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Volumn 38, Issue 7, 2005, Pages 874-881

Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins

Author keywords

Ascorbate; Free radicals; Nitric Oxide; Proteomics; S Nitrosothiols

Indexed keywords

ACETRIZOIC ACID; ASCORBIC ACID; BOVINE SERUM ALBUMIN; ELONGATION FACTOR 2; HEAT SHOCK PROTEIN 90; N ACETYL S NITROSOPENICILLAMINE; NITRIC OXIDE; S NITROSOCYSTEINE; S NITROSOGLUTATHIONE; S NITROSOTHIOL;

EID: 14644423288     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.12.012     Document Type: Article
Times cited : (104)

References (26)
  • 2
    • 0032735975 scopus 로고    scopus 로고
    • Neuronal protection and destruction by NO
    • S.A. Lipton Neuronal protection and destruction by NO (Review; 61 Refs) Cell Death Differ. 6 1999 943 951
    • (1999) Cell Death Differ. , vol.6 , pp. 943-951
    • Lipton, S.A.1
  • 5
    • 0029875840 scopus 로고    scopus 로고
    • S-Nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • L. Jia, C. Bonaventura, J. Bonaventura, and J.S. Stamler S-Nitrosohaemoglobin: a dynamic activity of blood involved in vascular control Nature 380 1996 221 226
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 9
    • 1042267391 scopus 로고    scopus 로고
    • Detection and proteomic identification of S-nitrosylated proteins in endothelial cells
    • A. Martinez-Ruiz, and S. Lamas Detection and proteomic identification of S-nitrosylated proteins in endothelial cells Arch. Biochem. Biophys. 423 2004 192 199
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 192-199
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 10
    • 2942558370 scopus 로고    scopus 로고
    • New insights into protein S-nitrosylation: Mitochondria as a model system
    • M.W. Foster, and J.S. Stamler New insights into protein S-nitrosylation: mitochondria as a model system J. Biol. Chem. 279 2004 25891 25897
    • (2004) J. Biol. Chem. , vol.279 , pp. 25891-25897
    • Foster, M.W.1    Stamler, J.S.2
  • 11
    • 0034256633 scopus 로고    scopus 로고
    • Reaction of ascorbic acid with S-nitrosothiols: Clear evidence for two distinct reaction pathways
    • A.J. Holmes, and D.L.H. Williams Reaction of ascorbic acid with S-nitrosothiols: clear evidence for two distinct reaction pathways J. Chem. Soc., Perkin Trans. 2 2000 1639 1644
    • (2000) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1639-1644
    • Holmes, A.J.1    Williams, D.L.H.2
  • 12
    • 0030200188 scopus 로고    scopus 로고
    • Role of ascorbic acid in the metabolism of S-nitroso-glutathione
    • M. Kashiba-Iwatsuki, M. Yamaguchi, and M. Inoue Role of ascorbic acid in the metabolism of S-nitroso-glutathione FEBS Lett. 389 1996 149 152
    • (1996) FEBS Lett. , vol.389 , pp. 149-152
    • Kashiba-Iwatsuki, M.1    Yamaguchi, M.2    Inoue, M.3
  • 13
    • 0034064525 scopus 로고    scopus 로고
    • Kinetics and mechanism of the decomposition of S-nitrosoglutathione by L-ascorbate and copper ion in aqueous solution to produce nitric oxide
    • J.N. Smith, and T.P. Dasgupta Kinetics and mechanism of the decomposition of S-nitrosoglutathione by L-ascorbate and copper ion in aqueous solution to produce nitric oxide Nitric Oxide 4 2000 57 66
    • (2000) Nitric Oxide , vol.4 , pp. 57-66
    • Smith, J.N.1    Dasgupta, T.P.2
  • 14
    • 37049112625 scopus 로고
    • An unusually stable thionitrite from N-acetyl-DL-penicillamine. X-Ray, crystal and molecular structure of 2-(acetylamino)-2-carboxy-1,1-dimethylethyl thionitrite
    • L. Field, R.V. Dilts, R. Ravichandran, P.G. Lanhert, and P.G. Carnahan An unusually stable thionitrite from N-acetyl-DL-penicillamine. X-Ray, crystal and molecular structure of 2-(acetylamino)-2-carboxy-1,1-dimethylethyl thionitrite J. Chem. Soc., Chem. Commun. 1978 249 250
    • (1978) J. Chem. Soc., Chem. Commun. , pp. 249-250
    • Field, L.1    Dilts, R.V.2    Ravichandran, R.3    Lanhert, P.G.4    Carnahan, P.G.5
  • 15
    • 2542516981 scopus 로고    scopus 로고
    • The mechanism of transmembrane S-nitrosothiol transport
    • Y. Zhang, and N. Hogg The mechanism of transmembrane S-nitrosothiol transport Proc. Natl. Acad. Sci. USA 101 2004 7891 7896
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7891-7896
    • Zhang, Y.1    Hogg, N.2
  • 16
    • 0000071405 scopus 로고
    • Some observations concerning the S-nitroso and S-phenylsulphonyl derivatives of L-cysteine and glutathione
    • T.W. Hart Some observations concerning the S-nitroso and S-phenylsulphonyl derivatives of L-cysteine and glutathione Tetrahedron Lett. 26 1985 2013 2026
    • (1985) Tetrahedron Lett. , vol.26 , pp. 2013-2026
    • Hart, T.W.1
  • 17
    • 4143071301 scopus 로고    scopus 로고
    • The formation and stability of S-nitrosothiols in RAW 264.7 cells
    • Y. Zhang, and N. Hogg The formation and stability of S-nitrosothiols in RAW 264.7 cells Am. J. Physiol. Lung Cell. Mol. Physiol. 287 2003 L467 L474
    • (2003) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.287
    • Zhang, Y.1    Hogg, N.2
  • 18
    • 0037251861 scopus 로고    scopus 로고
    • Methodologies for the sensitive and specific measurement of S-nitrosothiols, iron-nitrosyls, and nitrite in biological samples
    • B.K. Yang, E.X. Vivas, C.D. Reiter, and M.T. Gladwin Methodologies for the sensitive and specific measurement of S-nitrosothiols, iron-nitrosyls, and nitrite in biological samples Free Radic. Res. 37 2003 1 10
    • (2003) Free Radic. Res. , vol.37 , pp. 1-10
    • Yang, B.K.1    Vivas, E.X.2    Reiter, C.D.3    Gladwin, M.T.4
  • 19
    • 0037443130 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols
    • S. Li, and A.R. Whorton Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols Arch. Biochem. Biophys. 410 2003 269 279
    • (2003) Arch. Biochem. Biophys. , vol.410 , pp. 269-279
    • Li, S.1    Whorton, A.R.2
  • 20
    • 14644444757 scopus 로고    scopus 로고
    • Nitroxide scanning electron paramagnetic resonance of helices IV and V and the intervening loop in the lactose permaease of Escherichia Coli
    • M. Zhao, K.-C. Zen, J. Hernandez-Borrell, C. Altenbach, W.L. Hubbell, and R.H. Kaback Nitroxide scanning electron paramagnetic resonance of helices IV and V and the intervening loop in the lactose permaease of Escherichia Coli Biochemistry 38 1998 15977 15980
    • (1998) Biochemistry , vol.38 , pp. 15977-15980
    • Zhao, M.1    Zen, K.-C.2    Hernandez-Borrell, J.3    Altenbach, C.4    Hubbell, W.L.5    Kaback, R.H.6
  • 21
    • 0029841946 scopus 로고    scopus 로고
    • Effect of Oxidative Stress, Produced by cumene hydroperoxide, on the various steps of protein synthesis. Modification of elongation factor-2
    • A. Ayala, J. Parrado, M. Bougria, and A. Machado Effect of Oxidative Stress, Produced by cumene hydroperoxide, on the various steps of protein synthesis. Modification of elongation factor-2 J. Biol. Chem. 271 1996 23105 23110
    • (1996) J. Biol. Chem. , vol.271 , pp. 23105-23110
    • Ayala, A.1    Parrado, J.2    Bougria, M.3    MacHado, A.4
  • 22
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • J. Tamarit, E. Cabiscol, and J. Ros Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress J. Biol. Chem. 273 1998 3027 3032
    • (1998) J. Biol. Chem. , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 23
    • 0034282468 scopus 로고    scopus 로고
    • Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
    • E. Cabiscol, E. Piulats, P. Echave, E. Herrero, and J. Ros Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae J. Biol. Chem. 275 2000 27393 27398
    • (2000) J. Biol. Chem. , vol.275 , pp. 27393-27398
    • Cabiscol, E.1    Piulats, E.2    Echave, P.3    Herrero, E.4    Ros, J.5
  • 24
    • 0007821999 scopus 로고    scopus 로고
    • Hsp90 - News from the front
    • U. Jakob Hsp90 - news from the front Front. Biosci. 1 1996 309 317
    • (1996) Front. Biosci. , vol.1 , pp. 309-317
    • Jakob, U.1
  • 25
    • 0025909326 scopus 로고
    • Purification and characterization of the 65-kDa protein phosphorylated in murine macrophages by stimulation with bacterial lipopolysaccharide
    • H. Shinomiya, H. Hirata, and M. Nakano Purification and characterization of the 65-kDa protein phosphorylated in murine macrophages by stimulation with bacterial lipopolysaccharide J. Immunol. 146 1991 3617 3625
    • (1991) J. Immunol. , vol.146 , pp. 3617-3625
    • Shinomiya, H.1    Hirata, H.2    Nakano, M.3
  • 26
    • 0028933571 scopus 로고
    • Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide
    • H. Shinomiya, A. Hagi, M. Fukuzumi, M. Mizobuchi, H. Hirata, and S. Utsumi Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide J. Immunol. 154 1995 3471 3478
    • (1995) J. Immunol. , vol.154 , pp. 3471-3478
    • Shinomiya, H.1    Hagi, A.2    Fukuzumi, M.3    Mizobuchi, M.4    Hirata, H.5    Utsumi, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.