메뉴 건너뛰기




Volumn 1850, Issue 8, 2015, Pages 1527-1542

Glutathione during embryonic development

Author keywords

Cysteine; Development; Differentiation; Embryo; Glutathione; Redox potential

Indexed keywords

GLUTATHIONE; TRANSCRIPTION FACTOR;

EID: 84937771126     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.12.001     Document Type: Review
Times cited : (95)

References (168)
  • 1
    • 0037505644 scopus 로고    scopus 로고
    • Analysis of glutathione: Implication in redox and detoxification
    • A. Pastore, G. Federici, E. Bertini, and F. Piemonte Analysis of glutathione: implication in redox and detoxification Clin. Chim. Acta 333 2003 19 39
    • (2003) Clin. Chim. Acta , vol.333 , pp. 19-39
    • Pastore, A.1    Federici, G.2    Bertini, E.3    Piemonte, F.4
  • 2
    • 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
  • 3
    • 0033230043 scopus 로고    scopus 로고
    • Glutathione and its role in cellular functions
    • H. Sies Glutathione and its role in cellular functions Free Radic. Biol. Med. 27 1999 916 921
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 916-921
    • Sies, H.1
  • 4
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • C.E. Paulsen, and K.S. Carroll Orchestrating redox signaling networks through regulatory cysteine switches ACS Chem. Biol. 5 2009 47 62
    • (2009) ACS Chem. Biol. , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 5
    • 3042856307 scopus 로고    scopus 로고
    • Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal glutathione transferase 1
    • R. Svensson Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal glutathione transferase 1 Biochemistry (Easton) 43 2004 8869 8877
    • (2004) Biochemistry (Easton) , vol.43 , pp. 8869-8877
    • Svensson, R.1
  • 6
    • 0023092339 scopus 로고
    • Regulation of intracellular glutathione in rat embryos and visceral yolk sacs and its effect on 2-nitrosofluorene-induced malformations in the whole embryo culture system
    • C. Harris, M.J. Namkung, and M.R. Juchau Regulation of intracellular glutathione in rat embryos and visceral yolk sacs and its effect on 2-nitrosofluorene-induced malformations in the whole embryo culture system Toxicol. Appl. Pharmacol. 88 1987 141 152
    • (1987) Toxicol. Appl. Pharmacol. , vol.88 , pp. 141-152
    • Harris, C.1    Namkung, M.J.2    Juchau, M.R.3
  • 7
    • 0022928737 scopus 로고
    • Modulation of the embryotoxicity in vitro of reactive metabolites of 2-acetylaminofluorene by reduced glutathione and ascorbate and via sulfation
    • E.M. Faustman-Watts, M.J. Namkung, and M.R. Juchau Modulation of the embryotoxicity in vitro of reactive metabolites of 2-acetylaminofluorene by reduced glutathione and ascorbate and via sulfation Toxicol. Appl. Pharmacol. 86 1986 400 410
    • (1986) Toxicol. Appl. Pharmacol. , vol.86 , pp. 400-410
    • Faustman-Watts, E.M.1    Namkung, M.J.2    Juchau, M.R.3
  • 8
    • 0025963884 scopus 로고
    • Role of glutathione and hsp 70 in the acquisition of thermotolerance in postimplantation rat embryos
    • C. Harris, M.R. Juchau, and P.E. Mirkes Role of glutathione and hsp 70 in the acquisition of thermotolerance in postimplantation rat embryos Teratology 43 1991 229 239
    • (1991) Teratology , vol.43 , pp. 229-239
    • Harris, C.1    Juchau, M.R.2    Mirkes, P.E.3
  • 9
    • 0028464357 scopus 로고
    • Lindane embryotoxicity and differential alteration of cysteine and glutathione levels in rat embryos and visceral yolk sacs
    • T.L. McNutt, and C. Harris Lindane embryotoxicity and differential alteration of cysteine and glutathione levels in rat embryos and visceral yolk sacs Reprod. Toxicol. 8 1994 351 362
    • (1994) Reprod. Toxicol. , vol.8 , pp. 351-362
    • McNutt, T.L.1    Harris, C.2
  • 10
    • 0029610594 scopus 로고
    • Diamide-induced alterations of intracellular thiol status and the regulation of glucose metabolism in the developing rat conceptus in vitro
    • R. Hiranruengchok, and C. Harris Diamide-induced alterations of intracellular thiol status and the regulation of glucose metabolism in the developing rat conceptus in vitro Teratology 52 1995 205 214
    • (1995) Teratology , vol.52 , pp. 205-214
    • Hiranruengchok, R.1    Harris, C.2
  • 11
    • 0033226698 scopus 로고    scopus 로고
    • Differential alteration by thalidomide of the glutathione content of rat vs. Rabbit conceptuses in vitro
    • J.M. Hansen, E.W. Carney, and C. Harris Differential alteration by thalidomide of the glutathione content of rat vs. rabbit conceptuses in vitro Reprod. Toxicol. 13 1999 547 554
    • (1999) Reprod. Toxicol. , vol.13 , pp. 547-554
    • Hansen, J.M.1    Carney, E.W.2    Harris, C.3
  • 12
    • 0025832902 scopus 로고
    • The effect of in vivo glutathione depletion with buthionine sulfoximine on rat embryo development
    • B.F. Hales, and H. Brown The effect of in vivo glutathione depletion with buthionine sulfoximine on rat embryo development Teratology 44 1991 251 257
    • (1991) Teratology , vol.44 , pp. 251-257
    • Hales, B.F.1    Brown, H.2
  • 13
    • 0023219089 scopus 로고
    • Enhancement of the embryotoxicity of acrolein, but not phosphoramide mustard, by glutathione depletion in rat embryos in vitro
    • V.L. Slott, and B.F. Hales Enhancement of the embryotoxicity of acrolein, but not phosphoramide mustard, by glutathione depletion in rat embryos in vitro Biochem. Pharmacol. 36 1987 2019 2025
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 2019-2025
    • Slott, V.L.1    Hales, B.F.2
  • 14
    • 33847636101 scopus 로고    scopus 로고
    • Oxidative stress as a mechanism of teratogenesis
    • J.M. Hansen Oxidative stress as a mechanism of teratogenesis Birth Defects Res. C Embryo Today 78 2006 293 307
    • (2006) Birth Defects Res. C Embryo Today , vol.78 , pp. 293-307
    • Hansen, J.M.1
  • 15
    • 84871922476 scopus 로고    scopus 로고
    • Redox control of teratogenesis
    • J.M. Hansen, and C. Harris Redox control of teratogenesis Reprod. Toxicol. 35 2013 165 179
    • (2013) Reprod. Toxicol. , vol.35 , pp. 165-179
    • Hansen, J.M.1    Harris, C.2
  • 16
    • 84879492218 scopus 로고    scopus 로고
    • Inhibition of glutathione biosynthesis alters compartmental redox status and the thiol proteome in organogenesis-stage rat conceptuses
    • C. Harris, D.Z. Shuster, R. Roman Gomez, K.E. Sant, M.S. Reed, J. Pohl, and J.M. Hansen Inhibition of glutathione biosynthesis alters compartmental redox status and the thiol proteome in organogenesis-stage rat conceptuses Free Radic. Biol. Med. 63 2013 325 337
    • (2013) Free Radic. Biol. Med. , vol.63 , pp. 325-337
    • Harris, C.1    Shuster, D.Z.2    Roman Gomez, R.3    Sant, K.E.4    Reed, M.S.5    Pohl, J.6    Hansen, J.M.7
  • 17
    • 0003442818 scopus 로고    scopus 로고
    • 12th ed. Lippincott, Williams and Wilkins Baltimore, MD, USA
    • T. Sadler Langman's Medical Embryology 12th ed. 2012 Lippincott, Williams and Wilkins Baltimore, MD, USA
    • (2012) Langman's Medical Embryology
    • Sadler, T.1
  • 18
    • 4244124716 scopus 로고    scopus 로고
    • Nutrition of the human fetus during the first trimester - A review
    • G.J. Burton Nutrition of the human fetus during the first trimester - a review Placenta (Eastbourne) 22 Suppl. A 2001 S70 S77
    • (2001) Placenta (Eastbourne) , vol.22 , pp. S70-S77
    • Burton, G.J.1
  • 19
    • 0032034162 scopus 로고    scopus 로고
    • Quantitative studies on the mechanisms of amino acid supply to rat embryos during organogenesis
    • D.A. Beckman Quantitative studies on the mechanisms of amino acid supply to rat embryos during organogenesis Reprod. Toxicol. 12 1998 197 200
    • (1998) Reprod. Toxicol. , vol.12 , pp. 197-200
    • Beckman, D.A.1
  • 20
    • 5744247195 scopus 로고    scopus 로고
    • Spatial activities and induction of glutamate-cysteine ligase (GCL) in the postimplantation rat embryo and visceral yolk sac
    • J.M. Hansen, E. Lee, and C. Harris Spatial activities and induction of glutamate-cysteine ligase (GCL) in the postimplantation rat embryo and visceral yolk sac Toxicol. Sci. 81 2004 371 378
    • (2004) Toxicol. Sci. , vol.81 , pp. 371-378
    • Hansen, J.M.1    Lee, E.2    Harris, C.3
  • 21
    • 0027217661 scopus 로고
    • Glutathione biosynthesis in the postimplantation rat conceptus in vitro
    • C. Harris Glutathione biosynthesis in the postimplantation rat conceptus in vitro Toxicol. Appl. Pharmacol. 120 1993 247 256
    • (1993) Toxicol. Appl. Pharmacol. , vol.120 , pp. 247-256
    • Harris, C.1
  • 22
    • 0030912931 scopus 로고    scopus 로고
    • Depletion of glutathione during bovine oocyte maturation reversibly blocks the decondensation of the male pronucleus and pronuclear apposition during fertilization
    • P. Sutovsky, and G. Schatten Depletion of glutathione during bovine oocyte maturation reversibly blocks the decondensation of the male pronucleus and pronuclear apposition during fertilization Biol. Reprod. 56 1997 1503 1512
    • (1997) Biol. Reprod. , vol.56 , pp. 1503-1512
    • Sutovsky, P.1    Schatten, G.2
  • 23
    • 0027985632 scopus 로고
    • Status of glutathione during oxidant-induced oxidative stress in the preimplantation mouse embryo
    • C.S. Gardiner Status of glutathione during oxidant-induced oxidative stress in the preimplantation mouse embryo Biol. Reprod. 51 1994 1307 1314
    • (1994) Biol. Reprod. , vol.51 , pp. 1307-1314
    • Gardiner, C.S.1
  • 24
    • 84892441036 scopus 로고    scopus 로고
    • Inhibition of proteolysis in histiotrophic nutrition pathways alters DNA methylation and one-carbon metabolism in the organogenesis-stage rat conceptus
    • K.E. Sant, D.C. Dolinoy, M.S. Nahar, and C. Harris Inhibition of proteolysis in histiotrophic nutrition pathways alters DNA methylation and one-carbon metabolism in the organogenesis-stage rat conceptus J. Nutr. Biochem. 24 2013 1479 1487
    • (2013) J. Nutr. Biochem. , vol.24 , pp. 1479-1487
    • Sant, K.E.1    Dolinoy, D.C.2    Nahar, M.S.3    Harris, C.4
  • 25
    • 34247368534 scopus 로고    scopus 로고
    • Epigenetics in development
    • J.C. Kiefer Epigenetics in development Dev. Dyn. 236 2007 1144 1156
    • (2007) Dev. Dyn. , vol.236 , pp. 1144-1156
    • Kiefer, J.C.1
  • 26
    • 84887142536 scopus 로고    scopus 로고
    • The imprinted polycomb group gene Sfmbt2 is required for trophoblast maintenance and placenta development
    • K. Miri The imprinted polycomb group gene Sfmbt2 is required for trophoblast maintenance and placenta development Development (Cambridge) 140 2013 4480 4489
    • (2013) Development (Cambridge) , vol.140 , pp. 4480-4489
    • Miri, K.1
  • 27
    • 3342893136 scopus 로고    scopus 로고
    • Glutathione depletion modulates methanol, formaldehyde and formate toxicity in cultured rat conceptuses
    • C. Harris, M. Dixon, and J.M. Hansen Glutathione depletion modulates methanol, formaldehyde and formate toxicity in cultured rat conceptuses Cell Biol. Toxicol. 20 2004 133 145
    • (2004) Cell Biol. Toxicol. , vol.20 , pp. 133-145
    • Harris, C.1    Dixon, M.2    Hansen, J.M.3
  • 28
    • 0022900749 scopus 로고
    • Differential glutathione depletion by L-buthionine-S, R-sulfoximine in rat embryo versus visceral yolk sac in vivo and in vitro
    • C. Harris, A.G. Fantel, and M.R. Juchau Differential glutathione depletion by L-buthionine-S, R-sulfoximine in rat embryo versus visceral yolk sac in vivo and in vitro Biochem. Pharmacol. 35 1986 4437 4441
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 4437-4441
    • Harris, C.1    Fantel, A.G.2    Juchau, M.R.3
  • 29
    • 0028826242 scopus 로고
    • Glutathione status in chemical embryotoxicity: Synthesis, turnover and adduct formation
    • C. Harris, R. Hiranruengchok, E. Lee, R.M. Berberian, and G.E. Eurich Glutathione status in chemical embryotoxicity: synthesis, turnover and adduct formation Toxicol. in Vitro 9 1995 623 631
    • (1995) Toxicol. in Vitro , vol.9 , pp. 623-631
    • Harris, C.1    Hiranruengchok, R.2    Lee, E.3    Berberian, R.M.4    Eurich, G.E.5
  • 30
    • 33751197937 scopus 로고    scopus 로고
    • Depletion of glutathione induces 4-hydroxynonenal protein adducts and hydroxyurea teratogenicity in the organogenesis stage mouse embryo
    • J. Yan Depletion of glutathione induces 4-hydroxynonenal protein adducts and hydroxyurea teratogenicity in the organogenesis stage mouse embryo J. Pharmacol. Exp. Ther. 319 2006 613 621
    • (2006) J. Pharmacol. Exp. Ther. , vol.319 , pp. 613-621
    • Yan, J.1
  • 31
    • 84872527110 scopus 로고    scopus 로고
    • Glutathione-deficient mice have increased sensitivity to transplacental benzo[a]pyrene-induced premature ovarian failure and ovarian tumorigenesis
    • J. Lim Glutathione-deficient mice have increased sensitivity to transplacental benzo[a]pyrene-induced premature ovarian failure and ovarian tumorigenesis Cancer research (Chicago, Ill.) 73 2013 908 917
    • (2013) Cancer Research (Chicago, Ill.) , vol.73 , pp. 908-917
    • Lim, J.1
  • 32
    • 0024535595 scopus 로고
    • Modulation of the embryotoxicity and cytotoxicity elicited by 7-hydroxy-2-acetylaminofluorene and acetaminophen via deacetylation
    • K.L. Stark, C. Harris, and M.R. Juchau Modulation of the embryotoxicity and cytotoxicity elicited by 7-hydroxy-2-acetylaminofluorene and acetaminophen via deacetylation Toxicol. Appl. Pharmacol. 97 1989 548 560
    • (1989) Toxicol. Appl. Pharmacol. , vol.97 , pp. 548-560
    • Stark, K.L.1    Harris, C.2    Juchau, M.R.3
  • 33
    • 0025977816 scopus 로고
    • Morphological differences elicited by two weak acids, retinoic and valproic, in rat embryos grown in vitro
    • R.E. Seegmiller Morphological differences elicited by two weak acids, retinoic and valproic, in rat embryos grown in vitro Teratology (Philadelphia) 43 1991 133 150
    • (1991) Teratology (Philadelphia) , vol.43 , pp. 133-150
    • Seegmiller, R.E.1
  • 34
    • 81555195488 scopus 로고    scopus 로고
    • Valproic acid increases formation of reactive oxygen species and induces apoptosis in postimplantation embryos: A role for oxidative stress in valproic acid-induced neural tube defects
    • E.W.Y. Tung, and L.M. Winn Valproic acid increases formation of reactive oxygen species and induces apoptosis in postimplantation embryos: a role for oxidative stress in valproic acid-induced neural tube defects Mol. Pharmacol. 80 2011 979 987
    • (2011) Mol. Pharmacol. , vol.80 , pp. 979-987
    • Tung, E.W.Y.1    Winn, L.M.2
  • 35
    • 0031974132 scopus 로고    scopus 로고
    • Inhibition of embryonic retinoic acid synthesis by aldehydes of lipid peroxidation and prevention of inhibition by reduced glutathione and glutathione S-transferases
    • H. Chen Inhibition of embryonic retinoic acid synthesis by aldehydes of lipid peroxidation and prevention of inhibition by reduced glutathione and glutathione S-transferases Free Radic. Biol. Med. 24 1998 408 417
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 408-417
    • Chen, H.1
  • 36
    • 0347320849 scopus 로고    scopus 로고
    • A novel hypothesis for thalidomide-induced limb teratogenesis: Redox misregulation of the NF-kappaB pathway
    • J.M. Hansen A novel hypothesis for thalidomide-induced limb teratogenesis: redox misregulation of the NF-kappaB pathway Antioxid. Redox Signal. 6 2004 1 14
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 1-14
    • Hansen, J.M.1
  • 37
    • 0028464357 scopus 로고
    • Lindane embryotoxicity and differential alteration of cysteine and glutathione levels in rat embryos and visceral yolk sacs
    • T.L. McNutt, and C. Harris Lindane embryotoxicity and differential alteration of cysteine and glutathione levels in rat embryos and visceral yolk sacs Reprod. Toxicol. 8 1994 351 362
    • (1994) Reprod. Toxicol. , vol.8 , pp. 351-362
    • McNutt, T.L.1    Harris, C.2
  • 38
    • 33750063190 scopus 로고    scopus 로고
    • Increased susceptibility to phenytoin teratogenicity: Excessive generation of reactive oxygen species or impaired antioxidant defense?
    • F. Azarbayjani, L.A.H. Borg, and B.R. Danielsson Increased susceptibility to phenytoin teratogenicity: excessive generation of reactive oxygen species or impaired antioxidant defense? Basic Clin. Pharmacol. Toxicol. 99 2006 305 311
    • (2006) Basic Clin. Pharmacol. Toxicol. , vol.99 , pp. 305-311
    • Azarbayjani, F.1    Borg, L.A.H.2    Danielsson, B.R.3
  • 39
    • 0032566524 scopus 로고    scopus 로고
    • Free radical intermediates of phenytoin and related teratogens: Prostaglandin h synthase-catalyzed bioactivation, electron paramagnetic resonance spectrometry, and photochemical product analysis
    • T. Parman, G. Chen, and P.G. Wells Free radical intermediates of phenytoin and related teratogens: prostaglandin h synthase-catalyzed bioactivation, electron paramagnetic resonance spectrometry, and photochemical product analysis J. Biol. Chem. 273 1998 25079 25088
    • (1998) J. Biol. Chem. , vol.273 , pp. 25079-25088
    • Parman, T.1    Chen, G.2    Wells, P.G.3
  • 40
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • K.G. Reddie, and K.S. Carroll Expanding the functional diversity of proteins through cysteine oxidation Curr. Opin. Chem. Biol. 12 2008 746 754
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 41
    • 84904722403 scopus 로고    scopus 로고
    • Redox regulation by glutathione needs enzymes
    • C. Berndt, C.H. Lillig, and L. Flohe Redox regulation by glutathione needs enzymes Front. Pharmacol. 5 2014 168
    • (2014) Front. Pharmacol. , vol.5 , pp. 168
    • Berndt, C.1    Lillig, C.H.2    Flohe, L.3
  • 42
    • 84866486549 scopus 로고    scopus 로고
    • Oxidative stress, thiols, and redox profiles
    • C. Harris Oxidative stress, thiols, and redox profiles Methods Mol. Biol. 889 2012 325 346
    • (2012) Methods Mol. Biol. , vol.889 , pp. 325-346
    • Harris, C.1
  • 43
    • 0034963198 scopus 로고    scopus 로고
    • Spatial glutathione and cysteine distribution and chemical modulation in the early organogenesis-stage rat conceptus in utero
    • M.J. Beck, C. McLellan, R.L.-F. Lightle, M.A. Philbert, and C. Harris Spatial glutathione and cysteine distribution and chemical modulation in the early organogenesis-stage rat conceptus in utero Toxicol. Sci. 62 2001 92 102
    • (2001) Toxicol. Sci. , vol.62 , pp. 92-102
    • Beck, M.J.1    McLellan, C.2    Lightle, R.L.-F.3    Philbert, M.A.4    Harris, C.5
  • 44
    • 0036175546 scopus 로고    scopus 로고
    • Thalidomide modulates nuclear redox status and preferentially depletes glutathione in rabbit limb versus rat limb
    • J.M. Hansen, K.K. Harris, M.A. Philbert, and C. Harris Thalidomide modulates nuclear redox status and preferentially depletes glutathione in rabbit limb versus rat limb J. Pharmacol. Exp. Ther. 300 2002 768 776
    • (2002) J. Pharmacol. Exp. Ther. , vol.300 , pp. 768-776
    • Hansen, J.M.1    Harris, K.K.2    Philbert, M.A.3    Harris, C.4
  • 45
    • 0035873918 scopus 로고    scopus 로고
    • Differential antioxidant enzyme activities and glutathione content between rat and rabbit conceptuses
    • J.M. Hansen, H.-S. Choe, E.W. Carney, and C. Harris Differential antioxidant enzyme activities and glutathione content between rat and rabbit conceptuses Free Radic. Biol. Med. 30 2001 1078 1088
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1078-1088
    • Hansen, J.M.1    Choe, H.-S.2    Carney, E.W.3    Harris, C.4
  • 46
    • 0029850363 scopus 로고    scopus 로고
    • Sources of amino acids for protein synthesis during earlyorganogenesis in the rat. 4. Mechanisms before envelopment of the embryo by the yolk sac
    • D.A. Beckman, R.L. Brent, and J.B. Lloyd Sources of amino acids for protein synthesis during earlyorganogenesis in the rat. 4. Mechanisms before envelopment of the embryo by the yolk sac Placenta 17 1996 635 641
    • (1996) Placenta , vol.17 , pp. 635-641
    • Beckman, D.A.1    Brent, R.L.2    Lloyd, J.B.3
  • 47
    • 0030985171 scopus 로고    scopus 로고
    • Investigations into mechanisms of amino acid supply to the rat embryo using whole-embryo culture
    • D.A. Beckman Investigations into mechanisms of amino acid supply to the rat embryo using whole-embryo culture Int. J. Dev. Biol. 41 1997 315 318
    • (1997) Int. J. Dev. Biol. , vol.41 , pp. 315-318
    • Beckman, D.A.1
  • 48
    • 0026090201 scopus 로고
    • Sources of amino acids for protein synthesis during early organogenesis in the rat. 2. Exchange with amino acid and protein pools in embryo and yolk sac
    • D.A. Beckman, J.E. Pugarelli, T.R. Koszalka, R.L. Brent, and J.B. Lloyd Sources of amino acids for protein synthesis during early organogenesis in the rat. 2. Exchange with amino acid and protein pools in embryo and yolk sac Placenta 12 1991 37 46
    • (1991) Placenta , vol.12 , pp. 37-46
    • Beckman, D.A.1    Pugarelli, J.E.2    Koszalka, T.R.3    Brent, R.L.4    Lloyd, J.B.5
  • 49
    • 0025000359 scopus 로고
    • Methionine and neural tube closure in cultured rat embryos: Morphological and biochemical analyses
    • C.N. Coelho Methionine and neural tube closure in cultured rat embryos: morphological and biochemical analyses Teratology (Philadelphia) 42 1990 437 451
    • (1990) Teratology (Philadelphia) , vol.42 , pp. 437-451
    • Coelho, C.N.1
  • 50
    • 0026492351 scopus 로고
    • Methionine decreases the embryotoxicity of sodium valproate in the rat: In vivo and in vitro observations
    • P.G. Nosel Methionine decreases the embryotoxicity of sodium valproate in the rat: in vivo and in vitro observations Teratology (Philadelphia) 46 1992 499 507
    • (1992) Teratology (Philadelphia) , vol.46 , pp. 499-507
    • Nosel, P.G.1
  • 51
    • 0021240616 scopus 로고
    • Glutathione depletion and susceptibility
    • D.J. Reed Glutathione depletion and susceptibility Pharmacol. Rev. 36 1984 25S 33S
    • (1984) Pharmacol. Rev. , vol.36 , pp. 25S-33S
    • Reed, D.J.1
  • 52
    • 3142758491 scopus 로고    scopus 로고
    • Murine cystathionine gamma-lyase: Complete cDNA and genomic sequences, promoter activity, tissue distribution and developmental expression
    • I. Ishii Murine cystathionine gamma-lyase: complete cDNA and genomic sequences, promoter activity, tissue distribution and developmental expression Biochem. J. 381 2004 113 123
    • (2004) Biochem. J. , vol.381 , pp. 113-123
    • Ishii, I.1
  • 53
    • 0018168953 scopus 로고
    • Evidence that the gamma-glutamyl cycle functions in vivo using intracellular glutathione: Effects of amino acids and selective inhibition of enzymes
    • O.W. Griffith, R.J. Bridges, and A. Meister Evidence that the gamma-glutamyl cycle functions in vivo using intracellular glutathione: effects of amino acids and selective inhibition of enzymes Proc. Natl. Acad. Sci. U. S. A. 75 1978 5405 5408
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 5405-5408
    • Griffith, O.W.1    Bridges, R.J.2    Meister, A.3
  • 54
    • 0014876254 scopus 로고
    • The gamma-glutamyl cycle: A possible transport system for amino acids
    • M. Orlowski, and A. Meister The gamma-glutamyl cycle: a possible transport system for amino acids Proc. Natl. Acad. Sci. U. S. A. 67 1970 1248 1255
    • (1970) Proc. Natl. Acad. Sci. U. S. A. , vol.67 , pp. 1248-1255
    • Orlowski, M.1    Meister, A.2
  • 55
    • 0016635533 scopus 로고
    • Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione
    • P.G. Richman, and A. Meister Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione J. Biol. Chem. 250 1975 1422 1426
    • (1975) J. Biol. Chem. , vol.250 , pp. 1422-1426
    • Richman, P.G.1    Meister, A.2
  • 56
    • 3042802690 scopus 로고    scopus 로고
    • Glutathione: An overview of biosynthesis and modulation
    • M.E. Anderson Glutathione: an overview of biosynthesis and modulation Chem. Biol. Interact. 111-112 1998 1 14
    • (1998) Chem. Biol. Interact. , vol.111-112 , pp. 1-14
    • Anderson, M.E.1
  • 57
    • 0021848738 scopus 로고
    • Histochemical demonstration of exopeptidases in the rat visceral yolk-sac epithelium
    • P. Kugler Histochemical demonstration of exopeptidases in the rat visceral yolk-sac epithelium Histochemistry (Berlin) 82 1985 397 400
    • (1985) Histochemistry (Berlin) , vol.82 , pp. 397-400
    • Kugler, P.1
  • 58
    • 0021747221 scopus 로고
    • Comparative enzyme histochemical study on the visceral yolk sac endoderm in the rat in vivo and in vitro
    • A. Miki Comparative enzyme histochemical study on the visceral yolk sac endoderm in the rat in vivo and in vitro Histochemistry (Berlin) 81 1984 409 415
    • (1984) Histochemistry (Berlin) , vol.81 , pp. 409-415
    • Miki, A.1
  • 59
    • 0018635521 scopus 로고
    • A sensitive fluorimetric assay for γ-glutamyl transferase
    • G.D. Smith, J.L. Ding, and T.J. Peters A sensitive fluorimetric assay for γ-glutamyl transferase Anal. Biochem. 100 1979 136 139
    • (1979) Anal. Biochem. , vol.100 , pp. 136-139
    • Smith, G.D.1    Ding, J.L.2    Peters, T.J.3
  • 60
    • 0023220529 scopus 로고
    • Embryotoxicity elicited by inhibition of γ-glutamyltransferase by Acivicin and transferase antibodies in cultured rat embryos
    • K.L. Stark, C. Harris, and M.R. Juchau Embryotoxicity elicited by inhibition of γ-glutamyltransferase by Acivicin and transferase antibodies in cultured rat embryos Toxicol. Appl. Pharmacol. 89 1987 88 96
    • (1987) Toxicol. Appl. Pharmacol. , vol.89 , pp. 88-96
    • Stark, K.L.1    Harris, C.2    Juchau, M.R.3
  • 61
    • 0036190830 scopus 로고    scopus 로고
    • Promoting effect of β-mercaptoethanol on in vitro development under oxidative stress and cystine uptake of bovine embryos
    • M. Takahashi, T. Nagai, N. Okamura, H. Takahashi, and A. Okano Promoting effect of β-mercaptoethanol on in vitro development under oxidative stress and cystine uptake of bovine embryos Biol. Reprod. 66 2002 562 567
    • (2002) Biol. Reprod. , vol.66 , pp. 562-567
    • Takahashi, M.1    Nagai, T.2    Okamura, N.3    Takahashi, H.4    Okano, A.5
  • 62
    • 0015181434 scopus 로고
    • Uptake and incorporation of amino acids by the preimplantation mouse embryo
    • R.L. Brinster Uptake and incorporation of amino acids by the preimplantation mouse embryo J. Reprod. Fertil. 27 1971 329 338
    • (1971) J. Reprod. Fertil. , vol.27 , pp. 329-338
    • Brinster, R.L.1
  • 63
    • 0025319947 scopus 로고
    • L-2-Oxothiazolidine-4-carboxylate as a cysteine precursor: Efficacy for growth and hepatic glutathione synthesis in chicks and rats
    • T.K. Chung, M.A. Funk, and D.H. Baker L-2-Oxothiazolidine-4-carboxylate as a cysteine precursor: efficacy for growth and hepatic glutathione synthesis in chicks and rats J. Nutr. 120 1990 158 165
    • (1990) J. Nutr. , vol.120 , pp. 158-165
    • Chung, T.K.1    Funk, M.A.2    Baker, D.H.3
  • 64
    • 84875737737 scopus 로고    scopus 로고
    • Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes
    • M. Deponte Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes Biochim. Biophys. Acta Gen. Subj. 1830 2013 3217 3266
    • (2013) Biochim. Biophys. Acta Gen. Subj. , vol.1830 , pp. 3217-3266
    • Deponte, M.1
  • 65
    • 0029085193 scopus 로고
    • Glutathione redox cycle-driven recovery of reduced glutathione after oxidation by tertiary-butyl hydroperoxide in preimplantation mouse embryos
    • C.S. Gardiner, and D.J. Reed Glutathione redox cycle-driven recovery of reduced glutathione after oxidation by tertiary-butyl hydroperoxide in preimplantation mouse embryos Arch. Biochem. Biophys. 321 1995 6 12
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 6-12
    • Gardiner, C.S.1    Reed, D.J.2
  • 66
    • 33847359190 scopus 로고    scopus 로고
    • Regulation of redox metabolism in the mouse oocyte and embryo
    • R. Dumollard, Z. Ward, J. Carroll, and M.R. Duchen Regulation of redox metabolism in the mouse oocyte and embryo Development 134 2007 455 465
    • (2007) Development , vol.134 , pp. 455-465
    • Dumollard, R.1    Ward, Z.2    Carroll, J.3    Duchen, M.R.4
  • 67
    • 24644500066 scopus 로고    scopus 로고
    • The role of glutathione in mammalian gametes
    • Z. Luberda The role of glutathione in mammalian gametes Reprod. Biol. 5 2005 5 17
    • (2005) Reprod. Biol. , vol.5 , pp. 5-17
    • Luberda, Z.1
  • 68
    • 0344035676 scopus 로고    scopus 로고
    • Expression of genes encoding antioxidant enzymes in human and mouse oocytes during the final stages of maturation
    • S. El Mouatassim, P. Guérin, and Y. Ménézo Expression of genes encoding antioxidant enzymes in human and mouse oocytes during the final stages of maturation Mol. Hum. Reprod. 5 1999 720 725
    • (1999) Mol. Hum. Reprod. , vol.5 , pp. 720-725
    • El Mouatassim, S.1    Guérin, P.2    Ménézo, Y.3
  • 69
    • 0026545746 scopus 로고
    • Quantitative analysis of cellular glutathione in early preimplantation mouse embryos developing in vivo and in vitro
    • M.H. Nasr-Esfahani, and M.H. Johnson Quantitative analysis of cellular glutathione in early preimplantation mouse embryos developing in vivo and in vitro Hum. Reprod. 7 1992 1281 1290
    • (1992) Hum. Reprod. , vol.7 , pp. 1281-1290
    • Nasr-Esfahani, M.H.1    Johnson, M.H.2
  • 70
    • 0027214944 scopus 로고
    • Glutathione oxidation and embryotoxicity elicited by diamide in the developing rat conceptus in vitro
    • R. Hiranruengchok, and C. Harris Glutathione oxidation and embryotoxicity elicited by diamide in the developing rat conceptus in vitro Toxicol. Appl. Pharmacol. 120 1993 62 71
    • (1993) Toxicol. Appl. Pharmacol. , vol.120 , pp. 62-71
    • Hiranruengchok, R.1    Harris, C.2
  • 71
    • 0034906381 scopus 로고    scopus 로고
    • Spatial and temporal ontogenies of glutathione peroxidase and glutathione disulfide reductase during development of the prenatal rat
    • H. Choe, J.M. Hansen, and C. Harris Spatial and temporal ontogenies of glutathione peroxidase and glutathione disulfide reductase during development of the prenatal rat J. Biochem. Mol. Toxicol. 15 2001 197 206
    • (2001) J. Biochem. Mol. Toxicol. , vol.15 , pp. 197-206
    • Choe, H.1    Hansen, J.M.2    Harris, C.3
  • 72
    • 0024319288 scopus 로고
    • Modulation of embryonic glutathione reductase and phenytoin teratogenicity by 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU)
    • M. Wong, and P.G. Wells Modulation of embryonic glutathione reductase and phenytoin teratogenicity by 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) J. Pharmacol. Exp. Ther. 250 1989 336 342
    • (1989) J. Pharmacol. Exp. Ther. , vol.250 , pp. 336-342
    • Wong, M.1    Wells, P.G.2
  • 73
    • 0033160256 scopus 로고    scopus 로고
    • Tissue-specific changes in the activities of antioxidant enzymes during the development of the chicken embryo
    • P.F. Surai Tissue-specific changes in the activities of antioxidant enzymes during the development of the chicken embryo Br. Poult. Sci. 40 1999 397 405
    • (1999) Br. Poult. Sci. , vol.40 , pp. 397-405
    • Surai, P.F.1
  • 74
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • A. Holmgren Antioxidant function of thioredoxin and glutaredoxin systems Antioxid. Redox Signal. 2 2000 811 820
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 811-820
    • Holmgren, A.1
  • 75
    • 34548844721 scopus 로고    scopus 로고
    • Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia
    • Y.S. Ho, Y. Xiong, D.S. Ho, J. Gao, B.H. Chua, H. Pai, and J.J. Mieyal Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia Free Radic. Biol. Med. 43 2007 1299 1312
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1299-1312
    • Ho, Y.S.1    Xiong, Y.2    Ho, D.S.3    Gao, J.4    Chua, B.H.5    Pai, H.6    Mieyal, J.J.7
  • 76
    • 0034527829 scopus 로고    scopus 로고
    • Immunohistochemical localization of thioredoxin and glutaredoxin in mouse embryos and fetuses
    • M. Kobayashi, H. Nakamura, J. Yodoi, and K. Shiota Immunohistochemical localization of thioredoxin and glutaredoxin in mouse embryos and fetuses Antioxid. Redox Signal. 2 2000 653 663
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 653-663
    • Kobayashi, M.1    Nakamura, H.2    Yodoi, J.3    Shiota, K.4
  • 78
    • 84899794323 scopus 로고    scopus 로고
    • Zebrafish heart development is regulated via glutaredoxin 2 dependent migration and survival of neural crest cells
    • C. Berndt, G. Poschmann, K. Stuhler, A. Holmgren, and L. Brautigam Zebrafish heart development is regulated via glutaredoxin 2 dependent migration and survival of neural crest cells Redox Biol. 2 2014 673 678
    • (2014) Redox Biol. , vol.2 , pp. 673-678
    • Berndt, C.1    Poschmann, G.2    Stuhler, K.3    Holmgren, A.4    Brautigam, L.5
  • 80
    • 0016275313 scopus 로고
    • Glutathione S-transferases: The first enzymatic step in mercapturic acid formation
    • W.H. Habig, M.J. Pabst, and W.B. Jakoby Glutathione S-transferases: the first enzymatic step in mercapturic acid formation J. Biol. Chem. 249 1974 7130 7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 81
    • 34249809418 scopus 로고    scopus 로고
    • Beneficial effects of dithiothreitol on relative levels of glutathione S-transferase activity and thiols in oocytes, and cell number, DNA fragmentation and allocation at the blastocyst stage in the mouse
    • F. Rausell, J.F. Pertusa, V. Gómez-Piquer, C. Hermenegildo, M.A. García-Pérez, A. Cano, and J.J. Tarín Beneficial effects of dithiothreitol on relative levels of glutathione S-transferase activity and thiols in oocytes, and cell number, DNA fragmentation and allocation at the blastocyst stage in the mouse Mol. Reprod. Dev. 74 2007 860 869
    • (2007) Mol. Reprod. Dev. , vol.74 , pp. 860-869
    • Rausell, F.1    Pertusa, J.F.2    Gómez-Piquer, V.3    Hermenegildo, C.4    García-Pérez, M.A.5    Cano, A.6    Tarín, J.J.7
  • 82
    • 0037353915 scopus 로고    scopus 로고
    • Polychlorinated biphenyls affect gene expression in the rabbit preimplantation embryo
    • S. Kietz Polychlorinated biphenyls affect gene expression in the rabbit preimplantation embryo Mol. Reprod. Dev. 64 2003 251 260
    • (2003) Mol. Reprod. Dev. , vol.64 , pp. 251-260
    • Kietz, S.1
  • 83
    • 84953737134 scopus 로고    scopus 로고
    • Transcriptional profiles of glutathione-S-transferase isoforms, Cyp, and AOE genes in atrazine-exposed zebrafish embryos
    • (Epub ahead of print)
    • B. Glisic, J. Hrubik, S. Fa, N. Dopudj, R. Kovacevic, and N. Andric Transcriptional profiles of glutathione-S-transferase isoforms, Cyp, and AOE genes in atrazine-exposed zebrafish embryos Environ. Toxicol. 2014 10.1002/tox.22038 (Epub ahead of print)
    • (2014) Environ. Toxicol.
    • Glisic, B.1    Hrubik, J.2    Fa, S.3    Dopudj, N.4    Kovacevic, R.5    Andric, N.6
  • 84
    • 77949916874 scopus 로고    scopus 로고
    • Effect of acrylamide on chick embryonic liver glutathione S-transferases
    • R. Begum Sheikh, and T. Kedam Effect of acrylamide on chick embryonic liver glutathione S-transferases Mediterr. J. Nutr. Metab. 3 2010 31 38
    • (2010) Mediterr. J. Nutr. Metab. , vol.3 , pp. 31-38
    • Begum Sheikh, R.1    Kedam, T.2
  • 85
    • 0031809896 scopus 로고    scopus 로고
    • Localization of glutathione S-transferases alpha and pi in human embryonic tissues at 8 weeks gestational age
    • E.M. van Lieshout, M.F. Knapen, W.P. Lange, E.A. Steegers, and W.H. Peters Localization of glutathione S-transferases alpha and pi in human embryonic tissues at 8 weeks gestational age Hum. Reprod. 13 1998 1380 1386
    • (1998) Hum. Reprod. , vol.13 , pp. 1380-1386
    • Van Lieshout, E.M.1    Knapen, M.F.2    Lange, W.P.3    Steegers, E.A.4    Peters, W.H.5
  • 86
    • 0035152822 scopus 로고    scopus 로고
    • Glutathione S-transferases and thiol concentrations in embryonic and early fetal tissues
    • M.T.M. Raijmakers, E.A.P. Steegers, and W.H.M. Peters Glutathione S-transferases and thiol concentrations in embryonic and early fetal tissues Hum. Reprod. 16 2001 2445 2450
    • (2001) Hum. Reprod. , vol.16 , pp. 2445-2450
    • Raijmakers, M.T.M.1    Steegers, E.A.P.2    Peters, W.H.M.3
  • 87
    • 34247473444 scopus 로고    scopus 로고
    • A reducing redox environment promotes C2C12 myogenesis: Implications for regeneration in aged muscle
    • J.M. Hansen, M. Klass, C. Harris, and M. Csete A reducing redox environment promotes C2C12 myogenesis: implications for regeneration in aged muscle Cell Biol. Int. 31 2007 546 553
    • (2007) Cell Biol. Int. , vol.31 , pp. 546-553
    • Hansen, J.M.1    Klass, M.2    Harris, C.3    Csete, M.4
  • 88
    • 77954142412 scopus 로고    scopus 로고
    • Extracellular redox environments regulate adipocyte differentiation
    • B.R. Imhoff, and J.M. Hansen Extracellular redox environments regulate adipocyte differentiation Differentiation 80 2010 31 39
    • (2010) Differentiation , vol.80 , pp. 31-39
    • Imhoff, B.R.1    Hansen, J.M.2
  • 89
    • 79955535556 scopus 로고    scopus 로고
    • Differential redox potential profiles during adipogenesis and osteogenesis
    • B.R. Imhoff, and J.M. Hansen Differential redox potential profiles during adipogenesis and osteogenesis Cell. Mol. Biol. Lett. 16 2011 149 161
    • (2011) Cell. Mol. Biol. Lett. , vol.16 , pp. 149-161
    • Imhoff, B.R.1    Hansen, J.M.2
  • 91
    • 0020065765 scopus 로고
    • Gamma-glutamyl transpeptidase and glutathione in aging IMR-90 fibroblasts and in differentiating 3T3L1 preadipocytes
    • S. Takahashi, and M. Zeydel Gamma-glutamyl transpeptidase and glutathione in aging IMR-90 fibroblasts and in differentiating 3T3L1 preadipocytes Arch. Biochem. Biophys. 214 1982 260 267
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 260-267
    • Takahashi, S.1    Zeydel, M.2
  • 92
    • 28744434298 scopus 로고    scopus 로고
    • Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions
    • J.M. Hansen, H. Zhang, and D.P. Jones Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions Free Radic. Biol. Med. 40 2006 138 145
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 138-145
    • Hansen, J.M.1    Zhang, H.2    Jones, D.P.3
  • 93
    • 14844298802 scopus 로고    scopus 로고
    • Compartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling
    • P.J. Halvey, W.H. Watson, J.M. Hansen, Y.M. Go, A. Samali, and D.P. Jones Compartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling Biochem. J. 386 2005 215 219
    • (2005) Biochem. J. , vol.386 , pp. 215-219
    • Halvey, P.J.1    Watson, W.H.2    Hansen, J.M.3    Go, Y.M.4    Samali, A.5    Jones, D.P.6
  • 95
    • 0036372619 scopus 로고    scopus 로고
    • Redox potential of GSH/GSSG couple: Assay and biological significance
    • D.P. Jones Redox potential of GSH/GSSG couple: assay and biological significance Methods Enzymol. 348 2002 93 112
    • (2002) Methods Enzymol. , vol.348 , pp. 93-112
    • Jones, D.P.1
  • 96
    • 84875709337 scopus 로고    scopus 로고
    • The fairytale of the GSSG/GSH redox potential
    • L. Flohe The fairytale of the GSSG/GSH redox potential Biochim. Biophys. Acta 1830 2013 3139 3142
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3139-3142
    • Flohe, L.1
  • 97
    • 34548127870 scopus 로고    scopus 로고
    • Oxidation-reduction states of NADH in vivo: From animals to clinical use
    • A. Mayevsky, and B. Chance Oxidation-reduction states of NADH in vivo: from animals to clinical use Mitochondrion 7 2007 330 339
    • (2007) Mitochondrion , vol.7 , pp. 330-339
    • Mayevsky, A.1    Chance, B.2
  • 98
    • 0033858373 scopus 로고    scopus 로고
    • Modulation of glutathione and glutamate-L-cysteine ligase by methylmercury during mouse development
    • S.A. Thompson, C.C. White, C.M. Krejsa, D.L. Eaton, and T.J. Kavanagh Modulation of glutathione and glutamate-L-cysteine ligase by methylmercury during mouse development Toxicol. Sci. 57 2000 141 146
    • (2000) Toxicol. Sci. , vol.57 , pp. 141-146
    • Thompson, S.A.1    White, C.C.2    Krejsa, C.M.3    Eaton, D.L.4    Kavanagh, T.J.5
  • 99
    • 73349134315 scopus 로고    scopus 로고
    • Intracellular redox imbalance and extracellular amino acid metabolic abnormality contribute to arsenic-induced developmental retardation in mouse preimplantation embryos
    • C. Zhang, C. Liu, D. Li, N. Yao, X. Yuan, A. Yu, C. Lu, and X. Ma Intracellular redox imbalance and extracellular amino acid metabolic abnormality contribute to arsenic-induced developmental retardation in mouse preimplantation embryos J. Cell. Physiol. 222 2010 444 455
    • (2010) J. Cell. Physiol. , vol.222 , pp. 444-455
    • Zhang, C.1    Liu, C.2    Li, D.3    Yao, N.4    Yuan, X.5    Yu, A.6    Lu, C.7    Ma, X.8
  • 100
    • 84866339217 scopus 로고    scopus 로고
    • Oxidative damage and OGG1 expression induced by a combined effect of titanium dioxide nanoparticles and lead acetate in human hepatocytes
    • H. Du, X. Zhu, C. Fan, S. Xu, Y. Wang, and Y. Zhou Oxidative damage and OGG1 expression induced by a combined effect of titanium dioxide nanoparticles and lead acetate in human hepatocytes Environ. Toxicol. 27 2012 590 597
    • (2012) Environ. Toxicol. , vol.27 , pp. 590-597
    • Du, H.1    Zhu, X.2    Fan, C.3    Xu, S.4    Wang, Y.5    Zhou, Y.6
  • 102
    • 0035150407 scopus 로고    scopus 로고
    • Effects of phenytoin on glutathione status and oxidative stress biomarker gene mRNA levels in cultured precision human liver slices
    • E.P. Gallagher, and K.M. Sheehy Effects of phenytoin on glutathione status and oxidative stress biomarker gene mRNA levels in cultured precision human liver slices Toxicol. Sci. 59 2001 118 126
    • (2001) Toxicol. Sci. , vol.59 , pp. 118-126
    • Gallagher, E.P.1    Sheehy, K.M.2
  • 103
    • 76749126263 scopus 로고    scopus 로고
    • Ascorbic acid reverses valproic acid-induced inhibition of hoxa2 and maintains glutathione homeostasis in mouse embryos in culture
    • B. Zhang, X. Wang, and A.J. Nazarali Ascorbic acid reverses valproic acid-induced inhibition of hoxa2 and maintains glutathione homeostasis in mouse embryos in culture Cell. Mol. Neurobiol. 30 2010 137 148
    • (2010) Cell. Mol. Neurobiol. , vol.30 , pp. 137-148
    • Zhang, B.1    Wang, X.2    Nazarali, A.J.3
  • 104
    • 61349192318 scopus 로고    scopus 로고
    • Thalidomide resistance is based on the capacity of the glutathione-dependent antioxidant defense
    • J. Knobloch, K. Reimann, L.O. Klotz, and U. Ruther Thalidomide resistance is based on the capacity of the glutathione-dependent antioxidant defense Mol. Pharm. 5 2008 1138 1144
    • (2008) Mol. Pharm. , vol.5 , pp. 1138-1144
    • Knobloch, J.1    Reimann, K.2    Klotz, L.O.3    Ruther, U.4
  • 106
    • 84880685205 scopus 로고    scopus 로고
    • Deprenyl enhances the teratogenicity of hydroxyurea in organogenesis stage mouse embryos
    • A.E. Schlisser, and B.F. Hales Deprenyl enhances the teratogenicity of hydroxyurea in organogenesis stage mouse embryos Toxicol. Sci. 134 2013 391 399
    • (2013) Toxicol. Sci. , vol.134 , pp. 391-399
    • Schlisser, A.E.1    Hales, B.F.2
  • 107
    • 84904055215 scopus 로고    scopus 로고
    • Prenatal effects of retinoic acid on lumbar spinal cord development and liver antioxidants in rats
    • J. Vaskova, P. Patlevic, L. Vasko, and D. Kluchova Prenatal effects of retinoic acid on lumbar spinal cord development and liver antioxidants in rats Acta Histochem. 116 2014 855 862
    • (2014) Acta Histochem. , vol.116 , pp. 855-862
    • Vaskova, J.1    Patlevic, P.2    Vasko, L.3    Kluchova, D.4
  • 108
    • 84877156866 scopus 로고    scopus 로고
    • Acute ZnO nanoparticles exposure induces developmental toxicity, oxidative stress and DNA damage in embryo-larval zebrafish
    • X. Zhao, S. Wang, Y. Wu, H. You, and L. Lv Acute ZnO nanoparticles exposure induces developmental toxicity, oxidative stress and DNA damage in embryo-larval zebrafish Aquat. Toxicol. 136-137 2013 49 59
    • (2013) Aquat. Toxicol. , vol.136-137 , pp. 49-59
    • Zhao, X.1    Wang, S.2    Wu, Y.3    You, H.4    Lv, L.5
  • 109
    • 0034452902 scopus 로고    scopus 로고
    • Comparison of in vitro and in utero ethanol exposure on indices of oxidative stress
    • S.S. Akella, M.J. Beck, M.A. Philbert, and C. Harris Comparison of in vitro and in utero ethanol exposure on indices of oxidative stress In Vitr. Mol. Toxicol. 13 2000 281 296
    • (2000) Vitr. Mol. Toxicol. , vol.13 , pp. 281-296
    • Akella, S.S.1    Beck, M.J.2    Philbert, M.A.3    Harris, C.4
  • 110
    • 1642452751 scopus 로고    scopus 로고
    • Prenatal cocaine administration increases glutathione and alpha-tocopherol oxidation in fetal rat brain, Brain research
    • S. Gyawali, E.D. Borys, J.B. Koprich, M. Ptaszny, and S.O. McGuire Prenatal cocaine administration increases glutathione and alpha-tocopherol oxidation in fetal rat brain, Brain research Dev. Brain Res. 147 2003 77 84
    • (2003) Dev. Brain Res. , vol.147 , pp. 77-84
    • Gyawali, S.1    Borys, E.D.2    Koprich, J.B.3    Ptaszny, M.4    McGuire, S.O.5
  • 111
    • 25144494046 scopus 로고    scopus 로고
    • Alleviation of maternal hyperthermia-induced early embryonic death by administration of melatonin to mice
    • T. Matsuzuka, N. Sakamoto, M. Ozawa, A. Ushitani, M. Hirabayashi, and Y. Kanai Alleviation of maternal hyperthermia-induced early embryonic death by administration of melatonin to mice J. Pineal Res. 39 2005 217 223
    • (2005) J. Pineal Res. , vol.39 , pp. 217-223
    • Matsuzuka, T.1    Sakamoto, N.2    Ozawa, M.3    Ushitani, A.4    Hirabayashi, M.5    Kanai, Y.6
  • 112
    • 25144443988 scopus 로고    scopus 로고
    • Hypoxic stress in diabetic pregnancy contributes to impaired embryo gene expression and defective development by inducing oxidative stress
    • R. Li, M. Chase, S.K. Jung, P.J. Smith, and M.R. Loeken Hypoxic stress in diabetic pregnancy contributes to impaired embryo gene expression and defective development by inducing oxidative stress Am. J. Physiol. Endocrinol. Metab. 289 2005 E591 E599
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.289 , pp. E591-E599
    • Li, R.1    Chase, M.2    Jung, S.K.3    Smith, P.J.4    Loeken, M.R.5
  • 114
    • 33847633507 scopus 로고    scopus 로고
    • Mechanism of teratogenesis: Electron transfer, reactive oxygen species, and antioxidants
    • P. Kovacic, and R. Somanathan Mechanism of teratogenesis: electron transfer, reactive oxygen species, and antioxidants Birth Defects Res. C Embryo Today 78 2006 308 325
    • (2006) Birth Defects Res. C Embryo Today , vol.78 , pp. 308-325
    • Kovacic, P.1    Somanathan, R.2
  • 115
    • 36048978693 scopus 로고    scopus 로고
    • Effects of oxidative stress on embryonic development
    • P.A. Dennery Effects of oxidative stress on embryonic development Birth Defects Res. C Embryo Today 81 2007 155 162
    • (2007) Birth Defects Res. C Embryo Today , vol.81 , pp. 155-162
    • Dennery, P.A.1
  • 116
    • 0035002752 scopus 로고    scopus 로고
    • Reproductive toxins: Pervasive theme of oxidative stress and electron transfer
    • P. Kovacic, and J.D. Jacintho Reproductive toxins: pervasive theme of oxidative stress and electron transfer Curr. Med. Chem. 8 2001 863 892
    • (2001) Curr. Med. Chem. , vol.8 , pp. 863-892
    • Kovacic, P.1    Jacintho, J.D.2
  • 118
    • 84882816411 scopus 로고    scopus 로고
    • Oxidative stress
    • G. Fink, Academic Press San Diego, USA
    • H. Sies, and D.P. Jones Oxidative stress G. Fink, Encyclopedia of Stress 2007 Academic Press San Diego, USA 45 47
    • (2007) Encyclopedia of Stress , pp. 45-47
    • Sies, H.1    Jones, D.P.2
  • 119
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress
    • D.P. Jones Redefining oxidative stress Antioxid. Redox Signal. 8 2006 1865 1879
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1865-1879
    • Jones, D.P.1
  • 120
    • 0031149804 scopus 로고    scopus 로고
    • Redox state changes in density-dependent regulation of proliferation
    • D.E. Hutter, B.G. Till, and J.J. Greene Redox state changes in density-dependent regulation of proliferation Exp. Cell Res. 232 1997 435 438
    • (1997) Exp. Cell Res. , vol.232 , pp. 435-438
    • Hutter, D.E.1    Till, B.G.2    Greene, J.J.3
  • 121
    • 0031709365 scopus 로고    scopus 로고
    • Modulation of antioxidant enzymes, reactive oxygen species, and glutathione levels in manganese superoxide dismutase-overexpressing NIH/3T3 fibroblasts during the cell cycle
    • N. Li, and T.D. Oberley Modulation of antioxidant enzymes, reactive oxygen species, and glutathione levels in manganese superoxide dismutase-overexpressing NIH/3T3 fibroblasts during the cell cycle J. Cell. Physiol. 177 1998 148 160
    • (1998) J. Cell. Physiol. , vol.177 , pp. 148-160
    • Li, N.1    Oberley, T.D.2
  • 122
    • 34547110841 scopus 로고    scopus 로고
    • Glutathione is recruited into the nucleus in early phases of cell proliferation
    • J. Markovic, C. Borras, A. Ortega, J. Sastre, J. Vina, and F.V. Pallardo Glutathione is recruited into the nucleus in early phases of cell proliferation J. Biol. Chem. 282 2007 20416 20424
    • (2007) J. Biol. Chem. , vol.282 , pp. 20416-20424
    • Markovic, J.1    Borras, C.2    Ortega, A.3    Sastre, J.4    Vina, J.5    Pallardo, F.V.6
  • 123
    • 65049087578 scopus 로고    scopus 로고
    • Role of nuclear glutathione as a key regulator of cell proliferation
    • F.V. Pallardo, J. Markovic, J.L. Garcia, and J. Vina Role of nuclear glutathione as a key regulator of cell proliferation Mol. Asp. Med. 30 2009 77 85
    • (2009) Mol. Asp. Med. , vol.30 , pp. 77-85
    • Pallardo, F.V.1    Markovic, J.2    Garcia, J.L.3    Vina, J.4
  • 124
    • 78649560974 scopus 로고    scopus 로고
    • Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxidative defence shield
    • P.D. Vivancos, Y. Dong, K. Ziegler, J. Markovic, F.V. Pallardo, T.K. Pellny, P.J. Verrier, and C.H. Foyer Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxidative defence shield Plant J. 64 2010 825 838
    • (2010) Plant J. , vol.64 , pp. 825-838
    • Vivancos, P.D.1    Dong, Y.2    Ziegler, K.3    Markovic, J.4    Pallardo, F.V.5    Pellny, T.K.6    Verrier, P.J.7    Foyer, C.H.8
  • 125
    • 1642526587 scopus 로고    scopus 로고
    • Adipogenic differentiation of human adult stem cells from bone marrow stroma (MSCs)
    • I. Sekiya, B.L. Larson, J.T. Vuoristo, J.G. Cui, and D.J. Prockop Adipogenic differentiation of human adult stem cells from bone marrow stroma (MSCs) J. Bone Miner. Res. 19 2004 256 264
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 256-264
    • Sekiya, I.1    Larson, B.L.2    Vuoristo, J.T.3    Cui, J.G.4    Prockop, D.J.5
  • 126
    • 2342559147 scopus 로고    scopus 로고
    • An Alizarin red-based assay of mineralization by adherent cells in culture: Comparison with cetylpyridinium chloride extraction
    • C.A. Gregory, W.G. Gunn, A. Peister, and D.J. Prockop An Alizarin red-based assay of mineralization by adherent cells in culture: comparison with cetylpyridinium chloride extraction Anal. Biochem. 329 2004 77 84
    • (2004) Anal. Biochem. , vol.329 , pp. 77-84
    • Gregory, C.A.1    Gunn, W.G.2    Peister, A.3    Prockop, D.J.4
  • 127
    • 9444243245 scopus 로고    scopus 로고
    • Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control
    • D.P. Jones, Y.M. Go, C.L. Anderson, T.R. Ziegler, J.M. Kinkade Jr., and W.G. Kirlin Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control FASEB J. 18 2004 1246 1248
    • (2004) FASEB J. , vol.18 , pp. 1246-1248
    • Jones, D.P.1    Go, Y.M.2    Anderson, C.L.3    Ziegler, T.R.4    Kinkade, Jr.J.M.5    Kirlin, W.G.6
  • 129
    • 0030057750 scopus 로고    scopus 로고
    • Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress
    • T. Seres, V. Ravichandran, T. Moriguchi, K. Rokutan, J.A. Thomas, and R.B. Johnston Jr. Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress J. Immunol. 156 1996 1973 1980
    • (1996) J. Immunol. , vol.156 , pp. 1973-1980
    • Seres, T.1    Ravichandran, V.2    Moriguchi, T.3    Rokutan, K.4    Thomas, J.A.5    Johnston, Jr.R.B.6
  • 130
    • 33845936364 scopus 로고    scopus 로고
    • Selective protection of nuclear thioredoxin-1 and glutathione redox systems against oxidation during glucose and glutamine deficiency in human colonic epithelial cells
    • Y.M. Go, T.R. Ziegler, J.M. Johnson, L. Gu, J.M. Hansen, and D.P. Jones Selective protection of nuclear thioredoxin-1 and glutathione redox systems against oxidation during glucose and glutamine deficiency in human colonic epithelial cells Free Radic. Biol. Med. 42 2007 363 370
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 363-370
    • Go, Y.M.1    Ziegler, T.R.2    Johnson, J.M.3    Gu, L.4    Hansen, J.M.5    Jones, D.P.6
  • 132
    • 0037044782 scopus 로고    scopus 로고
    • Regulation of cAMP-dependent protein kinase activity by glutathionylation
    • K.M. Humphries, C. Juliano, and S.S. Taylor Regulation of cAMP-dependent protein kinase activity by glutathionylation J. Biol. Chem. 277 2002 43505 43511
    • (2002) J. Biol. Chem. , vol.277 , pp. 43505-43511
    • Humphries, K.M.1    Juliano, C.2    Taylor, S.S.3
  • 133
  • 134
    • 16544364554 scopus 로고    scopus 로고
    • Protein kinase function and glutathionylation
    • A.N. Anselmo, and M.H. Cobb Protein kinase function and glutathionylation Biochem. J. 381 2004 e1 e2
    • (2004) Biochem. J. , vol.381 , pp. e1-e2
    • Anselmo, A.N.1    Cobb, M.H.2
  • 135
    • 0034903753 scopus 로고    scopus 로고
    • Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine
    • F. Chu, N.E. Ward, and C.A. O'Brian Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine Carcinogenesis 22 2001 1221 1229
    • (2001) Carcinogenesis , vol.22 , pp. 1221-1229
    • Chu, F.1    Ward, N.E.2    O'Brian, C.A.3
  • 136
    • 4344686072 scopus 로고    scopus 로고
    • Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain
    • J.V. Cross, and D.J. Templeton Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain Biochem. J. 381 2004 675 683
    • (2004) Biochem. J. , vol.381 , pp. 675-683
    • Cross, J.V.1    Templeton, D.J.2
  • 137
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation
    • R.K. Rao, and L.W. Clayton Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation Biochem. Biophys. Res. Commun. 293 2002 610 616
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 138
    • 54049115864 scopus 로고    scopus 로고
    • Identification of PP2A as a crucial regulator of the NF-kappaB feedback loop: Its inhibition by UVB turns NF-kappaB into a pro-apoptotic factor
    • S. Barisic, E. Strozyk, N. Peters, H. Walczak, and D. Kulms Identification of PP2A as a crucial regulator of the NF-kappaB feedback loop: its inhibition by UVB turns NF-kappaB into a pro-apoptotic factor Cell Death Differ. 15 2008 1681 1690
    • (2008) Cell Death Differ. , vol.15 , pp. 1681-1690
    • Barisic, S.1    Strozyk, E.2    Peters, N.3    Walczak, H.4    Kulms, D.5
  • 140
    • 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
  • 142
    • 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
  • 143
  • 144
    • 77957315403 scopus 로고    scopus 로고
    • Redox compartmentalization and cellular stress
    • D.P. Jones, and Y.M. Go Redox compartmentalization and cellular stress Diabetes Obes. Metab. 12 Suppl. 2 2010 116 125
    • (2010) Diabetes Obes. Metab. , vol.12 , pp. 116-125
    • Jones, D.P.1    Go, Y.M.2
  • 145
    • 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
  • 146
    • 79954504166 scopus 로고    scopus 로고
    • Basic principles and emerging concepts in the redox control of transcription factors
    • R. Brigelius-Flohe, and L. Flohe Basic principles and emerging concepts in the redox control of transcription factors Antioxid. Redox Signal. 15 2011 2335 2381
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 2335-2381
    • Brigelius-Flohe, R.1    Flohe, L.2
  • 147
    • 0036363795 scopus 로고    scopus 로고
    • Gene expression and thiol redox state
    • C. Kretz-Remy, and A.P. Arrigo Gene expression and thiol redox state Methods Enzymol. 348 2002 200 215
    • (2002) Methods Enzymol. , vol.348 , pp. 200-215
    • Kretz-Remy, C.1    Arrigo, A.P.2
  • 148
    • 0033231351 scopus 로고    scopus 로고
    • Gene expression and the thiol redox state
    • A.P. Arrigo Gene expression and the thiol redox state Free Radic. Biol. Med. 27 1999 936 944
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 936-944
    • Arrigo, A.P.1
  • 149
    • 0036787835 scopus 로고    scopus 로고
    • Misregulation of gene expression in the redox-sensitive NF-kappab-dependent limb outgrowth pathway by thalidomide
    • J.M. Hansen, S.G. Gong, M. Philbert, and C. Harris Misregulation of gene expression in the redox-sensitive NF-kappab-dependent limb outgrowth pathway by thalidomide Dev. Dyn. 225 2002 186 194
    • (2002) Dev. Dyn. , vol.225 , pp. 186-194
    • Hansen, J.M.1    Gong, S.G.2    Philbert, M.3    Harris, C.4
  • 150
    • 33750523632 scopus 로고    scopus 로고
    • NF-kappaB activation by reactive oxygen species: Fifteen years later
    • G. Gloire, S. Legrand-Poels, and J. Piette NF-kappaB activation by reactive oxygen species: fifteen years later Biochem. Pharmacol. 72 2006 1493 1505
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 1493-1505
    • Gloire, G.1    Legrand-Poels, S.2    Piette, J.3
  • 152
    • 51049091712 scopus 로고    scopus 로고
    • Regulation by reversible S-glutathionylation: Molecular targets implicated in inflammatory diseases
    • M.D. Shelton, and J.J. Mieyal Regulation by reversible S-glutathionylation: molecular targets implicated in inflammatory diseases Mol. Cells 25 2008 332 346
    • (2008) Mol. Cells , vol.25 , pp. 332-346
    • Shelton, M.D.1    Mieyal, J.J.2
  • 155
    • 84859081898 scopus 로고    scopus 로고
    • The glutathionylation of p65 modulates NF-kappaB activity in 15-deoxy-Delta(1)(2), (1)(4)-prostaglandin J(2)-treated endothelial cells
    • Y.C. Lin, G.D. Huang, C.W. Hsieh, and B.S. Wung The glutathionylation of p65 modulates NF-kappaB activity in 15-deoxy-Delta(1)(2), (1)(4)-prostaglandin J(2)-treated endothelial cells Free Radic. Biol. Med. 52 2012 1844 1853
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1844-1853
    • Lin, Y.C.1    Huang, G.D.2    Hsieh, C.W.3    Wung, B.S.4
  • 158
    • 0032920883 scopus 로고    scopus 로고
    • Free radical-mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity
    • T. Parman, M.J. Wiley, and P.G. Wells Free radical-mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity Nat. Med. 5 1999 582 585
    • (1999) Nat. Med. , vol.5 , pp. 582-585
    • Parman, T.1    Wiley, M.J.2    Wells, P.G.3
  • 162
    • 0033662330 scopus 로고    scopus 로고
    • Fgf8 is required for outgrowth and patterning of the limbs
    • A.M. Moon, and M.R. Capecchi Fgf8 is required for outgrowth and patterning of the limbs Nat. Genet. 26 2000 455 459
    • (2000) Nat. Genet. , vol.26 , pp. 455-459
    • Moon, A.M.1    Capecchi, M.R.2
  • 163
    • 0032498962 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB activity results in disruption of the apical ectodermal ridge and aberrant limb morphogenesis
    • P.B. Bushdid, D.M. Brantley, F.E. Yull, G.L. Blaeuer, L.H. Hoffman, L. Niswander, and L.D. Kerr Inhibition of NF-kappaB activity results in disruption of the apical ectodermal ridge and aberrant limb morphogenesis Nature 392 1998 615 618
    • (1998) Nature , vol.392 , pp. 615-618
    • Bushdid, P.B.1    Brantley, D.M.2    Yull, F.E.3    Blaeuer, G.L.4    Hoffman, L.H.5    Niswander, L.6    Kerr, L.D.7
  • 164
    • 0032499286 scopus 로고    scopus 로고
    • Role of Rel/NF-kappaB transcription factors during the outgrowth of the vertebrate limb
    • Y. Kanegae, A.T. Tavares, J.C. Izpisua Belmonte, and I.M. Verma Role of Rel/NF-kappaB transcription factors during the outgrowth of the vertebrate limb Nature 392 1998 611 614
    • (1998) Nature , vol.392 , pp. 611-614
    • Kanegae, Y.1    Tavares, A.T.2    Izpisua Belmonte, J.C.3    Verma, I.M.4
  • 165
    • 84855837034 scopus 로고    scopus 로고
    • Inhibition of IkappaB kinase by thalidomide increases hepatitis C virus RNA replication
    • E. Rance, J.E. Tanner, and C. Alfieri Inhibition of IkappaB kinase by thalidomide increases hepatitis C virus RNA replication J. Viral Hepat. 19 2012 e73 e80
    • (2012) J. Viral Hepat. , vol.19 , pp. e73-e80
    • Rance, E.1    Tanner, J.E.2    Alfieri, C.3
  • 166
    • 33845476516 scopus 로고    scopus 로고
    • Reversal effect of thalidomide on established hepatic cirrhosis in rats via inhibition of nuclear factor-kappaB/inhibitor of nuclear factor-kappaB pathway
    • P. Lv, H.S. Luo, X.P. Zhou, Y.J. Xiao, S.C. Paul, X.M. Si, and Y.H. Zhou Reversal effect of thalidomide on established hepatic cirrhosis in rats via inhibition of nuclear factor-kappaB/inhibitor of nuclear factor-kappaB pathway Arch. Med. Res. 38 2007 15 27
    • (2007) Arch. Med. Res. , vol.38 , pp. 15-27
    • Lv, P.1    Luo, H.S.2    Zhou, X.P.3    Xiao, Y.J.4    Paul, S.C.5    Si, X.M.6    Zhou, Y.H.7
  • 167
    • 33845740735 scopus 로고    scopus 로고
    • A novel anticancer effect of thalidomide: Inhibition of intercellular adhesion molecule-1-mediated cell invasion and metastasis through suppression of nuclear factor-kappaB
    • Y.C. Lin, C.T. Shun, M.S. Wu, and C.C. Chen A novel anticancer effect of thalidomide: inhibition of intercellular adhesion molecule-1-mediated cell invasion and metastasis through suppression of nuclear factor-kappaB Clin. Cancer Res. 12 2006 7165 7173
    • (2006) Clin. Cancer Res. , vol.12 , pp. 7165-7173
    • Lin, Y.C.1    Shun, C.T.2    Wu, M.S.3    Chen, C.C.4
  • 168
    • 0037087402 scopus 로고    scopus 로고
    • Thalidomide suppresses NF-kappa B activation induced by TNF and H2O2, but not that activated by ceramide, lipopolysaccharides, or phorbol ester
    • S. Majumdar, B. Lamothe, and B.B. Aggarwal Thalidomide suppresses NF-kappa B activation induced by TNF and H2O2, but not that activated by ceramide, lipopolysaccharides, or phorbol ester J. Immunol. 168 2002 2644 2651
    • (2002) J. Immunol. , vol.168 , pp. 2644-2651
    • Majumdar, S.1    Lamothe, B.2    Aggarwal, B.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.