events and cell adhesion modulated by extracellular thiol/disulfide redox state
    • Y.M. Go, and D.P. Jones Intracellular proatherogenic events and cell adhesion modulated by extracellular thiol/disulfide redox state Circulation 111 2005 2973 2980
    • (2005) Circulation , vol.111 , pp. 2973-2980
    • Go, Y.M.1    Jones, D.P.2
  • 27
    • 0036890251 scopus 로고    scopus 로고
    • Extracellular thiol/disulfide redox state affects proliferation rate in a human colon carcinoma (Caco2) cell line
    • C.R. Jonas, T.R. Ziegler, L.H. Gu, and D.P. Jones Extracellular thiol/disulfide redox state affects proliferation rate in a human colon carcinoma (Caco2) cell line Free Radic. Biol. Med. 33 2002 1499 1506
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1499-1506
    • Jonas, C.R.1    Ziegler, T.R.2    Gu, L.H.3    Jones, D.P.4
  • 29
    • 0036103407 scopus 로고    scopus 로고
    • Plasma cystine concentration and redox state in aging and physical exercise
    • W. Hildebrandt, R. Kinscherf, K. Hauer, E. Holm, and W. Droge Plasma cystine concentration and redox state in aging and physical exercise Mech. Ageing Dev. 123 2002 1269 1281
    • (2002) Mech. Ageing Dev. , vol.123 , pp. 1269-1281
    • Hildebrandt, W.1    Kinscherf, R.2    Hauer, K.3    Holm, E.4    Droge, W.5
  • 32
    • 33846337794 scopus 로고    scopus 로고
    • Effects of long-term zinc supplementation on plasma thiol metabolites and redox status in patients with age-related macular degeneration
    • S.E. Moriarty-Craige, K.N. Ha, P. Sternberg Jr., M. Lynn, S. Bressler, G. Gensler, and D.P. Jones Effects of long-term zinc supplementation on plasma thiol metabolites and redox status in patients with age-related macular degeneration Am. J. Ophthalmol. 143 2007 206 211
    • (2007) Am. J. Ophthalmol. , vol.143 , pp. 206-211
    • Moriarty-Craige, S.E.1    Ha, K.N.2    Sternberg, Jr.P.3    Lynn, M.4    Bressler, S.5    Gensler, G.6    Jones, D.P.7
  • 33
    • 58649100256 scopus 로고    scopus 로고
    • Monocyte-endothelial cell interactions in the development of atherosclerosis
    • J. Mestas, and K. Ley Monocyte-endothelial cell interactions in the development of atherosclerosis Trends Cardiovasc. Med. 18 2008 228 232
    • (2008) Trends Cardiovasc. Med. , vol.18 , pp. 228-232
    • Mestas, J.1    Ley, K.2
  • 34
    • 0027241856 scopus 로고
    • The pathogenesis of atherosclerosis: A perspective for the 1990s
    • R. Ross The pathogenesis of atherosclerosis: a perspective for the 1990s Nature 362 1993 801 809
    • (1993) Nature , vol.362 , pp. 801-809
    • Ross, R.1
  • 35
    • 77957297487 scopus 로고    scopus 로고
    • Redox clamp model for study of extracellular thiols and disulfides in redox signaling
    • Y.M. Go, and D.P. Jones Redox clamp model for study of extracellular thiols and disulfides in redox signaling Meth. Enzymol. 474 2010 165 179
    • (2010) Meth. Enzymol. , vol.474 , pp. 165-179
    • Go, Y.M.1    Jones, D.P.2
  • 36
    • 0028043458 scopus 로고
    • Endothelial nitric oxide synthase membrane targeting: Evidence against involvement of a specific myristate receptor
    • L. Busconi, and T. Michel Endothelial nitric oxide synthase membrane targeting: evidence against involvement of a specific myristate receptor J. Biol. Chem. 269 1994 25016 25020
    • (1994) J. Biol. Chem. , vol.269 , pp. 25016-25020
    • Busconi, L.1    Michel, T.2
  • 38
    • 0034537132 scopus 로고    scopus 로고
    • Evidence for a NADH/NADPH oxidase in human umbilical vein endothelial cells using electron spin resonance
    • M.J. Somers, J.S. Burchfield, and D.G. Harrison Evidence for a NADH/NADPH oxidase in human umbilical vein endothelial cells using electron spin resonance Antioxid. Redox Signaling 2 2000 779 787
    • (2000) Antioxid. Redox Signaling , vol.2 , pp. 779-787
    • Somers, M.J.1    Burchfield, J.S.2    Harrison, D.G.3
  • 39
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • A. Holmgren Thioredoxin and glutaredoxin systems J. Biol. Chem. 264 1989 13963 13966
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 40
    • 0024465730 scopus 로고
    • Catalysis of thiol/disulfide exchange: Single-turnover reduction of protein disulfide-isomerase by glutathione and catalysis of peptide disulfide reduction
    • H.F. Gilbert Catalysis of thiol/disulfide exchange: single-turnover reduction of protein disulfide-isomerase by glutathione and catalysis of peptide disulfide reduction Biochemistry 28 1989 7298 7305
    • (1989) Biochemistry , vol.28 , pp. 7298-7305
    • Gilbert, H.F.1
  • 41
    • 70349823268 scopus 로고    scopus 로고
    • Thioredoxin-related protein 14, a new member of the thioredoxin family with disulfide reductase activity: Implication in the redox regulation of TNF-α signaling
    • W. Jeong, Y. Jung, H. Kim, S.J. Park, and S.G. Rhee Thioredoxin-related protein 14, a new member of the thioredoxin family with disulfide reductase activity: implication in the redox regulation of TNF-α signaling Free Radic. Biol. Med. 47 2009 1294 1303
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1294-1303
    • Jeong, W.1    Jung, Y.2    Kim, H.3    Park, S.J.4    Rhee, S.G.5
  • 42
    • 21744459518 scopus 로고    scopus 로고
    • Extracellular cysteine/cystine redox regulates the p44/p42 MAPK pathway by metalloproteinase-dependent epidermal growth factor receptor signaling
    • Y.S. Nkabyo, Y.M. Go, T.R. Ziegler, and D.P. Jones Extracellular cysteine/cystine redox regulates the p44/p42 MAPK pathway by metalloproteinase-dependent epidermal growth factor receptor signaling Am. J. Physiol. 289 2005 G70 G78
    • (2005) Am. J. Physiol. , vol.289
    • Nkabyo, Y.S.1    Go, Y.M.2    Ziegler, T.R.3    Jones, D.P.4
  • 43
    • 60349113228 scopus 로고    scopus 로고
    • Quantification of redox conditions in the nucleus
    • Y.M. Go, J. Pohl, and D.P. Jones Quantification of redox conditions in the nucleus R. Hancock, The Nucleus 2009 Humana Press Totowa, NJ 303 317
    • (2009) The Nucleus , pp. 303-317
    • Go, Y.M.1    Pohl, J.2    Jones, D.P.3
  • 44
    • 67650221201 scopus 로고    scopus 로고
    • Autophagy, redox signaling, and ventricular remodeling
    • N. Gurusamy, and D.K. Das Autophagy, redox signaling, and ventricular remodeling Antioxid. Redox Signaling 11 2009 1975 1988
    • (2009) Antioxid. Redox Signaling , vol.11 , pp. 1975-1988
    • Gurusamy, N.1    Das, D.K.2
  • 45
    • 34548399767 scopus 로고    scopus 로고
    • Cell survival under nutrient stress is dependent on metabolic conditions regulated by Akt and not by autophagic vacuoles
    • P. Bruno, A. Calastretti, M. Priulla, L. Asnaghi, F. Scarlatti, A. Nicolin, and G. Canti Cell survival under nutrient stress is dependent on metabolic conditions regulated by Akt and not by autophagic vacuoles Cell Signal. 19 2007 2118 2126
    • (2007) Cell Signal. , vol.19 , pp. 2118-2126
    • Bruno, P.1    Calastretti, A.2    Priulla, M.3    Asnaghi, L.4    Scarlatti, F.5    Nicolin, A.6    Canti, G.7
  • 46
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • R. Scherz-Shouval, E. Shvets, E. Fass, H. Shorer, L. Gil, and Z. Elazar Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4 EMBO J. 26 2007 1749 1760
    • (2007) EMBO J. , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 50
    • 32944468191 scopus 로고    scopus 로고
    • Bleomycin pulmonary toxicity has a negative impact on the outcome of patients with Hodgkin's lymphoma
    • W.G. Martin, K.M. Ristow, T.M. Habermann, J.P. Colgan, T.E. Witzig, and S.M. Ansell Bleomycin pulmonary toxicity has a negative impact on the outcome of patients with Hodgkin's lymphoma J. Clin. Oncol. 23 2005 7614 7620
    • (2005) J. Clin. Oncol. , vol.23 , pp. 7614-7620
    • Martin, W.G.1    Ristow, K.M.2    Habermann, T.M.3    Colgan, J.P.4    Witzig, T.E.5    Ansell, S.M.6
  • 52
    • 33745247801 scopus 로고    scopus 로고
    • Oxidative stress and ageing: Is ageing a cysteine deficiency syndrome?
    • W. Droge Oxidative stress and ageing: is ageing a cysteine deficiency syndrome? Philos. Trans. R. Soc. Lond. 360 2005 2355 2372
    • (2005) Philos. Trans. R. Soc. Lond. , vol.360 , pp. 2355-2372
    • Droge, W.1
  • 54
    • 0035499992 scopus 로고    scopus 로고
    • Augmented oxidative stress of platelets in chronic smokers: Mechanisms of impaired platelet-derived nitric oxide bioactivity and augmented platelet aggregability
    • Y. Takajo, H. Ikeda, N. Haramaki, T. Murohara, and T. Imaizumi Augmented oxidative stress of platelets in chronic smokers: mechanisms of impaired platelet-derived nitric oxide bioactivity and augmented platelet aggregability J. Am. Coll. Cardiol. 38 2001 1320 1327
    • (2001) J. Am. Coll. Cardiol. , vol.38 , pp. 1320-1327
    • Takajo, Y.1    Ikeda, H.2    Haramaki, N.3    Murohara, T.4    Imaizumi, T.5
  • 56
    • 0036967069 scopus 로고    scopus 로고
    • Smoking is associated with alterations of blood thiol-group related antioxidants in patients on hemodialysis
    • N.P. Wang, P.S. Lim, T.T. Chen, L.M. Thien, T.H. Wang, and W.M. Hsu Smoking is associated with alterations of blood thiol-group related antioxidants in patients on hemodialysis Nephron 92 2002 772 779
    • (2002) Nephron , vol.92 , pp. 772-779
    • Wang, N.P.1    Lim, P.S.2    Chen, T.T.3    Thien, L.M.4    Wang, T.H.5    Hsu, W.M.6
  • 57
    • 0037435609 scopus 로고    scopus 로고
    • Redox control of platelet aggregation
    • D.W. Essex, and M. Li Redox control of platelet aggregation Biochemistry 42 2003 129 136
    • (2003) Biochemistry , vol.42 , pp. 129-136
    • Essex, D.W.1    Li, M.2
  • 60
    • 56549113007 scopus 로고    scopus 로고
    • Clear differences in adiponectin level and glutathione redox status revealed in obese and normal-weight patients with psoriasis
    • S. Kaur, K. Zilmer, C. Kairane, M. Kals, and M. Zilmer Clear differences in adiponectin level and glutathione redox status revealed in obese and normal-weight patients with psoriasis Br. J. Dermatol. 159 2008 1364 1367
    • (2008) Br. J. Dermatol. , vol.159 , pp. 1364-1367
    • Kaur, S.1    Zilmer, K.2    Kairane, C.3    Kals, M.4    Zilmer, M.5
  • 61
    • 67649723393 scopus 로고    scopus 로고
    • The association of plasma cysteine and gamma-glutamyltransferase with BMI and obesity
    • A.K. Elshorbagy, H. Refsum, A.D. Smith, and I.M. Graham The association of plasma cysteine and gamma-glutamyltransferase with BMI and obesity Obes. Silver Spring 17 2009 1435 1440
    • (2009) Obes. Silver Spring , vol.17 , pp. 1435-1440
    • Elshorbagy, A.K.1    Refsum, H.2    Smith, A.D.3    Graham, I.M.4
  • 64
    • 10044283232 scopus 로고    scopus 로고
    • Adherence to the traditional Mediterranean diet is inversely associated with body mass index and obesity in a Spanish population
    • H. Schroder, J. Marrugat, J. Vila, M.I. Covas, and R. Elosua Adherence to the traditional Mediterranean diet is inversely associated with body mass index and obesity in a Spanish population J. Nutr. 134 2004 3355 3361
    • (2004) J. Nutr. , vol.134 , pp. 3355-3361
    • Schroder, H.1    Marrugat, J.2    Vila, J.3    Covas, M.I.4    Elosua, R.5
  • 65
    • 43449131541 scopus 로고    scopus 로고
    • Relation of plasma protein oxidation parameters and paraoxonase activity in the ageing population
    • U. Cakatay, R. Kayali, and H. Uzun Relation of plasma protein oxidation parameters and paraoxonase activity in the ageing population Clin. Exp. Med. 8 2008 51 57
    • (2008) Clin. Exp. Med. , vol.8 , pp. 51-57
    • Cakatay, U.1    Kayali, R.2    Uzun, H.3
  • 69
    • 79951492876 scopus 로고    scopus 로고
    • Reduced but not oxidized cerebrospinal fluid glutathione levels are lowered in Lewy body diseases
    • doi:10.1002/mds.23358
    • Maetzler, W.; Schmid, S. P.; Wurster, I.; Liepelt, I.; Gaenslen, A.; Gasser, T.; Berg, D. Reduced but not oxidized cerebrospinal fluid glutathione levels are lowered in Lewy body diseases. Mov. Disord. n/a. doi:10.1002/mds. 23358.
    • Mov. Disord. N/a
    • Maetzler, W.1    Schmid, S.P.2    Wurster, I.3    Liepelt, I.4    Gaenslen, A.5    Gasser, T.6    Berg, D.7
  • 70
    • 0033616356 scopus 로고    scopus 로고
    • Extracellular reduced glutathione increases neuronal vulnerability to combined chemical hypoxia and glucose deprivation
    • R.F. Regan, and Y. Guo Extracellular reduced glutathione increases neuronal vulnerability to combined chemical hypoxia and glucose deprivation Brain Res. 817 1999 145 150
    • (1999) Brain Res. , vol.817 , pp. 145-150
    • Regan, R.F.1    Guo, Y.2
  • 72
    • 0028864634 scopus 로고
    • Cerebrospinal fluid S-adenosylmethionine (SAMe) and glutathione concentrations in HIV infection: Effect of parenteral treatment with SAMe
    • A. Castagna, C. Le Grazie, A. Accordini, P. Giulidori, G. Cavalli, T. Bottiglieri, and A. Lazzarin Cerebrospinal fluid S-adenosylmethionine (SAMe) and glutathione concentrations in HIV infection: effect of parenteral treatment with SAMe Neurology 45 1995 1678 1683
    • (1995) Neurology , vol.45 , pp. 1678-1683
    • Castagna, A.1    Le Grazie, C.2    Accordini, A.3    Giulidori, P.4    Cavalli, G.5    Bottiglieri, T.6    Lazzarin, A.7
  • 73
    • 0037107162 scopus 로고    scopus 로고
    • Distribution of cystine/glutamate exchange transporter, system x(c)-, in the mouse brain
    • H. Sato, M. Tamba, S. Okuno, K. Sato, K. Keino-Masu, M. Masu, and S. Bannai Distribution of cystine/glutamate exchange transporter, system x(c)-, in the mouse brain J. Neurosci. 22 2002 8028 8033
    • (2002) J. Neurosci. , vol.22 , pp. 8028-8033
    • Sato, H.1    Tamba, M.2    Okuno, S.3    Sato, K.4    Keino-Masu, K.5    Masu, M.6    Bannai, S.7
  • 76
    • 0029991011 scopus 로고    scopus 로고
    • Plasma methionine and cysteine kinetics in response to an intravenous glutathione infusion in adult humans
    • N.K. Fukagawa, A.M. Ajami, and V.R. Young Plasma methionine and cysteine kinetics in response to an intravenous glutathione infusion in adult humans Am. J. Physiol. 270 1996 E209 E214
    • (1996) Am. J. Physiol. , vol.270
    • Fukagawa, N.K.1    Ajami, A.M.2    Young, V.R.3
  • 77
    • 0030743138 scopus 로고    scopus 로고
    • Effect of cystine intake on methionine kinetics and oxidation determined with oral tracers of methionine and cysteine in healthy adults
    • C.A. Raguso, A.M. Ajami, R. Gleason, and V.R. Young Effect of cystine intake on methionine kinetics and oxidation determined with oral tracers of methionine and cysteine in healthy adults Am. J. Clin. Nutr. 66 1997 283 292
    • (1997) Am. J. Clin. Nutr. , vol.66 , pp. 283-292
    • Raguso, C.A.1    Ajami, A.M.2    Gleason, R.3    Young, V.R.4
  • 78
    • 0033968481 scopus 로고    scopus 로고
    • Cysteine kinetics and oxidation at different intakes of methionine and cystine in young adults
    • C.A. Raguso, M.M. Regan, and V.R. Young Cysteine kinetics and oxidation at different intakes of methionine and cystine in young adults Am. J. Clin. Nutr. 71 2000 491 499
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 491-499
    • Raguso, C.A.1    Regan, M.M.2    Young, V.R.3
  • 79
    • 70349945220 scopus 로고    scopus 로고
    • Dietary sulfur amino acid effects on fasting plasma cysteine/cystine redox potential in humans
    • doi:10.1016/j.physletb.2003.10.071
    • Jones, D. P.; Park, Y.; Gletsu-Miller, N.; Liang, Y.; Yu, T.; Accardi, C. J.; Ziegler, T. R. Dietary sulfur amino acid effects on fasting plasma cysteine/cystine redox potential in humans. Nutrition. doi:10.1016/j.physletb. 2003.10.071.
    • Nutrition
    • Jones, D.P.1    Park, Y.2    Gletsu-Miller, N.3    Liang, Y.4    Yu, T.5    Accardi, C.J.6    Ziegler, T.R.7
  • 80
    • 0028143805 scopus 로고
    • Clearance of glutathione disulfide from rat mesenteric vasculature
    • L.J. Dahm, and D.P. Jones Clearance of glutathione disulfide from rat mesenteric vasculature Toxicol. Appl. Pharmacol. 129 1994 272 282
    • (1994) Toxicol. Appl. Pharmacol. , vol.129 , pp. 272-282
    • Dahm, L.J.1    Jones, D.P.2
  • 82
    • 77949747280 scopus 로고    scopus 로고
    • Postprandial cysteine/cystine redox potential in human plasma varies with meal content of sulfur amino acids
    • Y. Park, T.R. Ziegler, N. Gletsu-Miller, Y. Liang, T. Yu, C.J. Accardi, and D.P. Jones Postprandial cysteine/cystine redox potential in human plasma varies with meal content of sulfur amino acids J. Nutr. 140 2010 760 765
    • (2010) J. Nutr. , vol.140 , pp. 760-765
    • Park, Y.1    Ziegler, T.R.2    Gletsu-Miller, N.3    Liang, Y.4    Yu, T.5    Accardi, C.J.6    Jones, D.P.7
  • 84
    • 3142729014 scopus 로고    scopus 로고
    • Sulfur amino acid metabolism: Pathways for production and removal of homocysteine and cysteine
    • M.H. Stipanuk Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine Annu. Rev. Nutr. 24 2004 539 577
    • (2004) Annu. Rev. Nutr. , vol.24 , pp. 539-577
    • Stipanuk, M.H.1
  • 86
    • 0029257541 scopus 로고
    • Homocysteine species as components of plasma redox thiol status
    • P.M. Ueland Homocysteine species as components of plasma redox thiol status Clin. Chem. 41 1995 340 342
    • (1995) Clin. Chem. , vol.41 , pp. 340-342
    • Ueland, P.M.1
  • 89
    • 19244365393 scopus 로고    scopus 로고
    • Stress, protein (mis)folding, and signaling: The redox connection
    • R. Sitia, and S.N. Molteni Stress, protein (mis)folding, and signaling: the redox connection Sci. STKE 2004 2004 pe27
    • (2004) Sci. STKE , vol.2004 , pp. 27
    • Sitia, R.1    Molteni, S.N.2
  • 90
    • 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
  • 91
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • F.Q. Schafer, and G.R. Buettner Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radic. Biol. Med. 30 2001 1191 1212
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 92
    • 49349085256 scopus 로고    scopus 로고
    • Redox compartmentalization in eukaryotic cells
    • Y.M. Go, and D.P. Jones Redox compartmentalization in eukaryotic cells Biochim. Biophys. Acta 1780 2008 1273 1290
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1273-1290
    • Go, Y.M.1    Jones, D.P.2
  • 94
    • 39949085437 scopus 로고    scopus 로고
    • Nonequilibrium thermodynamics of thiol/disulfide redox systems: A perspective on redox systems biology
    • M. Kemp, Y.M. Go, and D.P. Jones Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology Free Radic. Biol. Med. 44 2008 921 937
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 921-937
    • Kemp, M.1    Go, Y.M.2    Jones, D.P.3
  • 96
    • 0027952488 scopus 로고
    • Changes in plasma glutathione concentrations, turnover, and disposal in developing rats
    • M. Ookhtens, A.V. Mittur, and N.A. Erhart Changes in plasma glutathione concentrations, turnover, and disposal in developing rats Am. J. Physiol. 266 1994 R979 R988
    • (1994) Am. J. Physiol. , vol.266
    • Ookhtens, M.1    Mittur, A.V.2    Erhart, N.A.3
  • 97
    • 33646807833 scopus 로고    scopus 로고
    • Mammalian cysteine metabolism: New insights into regulation of cysteine metabolism
    • M.H. Stipanuk, J.E. Dominy Jr., J.I. Lee, and R.M. Coloso Mammalian cysteine metabolism: new insights into regulation of cysteine metabolism J. Nutr. 136 2006 1652S 1659S
    • (2006) J. Nutr. , vol.136
    • Stipanuk, M.H.1    Dominy, Jr.J.E.2    Lee, J.I.3    Coloso, R.M.4
  • 99
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • D.P. Jones Radical-free biology of oxidative stress Am. J. Physiol. Cell Physiol. 295 2008 C849 C868
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Jones, D.P.1
  • 100
    • 3142685079 scopus 로고    scopus 로고
    • Extracellular thiols and thiol/disulfide redox in metabolism
    • S.E. Moriarty-Craige, and D.P. Jones Extracellular thiols and thiol/disulfide redox in metabolism Annu. Rev. Nutr. 24 2004 481 509
    • (2004) Annu. Rev. Nutr. , vol.24 , pp. 481-509
    • Moriarty-Craige, S.E.1    Jones, D.P.2
  • 101
    • 0029762379 scopus 로고    scopus 로고
    • Low plasma glutamine in combination with high glutamate levels indicate risk for loss of body cell mass in healthy individuals: The effect of N-acetyl-cysteine
    • R. Kinscherf, V. Hack, T. Fischbach, B. Friedmann, C. Weiss, L. Edler, P. Bartsch, and W. Droge Low plasma glutamine in combination with high glutamate levels indicate risk for loss of body cell mass in healthy individuals: the effect of N-acetyl-cysteine J. Mol. Med. (Berlin) 74 1996 393 400
    • (1996) J. Mol. Med. (Berlin) , vol.74 , pp. 393-400
    • Kinscherf, R.1    Hack, V.2    Fischbach, T.3    Friedmann, B.4    Weiss, C.5    Edler, L.6    Bartsch, P.7    Droge, W.8
  • 103
    • 38949103453 scopus 로고    scopus 로고
    • Aberrant insulin receptor signaling and amino acid homeostasis as a major cause of oxidative stress in aging
    • W. Droge, and R. Kinscherf Aberrant insulin receptor signaling and amino acid homeostasis as a major cause of oxidative stress in aging Antioxid. Redox Signaling 10 2008 661 678
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 661-678
    • Droge, W.1    Kinscherf, R.2
  • 104
    • 0017339770 scopus 로고
    • Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue
    • J. Isaacs, and F. Binkley Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue Biochim. Biophys. Acta 497 1977 192 204
    • (1977) Biochim. Biophys. Acta , vol.497 , pp. 192-204
    • Isaacs, J.1    Binkley, F.2
  • 105
    • 0021866476 scopus 로고
    • Diurnal fluctuation and pharmacological alteration of mouse organ glutathione content
    • H. Jaeschke, and A. Wendel Diurnal fluctuation and pharmacological alteration of mouse organ glutathione content Biochem. Pharmacol. 34 1985 1029 1033
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1029-1033
    • Jaeschke, H.1    Wendel, A.2
  • 106
    • 77956242964 scopus 로고    scopus 로고
    • Vascular oxidative stress and inflammation increase with age: Ameliorating effects of alpha-lipoic acid supplementation
    • L. Li, A. Smith, T.M. Hagen, and B. Frei Vascular oxidative stress and inflammation increase with age: ameliorating effects of alpha-lipoic acid supplementation Ann. NY Acad. Sci. 1203 2010 151 159
    • (2010) Ann. NY Acad. Sci. , vol.1203 , pp. 151-159
    • Li, L.1    Smith, A.2    Hagen, T.M.3    Frei, B.4
  • 108
    • 0000208163 scopus 로고
    • The identity of diaphorase and lipoyl dehydrogenase
    • V. Massey The identity of diaphorase and lipoyl dehydrogenase Biochim. Biophys. Acta 37 1960 314 322
    • (1960) Biochim. Biophys. Acta , vol.37 , pp. 314-322
    • Massey, V.1
  • 109
    • 1542723493 scopus 로고    scopus 로고
    • Decline in transcriptional activity of Nrf2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid
    • J.H. Suh, S.V. Shenvi, B.M. Dixon, H. Liu, A.K. Jaiswal, R.M. Liu, and T.M. Hagen Decline in transcriptional activity of Nrf2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid Proc. Natl Acad. Sci. USA 101 2004 3381 3386
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3381-3386
    • Suh, J.H.1    Shenvi, S.V.2    Dixon, B.M.3    Liu, H.4    Jaiswal, A.K.5    Liu, R.M.6    Hagen, T.M.7
  • 111
    • 32444450678 scopus 로고    scopus 로고
    • Zinc supplementation of young men alters metallothionein, zinc transporter, and cytokine gene expression in leukocyte populations
    • T.B. Aydemir, R.K. Blanchard, and R.J. Cousins Zinc supplementation of young men alters metallothionein, zinc transporter, and cytokine gene expression in leukocyte populations Proc. Natl Acad. Sci. USA 103 2006 1699 1704
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 1699-1704
    • Aydemir, T.B.1    Blanchard, R.K.2    Cousins, R.J.3
  • 112
    • 0034792801 scopus 로고    scopus 로고
    • Effects of intracellular zinc depletion on metallothionein and ZIP2 transporter expression and apoptosis
    • J. Cao, J.A. Bobo, J.P. Liuzzi, and R.J. Cousins Effects of intracellular zinc depletion on metallothionein and ZIP2 transporter expression and apoptosis J. Leukoc. Biol. 70 2001 559 566
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 559-566
    • Cao, J.1    Bobo, J.A.2    Liuzzi, J.P.3    Cousins, R.J.4
  • 113
    • 0025019792 scopus 로고
    • Erythrocyte metallothionein as an index of zinc status in humans
    • A. Grider, L.B. Bailey, and R.J. Cousins Erythrocyte metallothionein as an index of zinc status in humans Proc. Natl Acad. Sci. USA 87 1990 1259 1262
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1259-1262
    • Grider, A.1    Bailey, L.B.2    Cousins, R.J.3
  • 114
    • 0034058549 scopus 로고    scopus 로고
    • The function of zinc metallothionein: A link between cellular zinc and redox state
    • W. Maret The function of zinc metallothionein: a link between cellular zinc and redox state J. Nutr. 130 2000 1455S 1458S
    • (2000) J. Nutr. , vol.130
    • Maret, W.1
  • 115
    • 0032584078 scopus 로고    scopus 로고
    • The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase
    • L.J. Jiang, W. Maret, and B.L. Vallee The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase Proc. Natl Acad. Sci. USA 95 1998 3483 3488
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3483-3488
    • Jiang, L.J.1    Maret, W.2    Vallee, B.L.3
  • 116
    • 0022504716 scopus 로고
    • Purification and properties of the membranal thiol oxidase from porcine kidney
    • L.H. Lash, and D.P. Jones Purification and properties of the membranal thiol oxidase from porcine kidney Arch. Biochem. Biophys. 247 1986 120 130
    • (1986) Arch. Biochem. Biophys. , vol.247 , pp. 120-130
    • Lash, L.H.1    Jones, D.P.2
  • 117
    • 0026726571 scopus 로고
    • Expression of recombinant myeloperoxidase using a baculovirus expression system
    • K.L. Taylor, D.J. Uhlinger, and J.M. Kinkade Jr. Expression of recombinant myeloperoxidase using a baculovirus expression system Biochem. Biophys. Res. Commun. 187 1992 1572 1578
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1572-1578
    • Taylor, K.L.1    Uhlinger, D.J.2    Kinkade, Jr.J.M.3
  • 118
    • 35348921812 scopus 로고    scopus 로고
    • Extracellular cysteine/cystine redox potential controls lung fibroblast proliferation and matrix expression through upregulation of transforming growth factor-beta
    • A. Ramirez, B. Ramadan, J.D. Ritzenthaler, H.N. Rivera, D.P. Jones, and J. Roman Extracellular cysteine/cystine redox potential controls lung fibroblast proliferation and matrix expression through upregulation of transforming growth factor-beta Am. J. Physiol. Lung Cell. Mol. Physiol. 293 2007 L972 L981
    • (2007) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.293
    • Ramirez, A.1    Ramadan, B.2    Ritzenthaler, J.D.3    Rivera, H.N.4    Jones, D.P.5    Roman, J.6
  • 119
    • 77952356394 scopus 로고    scopus 로고
    • Oxidation of plasma cysteine/cystine and GSH/GSSG redox potentials by acetaminophen and sulfur amino acid insufficiency in humans
    • Y.O. Mannery, T.R. Ziegler, Y. Park, and D. Jones Oxidation of plasma cysteine/cystine and GSH/GSSG redox potentials by acetaminophen and sulfur amino acid insufficiency in humans J. Pharmacol. Exp. Ther. 333 2010 939 947
    • (2010) J. Pharmacol. Exp. Ther. , vol.333 , pp. 939-947
    • Mannery, Y.O.1    Ziegler, T.R.2    Park, Y.3    Jones, D.4
  • 122
    • 72249090399 scopus 로고    scopus 로고
    • Dietary sulfur amino acid supplementation reduces small bowel thiol/disulfide redox state and stimulates ileal mucosal growth after massive small bowel resection in rats
    • Y. Shyntum, S.S. Iyer, J. Tian, L. Hao, Y.O. Mannery, D.P. Jones, and T.R. Ziegler Dietary sulfur amino acid supplementation reduces small bowel thiol/disulfide redox state and stimulates ileal mucosal growth after massive small bowel resection in rats J. Nutr. 139 2009 2272 2278
    • (2009) J. Nutr. , vol.139 , pp. 2272-2278
    • Shyntum, Y.1    Iyer, S.S.2    Tian, J.3    Hao, L.4    Mannery, Y.O.5    Jones, D.P.6    Ziegler, T.R.7
  • 125
    • 0033597349 scopus 로고    scopus 로고
    • Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins
    • H. Sato, M. Tamba, T. Ishii, and S. Bannai Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins J. Biol. Chem. 274 1999 11455 11458
    • (1999) J. Biol. Chem. , vol.274 , pp. 11455-11458
    • Sato, H.1    Tamba, M.2    Ishii, T.3    Bannai, S.4
  • 126
    • 58149342069 scopus 로고    scopus 로고
    • Oxidation of plasma cysteine/cystine redox state in endotoxin-induced lung injury
    • S.S. Iyer, D.P. Jones, K.L. Brigham, and M. Rojas Oxidation of plasma cysteine/cystine redox state in endotoxin-induced lung injury Am. J. Respir. Cell Mol. Biol. 40 2009 90 98
    • (2009) Am. J. Respir. Cell Mol. Biol. , vol.40 , pp. 90-98
    • Iyer, S.S.1    Jones, D.P.2    Brigham, K.L.3    Rojas, M.4
  • 127
    • 78149282342 scopus 로고    scopus 로고
    • An oxidized extracellular oxidation-reduction state increases nox1 expression and proliferation in vascular smooth muscle cells via epidermal growth factor receptor activation
    • B. Stanic, M. Katsuyama, and F.J. Miller Jr. An oxidized extracellular oxidation-reduction state increases nox1 expression and proliferation in vascular smooth muscle cells via epidermal growth factor receptor activation Arterioscler. Thromb. Vasc. Biol. 30 2010 2234 2241
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 2234-2241
    • Stanic, B.1    Katsuyama, M.2    Miller, Jr.F.J.3
  • 129
    • 33749339309 scopus 로고    scopus 로고
    • Angiotensin II-mediated oxidative stress and procollagen-1 expression in cardiac fibroblasts: Blockade by pravastatin and pioglitazone
    • J. Chen, and J.L. Mehta Angiotensin II-mediated oxidative stress and procollagen-1 expression in cardiac fibroblasts: blockade by pravastatin and pioglitazone Am. J. Physiol. Heart Circ. Physiol. 291 2006 H1738 H1745
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.291
    • Chen, J.1    Mehta, J.L.2
  • 132
    • 26244432793 scopus 로고    scopus 로고
    • Proliferating fibroblasts at the invading tumour edge of colorectal adenocarcinomas are associated with endogenous markers of hypoxia, acidity, and oxidative stress
    • E. Sivridis, A. Giatromanolaki, and M.I. Koukourakis Proliferating fibroblasts at the invading tumour edge of colorectal adenocarcinomas are associated with endogenous markers of hypoxia, acidity, and oxidative stress J. Clin. Pathol. 58 2005 1033 1038
    • (2005) J. Clin. Pathol. , vol.58 , pp. 1033-1038
    • Sivridis, E.1    Giatromanolaki, A.2    Koukourakis, M.I.3
  • 133
    • 0033026854 scopus 로고    scopus 로고
    • Fibrous cap formation or destruction - The critical importance of vascular smooth muscle cell proliferation, migration and matrix formation
    • A.C. Newby, and A.B. Zaltsman Fibrous cap formation or destruction-the critical importance of vascular smooth muscle cell proliferation, migration and matrix formation Cardiovasc. Res. 41 1999 345 360
    • (1999) Cardiovasc. Res. , vol.41 , pp. 345-360
    • Newby, A.C.1    Zaltsman, A.B.2
  • 134
    • 65549143134 scopus 로고    scopus 로고
    • High dietary methionine plus cholesterol stimulates early atherosclerosis and late fibrous cap development which is associated with a decrease in GRP78 positive plaque cells
    • A. Zulli, and D.L. Hare High dietary methionine plus cholesterol stimulates early atherosclerosis and late fibrous cap development which is associated with a decrease in GRP78 positive plaque cells Int. J. Exp. Pathol. 90 2009 311 320
    • (2009) Int. J. Exp. Pathol. , vol.90 , pp. 311-320
    • Zulli, A.1    Hare, D.L.2
  • 135
    • 73149085941 scopus 로고    scopus 로고
    • Extracellular redox status regulates Nrf2 activation through mitochondrial reactive oxygen species
    • B.R. Imhoff, and J.M. Hansen Extracellular redox status regulates Nrf2 activation through mitochondrial reactive oxygen species Biochem. J. 424 2009 491 500
    • (2009) Biochem. J. , vol.424 , pp. 491-500
    • Imhoff, B.R.1    Hansen, J.M.2
  • 136
    • 0345530940 scopus 로고    scopus 로고
    • Thiols, malonaldehyde and total antioxidant status in the Turkish patients with type 2 diabetes mellitus
    • B.S. Duman, M. Ozturk, S. Yilmazeri, and H. Hatemi Thiols, malonaldehyde and total antioxidant status in the Turkish patients with type 2 diabetes mellitus Tohoku J. Exp. Med. 201 2003 147 155
    • (2003) Tohoku J. Exp. Med. , vol.201 , pp. 147-155
    • Duman, B.S.1    Ozturk, M.2    Yilmazeri, S.3    Hatemi, H.4


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