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Volumn 13, Issue 29, 2007, Pages 2952-2978

Interactive endogenous small molecule (gaseous) signaling: Implications for teratogenesis

Author keywords

Carbon monoxide; Dioxygen; Hydrogen sulfide; Nitric oxide; Signal transduction; Teratogenesis

Indexed keywords

CARBON DIOXIDE; CYTOCHROME C OXIDASE; GROWTH FACTOR RECEPTOR; HYDROGEN SULFIDE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 1BETA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; METALLOPROTEIN; NITRIC OXIDE; OXYGEN; PROTEIN TYROSINE PHOSPHATASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TRANSCRIPTION FACTOR; TYROSINE KINASE RECEPTOR;

EID: 36248940497     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161207782110525     Document Type: Review
Times cited : (26)

References (378)
  • 2
    • 0036512441 scopus 로고    scopus 로고
    • From O2 to H2S: A landscape view of gas biology
    • Kashiba M, Kajimura M, Goda N, Suematsu M. From O2 to H2S: A landscape view of gas biology. Keio J Med 2002; 51 (1): 1-10.
    • (2002) Keio J Med , vol.51 , Issue.1 , pp. 1-10
    • Kashiba, M.1    Kajimura, M.2    Goda, N.3    Suematsu, M.4
  • 5
    • 0004052075 scopus 로고
    • New York, Oxford University Press
    • Sawyer DT. Oxygen chemistry. New York, Oxford University Press 1991.
    • (1991) Oxygen chemistry
    • Sawyer, D.T.1
  • 6
    • 2142798407 scopus 로고
    • Overview of the energetics and reactivity of oxygen (Chapter 1)
    • Foote CS, Valentine JS, Greenberg A, Liebman JF Eds, London, Blackie Academic and Professional
    • Ho RYN, Liebman JF, Valentine JS. Overview of the energetics and reactivity of oxygen (Chapter 1). In: Foote CS, Valentine JS, Greenberg A, Liebman JF Eds, Active oxygen chemistry. London, Blackie Academic and Professional 1995; 1-23.
    • (1995) Active oxygen chemistry , pp. 1-23
    • Ho, R.Y.N.1    Liebman, J.F.2    Valentine, J.S.3
  • 7
    • 0001252044 scopus 로고
    • Properties and reactions of singlet oxygen (Chapter 4)
    • Foote CS, Valentine JS, Greenberg A and Liebman JF, Eds, London, Blackie Academic and Professional
    • Foote CS, Clennan EL. Properties and reactions of singlet oxygen (Chapter 4). In: Foote CS, Valentine JS, Greenberg A and Liebman JF, Eds. Active oxygen chemistry. London, Blackie Academic and Professional 1995: 105-40.
    • (1995) Active oxygen chemistry , pp. 105-140
    • Foote, C.S.1    Clennan, E.L.2
  • 8
    • 0002026040 scopus 로고
    • Biological reactions of dioxygen: An introduction
    • Valentine JS, Foote CS, Greenberg A, Liebman JF Eds, London, Blackie Academic and Professional
    • Ho RYN, Liebman JF, Valentine JS. Biological reactions of dioxygen: An introduction. In: Valentine JS, Foote CS, Greenberg A, Liebman JF Eds, Active oxygen in biochemistry. London, Blackie Academic and Professional 1995; 1-36.
    • (1995) Active oxygen in biochemistry , pp. 1-36
    • Ho, R.Y.N.1    Liebman, J.F.2    Valentine, J.S.3
  • 9
    • 36348989354 scopus 로고    scopus 로고
    • Eds, Biological inorganic chemistry, structure and reactivity. Sausalito, University Science Books
    • Yoshikawa S. Reducing dioxygen to water: Cytochrome c oxidase (Chapter XI.6). In: Bertini I, Gray HB, Stiefel EI, Valentine JS Eds, Biological inorganic chemistry, structure and reactivity. Sausalito, University Science Books 2006; 413-26.
    • (2006) Reducing dioxygen to water: Cytochrome c oxidase (Chapter XI.6) , pp. 413-426
    • Yoshikawa, S.1
  • 11
    • 13244274902 scopus 로고    scopus 로고
    • Yin H, Porter NA. New insights regarding the autoxidation. of polyunsaturated fatty acids. Antiox Redox Signal 2005; 7(1,2): 170-84.
    • Yin H, Porter NA. New insights regarding the autoxidation. of polyunsaturated fatty acids. Antiox Redox Signal 2005; 7(1,2): 170-84.
  • 12
    • 0842302396 scopus 로고    scopus 로고
    • Isoprostanes: Novel bioactive products of lipid peroxidation
    • Basu S. Isoprostanes: Novel bioactive products of lipid peroxidation. Free Rad Res 2004; 38(2): 105-22.
    • (2004) Free Rad Res , vol.38 , Issue.2 , pp. 105-122
    • Basu, S.1
  • 15
    • 0001531847 scopus 로고    scopus 로고
    • Iron-sulfur proteins with nonredox functions
    • Flint DH, Allen RM. Iron-sulfur proteins with nonredox functions Chem Rev 1996; 96: 2315-34.
    • (1996) Chem Rev , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 16
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: Thiol chemistry defines which rective oxygen and nitrogen species can act as second messengers
    • Forman HJ, Fukuto JM and Torres M. Redox signaling: Thiol chemistry defines which rective oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 2004; 287: C246-56.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 17
    • 33646698671 scopus 로고    scopus 로고
    • Stone JR, Yang S. Hydrogen peroxide: A signaling messenger. Antiox Redox Signal 2006; 8(3,4): 243-70.
    • Stone JR, Yang S. Hydrogen peroxide: A signaling messenger. Antiox Redox Signal 2006; 8(3,4): 243-70.
  • 18
    • 0042314356 scopus 로고    scopus 로고
    • Sulfur and selenium: The role of oxidation state in protein structure and function
    • Jacob C, Giles GI, Giles NM, Sies H. Sulfur and selenium: The role of oxidation state in protein structure and function. Angew Chem Int Ed 2003; 42: 4742-58.
    • (2003) Angew Chem Int Ed , vol.42 , pp. 4742-4758
    • Jacob, C.1    Giles, G.I.2    Giles, N.M.3    Sies, H.4
  • 19
    • 0842348252 scopus 로고    scopus 로고
    • An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems
    • Stone JR. An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems. Arch Biochem Biophys 2004; 422: 119-24
    • (2004) Arch Biochem Biophys , vol.422 , pp. 119-124
    • Stone, J.R.1
  • 20
    • 0004779396 scopus 로고
    • Mechanisms of oxygen metabolism
    • Mason HS. Mechanisms of oxygen metabolism. Science 1957; 125: 1185-8.
    • (1957) Science , vol.125 , pp. 1185-1188
    • Mason, H.S.1
  • 21
    • 0018651820 scopus 로고
    • Effect of oxygen concentration on morphogenesis of cranial neural folds and neural crest in cultured embryos
    • Morriss GM, New DA. Effect of oxygen concentration on morphogenesis of cranial neural folds and neural crest in cultured embryos. J Embryol Exp Morphol 1979; 54: 17-35.
    • (1979) J Embryol Exp Morphol , vol.54 , pp. 17-35
    • Morriss, G.M.1    New, D.A.2
  • 23
    • 0026782588 scopus 로고
    • Oxygen measurements in endometrial and trophoblastic tissues during early pregnancy
    • Rodesch F, Simon P, Donner C, Jauniaux E. Oxygen measurements in endometrial and trophoblastic tissues during early pregnancy. Obstet Gynecol 1992; 80(2): 283-85.
    • (1992) Obstet Gynecol , vol.80 , Issue.2 , pp. 283-285
    • Rodesch, F.1    Simon, P.2    Donner, C.3    Jauniaux, E.4
  • 25
    • 33750050271 scopus 로고    scopus 로고
    • Oxygen tension regulates chondrocyte dfferentiation and function during endochondral ossification
    • Hirao M, Tamai N, Tsumaki N, Yoshikawa H, Myoui A. Oxygen tension regulates chondrocyte dfferentiation and function during endochondral ossification. J Biol Chem 2006; 281(41): 31079-92.
    • (2006) J Biol Chem , vol.281 , Issue.41 , pp. 31079-31092
    • Hirao, M.1    Tamai, N.2    Tsumaki, N.3    Yoshikawa, H.4    Myoui, A.5
  • 26
    • 24744459687 scopus 로고    scopus 로고
    • Cellular and molecular interactions regulating skeleto-genesis
    • Colnot C. Cellular and molecular interactions regulating skeleto-genesis. J Cell Biochem 2005; 95: 688-97.
    • (2005) J Cell Biochem , vol.95 , pp. 688-697
    • Colnot, C.1
  • 27
    • 33644968171 scopus 로고    scopus 로고
    • Differential levels of tissue hypoxia in the developing chicken heart
    • Wikenheiser J, Doughman Y-Q, Fisher SA, Watanabe M. Differential levels of tissue hypoxia in the developing chicken heart. Dev Dyn 2006; 235: 115-23.
    • (2006) Dev Dyn , vol.235 , pp. 115-123
    • Wikenheiser, J.1    Doughman, Y.-Q.2    Fisher, S.A.3    Watanabe, M.4
  • 28
    • 0023810959 scopus 로고
    • Effects of oxygen concentration on embryonic deve4opment in rats: A light and electron microscopic study using whole-embryo culture techniques
    • Miki A, Fujimoto E, Ohsaki T, Mizoguti H. Effects of oxygen concentration on embryonic deve4opment in rats: A light and electron microscopic study using whole-embryo culture techniques. Anat Embryol (Berl) 1988; 178: 337-43.
    • (1988) Anat Embryol (Berl) , vol.178 , pp. 337-343
    • Miki, A.1    Fujimoto, E.2    Ohsaki, T.3    Mizoguti, H.4
  • 29
    • 0031026171 scopus 로고    scopus 로고
    • Oxygen-induced embryopathy and the significance of glutathione-dependent antioxidant system in the rat embryo during early organogenesis
    • Ishibashi M, Akazawa S, Sakamaki H, Matsumoto K, Yamasaki H, Yamaguchi Y, et al. Oxygen-induced embryopathy and the significance of glutathione-dependent antioxidant system in the rat embryo during early organogenesis. Free Rad Biol Med 1997; 22(3) 447-54.
    • (1997) Free Rad Biol Med , vol.22 , Issue.3 , pp. 447-454
    • Ishibashi, M.1    Akazawa, S.2    Sakamaki, H.3    Matsumoto, K.4    Yamasaki, H.5    Yamaguchi, Y.6
  • 31
    • 0034819597 scopus 로고    scopus 로고
    • Maternal vascularization of the human placenta: Does the embryo develop in a hypoxic environment?
    • Burton GJ, Jauniaux E. Maternal vascularization of the human placenta: does the embryo develop in a hypoxic environment? Gynecol Obstet Fertil 2001; 29(7-8): 503-08.
    • (2001) Gynecol Obstet Fertil , vol.29 , Issue.7-8 , pp. 503-508
    • Burton, G.J.1    Jauniaux, E.2
  • 32
    • 0035062024 scopus 로고    scopus 로고
    • Evaluation of respiratory gases and acid-base gradients in human fetal fluids and uteroplacental tissue between 7 and 16 weeks' gestation
    • Jauniaux E, Watson A, Burton G. Evaluation of respiratory gases and acid-base gradients in human fetal fluids and uteroplacental tissue between 7 and 16 weeks' gestation. Am J Obstet Gynecol 2001; 184(5): 998-1003.
    • (2001) Am J Obstet Gynecol , vol.184 , Issue.5 , pp. 998-1003
    • Jauniaux, E.1    Watson, A.2    Burton, G.3
  • 33
    • 0141739367 scopus 로고    scopus 로고
    • Physiological implications of the materno-fetal oxygen gradient in human early pregnancy
    • Jauniaux E, Gulbis B, Burton GJ. Physiological implications of the materno-fetal oxygen gradient in human early pregnancy. Reprod Biomed Online 2003; 7(2): 250-3.
    • (2003) Reprod Biomed Online , vol.7 , Issue.2 , pp. 250-253
    • Jauniaux, E.1    Gulbis, B.2    Burton, G.J.3
  • 34
    • 0141838123 scopus 로고    scopus 로고
    • The human first trimester gestational sac limits rather than facilitates oxygen transfer to the foetus - a review
    • Juniaux E, Gulbis B, Burton GJ. The human first trimester gestational sac limits rather than facilitates oxygen transfer to the foetus - a review. Placenta 2003b; 24(Suppl A): S86-93.
    • (2003) Placenta , vol.24 , Issue.SUPPL. A
    • Juniaux, E.1    Gulbis, B.2    Burton, G.J.3
  • 35
    • 0035142809 scopus 로고    scopus 로고
    • Determination of hypoxic region by hypoxia marker in developing mouse embryos in vivo: A possible signal for vessel development
    • Lee YM, Jeong CH, Koo SY, Son MJ, Song HS, Bae SK, et al. Determination of hypoxic region by hypoxia marker in developing mouse embryos in vivo: A possible signal for vessel development. Dev Dyn 2001; 220(2):175-86.
    • (2001) Dev Dyn , vol.220 , Issue.2 , pp. 175-186
    • Lee, Y.M.1    Jeong, C.H.2    Koo, S.Y.3    Son, M.J.4    Song, H.S.5    Bae, S.K.6
  • 36
    • 0032100732 scopus 로고    scopus 로고
    • HEF-1 alpha is required for solid tumor formation and embryonic vascularization
    • Ryan HE, Lo J, Johnson RS. HEF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J 1998; 17(11): 3005-15.
    • (1998) EMBO J , vol.17 , Issue.11 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 38
    • 28944437229 scopus 로고    scopus 로고
    • Erythropoiesis and red cell function in vertebrate embryos
    • Baumann R, Dragon S. Erythropoiesis and red cell function in vertebrate embryos. Eur J Clin Invest 2005; 35(Suppl 3): 2-12.
    • (2005) Eur J Clin Invest , vol.35 , Issue.SUPPL. 3 , pp. 2-12
    • Baumann, R.1    Dragon, S.2
  • 39
    • 4143097008 scopus 로고    scopus 로고
    • What is the purpose of the embryonic heart beat? Or how facts can ultimately prevail over physiological dogma
    • Burggren WW. What is the purpose of the embryonic heart beat? Or how facts can ultimately prevail over physiological dogma. Physiol Biochem Zoology 2004; 77(3): 333-45.
    • (2004) Physiol Biochem Zoology , vol.77 , Issue.3 , pp. 333-345
    • Burggren, W.W.1
  • 42
    • 0033032309 scopus 로고    scopus 로고
    • Altered blood pressure course during normal preganancy and increased preeclampsia at high altitude (3100 meters) in Colorado
    • Palmer SK, Moore LG, Young D, Gregger B, Berman JC, Zamudio S. Altered blood pressure course during normal preganancy and increased preeclampsia at high altitude (3100 meters) in Colorado. Am J Obstet Gynecol 1999; 180: 1161-8.
    • (1999) Am J Obstet Gynecol , vol.180 , pp. 1161-1168
    • Palmer, S.K.1    Moore, L.G.2    Young, D.3    Gregger, B.4    Berman, J.C.5    Zamudio, S.6
  • 43
  • 44
    • 0023764310 scopus 로고
    • Altitude, low birth weight, and infant mortality in Colorado
    • Unger C, Weiser JK, McCullough RE, Keefer S, Moore LG. Altitude, low birth weight, and infant mortality in Colorado. JAMA 1988; 259(23): 3427-32.
    • (1988) JAMA , vol.259 , Issue.23 , pp. 3427-3432
    • Unger, C.1    Weiser, J.K.2    McCullough, R.E.3    Keefer, S.4    Moore, L.G.5
  • 45
    • 0041629292 scopus 로고    scopus 로고
    • Fetal growth restriction and maternal oxygen transport during high altitude preganancy
    • Moore LG. Fetal growth restriction and maternal oxygen transport during high altitude preganancy. High Alt Med Biol 2003; 4(2): 141-56.
    • (2003) High Alt Med Biol , vol.4 , Issue.2 , pp. 141-156
    • Moore, L.G.1
  • 47
    • 33847613365 scopus 로고    scopus 로고
    • Catecholamine secretion from rat foetal adrenal chromaffin cells and hypoxia sensitivity
    • Bournaud R, Hidalgo J, Yu H, Girard E, Shimahara T. Catecholamine secretion from rat foetal adrenal chromaffin cells and hypoxia sensitivity. Pflugers Arch 2007; 454(1): 83-92.
    • (2007) Pflugers Arch , vol.454 , Issue.1 , pp. 83-92
    • Bournaud, R.1    Hidalgo, J.2    Yu, H.3    Girard, E.4    Shimahara, T.5
  • 48
    • 33845685603 scopus 로고    scopus 로고
    • Maternal oxytocin triggers a transient inhibitory switch in GABA signaling in the fetal brain during delivery
    • Tyzio R, Cossart R, Khalilov I, Minlebaev M, Hübner CA, Represa A, et al. Maternal oxytocin triggers a transient inhibitory switch in GABA signaling in the fetal brain during delivery. Science 2006; 314: 1788-92.
    • (2006) Science , vol.314 , pp. 1788-1792
    • Tyzio, R.1    Cossart, R.2    Khalilov, I.3    Minlebaev, M.4    Hübner, C.A.5    Represa, A.6
  • 49
    • 22244440847 scopus 로고    scopus 로고
    • Proline hydroxylation and gene expression. Annu
    • Kaelin WG Jr. Proline hydroxylation and gene expression. Annu Rev Biochem. 2005; 74: 115-28.
    • (2005) Rev Biochem , vol.74 , pp. 115-128
    • Kaelin Jr., W.G.1
  • 50
    • 0031000736 scopus 로고    scopus 로고
    • A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1α regulates the VEGF expression and is potentially involved in lung and vascular development
    • Ema M, Taya S, Yokotani N, Sogawa K, Matsuda Y, Fujii-Kuriyama Y. A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1α regulates the VEGF expression and is potentially involved in lung and vascular development. Proc Natl Acad Sci USA 1997; 94(9): 4273-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.9 , pp. 4273-4278
    • Ema, M.1    Taya, S.2    Yokotani, N.3    Sogawa, K.4    Matsuda, Y.5    Fujii-Kuriyama, Y.6
  • 51
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian H, McKnight SL, Russell DW. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev 1997; 11: 72-82.
    • (1997) Genes Dev , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 52
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang GL, Jiang B-H, Rue EA, Semenza GL. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci USA 1995; 92(12): 5510-4.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.12 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.-H.2    Rue, E.A.3    Semenza, G.L.4
  • 53
    • 33745490023 scopus 로고    scopus 로고
    • HIF-dependent hematopoietic factors regulate the development of the embryonic vasculature
    • Ramirez-Bergeron DL, Runge A, Adelman DM, Gohil M, Simon MC. HIF-dependent hematopoietic factors regulate the development of the embryonic vasculature. Dev Cell 2006; 11(1): 81-92.
    • (2006) Dev Cell , vol.11 , Issue.1 , pp. 81-92
    • Ramirez-Bergeron, D.L.1    Runge, A.2    Adelman, D.M.3    Gohil, M.4    Simon, M.C.5
  • 54
    • 0345491599 scopus 로고    scopus 로고
    • Differential roles of hypoxia-inducible factor 1 alpha (HIF-1-alpha) and HIF-2alpha in hypoxic gene regulation
    • Hu CJ, Wang LY, Chodosh LA, Keith B, Simon MC. Differential roles of hypoxia-inducible factor 1 alpha (HIF-1-alpha) and HIF-2alpha in hypoxic gene regulation. Mol Cell Biol 2003; 23(24): 9361-74.
    • (2003) Mol Cell Biol , vol.23 , Issue.24 , pp. 9361-9374
    • Hu, C.J.1    Wang, L.Y.2    Chodosh, L.A.3    Keith, B.4    Simon, M.C.5
  • 55
    • 0038788826 scopus 로고    scopus 로고
    • Hypoxia-induced gene expression occurs solely through the action of hypoxia-inducible factor 1alpha (HIF-1alpha): Role of cytoplasmic trapping of HIF-2alpha
    • Park SK, Dadak AM, Haase VH, Fontana L, Giaccia AJ, Johnson RS. Hypoxia-induced gene expression occurs solely through the action of hypoxia-inducible factor 1alpha (HIF-1alpha): Role of cytoplasmic trapping of HIF-2alpha. Mol Cell Biol 2003; 23(14): 4959-71.
    • (2003) Mol Cell Biol , vol.23 , Issue.14 , pp. 4959-4971
    • Park, S.K.1    Dadak, A.M.2    Haase, V.H.3    Fontana, L.4    Giaccia, A.J.5    Johnson, R.S.6
  • 56
    • 0141988698 scopus 로고    scopus 로고
    • Predominant role of hypoxia-inducible transcription factor (Hif)-1alpha versus Hif-2alpha in regulation of the transcriptional response to hypoxia
    • Sowter HM, Raval RR, Moore JW, Ratcliffe PJ, Harris AL. Predominant role of hypoxia-inducible transcription factor (Hif)-1alpha versus Hif-2alpha in regulation of the transcriptional response to hypoxia. Cancer Res 2003; 63(19): 6130-4.
    • (2003) Cancer Res , vol.63 , Issue.19 , pp. 6130-6134
    • Sowter, H.M.1    Raval, R.R.2    Moore, J.W.3    Ratcliffe, P.J.4    Harris, A.L.5
  • 58
    • 0035969508 scopus 로고    scopus 로고
    • Inhibitory PAS domain is a negative regulator of hypoxia-inducible gene expression
    • Makino Y, Cao R, Svensson K, Bertilsson G, Asman M, Tanaka H, et al. Inhibitory PAS domain is a negative regulator of hypoxia-inducible gene expression, Nature 2001; 414(6863): 550-4.
    • (2001) Nature , vol.414 , Issue.6863 , pp. 550-554
    • Makino, Y.1    Cao, R.2    Svensson, K.3    Bertilsson, G.4    Asman, M.5    Tanaka, H.6
  • 59
    • 0037031808 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus
    • Makino Y, Kanopka A, Wilson WJ, Tanaka H, Poellinger L. Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus. J Biol Chem 2002; 277(36): 32405-8.
    • (2002) J Biol Chem , vol.277 , Issue.36 , pp. 32405-32408
    • Makino, Y.1    Kanopka, A.2    Wilson, W.J.3    Tanaka, H.4    Poellinger, L.5
  • 60
    • 33745303045 scopus 로고    scopus 로고
    • Hypoxia signaling in cancer and approaches to enforce tumor regression
    • Pouysségur J, Dayan F, Mazure NM. Hypoxia signaling in cancer and approaches to enforce tumor regression. Nature 2006; 441: 437-43.
    • (2006) Nature , vol.441 , pp. 437-443
    • Pouysségur, J.1    Dayan, F.2    Mazure, N.M.3
  • 61
    • 0027427588 scopus 로고
    • Characterization of hypoxia-inducible factor 1 and regulation of DNA-binding activity by hypoxia
    • Wang GL, Semenza GL. Characterization of hypoxia-inducible factor 1 and regulation of DNA-binding activity by hypoxia. J Biol Chem 1993; 268(29): 21513-8.
    • (1993) J Biol Chem , vol.268 , Issue.29 , pp. 21513-21518
    • Wang, G.L.1    Semenza, G.L.2
  • 62
    • 0032508691 scopus 로고    scopus 로고
    • Hypoxia-inducible mammalian gene expression analyzed in vivo at a TATA-driven promoter
    • Okino ST, Chichester CH, Whitlock JP Jr. Hypoxia-inducible mammalian gene expression analyzed in vivo at a TATA-driven promoter. J Biol Chem 1998; 273(37): 23837-43.
    • (1998) J Biol Chem , vol.273 , Issue.37 , pp. 23837-23843
    • Okino, S.T.1    Chichester, C.H.2    Whitlock Jr., J.P.3
  • 63
    • 0036320934 scopus 로고    scopus 로고
    • Cellular adaptation to hypoxia: O2-sensing protein hydroxylases, hypoxia-inducible transcription factors, and O2-regulated gene expression
    • Wenger RH. Cellular adaptation to hypoxia: O2-sensing protein hydroxylases, hypoxia-inducible transcription factors, and O2-regulated gene expression. FASEB J 2002; 16(10): 1151-62.
    • (2002) FASEB J , vol.16 , Issue.10 , pp. 1151-1162
    • Wenger, R.H.1
  • 64
    • 0034904751 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 alpha (HIF-1 alpha) escapes O(2)-driven proteosomal degradation irrespective of its subcellular localization: Nucleus or cytoplasm
    • Berra E, Roux D, Richard DE, Pouysségur J. Hypoxia-inducible factor-1 alpha (HIF-1 alpha) escapes O(2)-driven proteosomal degradation irrespective of its subcellular localization: Nucleus or cytoplasm. EMBO Rep 2001; 2(7): 615-20.
    • (2001) EMBO Rep , vol.2 , Issue.7 , pp. 615-620
    • Berra, E.1    Roux, D.2    Richard, D.E.3    Pouysségur, J.4
  • 66
    • 0035753241 scopus 로고    scopus 로고
    • Delta4, an endothelial specific notch ligand expressed at sites of physiological and tumor angiogenesis
    • Mailhos C, Modlich U, Lewis J, Harris A, Bicknell R, Ish-Horowicz D. Delta4, an endothelial specific notch ligand expressed at sites of physiological and tumor angiogenesis. Differentiation 2001; 69(2-3): 135-44.
    • (2001) Differentiation , vol.69 , Issue.2-3 , pp. 135-144
    • Mailhos, C.1    Modlich, U.2    Lewis, J.3    Harris, A.4    Bicknell, R.5    Ish-Horowicz, D.6
  • 67
    • 25444506836 scopus 로고    scopus 로고
    • Up-regulation of delta-like 4 ligand in human tumor vasculature and the role of basal expression in endothelial cell function
    • Patel NS, Li JL, Generali D, Poulsom R, Cranston DW, Harris AL. Up-regulation of delta-like 4 ligand in human tumor vasculature and the role of basal expression in endothelial cell function. Cancer Res 2005; 65(19): 8690-7.
    • (2005) Cancer Res , vol.65 , Issue.19 , pp. 8690-8697
    • Patel, N.S.1    Li, J.L.2    Generali, D.3    Poulsom, R.4    Cranston, D.W.5    Harris, A.L.6
  • 68
    • 27644561755 scopus 로고    scopus 로고
    • Hypoxia requires Notch signaling to maintain the undifferentiated cell state
    • Gustafsson MV, Zheng X, Pereira T, Gradin K, Jin S, Lundkvist J, et al. Hypoxia requires Notch signaling to maintain the undifferentiated cell state. Dev Cell 2005; 9: 617-28.
    • (2005) Dev Cell , vol.9 , pp. 617-628
    • Gustafsson, M.V.1    Zheng, X.2    Pereira, T.3    Gradin, K.4    Jin, S.5    Lundkvist, J.6
  • 69
    • 33845642740 scopus 로고    scopus 로고
    • Hypoxia-mediated activation of D114-Notch-Hey2 signaling in endothelial progenitor cells and adoption of arterial cell fate
    • Diez H, Fischer A, Winkler A, Hu CJ, Hatzopoulos AK, Breier G, et al. Hypoxia-mediated activation of D114-Notch-Hey2 signaling in endothelial progenitor cells and adoption of arterial cell fate. Exp Cell Res 2007; 313: 1-9.
    • (2007) Exp Cell Res , vol.313 , pp. 1-9
    • Diez, H.1    Fischer, A.2    Winkler, A.3    Hu, C.J.4    Hatzopoulos, A.K.5    Breier, G.6
  • 70
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • Bunn HF, Poyton RO. Oxygen sensing and molecular adaptation to hypoxia. Physiol Rev 1996; 76(3): 839-85.
    • (1996) Physiol Rev , vol.76 , Issue.3 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2
  • 71
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: The paradox of increased reactive oxygen species during hypoxia
    • Guzy RD, Schumacker PT. Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp Physiol 2006; 91(5): 807-19.
    • (2006) Exp Physiol , vol.91 , Issue.5 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 72
    • 0014010888 scopus 로고
    • Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron transport particles
    • Jensen PK. Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron transport particles. Biochim Biophys Acta, 1966; 122: 157-66.
    • (1966) Biochim Biophys Acta , vol.122 , pp. 157-166
    • Jensen, P.K.1
  • 73
    • 0029763762 scopus 로고    scopus 로고
    • Molecular oxygen modulates cytochrome c oxidase function
    • Chandel NS, Budinger GR, Schumacker PT. Molecular oxygen modulates cytochrome c oxidase function. J Biol Chem 1996; 271(31): 18672-7.
    • (1996) J Biol Chem , vol.271 , Issue.31 , pp. 18672-18677
    • Chandel, N.S.1    Budinger, G.R.2    Schumacker, P.T.3
  • 74
    • 0030855493 scopus 로고    scopus 로고
    • Cellular respiration during hypoxia. Role of cytochrome oxidase as the oxygen sensor in hepatocytes
    • Chandel NS, Budinger GR, Choe SH, Schumacker PT. Cellular respiration during hypoxia. Role of cytochrome oxidase as the oxygen sensor in hepatocytes. J Biol Chem 1997, 272(30): 18808-16.
    • (1997) J Biol Chem , vol.272 , Issue.30 , pp. 18808-18816
    • Chandel, N.S.1    Budinger, G.R.2    Choe, S.H.3    Schumacker, P.T.4
  • 75
    • 0029060562 scopus 로고
    • Inhibition of cytochrome-c oxidase activity during prolonged hypoxia
    • Chandel N, Budinger GR, Kemp RA, Schumacker PT. Inhibition of cytochrome-c oxidase activity during prolonged hypoxia. Am J Physiol 1995; 268(6 Pt 1): L918-25.
    • (1995) Am J Physiol , vol.268 , Issue.6 PART 1
    • Chandel, N.1    Budinger, G.R.2    Kemp, R.A.3    Schumacker, P.T.4
  • 77
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol 2003; 552: 335-44.
    • (2003) J Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 78
    • 1942453399 scopus 로고    scopus 로고
    • The effect of mitochondrial inhibitors on membrane currents in isolated neonatal rat carotid body type I cells
    • Wyatt CN, Buckler KJ. The effect of mitochondrial inhibitors on membrane currents in isolated neonatal rat carotid body type I cells. J Physiol 2004; 556: 175-91.
    • (2004) J Physiol , vol.556 , pp. 175-191
    • Wyatt, C.N.1    Buckler, K.J.2
  • 79
    • 33845492679 scopus 로고    scopus 로고
    • A phenotypic perspective on Mammalian oxygen sensor candidates
    • Baysal BE. A phenotypic perspective on Mammalian oxygen sensor candidates. Ann NY Acad Sci 2006; 1073: 221-33.
    • (2006) Ann NY Acad Sci , vol.1073 , pp. 221-233
    • Baysal, B.E.1
  • 81
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard K, Krause KH. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 2007; 87(1): 245-313.
    • (2007) Physiol Rev , vol.87 , Issue.1 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 83
    • 0023041664 scopus 로고
    • 2- -forming NADPH oxidase of the phagocytes: Nature, mechanisms of activation and function
    • 2- -forming NADPH oxidase of the phagocytes: nature, mechanisms of activation and function. Biochim Biophys Acta, 1986; 853(1): 65-89.
    • (1986) Biochim Biophys Acta , vol.853 , Issue.1 , pp. 65-89
    • Rossi, F.1
  • 85
    • 0035030363 scopus 로고    scopus 로고
    • Respiratory control in neonatal mice with NADPH oxidase deficiency
    • Kazemian P, Stephenson R, Yeger H, Cutz E. Respiratory control in neonatal mice with NADPH oxidase deficiency. Resp Physiol 2001; 126:89-101.
    • (2001) Resp Physiol , vol.126 , pp. 89-101
    • Kazemian, P.1    Stephenson, R.2    Yeger, H.3    Cutz, E.4
  • 90
    • 10844248490 scopus 로고    scopus 로고
    • Hemeoxygenase-2 is an oxygen sensor for a calcium-sensitive potassium channel
    • Williams SE, Wootton P, Mason HS, Bould J, Iles DE, Riccardi D, et al. Hemeoxygenase-2 is an oxygen sensor for a calcium-sensitive potassium channel. Science 2004; 306: 2093-7.
    • (2004) Science , vol.306 , pp. 2093-2097
    • Williams, S.E.1    Wootton, P.2    Mason, H.S.3    Bould, J.4    Iles, D.E.5    Riccardi, D.6
  • 91
    • 29244463866 scopus 로고    scopus 로고
    • Does AMP-activated protein kinase couple inhibition of mitochondrial oxidative phosphorylation by hypoxia to calcium signaling in O2-sensing cells?
    • Evans AM, Mustard KJ, Wyatt CN, Peers C, Dipp M, Kumar P, et al. Does AMP-activated protein kinase couple inhibition of mitochondrial oxidative phosphorylation by hypoxia to calcium signaling in O2-sensing cells? J Biol Chem 2005; 280(50): 41504-11.
    • (2005) J Biol Chem , vol.280 , Issue.50 , pp. 41504-41511
    • Evans, A.M.1    Mustard, K.J.2    Wyatt, C.N.3    Peers, C.4    Dipp, M.5    Kumar, P.6
  • 92
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keapl-Nrf2-ARE pathway
    • Kensler TW, Wakabayashi N, Biswal S. Cell survival responses to environmental stresses via the Keapl-Nrf2-ARE pathway. Annu Rev Pharmacol Toxicol 2007; 47: 89-116.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 93
    • 4544294365 scopus 로고    scopus 로고
    • The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: Oxidative stress sensing by a Cul3-Keap1 ligase
    • Cullinan SB, Gordan JD, Jin J, Harper JW, Diehl JA. The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase. Mol Cell Biol 2004; 24(19): 8477-86.
    • (2004) Mol Cell Biol , vol.24 , Issue.19 , pp. 8477-8486
    • Cullinan, S.B.1    Gordan, J.D.2    Jin, J.3    Harper, J.W.4    Diehl, J.A.5
  • 94
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi A, Kang M-I, Okawa H, Ohtsuji M, Zenke Y, Chiba T, et al. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol Cell Biol 2004; 24: 7130-9.
    • (2004) Mol Cell Biol , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.-I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6
  • 95
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • Zhang DD, Lo SC, Cross JV, Templeton DJ, Hannink M. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol Cell Biol 2004; 24: 10941-53.
    • (2004) Mol Cell Biol , vol.24 , pp. 10941-10953
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 96
    • 33744953050 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 568 controls nuclear export of Nrf2
    • Jain AK, Jaiswal AK. Phosphorylation of tyrosine 568 controls nuclear export of Nrf2. J Biol Chem 2006; 281(17): 12132-42.
    • (2006) J Biol Chem , vol.281 , Issue.17 , pp. 12132-12142
    • Jain, A.K.1    Jaiswal, A.K.2
  • 97
    • 0025948113 scopus 로고
    • The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • Rushmore TH. Morton MR, Pickett CB. The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J Biol Chem 1991; 266(18):11632-9.
    • (1991) J Biol Chem , vol.266 , Issue.18 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 98
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism
    • Tong KI, Kobayashi A, Katsuoka F, Yamamoto M. Two-site substrate recognition model for the Keap1-Nrf2 system: A hinge and latch mechanism. Biol Chem 2006; 387:1311-20.
    • (2006) Biol Chem , vol.387 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 99
    • 0032907687 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF) and its receptors
    • Neufeld G, Cohen T, Gengrinovitch S, Poltorak Z. Vascular endothelial growth factor (VEGF) and its receptors. FASEB J 1999; 13: 9-22.
    • (1999) FASEB J , vol.13 , pp. 9-22
    • Neufeld, G.1    Cohen, T.2    Gengrinovitch, S.3    Poltorak, Z.4
  • 100
    • 0033597766 scopus 로고    scopus 로고
    • Fyn and JAK2 mediate Ras activation by reactive oxygen species
    • Abe J, Berk BC. Fyn and JAK2 mediate Ras activation by reactive oxygen species. J Biol Chem 1999; 274(30): 21003-10.
    • (1999) J Biol Chem , vol.274 , Issue.30 , pp. 21003-21010
    • Abe, J.1    Berk, B.C.2
  • 102
    • 4143145395 scopus 로고    scopus 로고
    • Hypoxia and the regulation of mitogen-activated protein kinases: Gene transcription and the assessment of potential pharmacologic therapeutic interventions
    • Haddad JJ. Hypoxia and the regulation of mitogen-activated protein kinases: Gene transcription and the assessment of potential pharmacologic therapeutic interventions. Int Immunopharmacol 2004; 4:1249-85.
    • (2004) Int Immunopharmacol , vol.4 , pp. 1249-1285
    • Haddad, J.J.1
  • 103
    • 33750909999 scopus 로고    scopus 로고
    • Reactive oxygen species-induced activation of the MAP kinase signaling pathways
    • McCubrey JA, LaHair MM, Franklin RA. Reactive oxygen species-induced activation of the MAP kinase signaling pathways. Anjioxid Redox Signal 2006; 8(9/10): 1775-89.
    • (2006) Anjioxid Redox Signal , vol.8 , Issue.9-10 , pp. 1775-1789
    • McCubrey, J.A.1    LaHair, M.M.2    Franklin, R.A.3
  • 105
    • 15044358594 scopus 로고    scopus 로고
    • New roles for the LKB1-AMPK pathway
    • Hardie, D. G. New roles for the LKB1-AMPK pathway. Curr Opin Cell Biol 2005; 17: 167-73.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 167-173
    • Hardie, D.G.1
  • 106
    • 10044276784 scopus 로고    scopus 로고
    • The hypoxia-induced paralog Scylla and Charybdis inhibit growth by down-regulating S6K activity upstream of TSC in Drosophila
    • Reiling JH, Hafen E. The hypoxia-induced paralog Scylla and Charybdis inhibit growth by down-regulating S6K activity upstream of TSC in Drosophila. Genes Dev 2004; 18: 2879-92.
    • (2004) Genes Dev , vol.18 , pp. 2879-2892
    • Reiling, J.H.1    Hafen, E.2
  • 107
    • 10044276783 scopus 로고    scopus 로고
    • Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex
    • Brugarolas J, Lei K, Hurley RL, Manning BD, Reiling JH, Hafen E, et al. Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex. Genes Dev 2004; 18(23): 2893-904.
    • (2004) Genes Dev , vol.18 , Issue.23 , pp. 2893-2904
    • Brugarolas, J.1    Lei, K.2    Hurley, R.L.3    Manning, B.D.4    Reiling, J.H.5    Hafen, E.6
  • 108
    • 33748752151 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity
    • Schieke SM, Phillips D, McCoy JP Jr, Aponte, AM, Shen R-F, Balaban RS, et al. The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity. J Biol Chem 2006; 281(37): 27643-52.
    • (2006) J Biol Chem , vol.281 , Issue.37 , pp. 27643-27652
    • Schieke, S.M.1    Phillips, D.2    McCoy Jr, J.P.3    Aponte, A.M.4    Shen, R.-F.5    Balaban, R.S.6
  • 109
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks NK. Redox redux: Revisiting PTPs and the control of cell signaling. Cell 2005; 121(5):667-70.
    • (2005) Cell , vol.121 , Issue.5 , pp. 667-670
    • Tonks, N.K.1
  • 110
  • 111
    • 0033233243 scopus 로고    scopus 로고
    • 2 homeostasis by hypoxia-inducible factor 1
    • 2 homeostasis by hypoxia-inducible factor 1. Annu Rev Cell Dev Biol 1999; 15: 551-78
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 551-578
    • Semenza, G.L.1
  • 112
    • 0026456161 scopus 로고
    • Mammalian nitric oxide synthases
    • Ed, Adv Enzymol New York, Wiley and sons
    • Stuehr DJ, Griffith OW. Mammalian nitric oxide synthases. In: Meister A Ed, Adv Enzymol volume 65. New York, Wiley and sons 1992; 287-347.
    • (1992) Meister A , vol.65 , pp. 287-347
    • Stuehr, D.J.1    Griffith, O.W.2
  • 113
    • 0031435306 scopus 로고    scopus 로고
    • Soluble guanylate cyclase: The forgotten sibling. Trends
    • Hobbs AJ. Soluble guanylate cyclase: The forgotten sibling. Trends Pharmacol Sci 1997; 18: 484-91.
    • (1997) Pharmacol Sci , vol.18 , pp. 484-491
    • Hobbs, A.J.1
  • 115
    • 0033549530 scopus 로고    scopus 로고
    • Nitric oxide: A unique endogenous signaling molecule in vascular biology (Nobel Lecture)
    • Ignarro LJ. Nitric oxide: A unique endogenous signaling molecule in vascular biology (Nobel Lecture). Angew Chem Int Ed (1999); 38: 1882-92.
    • (1999) Angew Chem Int Ed , vol.38 , pp. 1882-1892
    • Ignarro, L.J.1
  • 116
    • 0036272812 scopus 로고    scopus 로고
    • Preconditioning-mediated neuro-protection: Role of nitric oxide, cGMP, and new protein expression
    • Andoh T, Chock PB, Chiueh CC. Preconditioning-mediated neuro-protection: Role of nitric oxide, cGMP, and new protein expression. Annals N Y Acad Sci 2002; 962: 1-7.
    • (2002) Annals N Y Acad Sci , vol.962 , pp. 1-7
    • Andoh, T.1    Chock, P.B.2    Chiueh, C.C.3
  • 117
    • 0037428498 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinase regulates the expression of thioredoxin and thioredoxin per-oxidase-1 during homesis in response to oxidative stress-induced apoptosis
    • Andoh T, Chiueh CC, Chock PB. Cyclic GMP-dependent protein kinase regulates the expression of thioredoxin and thioredoxin per-oxidase-1 during homesis in response to oxidative stress-induced apoptosis. J Biol Chem 2003; 278(2): 885-90.
    • (2003) J Biol Chem , vol.278 , Issue.2 , pp. 885-890
    • Andoh, T.1    Chiueh, C.C.2    Chock, P.B.3
  • 118
    • 1642358516 scopus 로고    scopus 로고
    • The early ontogeny of neuronal nitric oxide synthase systems in the zebrafish
    • Holmqvist B, Ellingsen B, Forsell J, Zhdanova I, Alm P. The early ontogeny of neuronal nitric oxide synthase systems in the zebrafish. J Exp Biol 2004; 207(Pt6): 923-35.
    • (2004) J Exp Biol , vol.207 , Issue.PT6 , pp. 923-935
    • Holmqvist, B.1    Ellingsen, B.2    Forsell, J.3    Zhdanova, I.4    Alm, P.5
  • 120
    • 0025146122 scopus 로고
    • The role of nitric oxides as effector molecules of parasite killing
    • James SL, Hibbs JB Jr. The role of nitric oxides as effector molecules of parasite killing. Parasitol Today 1990; 6: 303-5.
    • (1990) Parasitol Today , vol.6 , pp. 303-305
    • James, S.L.1    Hibbs Jr., J.B.2
  • 122
    • 0029790939 scopus 로고    scopus 로고
    • Physiological and pathophysiological roles of nitric oxide in the central nervous system
    • Szabo C. Physiological and pathophysiological roles of nitric oxide in the central nervous system. Brain Res Bull 1999; 41: 131-41.
    • (1999) Brain Res Bull , vol.41 , pp. 131-141
    • Szabo, C.1
  • 124
    • 0027280338 scopus 로고
    • Pathological implications of nitric oxide, superoxide and peroxynitrite formation
    • Beckman JS, Crow JP. Pathological implications of nitric oxide, superoxide and peroxynitrite formation. Biochem Soc Trans 1993; 21: 330-4.
    • (1993) Biochem Soc Trans , vol.21 , pp. 330-334
    • Beckman, J.S.1    Crow, J.P.2
  • 126
    • 0026683354 scopus 로고
    • Does nitric oxide mediate autoimmune destruction of beta-cells? Possible therapeutic interventions in IDDM
    • Corbett JA, McDaniel AL. Does nitric oxide mediate autoimmune destruction of beta-cells? Possible therapeutic interventions in IDDM. Diabetes 1992; 41: 897-903.
    • (1992) Diabetes , vol.41 , pp. 897-903
    • Corbett, J.A.1    McDaniel, A.L.2
  • 127
    • 0027304915 scopus 로고
    • Pancreatic islet cells are highly susceptible towards the cytotoxic effects of chemically generated nitric oxide
    • Kroncke K-D, Brenner H-H, Rodrigue M-L, Etzkorn K, Noack EA, Kolb H, et al. Pancreatic islet cells are highly susceptible towards the cytotoxic effects of chemically generated nitric oxide. Biochim Biophys Acta 1993; 1182: 221-9.
    • (1993) Biochim Biophys Acta , vol.1182 , pp. 221-229
    • Kroncke, K.-D.1    Brenner, H.-H.2    Rodrigue, M.-L.3    Etzkorn, K.4    Noack, E.A.5    Kolb, H.6
  • 130
    • 0029040804 scopus 로고
    • Nitric oxide protects against alkyl peroxide-mediated cytotoxicity: Further insights into the role nitric oxide plays in oxidative stress
    • Wink DA, Cook JA, Krishna MC, Hanbauer I, DeGraff W, Gamson J, et al. Nitric oxide protects against alkyl peroxide-mediated cytotoxicity: Further insights into the role nitric oxide plays in oxidative stress. Arch Biochem Biophys 1995; 319: 402-7.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 402-407
    • Wink, D.A.1    Cook, J.A.2    Krishna, M.C.3    Hanbauer, I.4    DeGraff, W.5    Gamson, J.6
  • 131
    • 0030586329 scopus 로고    scopus 로고
    • The effect of various nitric oxide donor agents on hydrogen peroxide-mediated toxicity: A direct correlation between nitric oxide formation and protection
    • Wink DA, Cook JA, Pacelli R, DeGraff W, Garrison J, Liebmann J, et al. The effect of various nitric oxide donor agents on hydrogen peroxide-mediated toxicity: A direct correlation between nitric oxide formation and protection. Arch Biochem Biophys 1996; 331(2): 241-8.
    • (1996) Arch Biochem Biophys , vol.331 , Issue.2 , pp. 241-248
    • Wink, D.A.1    Cook, J.A.2    Pacelli, R.3    DeGraff, W.4    Garrison, J.5    Liebmann, J.6
  • 133
    • 0026584898 scopus 로고
    • Nitric oxide, and inhibitor of lipid oxidation by lipoxygenase, cyclooxygenase and hemoglobin
    • Kanner J, Harel S, Granit R. Nitric oxide, and inhibitor of lipid oxidation by lipoxygenase, cyclooxygenase and hemoglobin. Lipids 1992; 27(1): 46-9.
    • (1992) Lipids , vol.27 , Issue.1 , pp. 46-49
    • Kanner, J.1    Harel, S.2    Granit, R.3
  • 134
    • 0029815841 scopus 로고    scopus 로고
    • Nitric oxide and metal-catalyzed reactions
    • Kanner J. Nitric oxide and metal-catalyzed reactions. Methods Enzymol 1996; 269: 218-29.
    • (1996) Methods Enzymol , vol.269 , pp. 218-229
    • Kanner, J.1
  • 135
    • 0029445068 scopus 로고
    • Chemistry of nitric oxide: Biologically relevant aspects
    • Fukuto JM. Chemistry of nitric oxide: Biologically relevant aspects. Adv Pharmacol 1995; 134: 1-15.
    • (1995) Adv Pharmacol , vol.134 , pp. 1-15
    • Fukuto, J.M.1
  • 136
    • 0002555527 scopus 로고    scopus 로고
    • The chemical properties of nitric oxide and related nitrogen oxides (Chapter 2)
    • Ignarro LJ Ed, San Diego, Academic Press
    • Fukuto JM, Cho JY, Switzer CH. The chemical properties of nitric oxide and related nitrogen oxides (Chapter 2). In: Ignarro LJ Ed, Nitric oxide biology and pathobiology. San Diego, Academic Press 2000; 23-40.
    • (2000) Nitric oxide biology and pathobiology , pp. 23-40
    • Fukuto, J.M.1    Cho, J.Y.2    Switzer, C.H.3
  • 137
    • 0027253654 scopus 로고    scopus 로고
    • Ford PC, Wink DA, Stanbury DM. Autoxidation kinetics of aqueous nitric oxide. FEBS Lett 1993; 326(1,2,3): 1-3.
    • Ford PC, Wink DA, Stanbury DM. Autoxidation kinetics of aqueous nitric oxide. FEBS Lett 1993; 326(1,2,3): 1-3.
  • 138
    • 0032478104 scopus 로고    scopus 로고
    • Accelerated reaction of nitric oxide with O2 within the hydrophobic interior of biological membranes
    • Liu X, Miller MJS, Joshi MS, Thomas DD, Lancaster JR. Accelerated reaction of nitric oxide with O2 within the hydrophobic interior of biological membranes. Proc Natl Acad Sci USA 1998; 95(5): 2175-9.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.5 , pp. 2175-2179
    • Liu, X.1    Miller, M.J.S.2    Joshi, M.S.3    Thomas, D.D.4    Lancaster, J.R.5
  • 140
    • 0029037495 scopus 로고
    • The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
    • Pryor WA, Squadrito GL. The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide. Am J Physiol Lung Cell Mol Physiol 1995; 268: L699-722.
    • (1995) Am J Physiol Lung Cell Mol Physiol , vol.268
    • Pryor, W.A.1    Squadrito, G.L.2
  • 141
    • 0000892477 scopus 로고    scopus 로고
    • In Vivo aspects of nitric oxide (NO) chemistry: Does peroxynitrite (OONO) play a major role in cytotoxicity?
    • Fukuto JM, Ignarro LJ. In Vivo aspects of nitric oxide (NO) chemistry: Does peroxynitrite (OONO) play a major role in cytotoxicity? Acc Chem Res 1997; 30 (4): 149-52.
    • (1997) Acc Chem Res , vol.30 , Issue.4 , pp. 149-152
    • Fukuto, J.M.1    Ignarro, L.J.2
  • 142
    • 0032715834 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite. The ugly, the uglier and the not so good
    • Halliwell B, Zhao K, Whiteman M. Nitric oxide and peroxynitrite. The ugly, the uglier and the not so good. Free Rad Res 1999; 31: 651-69
    • (1999) Free Rad Res , vol.31 , pp. 651-669
    • Halliwell, B.1    Zhao, K.2    Whiteman, M.3
  • 143
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydrals. The cytotoxic potential of superoxide and nitric oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite oxidation of sulfhydrals. The cytotoxic potential of superoxide and nitric oxide. J Biol Chem 1991; 266(7): 4244-50.
    • (1991) J Biol Chem , vol.266 , Issue.7 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 144
    • 0028335587 scopus 로고
    • Peroxynitrite-mediated oxidation of albumin to the protein-thiyl free radical
    • Gatti RM, Radi R, Augusto O. Peroxynitrite-mediated oxidation of albumin to the protein-thiyl free radical. FEBS Lett 1994; 348(3): 287-90.
    • (1994) FEBS Lett , vol.348 , Issue.3 , pp. 287-290
    • Gatti, R.M.1    Radi, R.2    Augusto, O.3
  • 145
    • 0029939154 scopus 로고    scopus 로고
    • Characterization of sulfur-centered radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite. ESR-spin trapping and oxygen uptake studies
    • Karoui H, Hogg N, Frejaville C, Tordo P, Kalyanaraman B. Characterization of sulfur-centered radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite. ESR-spin trapping and oxygen uptake studies. J Biol Chem 1996; 271(11): 6000-9.
    • (1996) J Biol Chem , vol.271 , Issue.11 , pp. 6000-6009
    • Karoui, H.1    Hogg, N.2    Frejaville, C.3    Tordo, P.4    Kalyanaraman, B.5
  • 146
    • 0029680493 scopus 로고    scopus 로고
    • Lymar SV, Hurst JK. Carbon dioxide: Physiological catalyst for peroxynitrite-mediated cellular damage or cellular protectant? Chem Res Toxicol 1996; 9(5): 845-50.
    • Lymar SV, Hurst JK. Carbon dioxide: Physiological catalyst for peroxynitrite-mediated cellular damage or cellular protectant? Chem Res Toxicol 1996; 9(5): 845-50.
  • 147
    • 0030600565 scopus 로고    scopus 로고
    • Carbon dioxide catalysis of the rection of peroxynitrite with ethyl acetoacetate: An example of aliphatic nitration by peroxynitrite
    • Uppu RM, Pryor WA. Carbon dioxide catalysis of the rection of peroxynitrite with ethyl acetoacetate: An example of aliphatic nitration by peroxynitrite. Biochem Biophys Res Commun 1996; 229(3): 764-9.
    • (1996) Biochem Biophys Res Commun , vol.229 , Issue.3 , pp. 764-769
    • Uppu, R.M.1    Pryor, W.A.2
  • 149
    • 0000399717 scopus 로고
    • Photochemistry of nitric oxide adducts of water soluble iron(III) porphyrins and ferriberno-proteins by nanosecond laser photolysis
    • Hoshino M, Ozawa K, Seki H, Ford PC. Photochemistry of nitric oxide adducts of water soluble iron(III) porphyrins and ferriberno-proteins by nanosecond laser photolysis. J Am Chem Soc 1993; 115(21): 9568-75.
    • (1993) J Am Chem Soc , vol.115 , Issue.21 , pp. 9568-9575
    • Hoshino, M.1    Ozawa, K.2    Seki, H.3    Ford, P.C.4
  • 150
    • 0030752458 scopus 로고    scopus 로고
    • Redox modulation of iron regulatory proteins by peroxynitrite
    • Bouton C, Hirling H, Drapier JC. Redox modulation of iron regulatory proteins by peroxynitrite. J Biol Chem 1997; 272(32): 19969-75.
    • (1997) J Biol Chem , vol.272 , Issue.32 , pp. 19969-19975
    • Bouton, C.1    Hirling, H.2    Drapier, J.C.3
  • 151
    • 0030033203 scopus 로고    scopus 로고
    • Evidence that nitric oxide enhances cadmium toxicity by displacing the metal from metallothionein
    • Misra RR, Hochadel JF, Smith GT, Cook JC, Waalkes MP, Wink DA. Evidence that nitric oxide enhances cadmium toxicity by displacing the metal from metallothionein. Chem Res Toxicol 1996; 9(1): 326-32.
    • (1996) Chem Res Toxicol , vol.9 , Issue.1 , pp. 326-332
    • Misra, R.R.1    Hochadel, J.F.2    Smith, G.T.3    Cook, J.C.4    Waalkes, M.P.5    Wink, D.A.6
  • 152
    • 0028351149 scopus 로고
    • Nitric oxide destroys zinc-sulfur clusters inducing zinc release from metallothionein and inhibition of the zinc finger-type yeast transcription activator LAC9
    • Kroncke K-D, Fehsel K, Schmidt T, Zenke FT, Dasting I, Wesener JR, et al. Nitric oxide destroys zinc-sulfur clusters inducing zinc release from metallothionein and inhibition of the zinc finger-type yeast transcription activator LAC9. Biochem Biophys Res Commun 1994; 200(2): 1105-10.
    • (1994) Biochem Biophys Res Commun , vol.200 , Issue.2 , pp. 1105-1110
    • Kroncke, K.-D.1    Fehsel, K.2    Schmidt, T.3    Zenke, F.T.4    Dasting, I.5    Wesener, J.R.6
  • 153
    • 0028937652 scopus 로고
    • Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite
    • Crow JP, Beckman JS, McCord JM. Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite. Biochemistry 1995; 34(11): 3544-52.
    • (1995) Biochemistry , vol.34 , Issue.11 , pp. 3544-3552
    • Crow, J.P.1    Beckman, J.S.2    McCord, J.M.3
  • 154
    • 0034646456 scopus 로고    scopus 로고
    • The interaction of nitric oxide (NO) with the yeast transcription factor Acel: A model system for NO-protein thiol interactions with implications to metal metabolism
    • Shinyashiki M, Chiang KT, Switzer CH, Gralla EB, Valentine JS, Thiele DJ, Fukuto JM. The interaction of nitric oxide (NO) with the yeast transcription factor Acel: A model system for NO-protein thiol interactions with implications to metal metabolism. Proc Natl Acad Sci USA 2000; 97(6): 2491-6.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.6 , pp. 2491-2496
    • Shinyashiki, M.1    Chiang, K.T.2    Switzer, C.H.3    Gralla, E.B.4    Valentine, J.S.5    Thiele, D.J.6    Fukuto, J.M.7
  • 155
    • 0034657373 scopus 로고    scopus 로고
    • Effetts of nitric oxide on the copper-responsive transcription factor Acel in Saccharomyces cerevisiae: Cytotoxic and cytoprotective actions of
    • Chiang KT, Shinyashiki M, Switzer CH, Valentine JS, Gralla EB, Thiele DJ, et al. Effetts of nitric oxide on the copper-responsive transcription factor Acel in Saccharomyces cerevisiae: Cytotoxic and cytoprotective actions of NO. Arch Biochem Biophys 2000; 377: 296-303.
    • (2000) Arch Biochem Biophys , vol.377 , pp. 296-303
    • Chiang, K.T.1    Shinyashiki, M.2    Switzer, C.H.3    Valentine, J.S.4    Gralla, E.B.5    Thiele, D.J.6
  • 156
    • 0031029150 scopus 로고    scopus 로고
    • A novel reaction mechanism for the formation of S-nitrosothiol in vivo
    • Gow AJ, Buerk DG, Ischiropoulos H. A novel reaction mechanism for the formation of S-nitrosothiol in vivo. J Biol Chem 1997; 272(5): 2841-5
    • (1997) J Biol Chem , vol.272 , Issue.5 , pp. 2841-2845
    • Gow, A.J.1    Buerk, D.G.2    Ischiropoulos, H.3
  • 157
    • 0030948844 scopus 로고    scopus 로고
    • Mechanism for the inhibition of aldehyde dehydrogenase by nitric oxide
    • DeMaster EG, Redfern B, Quast BJ, Dahlseid T, Nagawawa HT. Mechanism for the inhibition of aldehyde dehydrogenase by nitric oxide. Alcohol 1997; 14(2): 181-89.
    • (1997) Alcohol , vol.14 , Issue.2 , pp. 181-189
    • DeMaster, E.G.1    Redfern, B.2    Quast, B.J.3    Dahlseid, T.4    Nagawawa, H.T.5
  • 158
    • 32244434531 scopus 로고    scopus 로고
    • Zhao YL, Houk KN. Thionitoxides, RSNHO*: The structure of the SNO moiety in S-Nitrosohemaglobin, a possible NO reservoir and transporter. J Am Chem Soc 2006; 128(5): 1422-3.
    • Zhao YL, Houk KN. Thionitoxides, RSNHO*: The structure of the SNO moiety in "S-Nitrosohemaglobin", a possible NO reservoir and transporter. J Am Chem Soc 2006; 128(5): 1422-3.
  • 159
    • 0032951905 scopus 로고    scopus 로고
    • Nitric oxide and iron proteins
    • Cooper CE. Nitric oxide and iron proteins. Biochem Biophys Acta 1999; 1411(2-3): 290-309.
    • (1999) Biochem Biophys Acta , vol.1411 , Issue.2-3 , pp. 290-309
    • Cooper, C.E.1
  • 160
    • 0029836494 scopus 로고    scopus 로고
    • Nitric oxide regulation of lipid oxidation reactions: Formation and analysis of nitrogen-containing oxidized lipid derivatives
    • Rubbo H, Freeman BA. Nitric oxide regulation of lipid oxidation reactions: Formation and analysis of nitrogen-containing oxidized lipid derivatives. Methods Enzymol 1996; 269: 385-94.
    • (1996) Methods Enzymol , vol.269 , pp. 385-394
    • Rubbo, H.1    Freeman, B.A.2
  • 161
    • 0025874048 scopus 로고
    • Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide. Arch Biochem Biophys 1991; 288(2): 481-7.
    • (1991) Arch Biochem Biophys , vol.288 , Issue.2 , pp. 481-487
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 162
    • 0026676388 scopus 로고
    • The simultaneous-generation of superoxide and nitric oxide can initiate lipid peroxidation in human low density lipoprotein
    • Darley-Usmar VM, Hogg N, O'Leary VJ, Wilson MT, Moncado S. The simultaneous-generation of superoxide and nitric oxide can initiate lipid peroxidation in human low density lipoprotein. Free Radic Res Commun 1992; 17(1): 9-20.
    • (1992) Free Radic Res Commun , vol.17 , Issue.1 , pp. 9-20
    • Darley-Usmar, V.M.1    Hogg, N.2    O'Leary, V.J.3    Wilson, M.T.4    Moncado, S.5
  • 163
    • 0036090811 scopus 로고    scopus 로고
    • Biological chemistry of carbon monoxide
    • Piantadosi CA. Biological chemistry of carbon monoxide. Antiox Red Sig 2002; 4: 259-70.
    • (2002) Antiox Red Sig , vol.4 , pp. 259-270
    • Piantadosi, C.A.1
  • 164
    • 0023000351 scopus 로고
    • Mitochondrial oxygenation of carbon monoxide
    • Young LJ, Caughey WS. Mitochondrial oxygenation of carbon monoxide. Biochem J 1986; 239: 225-7.
    • (1986) Biochem J , vol.239 , pp. 225-227
    • Young, L.J.1    Caughey, W.S.2
  • 166
    • 0031758561 scopus 로고    scopus 로고
    • Platt JL, Nath KA. Herne oxygenase: Protective gene or Trojan horse. Nature Med 1998; 4: 1364-5.
    • Platt JL, Nath KA. Herne oxygenase: Protective gene or Trojan horse. Nature Med 1998; 4: 1364-5.
  • 167
    • 0036671624 scopus 로고    scopus 로고
    • Heme degradation and human disease: Diversity is the soul of life
    • Shibahara S, Kitamuro T, Takahashi K. Heme degradation and human disease: Diversity is the soul of life. Antioxid Redox Signal 2002; 4: 593-602.
    • (2002) Antioxid Redox Signal , vol.4 , pp. 593-602
    • Shibahara, S.1    Kitamuro, T.2    Takahashi, K.3
  • 168
    • 0036007306 scopus 로고    scopus 로고
    • The saga of leucine zippers continues in response to oxidative stress
    • Otterbein LE, Choi AMK.- The saga of leucine zippers continues in response to oxidative stress. Am J Respir Cell Mol Biol, 2000; 2: 161-3.
    • (2000) Am J Respir Cell Mol Biol , vol.2 , pp. 161-163
    • Otterbein, L.E.1    Choi, A.M.K.2
  • 169
    • 0035983247 scopus 로고    scopus 로고
    • Heme oxygenase-1, the emerging molecule has arrived
    • Morse D, Choi AMK. Heme oxygenase-1, the emerging molecule has arrived. Am J Resp Cell Mol Biol 2002; 27: 8-16.
    • (2002) Am J Resp Cell Mol Biol , vol.27 , pp. 8-16
    • Morse, D.1    Choi, A.M.K.2
  • 170
    • 1942539932 scopus 로고    scopus 로고
    • Marked developmental changes in heme oxygenase-1 (HO-1) expression in the mouse placenta: Correlation between HO-1 expression and placental development
    • Watanabe S, Akagi R, Mori M, Tsuchiya T, Sassa S. Marked developmental changes in heme oxygenase-1 (HO-1) expression in the mouse placenta: correlation between HO-1 expression and placental development. Placenta 2004; 25(5): 387-95.
    • (2004) Placenta , vol.25 , Issue.5 , pp. 387-395
    • Watanabe, S.1    Akagi, R.2    Mori, M.3    Tsuchiya, T.4    Sassa, S.5
  • 172
    • 0033732757 scopus 로고    scopus 로고
    • Mechanism of heme degradation by heme xoygenase
    • Yoshida T, Migitar CT. Mechanism of heme degradation by heme xoygenase. J Inorg Biochem 2000; 82: 33-41.
    • (2000) J Inorg Biochem , vol.82 , pp. 33-41
    • Yoshida, T.1    Migitar, C.T.2
  • 174
    • 0037180940 scopus 로고    scopus 로고
    • Heme-oxygenase overexpression protects rat hearts from cold ischemia/ reperfusion injury via an anti-apoptotic pathway
    • Katori M, Buelow R, Ke B, Ma J, Cotto AJ, Iyer S, et al. Heme-oxygenase overexpression protects rat hearts from cold ischemia/ reperfusion injury via an anti-apoptotic pathway. Transplantation 2002; 73: 287-92.
    • (2002) Transplantation , vol.73 , pp. 287-292
    • Katori, M.1    Buelow, R.2    Ke, B.3    Ma, J.4    Cotto, A.J.5    Iyer, S.6
  • 175
    • 0034705371 scopus 로고    scopus 로고
    • Prevention of hypoxia-induced pulmonary hypertension by enhancement of endogenous heme oxygenase
    • Christou H, Morita T, Hsieh CM, Koike H, Arkonac B, Perrella M, et al. Prevention of hypoxia-induced pulmonary hypertension by enhancement of endogenous heme oxygenase. Circ Res 2001; 86: 1224-9.
    • (2001) Circ Res , vol.86 , pp. 1224-1229
    • Christou, H.1    Morita, T.2    Hsieh, C.M.3    Koike, H.4    Arkonac, B.5    Perrella, M.6
  • 176
    • 0036019201 scopus 로고    scopus 로고
    • Heme oxygenase 1 gene transfer prevents CD95/fas ligand-mediated apoptosis and improves allograft survival via carbon monoxide signaling pathway
    • Ke B, Buelow R, Shen X-D, Melinek J, Amersi F, Gao F, et al. Heme oxygenase 1 gene transfer prevents CD95/fas ligand-mediated apoptosis and improves allograft survival via carbon monoxide signaling pathway. Hum Gene Ther 2002; 1: 1189-99.
    • (2002) Hum Gene Ther , vol.1 , pp. 1189-1199
    • Ke, B.1    Buelow, R.2    Shen, X.-D.3    Melinek, J.4    Amersi, F.5    Gao, F.6
  • 177
  • 179
    • 0035039579 scopus 로고    scopus 로고
    • Paradoxical rescue from ischemic lung injury by inhaled carbon monoxide driven by derepression of fibrinolysis
    • Fujita T, Toda K, Karimova A, Yan S-F, Naka Y, Yet S-F, et al. Paradoxical rescue from ischemic lung injury by inhaled carbon monoxide driven by derepression of fibrinolysis. Nat Med 2001; 7: 598-604.
    • (2001) Nat Med , vol.7 , pp. 598-604
    • Fujita, T.1    Toda, K.2    Karimova, A.3    Yan, S.-F.4    Naka, Y.5    Yet, S.-F.6
  • 180
    • 0034071424 scopus 로고    scopus 로고
    • Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway
    • Otterbein LE, Bach FH, Alam J, Soares M, Tao Lu H, Wysk M, et al. Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway. Nat Med 2000; 6: 422-8.
    • (2000) Nat Med , vol.6 , pp. 422-428
    • Otterbein, L.E.1    Bach, F.H.2    Alam, J.3    Soares, M.4    Tao, L.H.5    Wysk, M.6
  • 181
    • 0033452295 scopus 로고    scopus 로고
    • Heme oxygenase-1: A redoubtable response that limits reperfusion injury in the transplanted adipose liver
    • Nath KA. Heme oxygenase-1: A redoubtable response that limits reperfusion injury in the transplanted adipose liver. J Clin Invest 1999, 104(11): 1485-6.
    • (1999) J Clin Invest , vol.104 , Issue.11 , pp. 1485-1486
    • Nath, K.A.1
  • 182
    • 0031041377 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase gene in response to hypoxia
    • Lee PJ, Jiang BH, Chin NV, Iyer J, Alam GL, Choi AM. Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase gene in response to hypoxia. J Biol Chem 1997; 272(9): 5375-81.
    • (1997) J Biol Chem , vol.272 , Issue.9 , pp. 5375-5381
    • Lee, P.J.1    Jiang, B.H.2    Chin, N.V.3    Iyer, J.4    Alam, G.L.5    Choi, A.M.6
  • 183
    • 0027534465 scopus 로고
    • Cytokine induction of haem oxygenase mRNA in mouse liver: Interleukin 1 transcriptionally activates haem oxygenase
    • Rizzardini M, Terao M. Falciani F, Cantoni L. Cytokine induction of haem oxygenase mRNA in mouse liver: Interleukin 1 transcriptionally activates haem oxygenase. Biochem J 1993; 290: 343-7.
    • (1993) Biochem J , vol.290 , pp. 343-347
    • Rizzardini, M.1    Terao, M.2    Falciani, F.3    Cantoni, L.4
  • 187
    • 0141707960 scopus 로고    scopus 로고
    • Suppression of inflammatory cytokine production by carbon monoxide involves the JNK pathway and AP-1
    • Morse D, Pischke SE, Zhou Z, Davis RJ, Flavell RA, Loop T, et al. Suppression of inflammatory cytokine production by carbon monoxide involves the JNK pathway and AP-1. J Biol Chem 2003; 278(39): 36993-8.
    • (2003) J Biol Chem , vol.278 , Issue.39 , pp. 36993-36998
    • Morse, D.1    Pischke, S.E.2    Zhou, Z.3    Davis, R.J.4    Flavell, R.A.5    Loop, T.6
  • 188
    • 0036845556 scopus 로고    scopus 로고
    • Two's company, three's a crowd: Can H2S be the third endogenous gaseous transmitter?
    • Wang R. Two's company, three's a crowd: Can H2S be the third endogenous gaseous transmitter? FASEB J 2002; 16(13): 1792-8.
    • (2002) FASEB J , vol.16 , Issue.13 , pp. 1792-1798
    • Wang, R.1
  • 189
    • 0042763556 scopus 로고    scopus 로고
    • The gasotransmitter role of hydrogen sulfide
    • Wang R. The gasotransmitter role of hydrogen sulfide. Antioxid Redox Signal 2003; 5(4): 493-501.
    • (2003) Antioxid Redox Signal , vol.5 , Issue.4 , pp. 493-501
    • Wang, R.1
  • 190
    • 0001874683 scopus 로고
    • Reduction potentials involving inorganic free radicals in aqueous solution
    • Stanbury DM. Reduction potentials involving inorganic free radicals in aqueous solution. Adv Inorg Chem 1989; 33: 69-138.
    • (1989) Adv Inorg Chem , vol.33 , pp. 69-138
    • Stanbury, D.M.1
  • 191
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: Lipid peroxidation, alpha-tocopherol and ascorbate
    • Buettner GR. The pecking order of free radicals and antioxidants: Lipid peroxidation, alpha-tocopherol and ascorbate. Arch Biochem Biophys 1993; 300(2): 535-43.
    • (1993) Arch Biochem Biophys , vol.300 , Issue.2 , pp. 535-543
    • Buettner, G.R.1
  • 192
    • 3042651344 scopus 로고    scopus 로고
    • Endogenous production of hydrogen sulfide in mamals
    • Kamoun P. Endogenous production of hydrogen sulfide in mamals. Amino Acids 2004; 26: 243-54.
    • (2004) Amino Acids , vol.26 , pp. 243-254
    • Kamoun, P.1
  • 193
    • 9744276776 scopus 로고    scopus 로고
    • Redox regulation and reaction mechanism of human cystathionine-beta-synthase: A PLP-dependent hemesensor protein
    • Banerjee R, Zou CG. Redox regulation and reaction mechanism of human cystathionine-beta-synthase: A PLP-dependent hemesensor protein. Arch Biochem Biophys 2005; 433(1): 144-56.
    • (2005) Arch Biochem Biophys , vol.433 , Issue.1 , pp. 144-156
    • Banerjee, R.1    Zou, C.G.2
  • 194
    • 0037044721 scopus 로고    scopus 로고
    • A novel enhancing mechanism for hydrogen sulfide-producing activity of cystathionine beta-synthase
    • Eto K, Kimura H. A novel enhancing mechanism for hydrogen sulfide-producing activity of cystathionine beta-synthase. J Biol Chem 2002; 277(45): 42680-5.
    • (2002) J Biol Chem , vol.277 , Issue.45 , pp. 42680-42685
    • Eto, K.1    Kimura, H.2
  • 195
    • 0037927972 scopus 로고    scopus 로고
    • Hydrogen sulfide induces serum-independent cell cycle entry in nontransformed rat intestinal epithelial cells
    • Deplancke B, Gaskins HR. Hydrogen sulfide induces serum-independent cell cycle entry in nontransformed rat intestinal epithelial cells. FASEB J 2003; 17(10): 1310-2.
    • (2003) FASEB J , vol.17 , Issue.10 , pp. 1310-1312
    • Deplancke, B.1    Gaskins, H.R.2
  • 196
    • 0031589557 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide
    • Hosoki R, Matsuki N, Kimura H. The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide. Biochem Biophys Res Commun 1997; 237: 527-31.
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 527-531
    • Hosoki, R.1    Matsuki, N.2    Kimura, H.3
  • 198
    • 0035893841 scopus 로고    scopus 로고
    • Characterization of NO binding to human cystathionine beta-synthase: Possible implication of the effects of CO and NO binding to the human enzyme
    • Taoka S, Banerjee R. Characterization of NO binding to human cystathionine beta-synthase: Possible implication of the effects of CO and NO binding to the human enzyme. J Inorg Biochem 2001; 87: 245-51
    • (2001) J Inorg Biochem , vol.87 , pp. 245-251
    • Taoka, S.1    Banerjee, R.2
  • 199
    • 0020082098 scopus 로고
    • The development of cystathionase activity during the first year of life
    • Zlotkin SH, Anderson GH. The development of cystathionase activity during the first year of life. Pediatr Res 1982; 16: 65-8.
    • (1982) Pediatr Res , vol.16 , pp. 65-68
    • Zlotkin, S.H.1    Anderson, G.H.2
  • 200
    • 0030894008 scopus 로고    scopus 로고
    • L-cysteine membolism in guinea pig and rat tissues
    • Wrobel M, Ubuka T, Yao WB, Abe T. L-cysteine membolism in guinea pig and rat tissues. Comp Biochem Physiol 1997; 116B: 223-6.
    • (1997) Comp Biochem Physiol , vol.116 B , pp. 223-226
    • Wrobel, M.1    Ubuka, T.2    Yao, W.B.3    Abe, T.4
  • 201
    • 0014931232 scopus 로고
    • Absence of cystathionase in human fetal liver: Is cystine essential?
    • Sturman JA, Gaull G, Raiha NC. Absence of cystathionase in human fetal liver: Is cystine essential? Science 1970, 169: 74-6.
    • (1970) Science , vol.169 , pp. 74-76
    • Sturman, J.A.1    Gaull, G.2    Raiha, N.C.3
  • 202
    • 0015357403 scopus 로고
    • Developm mammalian sulfur metabolism: Absence of cystathionase in human fetal tissues
    • Gaull G, Sturman JA, Raiha NC. Developm mammalian sulfur metabolism: absence of cystathionase in human fetal tissues. Pediatr Res 1972; 6: 538-47.
    • (1972) Pediatr Res , vol.6 , pp. 538-547
    • Gaull, G.1    Sturman, J.A.2    Raiha, N.C.3
  • 203
    • 0034176207 scopus 로고    scopus 로고
    • Human cystathionine gamma lyase: Developmental and in vitro expression of two isoforms
    • Levonen AL, Lapatto R, Saksela M, Raivio KO. Human cystathionine gamma lyase: Developmental and in vitro expression of two isoforms. Biochem J 2000; 347: 291-5.
    • (2000) Biochem J , vol.347 , pp. 291-295
    • Levonen, A.L.1    Lapatto, R.2    Saksela, M.3    Raivio, K.O.4
  • 204
    • 0031666759 scopus 로고    scopus 로고
    • Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: Confocal. laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis
    • Nagahara N, Ito T, Kitamura H, Nishino, T. Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: Confocal. laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis. Histochem Cell Biol, 1998; 110: 243-50.
    • (1998) Histochem Cell Biol , vol.110 , pp. 243-250
    • Nagahara, N.1    Ito, T.2    Kitamura, H.3    Nishino, T.4
  • 205
    • 0015581881 scopus 로고
    • Metabolism of sulfur containing amino acids in a patient excreting β-mercaptolactate-cysteine disulfide
    • Crawhall JC, Purkiss P, Stanbury JP. Metabolism of sulfur containing amino acids in a patient excreting β-mercaptolactate-cysteine disulfide. Biochem Med 1973; 7:103-11.
    • (1973) Biochem Med , vol.7 , pp. 103-111
    • Crawhall, J.C.1    Purkiss, P.2    Stanbury, J.P.3
  • 206
    • 0033364449 scopus 로고    scopus 로고
    • The effect of nitrogen oxide level modulation on the content of thiol compounds and anaerobic sulfur metabolism in mice brains
    • Sokolowska M, Wlodek L, Srebro Z, Wrobel M. The effect of nitrogen oxide level modulation on the content of thiol compounds and anaerobic sulfur metabolism in mice brains. Neurobiology 1999; 7: 461-77.
    • (1999) Neurobiology , vol.7 , pp. 461-477
    • Sokolowska, M.1    Wlodek, L.2    Srebro, Z.3    Wrobel, M.4
  • 208
    • 0034614354 scopus 로고    scopus 로고
    • Hydrogen sulfide induces cyclic AMP and modulates the NMDA receptor
    • Kimura M. Hydrogen sulfide induces cyclic AMP and modulates the NMDA receptor. Biochem Biophys Res Commun 2000; 267: 129-33.
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 129-133
    • Kimura, M.1
  • 209
    • 0030911620 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase and protein kinase c phosphorylate N-methyl D-aspartate receptors at different sites
    • Leonard AS, Hell JS. Cyclic AMP-dependent protein kinase and protein kinase c phosphorylate N-methyl D-aspartate receptors at different sites. J Biol Chem 1997; 272(18): 12107-15.
    • (1997) J Biol Chem , vol.272 , Issue.18 , pp. 12107-12115
    • Leonard, A.S.1    Hell, J.S.2
  • 210
    • 0036700930 scopus 로고    scopus 로고
    • Hydrogen sulfide as a neuromodulator
    • Kimura M. Hydrogen sulfide as a neuromodulator. Mol Neurobiol 2002; 26: 13-9.
    • (2002) Mol Neurobiol , vol.26 , pp. 13-19
    • Kimura, M.1
  • 211
    • 2442655642 scopus 로고    scopus 로고
    • Hydrogen sulfide induces calcium waves in astrocytes
    • Nagai Y, Tsugane M, Oka J, Kimura H. Hydrogen sulfide induces calcium waves in astrocytes. FASEB J 2004; 18: 557-9.
    • (2004) FASEB J , vol.18 , pp. 557-559
    • Nagai, Y.1    Tsugane, M.2    Oka, J.3    Kimura, H.4
  • 212
    • 0036073185 scopus 로고    scopus 로고
    • 2S-induced vasorelaxation and underlying cellular and molecular mechanisms
    • 2S-induced vasorelaxation and underlying cellular and molecular mechanisms. Am J Physiol 2002; 283: H474-80.
    • (2002) Am J Physiol , vol.283
    • Zhao, W.1    Wang, R.2
  • 213
    • 0036737715 scopus 로고    scopus 로고
    • The smooth muscle relaxant effect of hydrogen sulphide in vitro: Evidence for a physiological role to control intestinal contractility
    • Teague B, Asiedu S, Moore PK. The smooth muscle relaxant effect of hydrogen sulphide in vitro: Evidence for a physiological role to control intestinal contractility. Br J Pharmacol 2002; 137: 139-45.
    • (2002) Br J Pharmacol , vol.137 , pp. 139-145
    • Teague, B.1    Asiedu, S.2    Moore, P.K.3
  • 214
    • 33745678257 scopus 로고    scopus 로고
    • Molecular and functional differences between heart mKv1.7 channel isoforms
    • Finol-Urdaneta RK, Struver N, Terlau H. Molecular and functional differences between heart mKv1.7 channel isoforms. J Gen Physiol 2006; 128(1): 133-45.
    • (2006) J Gen Physiol , vol.128 , Issue.1 , pp. 133-145
    • Finol-Urdaneta, R.K.1    Struver, N.2    Terlau, H.3
  • 215
    • 0036125211 scopus 로고    scopus 로고
    • Oxidative stress and potassium channel function
    • Liu Y, Gutterman DD. Oxidative stress and potassium channel function. Clin Exp Pharmacol Physiol 2002; 29(4): 305-11.
    • (2002) Clin Exp Pharmacol Physiol , vol.29 , Issue.4 , pp. 305-311
    • Liu, Y.1    Gutterman, D.D.2
  • 216
    • 33749182774 scopus 로고    scopus 로고
    • Hydrogen sulfide mediates hypoxia-induced relaxation of trout urinary bladder smooth muscle
    • Dombkowski RA, Doellman MM, Head SK, Olson KR. Hydrogen sulfide mediates hypoxia-induced relaxation of trout urinary bladder smooth muscle. J Exp Biol 2006; 209(Pt. 16): 3234-40.
    • (2006) J Exp Biol , vol.209 , Issue.PART. 16 , pp. 3234-3240
    • Dombkowski, R.A.1    Doellman, M.M.2    Head, S.K.3    Olson, K.R.4
  • 217
    • 33749181930 scopus 로고    scopus 로고
    • Hydrogen sulfide as an oxygen sensor/transducer in vertebrate hypoxic vasoconstriction and hypoxic vasodilation
    • Olson KR, Dombkowski RA, Russell MJ, Doellman MM, Head SK, Whitfield NL, et al. Hydrogen sulfide as an oxygen sensor/transducer in vertebrate hypoxic vasoconstriction and hypoxic vasodilation. J Exp Biol 2006; 209(Pt 20): 4011-23.
    • (2006) J Exp Biol , vol.209 , Issue.PART 20 , pp. 4011-4023
    • Olson, K.R.1    Dombkowski, R.A.2    Russell, M.J.3    Doellman, M.M.4    Head, S.K.5    Whitfield, N.L.6
  • 218
    • 33645102456 scopus 로고    scopus 로고
    • Evidence for the formation of a novel nitrosothiol from the gaseous mediators nitric oxide and hydrogeti sulphide
    • Whiteman M, Li L, Kostetsid I, Chu SH, Siau JL, Bhatia M, et al. Evidence for the formation of a novel nitrosothiol from the gaseous mediators nitric oxide and hydrogeti sulphide. Biochem Biophys Res Commun 2006; 343(1): 303-110.
    • (2006) Biochem Biophys Res Commun , vol.343 , Issue.1 , pp. 303-110
    • Whiteman, M.1    Li, L.2    Kostetsid, I.3    Chu, S.H.4    Siau, J.L.5    Bhatia, M.6
  • 219
    • 0033605676 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide
    • Huang LE, Willmore WG, Gu J, Goldberg MA, Bunn HF. Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide. J Biol Chem 1999; (13): 9038-44.
    • (1999) J Biol Chem , vol.13 , pp. 9038-9044
    • Huang, L.E.1    Willmore, W.G.2    Gu, J.3    Goldberg, M.A.4    Bunn, H.F.5
  • 220
    • 0031041377 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates tianscriptional activation of the heme oxygenase-1
    • Lee PJ, Jiang BH, Chin BY, Iyer NV, Alam J, Semenza GL, et al. Hypoxia-inducible factor-1 mediates tianscriptional activation of the heme oxygenase-1. J Biol Chem 1997; 272(9): 5375-81.
    • (1997) J Biol Chem , vol.272 , Issue.9 , pp. 5375-5381
    • Lee, P.J.1    Jiang, B.H.2    Chin, B.Y.3    Iyer, N.V.4    Alam, J.5    Semenza, G.L.6
  • 221
    • 23744443462 scopus 로고    scopus 로고
    • HIF-1 activation attenuates postischemic myocardial injury: Role for heme oxygenase-1 in modulating microvascular chemokine generation
    • Ockaili R, Nataraja R, Salloam F, Fisher BJ, Jones D, Fowler AA III, et al. HIF-1 activation attenuates postischemic myocardial injury: role for heme oxygenase-1 in modulating microvascular chemokine generation: Am J Physiol Heart Circ Physiol 2005; 289: H542-8.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Ockaili, R.1    Nataraja, R.2    Salloam, F.3    Fisher, B.J.4    Jones, D.5    Fowler III, A.A.6
  • 222
    • 33745115862 scopus 로고    scopus 로고
    • Hydrogen sulfide inhibits nitric oxide production and nuclear factor kB via heme oxygenase-' expression in RAW264.7 macrophages stimulated with lipopolysaccharide
    • Oh GS, Pae HO, Lee BS Kim BN, Kim JM, Kim MR, et al. Hydrogen sulfide inhibits nitric oxide production and nuclear factor kB via heme oxygenase-' expression in RAW264.7 macrophages stimulated with lipopolysaccharide. Free Rad Biol Med 2006; 41: 106-19.
    • (2006) Free Rad Biol Med , vol.41 , pp. 106-119
    • Oh, G.S.1    Pae, H.O.2    Lee, B.S.3    Kim, B.N.4    Kim, J.M.5    Kim, M.R.6
  • 223
    • 0023234054 scopus 로고
    • Hydrogen peroxide elicits pulmonary arterial relaxation and guanylate cyclase activation
    • Burke TM, Wolin MS. Hydrogen peroxide elicits pulmonary arterial relaxation and guanylate cyclase activation. Am J Physiol Heart Circ Physiol 1987; 252: H721-32.
    • (1987) Am J Physiol Heart Circ Physiol , vol.252
    • Burke, T.M.1    Wolin, M.S.2
  • 224
    • 22444433668 scopus 로고    scopus 로고
    • Oxidant and redox signaling in vascular oxygen sensing mechanisms: Basic concepts, current controversies, and potential importance of cytosolic NADPH
    • Wolin MS, Ahmad M, Gupte SA. Oxidant and redox signaling in vascular oxygen sensing mechanisms: Basic concepts, current controversies, and potential importance of cytosolic NADPH. Am J Physiol Lung Cell Mol Physiol 2005; 289: L159-73.
    • (2005) Am J Physiol Lung Cell Mol Physiol , vol.289
    • Wolin, M.S.1    Ahmad, M.2    Gupte, S.A.3
  • 225
    • 29844442868 scopus 로고    scopus 로고
    • Carbon monoxide: Endogenous production, physiological functions and pharmacological applications
    • Wu L, Wang R. Carbon monoxide: Endogenous production, physiological functions and pharmacological applications. Pharmacol Rev 2005; 57(4): 585-630.
    • (2005) Pharmacol Rev , vol.57 , Issue.4 , pp. 585-630
    • Wu, L.1    Wang, R.2
  • 226
    • 0030669601 scopus 로고    scopus 로고
    • Regulation of heme oxygenase-1 gene expression in vascular smooth muscle cells by nitric oxide
    • Hartsfield CL, Alam J, Cook JL, Choi AMK. Regulation of heme oxygenase-1 gene expression in vascular smooth muscle cells by nitric oxide. Am J Physiol 1997; 273: L980-8.
    • (1997) Am J Physiol , vol.273
    • Hartsfield, C.L.1    Alam, J.2    Cook, J.L.3    Choi, A.M.K.4
  • 227
    • 0032918830 scopus 로고    scopus 로고
    • Nitric oxide induces heme oxygenase-1 gene expression in mesangial cells
    • Datta PK, Lianos EA. Nitric oxide induces heme oxygenase-1 gene expression in mesangial cells. Kidney Int 1999; 55(5): 1734-9.
    • (1999) Kidney Int , vol.55 , Issue.5 , pp. 1734-1739
    • Datta, P.K.1    Lianos, E.A.2
  • 229
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-senstitive stabilization of its alpha subunit
    • Huang LE, Arany Z, Livingston DM, Bunn HF. Activation of hypoxia-inducible transcription factor depends primarily upon redox-senstitive stabilization of its alpha subunit. J Biol Chem 1996; 271(50): 32253-9.
    • (1996) J Biol Chem , vol.271 , Issue.50 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 230
    • 33947628672 scopus 로고    scopus 로고
    • Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species
    • Zuckerbraun BS, Chin BY, Bilban M, de Costa d'Avila J, Rao J, Billiar TR, et al. Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species. FASEB J 2007; 21(4): 1099-106.
    • (2007) FASEB J , vol.21 , Issue.4 , pp. 1099-1106
    • Zuckerbraun, B.S.1    Chin, B.Y.2    Bilban, M.3    de Costa d'Avila, J.4    Rao, J.5    Billiar, T.R.6
  • 231
    • 34249782874 scopus 로고    scopus 로고
    • The mechanisms of cytochrome c oxidase inhibition by nitric oxide
    • Antunes F, Cadenas E. The mechanisms of cytochrome c oxidase inhibition by nitric oxide. Front Biosci 2007; 12: 975-85.
    • (2007) Front Biosci , vol.12 , pp. 975-985
    • Antunes, F.1    Cadenas, E.2
  • 232
    • 0016742498 scopus 로고
    • 3. Isosteric and allosteric shifts of the reduced α-peak
    • 3. Isosteric and allosteric shifts of the reduced α-peak. Biochim Biophys Acta 1975; 396: 24-35.
    • (1975) Biochim Biophys Acta , vol.396 , pp. 24-35
    • Nicholls, P.1
  • 233
    • 15544369982 scopus 로고    scopus 로고
    • Developmental origins of the metabolic syndrome: Prediction, plasticity, and programming
    • McMillen IC, Robinson JS. Developmental origins of the metabolic syndrome: Prediction, plasticity, and programming. Physiol Rev 2005; 85(2): 571-633.
    • (2005) Physiol Rev , vol.85 , Issue.2 , pp. 571-633
    • McMillen, I.C.1    Robinson, J.S.2
  • 234
    • 0032694302 scopus 로고    scopus 로고
    • The broad spectrum of responses to oxidants in proliferating cells: A new paradigm for oxidative stress
    • Davies KJA. The broad spectrum of responses to oxidants in proliferating cells: A new paradigm for oxidative stress. IUBMB Life 1999; 48: 41-7
    • (1999) IUBMB Life , vol.48 , pp. 41-47
    • Davies, K.J.A.1
  • 235
    • 0018028225 scopus 로고
    • The effect of oxygen on the development of preimplantation mouse embryos in vitro
    • Quinn P, Harlow GM. The effect of oxygen on the development of preimplantation mouse embryos in vitro. J Exp Zool 1978; 206: 73-80
    • (1978) J Exp Zool , vol.206 , pp. 73-80
    • Quinn, P.1    Harlow, G.M.2
  • 236
    • 33846820500 scopus 로고    scopus 로고
    • The role of oxygen in rummant preimplantation embryo development and metabolism
    • Harvey AJ. The role of oxygen in rummant preimplantation embryo development and metabolism. Anim Reprod Sci 2007; 98: 113-28.
    • (2007) Anim Reprod Sci , vol.98 , pp. 113-128
    • Harvey, A.J.1
  • 237
    • 0014735447 scopus 로고
    • Effects of different oxygen concentrations on the development of rat embryos in culture
    • New DAT, Coppola PT. Effects of different oxygen concentrations on the development of rat embryos in culture. J Reprod Fertil 1970; 21: 109-18.
    • (1970) J Reprod Fertil , vol.21 , pp. 109-118
    • New, D.A.T.1    Coppola, P.T.2
  • 238
    • 0014782967 scopus 로고
    • Development of explanted rat fetuses in hyperbaric oxygen
    • New DAT, Coppola PT. Development of explanted rat fetuses in hyperbaric oxygen. Teratology 1970; 3: 153-62.
    • (1970) Teratology , vol.3 , pp. 153-162
    • New, D.A.T.1    Coppola, P.T.2
  • 239
    • 0022919381 scopus 로고
    • Malformations induced in cultured rat embryos by enzymatically generated active oxygen species
    • Jenkinson PC, Anderson D, Gangolli SD. Malformations induced in cultured rat embryos by enzymatically generated active oxygen species. Teratog Carcinog Mutagen 1986; 6: 547-54.
    • (1986) Teratog Carcinog Mutagen , vol.6 , pp. 547-554
    • Jenkinson, P.C.1    Anderson, D.2    Gangolli, S.D.3
  • 240
    • 0030945198 scopus 로고    scopus 로고
    • Aerobic glycolysis by proliferating cells: A protective strategy against reactive oxygen species
    • Brand KA, Hermfisse U. Aerobic glycolysis by proliferating cells: A protective strategy against reactive oxygen species. FASEB J 1997; 11: 388-95.
    • (1997) FASEB J , vol.11 , pp. 388-395
    • Brand, K.A.1    Hermfisse, U.2
  • 241
    • 0030944808 scopus 로고    scopus 로고
    • Carbon monoxide and the embryo
    • Robkin MA. Carbon monoxide and the embryo. Int J Dev Biol 1997; 41(2):283-9.
    • (1997) Int J Dev Biol , vol.41 , Issue.2 , pp. 283-289
    • Robkin, M.A.1
  • 242
    • 0009894925 scopus 로고
    • Teratogenic effects of hyperbaric oxygen
    • Ferm VH. Teratogenic effects of hyperbaric oxygen. Proc Soc Exp Biol Med 1964; 116: 975-6.
    • (1964) Proc Soc Exp Biol Med , vol.116 , pp. 975-976
    • Ferm, V.H.1
  • 243
    • 0015693556 scopus 로고
    • Malformations in rabbits following hyperbaric oxygenation
    • Grote W, Wagner WD. Malformations in rabbits following hyperbaric oxygenation. Klin Wochenschr 1973; 51: 248-50.
    • (1973) Klin Wochenschr , vol.51 , pp. 248-250
    • Grote, W.1    Wagner, W.D.2
  • 244
    • 0000187161 scopus 로고
    • Retrolental fibroplasias and prematurity in newborn rabbits induced by maternal hyperoxia
    • Fujikura R. Retrolental fibroplasias and prematurity in newborn rabbits induced by maternal hyperoxia. Am J Obstet Gynecol 1964; 90: 854-8.
    • (1964) Am J Obstet Gynecol , vol.90 , pp. 854-858
    • Fujikura, R.1
  • 245
    • 33845741242 scopus 로고    scopus 로고
    • The cellular basis for diverse responses to oxygen
    • Chandel NS, Budinger GR. The cellular basis for diverse responses to oxygen. Free Rad Biol Med 2007; 42(2): 165-74.
    • (2007) Free Rad Biol Med , vol.42 , Issue.2 , pp. 165-174
    • Chandel, N.S.1    Budinger, G.R.2
  • 246
    • 34247572370 scopus 로고    scopus 로고
    • VEGF-induced heme oxygenase-1 confers cytoprotection from lethal hyperoxia in vivo
    • Siner JM, Jiang G, Cohen ZI, Shan P, Zhang X, Lee CG, et al. VEGF-induced heme oxygenase-1 confers cytoprotection from lethal hyperoxia in vivo. FASEB J 2007; 21(7): 1422-32.
    • (2007) FASEB J , vol.21 , Issue.7 , pp. 1422-1432
    • Siner, J.M.1    Jiang, G.2    Cohen, Z.I.3    Shan, P.4    Zhang, X.5    Lee, C.G.6
  • 247
    • 33847291917 scopus 로고    scopus 로고
    • Carbon monoxide protects against hyperoxia-induced endothelial cell apoptosis by inhibiting reactive oxygen species formation
    • Wang X, Wang Y, Jiang G, Zhang SS, Otterbein LE, Fu XY, et al. Carbon monoxide protects against hyperoxia-induced endothelial cell apoptosis by inhibiting reactive oxygen species formation. J Biol Chem 2007; 282(3):1718-26.
    • (2007) J Biol Chem , vol.282 , Issue.3 , pp. 1718-1726
    • Wang, X.1    Wang, Y.2    Jiang, G.3    Zhang, S.S.4    Otterbein, L.E.5    Fu, X.Y.6
  • 248
    • 3242660994 scopus 로고    scopus 로고
    • Inhaled nitric oxide attenuates pulmonary hypertension and improves lung growth in infant rats after neonatal treatment with a VEGF receptor inhibitor
    • Tang JR, Markham NE, Lin YJ, McMurtry IF, Maxey A, Kinsella JP, et al. Inhaled nitric oxide attenuates pulmonary hypertension and improves lung growth in infant rats after neonatal treatment with a VEGF receptor inhibitor. Am J Physiol Lung Cell Mol Physiol 2004; 287: L344-51.
    • (2004) Am J Physiol Lung Cell Mol Physiol , vol.287
    • Tang, J.R.1    Markham, N.E.2    Lin, Y.J.3    McMurtry, I.F.4    Maxey, A.5    Kinsella, J.P.6
  • 251
    • 36349020518 scopus 로고    scopus 로고
    • Reactive oxygen species in the production of congenital malformations by known teratogenic agents and maternal conditions
    • Forman HJ, Fukuto J, Torres M Eds, Boston, Kluwer
    • Machado AF, Scott WJ, Collins MD. Reactive oxygen species in the production of congenital malformations by known teratogenic agents and maternal conditions. In: Forman HJ, Fukuto J, Torres M Eds, Signal transduction by reactive oxygen and nitrogen species: Pathways and chemical principles. Boston, Kluwer 2003; 379-406.
    • (2003) Signal transduction by reactive oxygen and nitrogen species: Pathways and chemical principles , pp. 379-406
    • Machado, A.F.1    Scott, W.J.2    Collins, M.D.3
  • 253
    • 0000792188 scopus 로고
    • Embryonic oxygen deficiency: A physiological approach to analysis of teratological mechanism
    • Grabowski CT. Embryonic oxygen deficiency: A physiological approach to analysis of teratological mechanism. Adv Teratol 1970; 4: 125-67.
    • (1970) Adv Teratol , vol.4 , pp. 125-167
    • Grabowski, C.T.1
  • 254
    • 0010740252 scopus 로고    scopus 로고
    • Hypoxia and altered redox status in embryotoxicity
    • Harris C. Hypoxia and altered redox status in embryotoxicity. Handbook Exp Pharmacol 1997; 124/I: 519-48.
    • (1997) Handbook Exp Pharmacol , vol.124 , Issue.I , pp. 519-548
    • Harris, C.1
  • 255
    • 33645307682 scopus 로고    scopus 로고
    • Effect of culturing mouse embryos under different oxygen concentrations on subsequent fetal and placental development
    • Feil D, Lane M, Roberts CT, Kelley RL, Edwards LJ, Thompson JG, et al. Effect of culturing mouse embryos under different oxygen concentrations on subsequent fetal and placental development. J Physiol 2006; 572(Part 1): 87-96.
    • (2006) J Physiol , vol.572 , Issue.PART 1 , pp. 87-96
    • Feil, D.1    Lane, M.2    Roberts, C.T.3    Kelley, R.L.4    Edwards, L.J.5    Thompson, J.G.6
  • 256
    • 84958698224 scopus 로고
    • Experimental production of congenital abnormalities: Timing and degree of anoxia as factors causing fetal deaths and congenital abnormalities in the mouse. N
    • Ingalls TH, Curley FJ, Prindle RA. Experimental production of congenital abnormalities: Timing and degree of anoxia as factors causing fetal deaths and congenital abnormalities in the mouse. N Engl J Med 1952; 247: 758-68.
    • (1952) Engl J Med , vol.247 , pp. 758-768
    • Ingalls, T.H.1    Curley, F.J.2    Prindle, R.A.3
  • 257
    • 36348993411 scopus 로고
    • Uber die teratogenetische Wirkung des Sauerstoffinangels in der Frühentwicklung. Ein Beitrag zur Kauselgenese der Missbildungen bei Mench und Tier
    • Rübsaamen H. Uber die teratogenetische Wirkung des Sauerstoffinangels in der Frühentwicklung. Ein Beitrag zur Kauselgenese der Missbildungen bei Mench und Tier. Beitr Pathol Anat 1952; 112: 336-79.
    • (1952) Beitr Pathol Anat , vol.112 , pp. 336-379
    • Rübsaamen, H.1
  • 258
    • 0001079419 scopus 로고
    • Principles governing the genesis of congenital malformations induced in mice by hypoxia
    • Ingalls TH, Curley FJ. Principles governing the genesis of congenital malformations induced in mice by hypoxia. N Engl J Med 1957; 257: 1121-7.
    • (1957) N Engl J Med , vol.257 , pp. 1121-1127
    • Ingalls, T.H.1    Curley, F.J.2
  • 259
    • 0141887842 scopus 로고
    • The teratogenic effects of graded doses of hypoxia on the chick embryo
    • Grabowski CT, Parr JA. The teratogenic effects of graded doses of hypoxia on the chick embryo. Am J Anat 1958; 103: 313-48.
    • (1958) Am J Anat , vol.103 , pp. 313-348
    • Grabowski, C.T.1    Parr, J.A.2
  • 260
    • 84965047922 scopus 로고
    • Analysis of intrauterine malformations of vertebral column induced by oxygen deficiency
    • Degenhardt KH, Knoche E. Analysis of intrauterine malformations of vertebral column induced by oxygen deficiency. Can Med Assoc J 1959; 80:441-5.
    • (1959) Can Med Assoc J , vol.80 , pp. 441-445
    • Degenhardt, K.H.1    Knoche, E.2
  • 261
    • 4544332184 scopus 로고    scopus 로고
    • Aquatic hypoxia is a teratogen and affects fish embryonic development
    • Shang EH, Wu RS. Aquatic hypoxia is a teratogen and affects fish embryonic development. Environ Sci Technol 2004; 38(18): 4763-7.
    • (2004) Environ Sci Technol , vol.38 , Issue.18 , pp. 4763-4767
    • Shang, E.H.1    Wu, R.S.2
  • 262
    • 0037415685 scopus 로고    scopus 로고
    • Nitric oxide-induced suspended animation promotes survival during hypoxia
    • Teodoro RO, O'Farrell PH. Nitric oxide-induced suspended animation promotes survival during hypoxia. EMBO J 2003; 22(3): 580-7.
    • (2003) EMBO J , vol.22 , Issue.3 , pp. 580-587
    • Teodoro, R.O.1    O'Farrell, P.H.2
  • 263
    • 36349036282 scopus 로고
    • Differenzierungsstörungen im mittleren und hinteren Korperdrittel des Hühnchens nach experimentellen Sauerstoffmangel in der Frühentwicklung
    • Büchner F. Differenzierungsstörungen im mittleren und hinteren Korperdrittel des Hühnchens nach experimentellen Sauerstoffmangel in der Frühentwicklung. Beitr Pathol Anat 1955; 115: 617-43.
    • (1955) Beitr Pathol Anat , vol.115 , pp. 617-643
    • Büchner, F.1
  • 264
    • 84961057612 scopus 로고
    • A quantitative study of the lethal and teratogenic effects of hypoxia on the three-day chick embryo
    • Grabowski CT. A quantitative study of the lethal and teratogenic effects of hypoxia on the three-day chick embryo. Am J Anat 1961; 109: 25-36.
    • (1961) Am J Anat , vol.109 , pp. 25-36
    • Grabowski, C.T.1
  • 265
    • 0022619079 scopus 로고
    • On the capacity of nitroheterocyclic compounds to elicit an unusual axial asymmetry in cultured rat embryos
    • Greenaway JC, Fantel A, Juchau MR. On the capacity of nitroheterocyclic compounds to elicit an unusual axial asymmetry in cultured rat embryos. Toxicol Appl Pharmacol 1986; 82: 307-5.
    • (1986) Toxicol Appl Pharmacol , vol.82 , pp. 307-305
    • Greenaway, J.C.1    Fantel, A.2    Juchau, M.R.3
  • 266
    • 0031847377 scopus 로고    scopus 로고
    • Teratogen-induced cell death in postimplantation mouse embryos: Differential tissue sensitivity and hallmarks of apoptosis
    • Mirkes PE, Little SA. Teratogen-induced cell death in postimplantation mouse embryos: Differential tissue sensitivity and hallmarks of apoptosis. Cell Death Differ 1998; 5(7): 592-600.
    • (1998) Cell Death Differ , vol.5 , Issue.7 , pp. 592-600
    • Mirkes, P.E.1    Little, S.A.2
  • 267
    • 33747603959 scopus 로고    scopus 로고
    • Mitochondrial dysmorphology in the neuroepithelium of rat embryos following a single dose of maternal hyperthermia during gestation
    • Padmanabhan, R, Al-Menhali NM, Tariq S, Shafiullah M. Mitochondrial dysmorphology in the neuroepithelium of rat embryos following a single dose of maternal hyperthermia during gestation. Exp Brain Res 2006; 173(2): 298-308.
    • (2006) Exp Brain Res , vol.173 , Issue.2 , pp. 298-308
    • Padmanabhan, R.1    Al-Menhali, N.M.2    Tariq, S.3    Shafiullah, M.4
  • 268
    • 37049246971 scopus 로고
    • Uterine vascular clamping: New procedure for the study of congenital maltormations
    • Brent RL, Franklin JB. Uterine vascular clamping: New procedure for the study of congenital maltormations. Science 1960; 132: 88-91.
    • (1960) Science , vol.132 , pp. 88-91
    • Brent, R.L.1    Franklin, J.B.2
  • 269
    • 0016215879 scopus 로고
    • Fetal pathology in rats following uterine vessel clamping on day 14 of gestation
    • Leist KH, Grauwiler J. Fetal pathology in rats following uterine vessel clamping on day 14 of gestation. Teratology 1974; 10: 55-68.
    • (1974) Teratology , vol.10 , pp. 55-68
    • Leist, K.H.1    Grauwiler, J.2
  • 270
    • 0019217756 scopus 로고
    • Differential embryonic cardiovascular responses to acute maternal uterine ischemia: An in vivo microscopic study of rabbit embryos with either intact or clamped umbilical cords
    • Millicovsky G, DeSesso JM. Differential embryonic cardiovascular responses to acute maternal uterine ischemia: An in vivo microscopic study of rabbit embryos with either intact or clamped umbilical cords. Teratology 1980; 22: 335-43.
    • (1980) Teratology , vol.22 , pp. 335-343
    • Millicovsky, G.1    DeSesso, J.M.2
  • 272
    • 0015369803 scopus 로고
    • Mitochondrial respiratory chain of carotid body and chemoreceptor response to changes in oxygen tension
    • Mills E, Jobsis FF. Mitochondrial respiratory chain of carotid body and chemoreceptor response to changes in oxygen tension. J Neurophysiol 1972; 35(4): 405-28.
    • (1972) J Neurophysiol , vol.35 , Issue.4 , pp. 405-428
    • Mills, E.1    Jobsis, F.F.2
  • 273
    • 0028210773 scopus 로고
    • Distribution of electrical potential, pH, free Ca+2, and volume inside cultured adult rabbit cardiac myocytes during chemical hypoxia: A multiparameter digitized confocal microscopic study
    • Chacon E, Reece JM, Nieminen A-L, Zahrebelski G, Herman B, Lemasters JJ. Distribution of electrical potential, pH, free Ca+2, and volume inside cultured adult rabbit cardiac myocytes during chemical hypoxia: A multiparameter digitized confocal microscopic study. Biophys J 1994; 66: 942-52.
    • (1994) Biophys J , vol.66 , pp. 942-952
    • Chacon, E.1    Reece, J.M.2    Nieminen, A.-L.3    Zahrebelski, G.4    Herman, B.5    Lemasters, J.J.6
  • 274
    • 33745225026 scopus 로고    scopus 로고
    • AMP-activated protein kinase-development of the energy sensor concept
    • Hardie DG, Hawley SA, Scott JW. AMP-activated protein kinase-development of the energy sensor concept. J Physiol 2006; 574(Pt 1): 7-15.
    • (2006) J Physiol , vol.574 , Issue.PART 1 , pp. 7-15
    • Hardie, D.G.1    Hawley, S.A.2    Scott, J.W.3
  • 275
    • 29344468832 scopus 로고    scopus 로고
    • Voltage-dependent anion channel (VDAC) as mitochondrial governator - thinking outside the box
    • Lemasters JJ, Holmuhamedov E. Voltage-dependent anion channel (VDAC) as mitochondrial governator - thinking outside the box. Biochim Biophys Acta 2006; 1762(2): 181-90.
    • (2006) Biochim Biophys Acta , vol.1762 , Issue.2 , pp. 181-190
    • Lemasters, J.J.1    Holmuhamedov, E.2
  • 276
    • 33744994383 scopus 로고    scopus 로고
    • Hypoxia-mediated degradation of Na,K-ATPase via mitochondrial reactive oxygen species and the ubiquitin-conjugating system
    • Comellas AP, Dada LA, Lecuona E, Pesce LM, Chandel NS, Quesada N, et al. Hypoxia-mediated degradation of Na,K-ATPase via mitochondrial reactive oxygen species and the ubiquitin-conjugating system. Circ Res 2006; 98(10): 1314-22.
    • (2006) Circ Res , vol.98 , Issue.10 , pp. 1314-1322
    • Comellas, A.P.1    Dada, L.A.2    Lecuona, E.3    Pesce, L.M.4    Chandel, N.S.5    Quesada, N.6
  • 277
    • 0015079718 scopus 로고
    • Studies of mitochondrial development during embryogenesis in the rat
    • Mackler B, Grace R, Duncan HM. Studies of mitochondrial development during embryogenesis in the rat. Arch Biochem Biophys 1971; 144(2): 603-10.
    • (1971) Arch Biochem Biophys , vol.144 , Issue.2 , pp. 603-610
    • Mackler, B.1    Grace, R.2    Duncan, H.M.3
  • 279
    • 26444439977 scopus 로고    scopus 로고
    • Mitochondrial regulation of oxygen sensing
    • Bell EL, Emerling BM, Chandel NS. Mitochondrial regulation of oxygen sensing. Mitochondrion 2005; 5(5): 322-32.
    • (2005) Mitochondrion , vol.5 , Issue.5 , pp. 322-332
    • Bell, E.L.1    Emerling, B.M.2    Chandel, N.S.3
  • 280
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou I, Cairns RA, Fontana L, Lim AL, Denko NC. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metab 2006; 3(3): 187-97.
    • (2006) Cell Metab , vol.3 , Issue.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 281
    • 9644254252 scopus 로고    scopus 로고
    • Trophoblast differentiation during embryo implantation and formation of the maternal-fetal interface
    • Red-Horse K, Zhou Y, Genbacev O, Prakobphol A, Fould R, McMaster M, et al. Trophoblast differentiation during embryo implantation and formation of the maternal-fetal interface. J Clin Invest 2004; 114(6): 744-54.
    • (2004) J Clin Invest , vol.114 , Issue.6 , pp. 744-754
    • Red-Horse, K.1    Zhou, Y.2    Genbacev, O.3    Prakobphol, A.4    Fould, R.5    McMaster, M.6
  • 282
    • 0016334266 scopus 로고
    • The effects of moderate hypoxia and moderate hypoxia plus hypercapnea on cardiac development in chick embryos
    • Jaffe OC. The effects of moderate hypoxia and moderate hypoxia plus hypercapnea on cardiac development in chick embryos. Teratology 1974; 10: 275-81.
    • (1974) Teratology , vol.10 , pp. 275-281
    • Jaffe, O.C.1
  • 286
    • 6944233515 scopus 로고    scopus 로고
    • Hypoxia affects mesoderm and enhances hemangioblast specification during early development
    • Ramirez-Bergeron DL, Runge A, Dahl KD, Fehling HJ, Keller G, Simon MC. Hypoxia affects mesoderm and enhances hemangioblast specification during early development. Development 2004; 131(18): 4623-34.
    • (2004) Development , vol.131 , Issue.18 , pp. 4623-4634
    • Ramirez-Bergeron, D.L.1    Runge, A.2    Dahl, K.D.3    Fehling, H.J.4    Keller, G.5    Simon, M.C.6
  • 287
    • 16344380951 scopus 로고    scopus 로고
    • Low O2 tensions and the prevention of differentiation of hES cells
    • Ezashi T, Das P, Roberts RM. Low O2 tensions and the prevention of differentiation of hES cells. Proc Natl Acad Sci USA 2005; 102(13): 4783-98.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.13 , pp. 4783-4798
    • Ezashi, T.1    Das, P.2    Roberts, R.M.3
  • 288
    • 0002346977 scopus 로고
    • Interaction between metabolism and ventilation: Effects of respiratory gases and temperature
    • Dempsey JA, Pack AI Eds, 2nd Edition, New York, NY, Marcel Dekker
    • Mortola JP, Gautier H. Interaction between metabolism and ventilation: effects of respiratory gases and temperature. In: Dempsey JA, Pack AI Eds, Regulation of breathing (2nd Edition). New York, NY, Marcel Dekker 1995; 1011-64.
    • (1995) Regulation of breathing , pp. 1011-1064
    • Mortola, J.P.1    Gautier, H.2
  • 289
    • 33847334775 scopus 로고    scopus 로고
    • Gaseous metabolism of the chicken embryo and hetchling during post-hypoxic recovery
    • Mortola JP, Besterman AD. Gaseous metabolism of the chicken embryo and hetchling during post-hypoxic recovery. Respir Physiol Neurobiol 2007; 156(2): 212-9.
    • (2007) Respir Physiol Neurobiol , vol.156 , Issue.2 , pp. 212-219
    • Mortola, J.P.1    Besterman, A.D.2
  • 290
    • 24644454814 scopus 로고    scopus 로고
    • Neuronal migration is transiently delayed by prenatal exposure to intermittent hypoxia. Birth Defects Res B Dev
    • Zechel JL, Gamboa JL, Peterson AG, Puchowicz MA, Selman WR, Lust WD. Neuronal migration is transiently delayed by prenatal exposure to intermittent hypoxia. Birth Defects Res B Dev Reprod Toxicol 2005; 74(4): 287-99.
    • (2005) Reprod Toxicol , vol.74 , Issue.4 , pp. 287-299
    • Zechel, J.L.1    Gamboa, J.L.2    Peterson, A.G.3    Puchowicz, M.A.4    Selman, W.R.5    Lust, W.D.6
  • 291
    • 0042905738 scopus 로고    scopus 로고
    • Catalase activity is regulated by c-Abl and Arg in the oxidative stress response
    • Cao C, Leng Y, Kufe D. Catalase activity is regulated by c-Abl and Arg in the oxidative stress response. J Biol Chem 2003; 278(32): 29667-75
    • (2003) J Biol Chem , vol.278 , Issue.32 , pp. 29667-29675
    • Cao, C.1    Leng, Y.2    Kufe, D.3
  • 292
    • 0042819604 scopus 로고    scopus 로고
    • Catalase is regulated by ubiquitination and proteosomal degradation. Role of the c-Abl and Arg tyrosine kinases
    • Cao C, Leng Y, Liu X, Yi Y, Li P, Kufe D. Catalase is regulated by ubiquitination and proteosomal degradation. Role of the c-Abl and Arg tyrosine kinases. Biochemistry 2003; 42: 10348-53.
    • (2003) Biochemistry , vol.42 , pp. 10348-10353
    • Cao, C.1    Leng, Y.2    Liu, X.3    Yi, Y.4    Li, P.5    Kufe, D.6
  • 293
    • 25144443988 scopus 로고    scopus 로고
    • Hypoxic stress in diabetic pregnancy contributes to impaired embryo gene expression and defective development by inducing oxidative stress
    • Li R, Chase M, Jung SK, Smith PJ, Loeken MR. Hypoxic stress in diabetic pregnancy contributes to impaired embryo gene expression and defective development by inducing oxidative stress. Am J Physiol Endocrinol Metab 2005; 289(4): E591-5.
    • (2005) Am J Physiol Endocrinol Metab , vol.289 , Issue.4
    • Li, R.1    Chase, M.2    Jung, S.K.3    Smith, P.J.4    Loeken, M.R.5
  • 294
    • 33745065205 scopus 로고    scopus 로고
    • The relationship between cleft lip, maxillary hypoplasia, hypoxia and phenytoin
    • Webster WS, Howe AM, Abela D, Oakes DJ. The relationship between cleft lip, maxillary hypoplasia, hypoxia and phenytoin. Curr Pharm Des 2006; 12(12): 1431-48.
    • (2006) Curr Pharm Des , vol.12 , Issue.12 , pp. 1431-1448
    • Webster, W.S.1    Howe, A.M.2    Abela, D.3    Oakes, D.J.4
  • 295
    • 18244366867 scopus 로고    scopus 로고
    • Abela D, Howe AM, Oakes DA, Webster WS. Maternal antioxidant supplementation does not reduce the incidence of phenytoin-induced cleft lip and related malformations in rats. Birth Defects Res B Dev Reprod Toxicol 2005; 74(2): 201-6.
    • Abela D, Howe AM, Oakes DA, Webster WS. Maternal antioxidant supplementation does not reduce the incidence of phenytoin-induced cleft lip and related malformations in rats. Birth Defects Res B Dev Reprod Toxicol 2005; 74(2): 201-6.
  • 296
    • 33750063190 scopus 로고    scopus 로고
    • Increased susceptibility to phenytoin teratogenicity: Excessive generation of reactive oxygen species or impaired antioxidant defense?
    • Azarbayjani F, Borg H, Danielsson BR. Increased susceptibility to phenytoin teratogenicity: Excessive generation of reactive oxygen species or impaired antioxidant defense? Basic Clin Pharmacol Toxicol 2006; 99(4): 305-11.
    • (2006) Basic Clin Pharmacol Toxicol , vol.99 , Issue.4 , pp. 305-311
    • Azarbayjani, F.1    Borg, H.2    Danielsson, B.R.3
  • 297
    • 0019460070 scopus 로고
    • Maternal hyperoxia greatly reduces the incidence of phenytoin-induced cleft lip and palate in A/J mice
    • Millicovsky G, Johnston MC. Maternal hyperoxia greatly reduces the incidence of phenytoin-induced cleft lip and palate in A/J mice. Science 1981; 212(4495): 671-2.
    • (1981) Science , vol.212 , Issue.4495 , pp. 671-672
    • Millicovsky, G.1    Johnston, M.C.2
  • 298
    • 15444342958 scopus 로고    scopus 로고
    • Cellular and developmental control of O2 homeostasis by by-poxia-inducible factor 1 alpha
    • Iyer NV, Kotch LE, Agani F, Leung SW, Laughner E, Wenger RH, et al. Cellular and developmental control of O2 homeostasis by by-poxia-inducible factor 1 alpha. Genes Dev 1998; 12: 149-62.
    • (1998) Genes Dev , vol.12 , pp. 149-162
    • Iyer, N.V.1    Kotch, L.E.2    Agani, F.3    Leung, S.W.4    Laughner, E.5    Wenger, R.H.6
  • 299
    • 0033562569 scopus 로고    scopus 로고
    • Defective vascularization of HIF-1α-null embryos is not associated with VEGF deficiency byt with mesenchymal cell death
    • Kotch LE, Iyer NV, Laughner E, Semenza GL. Defective vascularization of HIF-1α-null embryos is not associated with VEGF deficiency byt with mesenchymal cell death. Dev Biol 1999; 209: 254-67.
    • (1999) Dev Biol , vol.209 , pp. 254-267
    • Kotch, L.E.1    Iyer, N.V.2    Laughner, E.3    Semenza, G.L.4
  • 300
    • 0345490692 scopus 로고    scopus 로고
    • Cardia bifida, defective heart development and abnormal neural crest migration in embryos lacking hypoxia-inducible factor-1alpha
    • Compernolle V, Brusselmans K, Franco P, Moorman A, Dewerchin M, Collen D, et al. Cardia bifida, defective heart development and abnormal neural crest migration in embryos lacking hypoxia-inducible factor-1alpha. Cardiovasc Res 2003; 60: 569-79.
    • (2003) Cardiovasc Res , vol.60 , pp. 569-579
    • Compernolle, V.1    Brusselmans, K.2    Franco, P.3    Moorman, A.4    Dewerchin, M.5    Collen, D.6
  • 301
    • 0023761040 scopus 로고
    • Teratogens and craniofacial malformations: Relationship to cell death
    • Sulik KK, Cook CS, Webster WS. Teratogens and craniofacial malformations: Relationship to cell death. Development 1988; 103(Suppl.): 213-31.
    • (1988) Development , vol.103 , Issue.SUPPL. , pp. 213-231
    • Sulik, K.K.1    Cook, C.S.2    Webster, W.S.3
  • 302
    • 0343920277 scopus 로고    scopus 로고
    • Abnormal blood vessel development and lethality in embryos lacking a single VEGF allele
    • Carmeliet P, Ferreira V, Breier G, Pollefeyt S, Kieckens L, Gertsenstein M, et al. Abnormal blood vessel development and lethality in embryos lacking a single VEGF allele. Nature 1996; 380: 435-9.
    • (1996) Nature , vol.380 , pp. 435-439
    • Carmeliet, P.1    Ferreira, V.2    Breier, G.3    Pollefeyt, S.4    Kieckens, L.5    Gertsenstein, M.6
  • 303
    • 0032581277 scopus 로고    scopus 로고
    • Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation, and tumour angiogenesis
    • Carmeliet P, Dor Y, Herbert J-M, Fukumura D, Brusselmans K, Dewerchin M, et al. Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation, and tumour angiogenesis. Nature 1998; 394: 485-90.
    • (1998) Nature , vol.394 , pp. 485-490
    • Carmeliet, P.1    Dor, Y.2    Herbert, J.-M.3    Fukumura, D.4    Brusselmans, K.5    Dewerchin, M.6
  • 304
    • 0030004485 scopus 로고    scopus 로고
    • Heterozygous embryonic lethality induced by targeted inactivation of the VEGF gene
    • Ferrara N, Carver-Moore K, Chen H, Dowd M, Lu L, O'Shea KS, et al. Heterozygous embryonic lethality induced by targeted inactivation of the VEGF gene. Nature 1996; 380: 439-42.
    • (1996) Nature , vol.380 , pp. 439-442
    • Ferrara, N.1    Carver-Moore, K.2    Chen, H.3    Dowd, M.4    Lu, L.5    O'Shea, K.S.6
  • 305
    • 0034682513 scopus 로고    scopus 로고
    • Peng J, Zhang L, Drysdale L, Fong GH. The transcription factor EPAS-1/ hypoxia- inducible factor 2α plays an important role in vascular remodeling. Proc Natl Acad Sci USA 2000; 97(15): 8386-91.
    • Peng J, Zhang L, Drysdale L, Fong GH. The transcription factor EPAS-1/ hypoxia- inducible factor 2α plays an important role in vascular remodeling. Proc Natl Acad Sci USA 2000; 97(15): 8386-91.
  • 306
    • 0035983324 scopus 로고    scopus 로고
    • Loss of HIF-2α and inhibition of VEGF impair fetal lung maturation, whereas treatement with VEGF prevents fatal respiratory distress in premature mice
    • Compernolle V, Brusselmans K, Acker T, Hoet P, Tjwa M, Beck H, et al. Loss of HIF-2α and inhibition of VEGF impair fetal lung maturation, whereas treatement with VEGF prevents fatal respiratory distress in premature mice. Nat Med 2002; 8: 702-10.
    • (2002) Nat Med , vol.8 , pp. 702-710
    • Compernolle, V.1    Brusselmans, K.2    Acker, T.3    Hoet, P.4    Tjwa, M.5    Beck, H.6
  • 307
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxia responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • Tian H, Hammer RE, Matsumoto AM, Russell DW, McKnight SL. The hypoxia responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev 1998; 12: 3320-4.
    • (1998) Genes Dev , vol.12 , pp. 3320-3324
    • Tian, H.1    Hammer, R.E.2    Matsumoto, A.M.3    Russell, D.W.4    McKnight, S.L.5
  • 308
    • 0030943461 scopus 로고    scopus 로고
    • Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT
    • Maltepe E, Schmidt JV, Baunoch D, Bradfield CA, Simon MC. Abnormal angiogenesis and responses to glucose and oxygen deprivation in mice lacking the protein ARNT. Nature 1997; 386: 403-7.
    • (1997) Nature , vol.386 , pp. 403-407
    • Maltepe, E.1    Schmidt, J.V.2    Baunoch, D.3    Bradfield, C.A.4    Simon, M.C.5
  • 309
    • 17544384815 scopus 로고    scopus 로고
    • ARNT-deficient mice and placental differentiation
    • Kozak KR, Abbott B, Hankinson O. ARNT-deficient mice and placental differentiation. Dev Biol 1997; 191: 297-305.
    • (1997) Dev Biol , vol.191 , pp. 297-305
    • Kozak, K.R.1    Abbott, B.2    Hankinson, O.3
  • 310
    • 33750976389 scopus 로고    scopus 로고
    • Placental but not heart defects are associated with elevated hypoxia-inducible factor alpha levels in mice lacking prolyl hydroylase domain protein 2
    • Takeda K, Ho VC, Takeda H, Duan LJ, Nagy A, Fong GH. Placental but not heart defects are associated with elevated hypoxia-inducible factor alpha levels in mice lacking prolyl hydroylase domain protein 2. Mol Cell Biol 2006; 26(22): 8336-46.
    • (2006) Mol Cell Biol , vol.26 , Issue.22 , pp. 8336-8346
    • Takeda, K.1    Ho, V.C.2    Takeda, H.3    Duan, L.J.4    Nagy, A.5    Fong, G.H.6
  • 311
    • 0034671706 scopus 로고    scopus 로고
    • Placental cell fates are regulated in vivo by HIF-mediated hypoxia responses
    • Adelman DM, Gertsenstein M, Nagy A, Simon MC, Maltepe E. Placental cell fates are regulated in vivo by HIF-mediated hypoxia responses. Genes Dev 2000; 14: 3191-203.
    • (2000) Genes Dev , vol.14 , pp. 3191-3203
    • Adelman, D.M.1    Gertsenstein, M.2    Nagy, A.3    Simon, M.C.4    Maltepe, E.5
  • 314
    • 0035143977 scopus 로고    scopus 로고
    • Requirement of nitric oxide for murine oocyte maturation, embryo development, and trophoblast outgrowth in vitro
    • Sengoku K, Takuma N, Horikawa M, Tsuchiya K, Komori H, Sharifa D, et al. Requirement of nitric oxide for murine oocyte maturation, embryo development, and trophoblast outgrowth in vitro. Mol Reprod Dev 2001; 58(3): 262-8.
    • (2001) Mol Reprod Dev , vol.58 , Issue.3 , pp. 262-268
    • Sengoku, K.1    Takuma, N.2    Horikawa, M.3    Tsuchiya, K.4    Komori, H.5    Sharifa, D.6
  • 315
    • 27944484860 scopus 로고    scopus 로고
    • Embryotoxicity of the nitric oxide donor sodium nitroprusside in preimplantation bovine embryos In vitro
    • Orsi NM. Embryotoxicity of the nitric oxide donor sodium nitroprusside in preimplantation bovine embryos In vitro. Animal Reprod Sci 2006; 91: 225-36.
    • (2006) Animal Reprod Sci , vol.91 , pp. 225-236
    • Orsi, N.M.1
  • 316
    • 0028286723 scopus 로고
    • Dysmorphogenic effects of nitric oxide (NO) and NO-synthase inhibition: Studies with intra-amniotic injections of sodium nitroprusside and NG-monomethyl-L-arginine
    • Lee QP, Juchau MR. Dysmorphogenic effects of nitric oxide (NO) and NO-synthase inhibition: Studies with intra-amniotic injections of sodium nitroprusside and NG-monomethyl-L-arginine. Teratology 1994; 49: 452-64.
    • (1994) Teratology , vol.49 , pp. 452-464
    • Lee, Q.P.1    Juchau, M.R.2
  • 317
    • 0029865970 scopus 로고    scopus 로고
    • Apoptosis induced in cultured rat embryos by intra-amniotically microinjected sodium nitroprusside
    • Lee QP, Park HW, Thayer J, Mirkes PE, Juchau MR. Apoptosis induced in cultured rat embryos by intra-amniotically microinjected sodium nitroprusside. Teratology 1996; 53(1): 21-30.
    • (1996) Teratology , vol.53 , Issue.1 , pp. 21-30
    • Lee, Q.P.1    Park, H.W.2    Thayer, J.3    Mirkes, P.E.4    Juchau, M.R.5
  • 319
    • 0028845195 scopus 로고
    • Limb reduction defects after prenatal inhibition of nitric oxide synthase in rats
    • Pierce RL, Pierson DL, Liu H, Kadowitz PJ, Miller MJS. Limb reduction defects after prenatal inhibition of nitric oxide synthase in rats. Pediatr Res 1995; 38: 905-11.
    • (1995) Pediatr Res , vol.38 , pp. 905-911
    • Pierce, R.L.1    Pierson, D.L.2    Liu, H.3    Kadowitz, P.J.4    Miller, M.J.S.5
  • 320
    • 0031563524 scopus 로고    scopus 로고
    • The teratogenicity of N-nitro-L-arginine methyl ester (L-NAME), a nitric oxide synthase inhibitor in rats
    • Fantel AG, Nekabi N, Shepard TH, Cornel LM, Unis AS, Lemire RJ. The teratogenicity of N-nitro-L-arginine methyl ester (L-NAME), a nitric oxide synthase inhibitor in rats. Reprod Toxicol 1997; 11: 709-17.
    • (1997) Reprod Toxicol , vol.11 , pp. 709-717
    • Fantel, A.G.1    Nekabi, N.2    Shepard, T.H.3    Cornel, L.M.4    Unis, A.S.5    Lemire, R.J.6
  • 321
    • 0032845046 scopus 로고    scopus 로고
    • Role of free radicals in the limb teratogenicity of L-Name (N-nitro-L-arginine methyl ester): A new mechanistic model of vascular disruption
    • Fantel AG, Stamps LD, Tran TT, Mackler B, Person RE, Nekahi N. Role of free radicals in the limb teratogenicity of L-Name (N-nitro-L-arginine methyl ester): A new mechanistic model of vascular disruption. Teratology 1999; 60: 151-60.
    • (1999) Teratology , vol.60 , pp. 151-160
    • Fantel, A.G.1    Stamps, L.D.2    Tran, T.T.3    Mackler, B.4    Person, R.E.5    Nekahi, N.6
  • 322
    • 0033814453 scopus 로고    scopus 로고
    • Free radical formation and toxicity in the limb teratogenicity of L-NAME: A new mechanistic model of vascular disruption
    • Fantel AG, Stamps LD, Tran TT, Mackler B, Person RE, Nekahi N. Free radical formation and toxicity in the limb teratogenicity of L-NAME: A new mechanistic model of vascular disruption. Teratology 2000; 62: 237.
    • (2000) Teratology , vol.62 , pp. 237
    • Fantel, A.G.1    Stamps, L.D.2    Tran, T.T.3    Mackler, B.4    Person, R.E.5    Nekahi, N.6
  • 323
    • 0036234712 scopus 로고    scopus 로고
    • Involvement of mitochondria and other free radical sources in normal and abnormal fetal development. Ann NY
    • Fantel AG, Person RE. Involvement of mitochondria and other free radical sources in normal and abnormal fetal development. Ann NY Acad Sci 2002; 959: 424-33.
    • (2002) Acad Sci , vol.959 , pp. 424-433
    • Fantel, A.G.1    Person, R.E.2
  • 324
    • 0038309450 scopus 로고    scopus 로고
    • The nitric oxide synthesis inhibitor N-nitro-L-arginine methyl ester (L-NAME) causes limb defects in mouse fetuses: Protective effects of acute hyperoxia
    • Tiboni GM, Giampietro F, Di Giulio C. The nitric oxide synthesis inhibitor N-nitro-L-arginine methyl ester (L-NAME) causes limb defects in mouse fetuses: Protective effects of acute hyperoxia. Ped Res 2003; 54: 69-76.
    • (2003) Ped Res , vol.54 , pp. 69-76
    • Tiboni, G.M.1    Giampietro, F.2    Di Giulio, C.3
  • 325
    • 4344671737 scopus 로고    scopus 로고
    • Teratological consequences of nitric oxide synthesis inhibition
    • Tiboni GM, Clementini E. Teratological consequences of nitric oxide synthesis inhibition. Curr Pharm Des 2004; 10: 2759-67.
    • (2004) Curr Pharm Des , vol.10 , pp. 2759-2767
    • Tiboni, G.M.1    Clementini, E.2
  • 326
    • 33847232571 scopus 로고    scopus 로고
    • G-nitro-L-arginine methyl ester (L-NAME) in the mouse. Birth Defects Res B Dev
    • G-nitro-L-arginine methyl ester (L-NAME) in the mouse. Birth Defects Res B Dev Reprod Toxicol 2007; 80(1): 28-33.
    • (2007) Reprod Toxicol , vol.80 , Issue.1 , pp. 28-33
    • Tiboni, G.M.1    Marotta, F.2    Barbacane, L.3
  • 328
    • 0141891476 scopus 로고    scopus 로고
    • Carbon monoxide-induced axial skeletal dysmorphogenesis in chick embryo
    • Alexander PG, Tuan RS. Carbon monoxide-induced axial skeletal dysmorphogenesis in chick embryo. Birth Defects Res Part A Clin Mol Teratol 2003; 67: 219-30.
    • (2003) Birth Defects Res Part A Clin Mol Teratol , vol.67 , pp. 219-230
    • Alexander, P.G.1    Tuan, R.S.2
  • 329
    • 33646457351 scopus 로고    scopus 로고
    • The roles of nitric oxide in murine cardiovascular development
    • Nath AK, Madri JA. The roles of nitric oxide in murine cardiovascular development. Dev Biol 2006; 292: 25-33.
    • (2006) Dev Biol , vol.292 , pp. 25-33
    • Nath, A.K.1    Madri, J.A.2
  • 331
    • 3042758484 scopus 로고    scopus 로고
    • Nath AK, Enciso J, Kuniyasu M, Hao X-Y, Madri JA, Pinter E. Nitric oxide modulates murine yolk sac vasculogenesis and rescues glucose induced vasculopathy. Development 2004; 131: 2485-96.
    • Nath AK, Enciso J, Kuniyasu M, Hao X-Y, Madri JA, Pinter E. Nitric oxide modulates murine yolk sac vasculogenesis and rescues glucose induced vasculopathy. Development 2004; 131: 2485-96.
  • 333
    • 0035140309 scopus 로고    scopus 로고
    • Perinatal development of endothelial nitric oxide synthase-deficient mice
    • Hefler LA, Reyes CA, O'Brien WE, Gregg AR. Perinatal development of endothelial nitric oxide synthase-deficient mice. Biol Reprod 2001; 64: 666-73.
    • (2001) Biol Reprod , vol.64 , pp. 666-673
    • Hefler, L.A.1    Reyes, C.A.2    O'Brien, W.E.3    Gregg, A.R.4
  • 334
    • 0034704998 scopus 로고    scopus 로고
    • Abnormal aortic valve development in mice lacking endothelial nitric oxide synthase
    • Lee TC, Zhao YD, Courtman DW, Stewart DJ. Abnormal aortic valve development in mice lacking endothelial nitric oxide synthase. Circulation 2000; 101: 2345-8.
    • (2000) Circulation , vol.101 , pp. 2345-2348
    • Lee, T.C.1    Zhao, Y.D.2    Courtman, D.W.3    Stewart, D.J.4
  • 335
    • 0037072469 scopus 로고    scopus 로고
    • Development of heart failure and congenital defects in mice lacking endothelial nitric oxide synthase
    • Feng O, Song W, Lu X, Hamilton JA, Lei M, Peng T, et al. Development of heart failure and congenital defects in mice lacking endothelial nitric oxide synthase. Circulation 2002; 106: 873-9.
    • (2002) Circulation , vol.106 , pp. 873-879
    • Feng, O.1    Song, W.2    Lu, X.3    Hamilton, J.A.4    Lei, M.5    Peng, T.6
  • 336
    • 0034634282 scopus 로고    scopus 로고
    • Apoptosis during cardiovascular development
    • Fisher SA, Langille BL, Srivastava D. Apoptosis during cardiovascular development. Circ Res 2000; 87: 856-64.
    • (2000) Circ Res , vol.87 , pp. 856-864
    • Fisher, S.A.1    Langille, B.L.2    Srivastava, D.3
  • 337
    • 0032726394 scopus 로고    scopus 로고
    • Familial patent ductus arteriosus and bicuspid aortic valve with hand abnormalities: A novel heart-hand syndrome
    • Gelb BD, Zhang J, Sommer SO, Wasserman JM, Reitman, MJ, Willner JP. Familial patent ductus arteriosus and bicuspid aortic valve with hand abnormalities: A novel heart-hand syndrome. Am J Med Genet 1999; 87: 175-9.
    • (1999) Am J Med Genet , vol.87 , pp. 175-179
    • Gelb, B.D.1    Zhang, J.2    Sommer, S.O.3    Wasserman, J.M.4    Reitman, M.J.5    Willner, J.P.6
  • 339
    • 33748593396 scopus 로고    scopus 로고
    • Risk of limb deficiency defects associated with NAT1, NAT2, GSTT1, GSTM1 and NOS3 genetic variants, maternal smoking, and vitamin supplement intake
    • Carmichael SL, Shaw GM, Yang W, Iovannisci DM, Lammier E. Risk of limb deficiency defects associated with NAT1, NAT2, GSTT1, GSTM1 and NOS3 genetic variants, maternal smoking, and vitamin supplement intake. Am J Med Genet A 2006; 140: 1915-22.
    • (2006) Am J Med Genet A , vol.140 , pp. 1915-1922
    • Carmichael, S.L.1    Shaw, G.M.2    Yang, W.3    Iovannisci, D.M.4    Lammier, E.5
  • 340
    • 28944446275 scopus 로고    scopus 로고
    • Endothelial nitric oxide synthase (NOS3) genetic variants, maternal smoking, vitamin use, and risk of human orofacial clefts
    • Shaw GM, Iovannisci DM, Yang W, Finnell RH, Carmichael SL, Cheng S, et al. Endothelial nitric oxide synthase (NOS3) genetic variants, maternal smoking, vitamin use, and risk of human orofacial clefts. Am J Epidemiol 2005; 162: 1207-14.
    • (2005) Am J Epidemiol , vol.162 , pp. 1207-1214
    • Shaw, G.M.1    Iovannisci, D.M.2    Yang, W.3    Finnell, R.H.4    Carmichael, S.L.5    Cheng, S.6
  • 341
    • 0034807379 scopus 로고    scopus 로고
    • Transplacental exposure to methylene blue initiates teratogenesis in the mouse: Preliminary evidence for a mechanistic implication of cyclic GMP pathway disruption
    • Tiboni GM, Lamonaca D. Transplacental exposure to methylene blue initiates teratogenesis in the mouse: Preliminary evidence for a mechanistic implication of cyclic GMP pathway disruption. Teratology 2001; 64: 213-20.
    • (2001) Teratology , vol.64 , pp. 213-220
    • Tiboni, G.M.1    Lamonaca, D.2
  • 342
    • 0034754919 scopus 로고    scopus 로고
    • The soluble guanylate cyclase inhibitor methylene blue evokes preterm delivery and fetal growth restriction in a mouse model
    • Tiboni GM, Giampietro F, Lamonaca D. The soluble guanylate cyclase inhibitor methylene blue evokes preterm delivery and fetal growth restriction in a mouse model. In Vivo 2001; 15: 333-7.
    • (2001) In Vivo , vol.15 , pp. 333-337
    • Tiboni, G.M.1    Giampietro, F.2    Lamonaca, D.3
  • 343
    • 33644834949 scopus 로고    scopus 로고
    • Function of cGMP-dependent protein kinases as revealed by gene deletion
    • Hofmann F, Feil R, Kleppisch T, Schlossmann J. Function of cGMP-dependent protein kinases as revealed by gene deletion. Physiol Rev 2006; 86: 1-23.
    • (2006) Physiol Rev , vol.86 , pp. 1-23
    • Hofmann, F.1    Feil, R.2    Kleppisch, T.3    Schlossmann, J.4
  • 344
    • 0037025163 scopus 로고    scopus 로고
    • An essential role of N-terminal arginylation in cardiovascular development
    • Kwon YT, Kashina AS, Davydov IV, Hu R-G, An JY, Seo JW, et al. An essential role of N-terminal arginylation in cardiovascular development. Science 2002; 297: 96-9.
    • (2002) Science , vol.297 , pp. 96-99
    • Kwon, Y.T.1    Kashina, A.S.2    Davydov, I.V.3    Hu, R.-G.4    An, J.Y.5    Seo, J.W.6
  • 345
    • 27144557281 scopus 로고    scopus 로고
    • The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators
    • Hu R-G, Sheng J, Qi X, Xu Z, Takahashi TT, Varshavsky A. The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators. Nature 2005; 437(7061): 981-6.
    • (2005) Nature , vol.437 , Issue.7061 , pp. 981-986
    • Hu, R.-G.1    Sheng, J.2    Qi, X.3    Xu, Z.4    Takahashi, T.T.5    Varshavsky, A.6
  • 346
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1a by inhibition of prolyl hydroxylases
    • Metzen E, Zhou J, Jelkmann W, Fandrey J, Brune B. Nitric oxide impairs normoxic degradation of HIF-1a by inhibition of prolyl hydroxylases. Mol Biol Cell 2003; 14(8): 3470-81.
    • (2003) Mol Biol Cell , vol.14 , Issue.8 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brune, B.5
  • 347
    • 0037297175 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor synthesis by nitric oxide: Facts and controversies
    • Dulak J, Jozkowicz, A. Regulation of vascular endothelial growth factor synthesis by nitric oxide: Facts and controversies. Antioxid Redox Signal 2003; 5: 123-32.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 123-132
    • Dulak, J.1    Jozkowicz, A.2
  • 348
    • 36349013990 scopus 로고
    • The prenatal effect of carbon monoxide on albino rats and the resulting neuropathology
    • Wells LL. The prenatal effect of carbon monoxide on albino rats and the resulting neuropathology. Biologist 1933; 15: 80-1.
    • (1933) Biologist , vol.15 , pp. 80-81
    • Wells, L.L.1
  • 349
    • 0015499699 scopus 로고
    • Effect of moderate carbon-monoxide exposure on fetal development
    • Astrup P, Olsen HM, Trolle D, Kjeldsen, K. Effect of moderate carbon-monoxide exposure on fetal development. Lancet 1972; 2(7789): 1220-2.
    • (1972) Lancet , vol.2 , Issue.7789 , pp. 1220-1222
    • Astrup, P.1    Olsen, H.M.2    Trolle, D.3    Kjeldsen, K.4
  • 351
    • 0018393662 scopus 로고
    • Teratogenic potential of inhaled carbon monoxide in mice and rabbits
    • Schwetz BA, Smith FA, Leong BKJ, Staples RE. Teratogenic potential of inhaled carbon monoxide in mice and rabbits. Teratology 1979; 19: 385-91.
    • (1979) Teratology , vol.19 , pp. 385-391
    • Schwetz, B.A.1    Smith, F.A.2    Leong, B.K.J.3    Staples, R.E.4
  • 353
    • 0028852366 scopus 로고
    • Effects of carbon monoxide and hypoxia on cleft lip in AJ mice
    • Bailey LJ, Johnston MC, Billet, J. Effects of carbon monoxide and hypoxia on cleft lip in AJ mice. Cleft-Pal Craniofac J 1995; 32: 14-9.
    • (1995) Cleft-Pal Craniofac J , vol.32 , pp. 14-19
    • Bailey, L.J.1    Johnston, M.C.2    Billet, J.3
  • 355
    • 0020613867 scopus 로고
    • Forebrain damage in chick embryos exposed to carbon monoxide
    • Daughtrey WC, Newby-Schmidt MB, Norton S. Forebrain damage in chick embryos exposed to carbon monoxide. Teratology 1983; 28: 83-9.
    • (1983) Teratology , vol.28 , pp. 83-89
    • Daughtrey, W.C.1    Newby-Schmidt, M.B.2    Norton, S.3
  • 356
    • 0029585394 scopus 로고
    • Ultrastructural changes in 9-day old mouse embryos following maternal tobacco smoke inhalation
    • Bnait KS, Seller MJ. Ultrastructural changes in 9-day old mouse embryos following maternal tobacco smoke inhalation. Exp Toxicol Pathol 1995;.47: 453-61.
    • (1995) Exp Toxicol Pathol , vol.47 , pp. 453-461
    • Bnait, K.S.1    Seller, M.J.2
  • 357
  • 358
    • 0028880959 scopus 로고
    • Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice
    • Poss KD, Thomas MJ, Ebralidze, AK, O'Dell TJ, Tonegawa S. Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice. Neuron 1995; 15: 867-73.
    • (1995) Neuron , vol.15 , pp. 867-873
    • Poss, K.D.1    Thomas, M.J.2    Ebralidze, A.K.3    O'Dell, T.J.4    Tonegawa, S.5
  • 359
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron metabolism
    • Poss KD, Tonegawa S. Heme oxygenase 1 is required for mammalian iron metabolism. Proc Natl Acad Sci USA 1997; 94(20): 10919-24.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.20 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 360
    • 0141886322 scopus 로고    scopus 로고
    • Gastroschisis is caused by the combination of carbon monoxide and protein-zinc deficiencies. Birth Defects Res B Dev
    • Singh J. Gastroschisis is caused by the combination of carbon monoxide and protein-zinc deficiencies. Birth Defects Res B Dev Reprod Toxicol 2003; 68(4): 355-62.
    • (2003) Reprod Toxicol , vol.68 , Issue.4 , pp. 355-362
    • Singh, J.1
  • 361
    • 33745465489 scopus 로고    scopus 로고
    • Interaction of maternal protein and carbon monoxide on pup mortality in mice: Implications for global infant mortality. Birth Defects Res B Dev
    • Singh J. Interaction of maternal protein and carbon monoxide on pup mortality in mice: Implications for global infant mortality. Birth Defects Res B Dev Reprod Toxicol 2006; 77(3): 216-26.
    • (2006) Reprod Toxicol , vol.77 , Issue.3 , pp. 216-226
    • Singh, J.1
  • 362
    • 33751003546 scopus 로고    scopus 로고
    • CO-metal interaction: Vital signaling from a lethal gas
    • Boczkowski J, Poderoso JJ, Motterlini R. CO-metal interaction: Vital signaling from a lethal gas. Trends Biochem Sci 2006; 31 (11): 614-21
    • (2006) Trends Biochem Sci , vol.31 , Issue.11 , pp. 614-621
    • Boczkowski, J.1    Poderoso, J.J.2    Motterlini, R.3
  • 363
    • 0036140432 scopus 로고    scopus 로고
    • Ambient air pollution and risk of birth defects in Southern California
    • Ritz B, Yu F, Fruin S, Chapa G, Shaw GM, Harris JA. Ambient air pollution and risk of birth defects in Southern California. Am J Epidem 2002; 155: 17-25.
    • (2002) Am J Epidem , vol.155 , pp. 17-25
    • Ritz, B.1    Yu, F.2    Fruin, S.3    Chapa, G.4    Shaw, G.M.5    Harris, J.A.6
  • 365
    • 0034830612 scopus 로고    scopus 로고
    • Mental retardation in Down syndrome: A hydrogen sulfide hypothesis
    • Kamoun P. Mental retardation in Down syndrome: A hydrogen sulfide hypothesis. Med Hypoth 2001; 57: 399-92.
    • (2001) Med Hypoth , vol.57 , pp. 399-392
    • Kamoun, P.1
  • 366
    • 33748558473 scopus 로고    scopus 로고
    • Hydrogen sulfide: Clandestine microbial messenger?
    • Lloyd D. Hydrogen sulfide: Clandestine microbial messenger? Trends Microbiol 2006; 14(10): 456-62.
    • (2006) Trends Microbiol , vol.14 , Issue.10 , pp. 456-462
    • Lloyd, D.1
  • 367
    • 0014104046 scopus 로고
    • Thp toxicity of hydrogen sulfide and other sulfides
    • Evans CL. Thp toxicity of hydrogen sulfide and other sulfides. J Exp Physiol 1967; 52:231-48.
    • (1967) J Exp Physiol , vol.52 , pp. 231-248
    • Evans, C.L.1
  • 369
  • 370
    • 0006493641 scopus 로고
    • The scat of action of sulfide on pulmonary ventilation
    • Winder CV, Winder HO. The scat of action of sulfide on pulmonary ventilation. Am J Physiol 1933; 105: 337-52.
    • (1933) Am J Physiol , vol.105 , pp. 337-352
    • Winder, C.V.1    Winder, H.O.2
  • 372
    • 33746463692 scopus 로고    scopus 로고
    • The temporal architecture of eukaryotic growth
    • Lloyd D, Murray DB. The temporal architecture of eukaryotic growth. FEBS Lett 2006; 586: 2830-5.
    • (2006) FEBS Lett , vol.586 , pp. 2830-2835
    • Lloyd, D.1    Murray, D.B.2
  • 373
    • 0030584092 scopus 로고    scopus 로고
    • Nitric oxide regulates cell proliferation during Drosophila development
    • Kuzin B, Roberts I. Peunova N, Enikolopov G. Nitric oxide regulates cell proliferation during Drosophila development. Cell 1996; 87(4): 639-49
    • (1996) Cell , vol.87 , Issue.4 , pp. 639-649
    • Kuzin, B.1    Roberts, I.2    Peunova, N.3    Enikolopov, G.4
  • 374
    • 0242494080 scopus 로고    scopus 로고
    • Sdspended animation in C. elegans requires the spindle checkpoint
    • Nystul TG, Goldmark JP, Padilla PA, Roth MB. Sdspended animation in C. elegans requires the spindle checkpoint. Science 2003; 302(5647):1038-41.
    • (2003) Science , vol.302 , Issue.5647 , pp. 1038-1041
    • Nystul, T.G.1    Goldmark, J.P.2    Padilla, P.A.3    Roth, M.B.4
  • 375
    • 2942643921 scopus 로고    scopus 로고
    • Carbon monoxide-induced suspended animation protects against hypoxic damage in Caenorhabditis elegans
    • Nystul TG, Roth MB, Carbon monoxide-induced suspended animation protects against hypoxic damage in Caenorhabditis elegans. Proc Natl Acad Sci USA 2004; 101(24): 9133-36.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.24 , pp. 9133-9136
    • Nystul, T.G.1    Roth, M.B.2
  • 376
    • 33745106680 scopus 로고    scopus 로고
    • Whole embryo culture: An important tool in developmental toxicology today
    • Flick B, Klug S. Whole embryo culture: An important tool in developmental toxicology today. Curr Pharm Des 2006; 12(12): 1467-88
    • (2006) Curr Pharm Des , vol.12 , Issue.12 , pp. 1467-1488
    • Flick, B.1    Klug, S.2
  • 377
    • 33745083138 scopus 로고    scopus 로고
    • Teratogenic and developmental effects of lithium
    • Giles JJ, Bannigan JG. Teratogenic and developmental effects of lithium. Curr Pharm Des 2006; 12(12): 1531-41.
    • (2006) Curr Pharm Des , vol.12 , Issue.12 , pp. 1531-1541
    • Giles, J.J.1    Bannigan, J.G.2
  • 378
    • 33745764163 scopus 로고    scopus 로고
    • Natural product-derived small molecule activators of hypoxia-inducible factor-1 (HIF-1)
    • Nagle DG, Zhou YD, Natural product-derived small molecule activators of hypoxia-inducible factor-1 (HIF-1). Curr Pharm Des 2006; 12(21): 2673-88.
    • (2006) Curr Pharm Des , vol.12 , Issue.21 , pp. 2673-2688
    • Nagle, D.G.1    Zhou, Y.D.2


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