메뉴 건너뛰기




Volumn 21, Issue 7, 2010, Pages 1121-1129

Regulation of redox signaling involving chemical conjugation of protein thiols by nitric oxide and electrophiles

Author keywords

[No Author keywords available]

Indexed keywords

8 NITRO CYCLIC GMP; CYCLIC GMP; ELECTROPHILE; FATTY ACID; NITRIC OXIDE; REACTIVE NITROGEN SPECIES; S NITROSOTHIOL; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 77954869633     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc900396u     Document Type: Review
Times cited : (35)

References (101)
  • 1
    • 0028902552 scopus 로고
    • Nitric oxide synthases: Properties and catalytic mechanism
    • Griffith, O. W. and Stuehr, D. J. (1995) Nitric oxide synthases: properties and catalytic mechanism Annu. Rev. Physiol. 57, 707-736
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 707-736
    • Griffith, O.W.1    Stuehr, D.J.2
  • 2
    • 0022481682 scopus 로고
    • Cyclic guanosine monophosphate as a mediator of vasodilation
    • Murad, F. (1986) Cyclic guanosine monophosphate as a mediator of vasodilation J. Clin. Invest. 78, 1-5
    • (1986) J. Clin. Invest. , vol.78 , pp. 1-5
    • Murad, F.1
  • 3
    • 0025011298 scopus 로고
    • Localization of nitric oxide synthase indicating a neural role for nitric oxide
    • Bredt, D. S., Hwang, P. M., and Snyder, S. H. (1990) Localization of nitric oxide synthase indicating a neural role for nitric oxide Nature 347, 768-770
    • (1990) Nature , vol.347 , pp. 768-770
    • Bredt, D.S.1    Hwang, P.M.2    Snyder, S.H.3
  • 4
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan, C. (1992) Nitric oxide as a secretory product of mammalian cells FASEB J. 6, 3051-3064
    • (1992) FASEB J. , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 6
    • 33947583867 scopus 로고    scopus 로고
    • NO-cGMP signaling and regenerative medicine involving stem cells
    • Madhusoodanan, K. S. and Murad, F. (2007) NO-cGMP signaling and regenerative medicine involving stem cells Neurochem. Res. 32, 681-694
    • (2007) Neurochem. Res. , vol.32 , pp. 681-694
    • Madhusoodanan, K.S.1    Murad, F.2
  • 7
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • Walsh, C. T., Garneau-Tsodikova, S., and Gatto, G. J., Jr. (2005) Protein posttranslational modifications: the chemistry of proteome diversifications Angew. Chem., Int. Ed. Engl. 44, 7342-7372
    • (2005) Angew. Chem., Int. Ed. Engl. , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto Jr., G.J.3
  • 8
    • 33845478569 scopus 로고    scopus 로고
    • Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction
    • Spickett, C. M., Pitt, A. R., Morrice, N., and Kolch, W. (2006) Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction Biochim. Biophys. Acta 1764, 1823-1841
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1823-1841
    • Spickett, C.M.1    Pitt, A.R.2    Morrice, N.3    Kolch, W.4
  • 10
    • 63449139593 scopus 로고    scopus 로고
    • Two decades of new concepts in nitric oxide signaling: From the discovery of a gas messenger to the mediation of nonenzymatic posttranslational modifications
    • Martinez-Ruiz, A. and Lamas, S. (2009) Two decades of new concepts in nitric oxide signaling: from the discovery of a gas messenger to the mediation of nonenzymatic posttranslational modifications IUBMB Life 61, 91-98
    • (2009) IUBMB Life , vol.61 , pp. 91-98
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 11
    • 0034493914 scopus 로고    scopus 로고
    • Mechanisms of biological S-nitrosation and its measurement
    • Akaike, T. (2000) Mechanisms of biological S-nitrosation and its measurement Free Radic. Res. 33, 461-469
    • (2000) Free Radic. Res. , vol.33 , pp. 461-469
    • Akaike, T.1
  • 12
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. The prototypic redox-based signaling mechanism
    • Stamler, J. S., Lamas, S., and Fang, F. C. (2001) Nitrosylation. The prototypic redox-based signaling mechanism Cell 106, 675-683
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 17
    • 35348989753 scopus 로고    scopus 로고
    • Nitrated cyclic GMP as a new cellular signal
    • Feelisch, M. (2007) Nitrated cyclic GMP as a new cellular signal Nat. Chem. Biol. 3, 687-688
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 687-688
    • Feelisch, M.1
  • 19
    • 65449189551 scopus 로고    scopus 로고
    • Cytoprotective function of heme oxygenase 1 induced by a nitrated cyclic nucleotide formed during murine salmonellosis
    • Zaki, M. H., Fujii, S., Okamoto, T., Islam, S., Khan, S., Ahmed, K. A., Sawa, T., and Akaike, T. (2009) Cytoprotective function of heme oxygenase 1 induced by a nitrated cyclic nucleotide formed during murine salmonellosis J. Immunol. 182, 3746-3756
    • (2009) J. Immunol. , vol.182 , pp. 3746-3756
    • Zaki, M.H.1    Fujii, S.2    Okamoto, T.3    Islam, S.4    Khan, S.5    Ahmed, K.A.6    Sawa, T.7    Akaike, T.8
  • 20
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: Thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman, H. J., Fukuto, J. M., and Torres, M. (2004) Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers Am. J. Physiol. Cell Physiol. 287, C246-256
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287 , pp. 246-256
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 22
    • 33646745126 scopus 로고    scopus 로고
    • Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures
    • Eaton, P. (2006) Protein thiol oxidation in health and disease: techniques for measuring disulfides and related modifications in complex protein mixtures Free Radic. Biol. Med. 40, 1889-1899
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1889-1899
    • Eaton, P.1
  • 23
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn, C. C. and Hampton, M. B. (2008) Thiol chemistry and specificity in redox signaling Free Radic. Biol. Med. 45, 549-561
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 26
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • Szabo, C., Ischiropoulos, H., and Radi, R. (2007) Peroxynitrite: biochemistry, pathophysiology and development of therapeutics Nat. Rev. Drug Discovery 6, 662-680
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 27
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi, R., Beckman, J. S., Bush, K. M., and Freeman, B. A. (1991) Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide J. Biol. Chem. 266, 4244-4250
    • (1991) J. Biol. Chem. , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 30
    • 31544453292 scopus 로고    scopus 로고
    • Nitrative DNA damage in inflammation and its possible role in carcinogenesis
    • Sawa, T. and Ohshima, H. (2006) Nitrative DNA damage in inflammation and its possible role in carcinogenesis Nitric Oxide 14, 91-100
    • (2006) Nitric Oxide , vol.14 , pp. 91-100
    • Sawa, T.1    Ohshima, H.2
  • 31
    • 0035852024 scopus 로고    scopus 로고
    • A novel nitroimidazole compound formed during the reaction of peroxynitrite with 2′,3′,5′-tri-O-acetyl-guanosine
    • Niles, J. C., Wishnok, J. S., and Tannenbaum, S. R. (2001) A novel nitroimidazole compound formed during the reaction of peroxynitrite with 2′,3′,5′-tri-O-acetyl-guanosine J. Am. Chem. Soc. 123, 12147-12151
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 12147-12151
    • Niles, J.C.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 32
    • 0030577390 scopus 로고    scopus 로고
    • Effects of carbon dioxide/bicarbonate on induction of DNA single-strand breaks and formation of 8-nitroguanine, 8-oxoguanine and base-propenal mediated by peroxynitrite
    • Yermilov, V., Yoshie, Y., Rubio, J., and Ohshima, H. (1996) Effects of carbon dioxide/bicarbonate on induction of DNA single-strand breaks and formation of 8-nitroguanine, 8-oxoguanine and base-propenal mediated by peroxynitrite FEBS Lett. 399, 67-70
    • (1996) FEBS Lett. , vol.399 , pp. 67-70
    • Yermilov, V.1    Yoshie, Y.2    Rubio, J.3    Ohshima, H.4
  • 33
    • 0032171410 scopus 로고    scopus 로고
    • Oxidative chemistry of nitric oxide: The roles of superoxide, peroxynitrite, and carbon dioxide
    • Squadrito, G. L. and Pryor, W. A. (1998) Oxidative chemistry of nitric oxide: the roles of superoxide, peroxynitrite, and carbon dioxide Free Radic. Biol. Med. 25, 392-403
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 392-403
    • Squadrito, G.L.1    Pryor, W.A.2
  • 34
    • 4143113591 scopus 로고    scopus 로고
    • Red cell membrane and plasma linoleic acid nitration products: Synthesis, clinical identification, and quantitation
    • Baker, P. R., Schopfer, F. J., Sweeney, S., and Freeman, B. A. (2004) Red cell membrane and plasma linoleic acid nitration products: synthesis, clinical identification, and quantitation Proc. Natl. Acad. Sci. U.S.A. 101, 11577-11582
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11577-11582
    • Baker, P.R.1    Schopfer, F.J.2    Sweeney, S.3    Freeman, B.A.4
  • 35
    • 29644433449 scopus 로고    scopus 로고
    • Fatty acid transduction of nitric oxide signaling: Multiple nitrated unsaturated fatty acid derivatives exist in human blood and urine and serve as endogenous peroxisome proliferator-activated receptor ligands
    • Baker, P. R., Lin, Y., Schopfer, F. J., Woodcock, S. R., Groeger, A. L., Batthyany, C., Sweeney, S., Long, M. H., Iles, K. E., Baker, L. M., Branchaud, B. P., Chen, Y. E., and Freeman, B. A. (2005) Fatty acid transduction of nitric oxide signaling: multiple nitrated unsaturated fatty acid derivatives exist in human blood and urine and serve as endogenous peroxisome proliferator-activated receptor ligands J. Biol. Chem. 280, 42464-42475
    • (2005) J. Biol. Chem. , vol.280 , pp. 42464-42475
    • Baker, P.R.1    Lin, Y.2    Schopfer, F.J.3    Woodcock, S.R.4    Groeger, A.L.5    Batthyany, C.6    Sweeney, S.7    Long, M.H.8    Iles, K.E.9    Baker, L.M.10    Branchaud, B.P.11    Chen, Y.E.12    Freeman, B.A.13
  • 36
    • 0034758161 scopus 로고    scopus 로고
    • Vicinal nitrohydroxyeicosatrienoic acids: Vasodilator lipids formed by reaction of nitrogen dioxide with arachidonic acid
    • Balazy, M., Iesaki, T., Park, J. L., Jiang, H., Kaminski, P. M., and Wolin, M. S. (2001) Vicinal nitrohydroxyeicosatrienoic acids: vasodilator lipids formed by reaction of nitrogen dioxide with arachidonic acid J. Pharmacol. Exp. Ther. 299, 611-619
    • (2001) J. Pharmacol. Exp. Ther. , vol.299 , pp. 611-619
    • Balazy, M.1    Iesaki, T.2    Park, J.L.3    Jiang, H.4    Kaminski, P.M.5    Wolin, M.S.6
  • 37
    • 0141794273 scopus 로고    scopus 로고
    • Cholesteryl nitrolinoleate, a nitrated lipid present in human blood plasma and lipoproteins
    • Lima, E. S., Di Mascio, P., and Abdalla, D. S. (2003) Cholesteryl nitrolinoleate, a nitrated lipid present in human blood plasma and lipoproteins J. Lipid Res. 44, 1660-1666
    • (2003) J. Lipid Res. , vol.44 , pp. 1660-1666
    • Lima, E.S.1    Di Mascio, P.2    Abdalla, D.S.3
  • 38
    • 0037183523 scopus 로고    scopus 로고
    • Characterization of linoleic acid nitration in human blood plasma by mass spectrometry
    • Lima, E. S., Di Mascio, P., Rubbo, H., and Abdalla, D. S. (2002) Characterization of linoleic acid nitration in human blood plasma by mass spectrometry Biochemistry 41, 10717-10722
    • (2002) Biochemistry , vol.41 , pp. 10717-10722
    • Lima, E.S.1    Di Mascio, P.2    Rubbo, H.3    Abdalla, D.S.4
  • 42
    • 3543111961 scopus 로고    scopus 로고
    • Nitric oxide as an endogenous mutagen for Sendai virus without antiviral activity
    • Yoshitake, J., Akaike, T., Akuta, T., Tamura, F., Ogura, T., Esumi, H., and Maeda, H. (2004) Nitric oxide as an endogenous mutagen for Sendai virus without antiviral activity J. Virol. 78, 8709-8719
    • (2004) J. Virol. , vol.78 , pp. 8709-8719
    • Yoshitake, J.1    Akaike, T.2    Akuta, T.3    Tamura, F.4    Ogura, T.5    Esumi, H.6    Maeda, H.7
  • 43
    • 22544432235 scopus 로고    scopus 로고
    • Interleukin-1β induces death in chondrocyte-like ATDC5 cells through mitochondrial dysfunction and energy depletion in a reactive nitrogen and oxygen species-dependent manner
    • Yasuhara, R., Miyamoto, Y., Akaike, T., Akuta, T., Nakamura, M., Takami, M., Morimura, N., Yasu, K., and Kamijo, R. (2005) Interleukin-1β induces death in chondrocyte-like ATDC5 cells through mitochondrial dysfunction and energy depletion in a reactive nitrogen and oxygen species-dependent manner Biochem. J. 389, 315-323
    • (2005) Biochem. J. , vol.389 , pp. 315-323
    • Yasuhara, R.1    Miyamoto, Y.2    Akaike, T.3    Akuta, T.4    Nakamura, M.5    Takami, M.6    Morimura, N.7    Yasu, K.8    Kamijo, R.9
  • 44
    • 31644447230 scopus 로고    scopus 로고
    • Analysis of urinary 8-nitroguanine, a marker of nitrative nucleic acid damage, by high-performance liquid chromatography-electrochemical detection coupled with immunoaffinity purification: Association with cigarette smoking
    • Sawa, T., Tatemichi, M., Akaike, T., Barbin, A., and Ohshima, H. (2006) Analysis of urinary 8-nitroguanine, a marker of nitrative nucleic acid damage, by high-performance liquid chromatography-electrochemical detection coupled with immunoaffinity purification: association with cigarette smoking Free Radic. Biol. Med. 40, 711-720
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 711-720
    • Sawa, T.1    Tatemichi, M.2    Akaike, T.3    Barbin, A.4    Ohshima, H.5
  • 46
    • 33745853157 scopus 로고    scopus 로고
    • 8-Nitroguanine, a product of nitrative DNA damage caused by reactive nitrogen species: Formation, occurrence, and implications in inflammation and carcinogenesis
    • Ohshima, H., Sawa, T., and Akaike, T. (2006) 8-Nitroguanine, a product of nitrative DNA damage caused by reactive nitrogen species: formation, occurrence, and implications in inflammation and carcinogenesis Antioxid. Redox Signaling 8, 1033-1045
    • (2006) Antioxid. Redox Signaling , vol.8 , pp. 1033-1045
    • Ohshima, H.1    Sawa, T.2    Akaike, T.3
  • 48
    • 41149107750 scopus 로고    scopus 로고
    • Suppression of NO production and 8-nitroguanosine formation by phenol-containing endocrine-disrupting chemicals in LPS-stimulated macrophages: Involvement of estrogen receptor-dependent or -independent pathways
    • Yoshitake, J., Kato, K., Yoshioka, D., Sueishi, Y., Sawa, T., Akaike, T., and Yoshimura, T. (2008) Suppression of NO production and 8-nitroguanosine formation by phenol-containing endocrine-disrupting chemicals in LPS-stimulated macrophages: involvement of estrogen receptor-dependent or -independent pathways Nitric Oxide 18, 223-228
    • (2008) Nitric Oxide , vol.18 , pp. 223-228
    • Yoshitake, J.1    Kato, K.2    Yoshioka, D.3    Sueishi, Y.4    Sawa, T.5    Akaike, T.6    Yoshimura, T.7
  • 49
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • Jones, D. P. (2008) Radical-free biology of oxidative stress Am. J. Physiol. Cell Physiol. 295, C849-868
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295 , pp. 849-868
    • Jones, D.P.1
  • 51
    • 0033994516 scopus 로고    scopus 로고
    • Form, function, and regulation of protein tyrosine phosphatases and their involvement in human diseases
    • Li, L. and Dixon, J. E. (2000) Form, function, and regulation of protein tyrosine phosphatases and their involvement in human diseases Semin. Immunol. 12, 75-84
    • (2000) Semin. Immunol. , vol.12 , pp. 75-84
    • Li, L.1    Dixon, J.E.2
  • 52
    • 0037443130 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B in intact cells by S -nitrosothiols
    • Li, S. and Whorton, A. R. (2003) Regulation of protein tyrosine phosphatase 1B in intact cells by S -nitrosothiols Arch. Biochem. Biophys. 410, 269-279
    • (2003) Arch. Biochem. Biophys. , vol.410 , pp. 269-279
    • Li, S.1    Whorton, A.R.2
  • 53
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse, R. and Nagase, H. (2003) Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry Circ. Res. 92, 827-839
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 54
    • 0035800858 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation
    • Okamoto, T., Akaike, T., Sawa, T., Miyamoto, Y., van der Vliet, A., and Maeda, H. (2001) Activation of matrix metalloproteinases by peroxynitrite- induced protein S-glutathiolation via disulfide S-oxide formation J. Biol. Chem. 276, 29596-29602
    • (2001) J. Biol. Chem. , vol.276 , pp. 29596-29602
    • Okamoto, T.1    Akaike, T.2    Sawa, T.3    Miyamoto, Y.4    Van Der Vliet, A.5    Maeda, H.6
  • 56
    • 44349178194 scopus 로고    scopus 로고
    • Nitric oxide regulation of MMP-9 activation and its relationship to modifications of the cysteine switch
    • McCarthy, S. M., Bove, P. F., Matthews, D. E., Akaike, T., and van der Vliet, A. (2008) Nitric oxide regulation of MMP-9 activation and its relationship to modifications of the cysteine switch Biochemistry 47, 5832-5840
    • (2008) Biochemistry , vol.47 , pp. 5832-5840
    • McCarthy, S.M.1    Bove, P.F.2    Matthews, D.E.3    Akaike, T.4    Van Der Vliet, A.5
  • 57
    • 0000119940 scopus 로고
    • Structure of the metal clusters in rabbit liver metallothionein
    • Otvos, J. D. and Armitage, I. M. (1980) Structure of the metal clusters in rabbit liver metallothionein Proc. Natl. Acad. Sci. U.S.A. 77, 7094-7098
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 7094-7098
    • Otvos, J.D.1    Armitage, I.M.2
  • 59
    • 33747723380 scopus 로고    scopus 로고
    • Mammalian zinc transport, trafficking, and signals
    • Cousins, R. J., Liuzzi, J. P., and Lichten, L. A. (2006) Mammalian zinc transport, trafficking, and signals J. Biol. Chem. 281, 24085-24089
    • (2006) J. Biol. Chem. , vol.281 , pp. 24085-24089
    • Cousins, R.J.1    Liuzzi, J.P.2    Lichten, L.A.3
  • 61
    • 34447106867 scopus 로고    scopus 로고
    • The zinc/thiolate redox biochemistry of metallothionein and the control of zinc ion fluctuations in cell signaling
    • Krezel, A., Hao, Q., and Maret, W. (2007) The zinc/thiolate redox biochemistry of metallothionein and the control of zinc ion fluctuations in cell signaling Arch. Biochem. Biophys. 463, 188-200
    • (2007) Arch. Biochem. Biophys. , vol.463 , pp. 188-200
    • Krezel, A.1    Hao, Q.2    Maret, W.3
  • 62
    • 1942455887 scopus 로고    scopus 로고
    • Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles
    • Itoh, K., Tong, K. I., and Yamamoto, M. (2004) Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles Free Radic. Biol. Med. 36, 1208-1213
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1208-1213
    • Itoh, K.1    Tong, K.I.2    Yamamoto, M.3
  • 66
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza, G. L. (2003) Targeting HIF-1 for cancer therapy Nat. Rev. Cancer 3, 721-732
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 67
    • 0028816847 scopus 로고
    • Purification and characterization of hypoxia-inducible factor 1
    • Wang, G. L. and Semenza, G. L. (1995) Purification and characterization of hypoxia-inducible factor 1 J. Biol. Chem. 270, 1230-1237
    • (1995) J. Biol. Chem. , vol.270 , pp. 1230-1237
    • Wang, G.L.1    Semenza, G.L.2
  • 70
    • 0035573882 scopus 로고    scopus 로고
    • The pVHL-hIF-1 system. A key mediator of oxygen homeostasis
    • Maxwell, P. H., Pugh, C. W., and Ratcliffe, P. J. (2001) The pVHL-hIF-1 system. A key mediator of oxygen homeostasis Adv. Exp. Med. Biol. 502, 365-376
    • (2001) Adv. Exp. Med. Biol. , vol.502 , pp. 365-376
    • Maxwell, P.H.1    Pugh, C.W.2    Ratcliffe, P.J.3
  • 74
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • Haendeler, J., Hoffmann, J., Tischler, V., Berk, B. C., Zeiher, A. M., and Dimmeler, S. (2002) Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69 Nat. Cell Biol. 4, 743-749
    • (2002) Nat. Cell Biol. , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 75
    • 0038511319 scopus 로고    scopus 로고
    • S-Nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1
    • Sumbayev, V. V. (2003) S-Nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1 Arch. Biochem. Biophys. 415, 133-136
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 133-136
    • Sumbayev, V.V.1
  • 77
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • Levonen, A. L., Landar, A., Ramachandran, A., Ceaser, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., and Darley-Usmar, V. M. (2004) Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products Biochem. J. 378, 373-382
    • (2004) Biochem. J. , vol.378 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 78
    • 38649104828 scopus 로고    scopus 로고
    • Keap1 modification and nuclear accumulation in response to S -nitrosocysteine
    • Buckley, B. J., Li, S., and Whorton, A. R. (2008) Keap1 modification and nuclear accumulation in response to S -nitrosocysteine Free Radic. Biol. Med. 44, 692-698
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 692-698
    • Buckley, B.J.1    Li, S.2    Whorton, A.R.3
  • 79
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr, S., Hallak, H., de Boitte, A., Lapetina, E. G., and Brune, B. (1999) Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase J. Biol. Chem. 274, 9427-9430
    • (1999) J. Biol. Chem. , vol.274 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    De Boitte, A.3    Lapetina, E.G.4    Brune, B.5
  • 80
    • 33244472848 scopus 로고    scopus 로고
    • Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo
    • Fang, J. and Holmgren, A. (2006) Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo J. Am. Chem. Soc. 128, 1879-1885
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1879-1885
    • Fang, J.1    Holmgren, A.2
  • 81
    • 0033995950 scopus 로고    scopus 로고
    • Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation
    • Choi, Y. B., Tenneti, L., Le, D. A., Ortiz, J., Bai, G., Chen, H. S., and Lipton, S. A. (2000) Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation Nat. Neurosci. 3, 15-21
    • (2000) Nat. Neurosci. , vol.3 , pp. 15-21
    • Choi, Y.B.1    Tenneti, L.2    Le, D.A.3    Ortiz, J.4    Bai, G.5    Chen, H.S.6    Lipton, S.A.7
  • 84
    • 23844442198 scopus 로고    scopus 로고
    • Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase
    • Carbone, D. L., Doorn, J. A., Kiebler, Z., and Petersen, D. R. (2005) Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase Chem. Res. Toxicol. 18, 1324-1331
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1324-1331
    • Carbone, D.L.1    Doorn, J.A.2    Kiebler, Z.3    Petersen, D.R.4
  • 85
    • 33745315287 scopus 로고    scopus 로고
    • S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara, T., Nakamura, T., Yao, D., Shi, Z. Q., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., and Lipton, S. A. (2006) S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration Nature 441, 513-517
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4    Gu, Z.5    Ma, Y.6    Masliah, E.7    Nomura, Y.8    Lipton, S.A.9
  • 88
    • 0036259784 scopus 로고    scopus 로고
    • Role of nitric oxide in host defense in murine salmonellosis as a function of its antibacterial and antiapoptotic activities
    • Alam, M. S., Akaike, T., Okamoto, S., Kubota, T., Yoshitake, J., Sawa, T., Miyamoto, Y., Tamura, F., and Maeda, H. (2002) Role of nitric oxide in host defense in murine salmonellosis as a function of its antibacterial and antiapoptotic activities Infect. Immun. 70, 3130-3142
    • (2002) Infect. Immun. , vol.70 , pp. 3130-3142
    • Alam, M.S.1    Akaike, T.2    Okamoto, S.3    Kubota, T.4    Yoshitake, J.5    Sawa, T.6    Miyamoto, Y.7    Tamura, F.8    Maeda, H.9
  • 89
    • 55249112001 scopus 로고    scopus 로고
    • Nitric oxide produced in Peyer's patches exhibits antiapoptotic activity contributing to an antimicrobial effect in murine salmonellosis
    • Alam, M. S., Zaki, M. H., Sawa, T., Islam, S., Ahmed, K. A., Fujii, S., Okamoto, T., and Akaike, T. (2008) Nitric oxide produced in Peyer's patches exhibits antiapoptotic activity contributing to an antimicrobial effect in murine salmonellosis Microbiol. Immunol. 52, 197-208
    • (2008) Microbiol. Immunol. , vol.52 , pp. 197-208
    • Alam, M.S.1    Zaki, M.H.2    Sawa, T.3    Islam, S.4    Ahmed, K.A.5    Fujii, S.6    Okamoto, T.7    Akaike, T.8
  • 90
    • 2442535969 scopus 로고    scopus 로고
    • Nitric oxide-induced transcriptional up-regulation of protective genes by Nrf2 via the antioxidant response element counteracts apoptosis of neuroblastoma cells
    • Dhakshinamoorthy, S. and Porter, A. G. (2004) Nitric oxide-induced transcriptional up-regulation of protective genes by Nrf2 via the antioxidant response element counteracts apoptosis of neuroblastoma cells J. Biol. Chem. 279, 20096-20107
    • (2004) J. Biol. Chem. , vol.279 , pp. 20096-20107
    • Dhakshinamoorthy, S.1    Porter, A.G.2
  • 91
    • 0036740180 scopus 로고    scopus 로고
    • Pegylated zinc protoporphyrin: A water-soluble heme oxygenase inhibitor with tumor-targeting capacity
    • Sahoo, S. K., Sawa, T., Fang, J., Tanaka, S., Miyamoto, Y., Akaike, T., and Maeda, H. (2002) Pegylated zinc protoporphyrin: a water-soluble heme oxygenase inhibitor with tumor-targeting capacity Bioconjugate Chem. 13, 1031-1038
    • (2002) Bioconjugate Chem. , vol.13 , pp. 1031-1038
    • Sahoo, S.K.1    Sawa, T.2    Fang, J.3    Tanaka, S.4    Miyamoto, Y.5    Akaike, T.6    Maeda, H.7
  • 92
    • 0038418359 scopus 로고    scopus 로고
    • In vivo antitumor activity of pegylated zinc protoporphyrin: Targeted inhibition of heme oxygenase in solid tumor
    • Fang, J., Sawa, T., Akaike, T., Akuta, T., Sahoo, S. K., Khaled, G., Hamada, A., and Maeda, H. (2003) In vivo antitumor activity of pegylated zinc protoporphyrin: targeted inhibition of heme oxygenase in solid tumor Cancer Res. 63, 3567-3574
    • (2003) Cancer Res. , vol.63 , pp. 3567-3574
    • Fang, J.1    Sawa, T.2    Akaike, T.3    Akuta, T.4    Sahoo, S.K.5    Khaled, G.6    Hamada, A.7    Maeda, H.8
  • 93
    • 0842308157 scopus 로고    scopus 로고
    • Enhancement of chemotherapeutic response of tumor cells by a heme oxygenase inhibitor, pegylated zinc protoporphyrin
    • Fang, J., Sawa, T., Akaike, T., Greish, K., and Maeda, H. (2004) Enhancement of chemotherapeutic response of tumor cells by a heme oxygenase inhibitor, pegylated zinc protoporphyrin Int. J. Cancer 109, 1-8
    • (2004) Int. J. Cancer , vol.109 , pp. 1-8
    • Fang, J.1    Sawa, T.2    Akaike, T.3    Greish, K.4    Maeda, H.5
  • 96
    • 0036709597 scopus 로고    scopus 로고
    • Cellular glutathione and thiols metabolism
    • Dickinson, D. A. and Forman, H. J. (2002) Cellular glutathione and thiols metabolism Biochem. Pharmacol. 64, 1019-1026
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1019-1026
    • Dickinson, D.A.1    Forman, H.J.2
  • 97
    • 70349681975 scopus 로고    scopus 로고
    • Glutathione - A review on its role and significance in Parkinson's disease
    • Martin, H. L. and Teismann, P. (2009) Glutathione - a review on its role and significance in Parkinson's disease FASEB J. 23, 3263-3272
    • (2009) FASEB J. , vol.23 , pp. 3263-3272
    • Martin, H.L.1    Teismann, P.2
  • 98
    • 33144490305 scopus 로고    scopus 로고
    • Nuclear and mitochondrial compartmentation of oxidative stress and redox signaling
    • Hansen, J. M., Go, Y. M., and Jones, D. P. (2006) Nuclear and mitochondrial compartmentation of oxidative stress and redox signaling Annu. Rev. Pharmacol. Toxicol. 46, 215-234
    • (2006) Annu. Rev. Pharmacol. Toxicol. , vol.46 , pp. 215-234
    • Hansen, J.M.1    Go, Y.M.2    Jones, D.P.3
  • 99
    • 34250738347 scopus 로고    scopus 로고
    • Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences
    • Martinez-Ruiz, A. and Lamas, S. (2007) Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: convergences and divergences Cardiovasc. Res. 75, 220-228
    • (2007) Cardiovasc. Res. , vol.75 , pp. 220-228
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 100
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling
    • 2, a necessary evil for cell signaling Science 312, 1882-1883
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 101
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux, B. and Toledano, M. B. (2007) ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis Nat. Rev. Mol. Cell Biol. 8, 813-824
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.