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Volumn 4, Issue MAY, 2013, Pages

Nitric oxide-based protein modification: Formation and site-specificity of protein S-nitrosylation

Author keywords

Cysteineresidue; Nitricoxide; Post translational modification; Protein S nitrosylationprotein; Redox modification; S nitrosylation; Site specificity

Indexed keywords


EID: 84893728188     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2013.00137     Document Type: Review
Times cited : (156)

References (114)
  • 1
    • 43549098067 scopus 로고    scopus 로고
    • S-nitrosylated proteins of a medicinal CAM plant Kalanchoe pinnata-ribulose-1, 5-bisphosphate carboxylase/oxygenase activity targeted for inhibition
    • Abat, J. K., Mattoo, A. K., and Deswal, R. (2008). S-nitrosylated proteins of a medicinal CAM plant Kalanchoe pinnata-ribulose-1, 5-bisphosphate carboxylase/oxygenase activity targeted for inhibition. FEBS J. 275, 2862-2872.
    • (2008) FEBS J. , vol.275 , pp. 2862-2872
    • Abat, J.K.1    Mattoo, A.K.2    Deswal, R.3
  • 2
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • Alderton, W. K., Cooper, C. E., and Knowles, R. G. (2001). Nitric oxide synthases: structure, function and inhibition. Biochem. J. 357, 593-615.
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 3
    • 84862556342 scopus 로고    scopus 로고
    • Enzymatic mechanisms regulating protein S-nitrosylation: Implications in health and disease
    • Anand, P., and Stamler, J. S. (2012). Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease. J. Mol. Med. (Berl.) 90, 233-244.
    • (2012) J. Mol. Med. (Berl.) , vol.90 , pp. 233-244
    • Anand, P.1    Stamler, J.S.2
  • 4
    • 0028987969 scopus 로고
    • NO+, NO, and NO-donation by S-nitrosothiols: Implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation
    • Arnelle, D. R., and Stamler, J. S. (1995). NO+, NO, and NO-donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation. Arch. Biochem. Biophys. 318, 279-285.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 279-285
    • Arnelle, D.R.1    Stamler, J.S.2
  • 6
    • 84870721735 scopus 로고    scopus 로고
    • Nitric oxide-dependent posttranslational modification in plants: An update
    • Astier, J., and Lindermayr, C. (2012). Nitric oxide-dependent posttranslational modification in plants: an update. Int. J. Mol. Sci. 13, 15193-15208.
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 15193-15208
    • Astier, J.1    Lindermayr, C.2
  • 7
    • 33847709127 scopus 로고    scopus 로고
    • Metacaspase activity of Arabidopsis thaliana is regulated by S-nitrosylation of a critical cysteine residue
    • Belenghi, B., Romero-Puertas, M. C., Vercammen, D., Brackenier, A., Inze, D., Delledonne, M., et al. (2007). Metacaspase activity of Arabidopsis thaliana is regulated by S-nitrosylation of a critical cysteine residue. J. Biol. Chem. 282, 1352-1358.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1352-1358
    • Belenghi, B.1    Romero-Puertas, M.C.2    Vercammen, D.3    Brackenier, A.4    Inze, D.5    Delledonne, M.6
  • 8
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: Enzymatic mechanisms and cellular functions
    • Benhar, M., Forrester, M. T., and Stamler, J. S. (2009). Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat. Rev. Mol. Cell Biol. 10, 721-732.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 9
    • 1042267601 scopus 로고    scopus 로고
    • Apoplastic synthesis of nitric oxide by plant tissues
    • Bethke, P. C., Badger, M. R., and Jones, R. L. (2004). Apoplastic synthesis of nitric oxide by plant tissues. Plant Cell 16, 332-341.
    • (2004) Plant Cell , vol.16 , pp. 332-341
    • Bethke, P.C.1    Badger, M.R.2    Jones, R.L.3
  • 10
    • 33645242366 scopus 로고    scopus 로고
    • Nitric oxide reduces seed dormancy in Arabidopsis
    • Bethke, P. C., Libourel, I. G., and Jones, R. L. (2006). Nitric oxide reduces seed dormancy in Arabidopsis. J. Exp. Bot. 57, 517-526.
    • (2006) J. Exp. Bot. , vol.57 , pp. 517-526
    • Bethke, P.C.1    Libourel, I.G.2    Jones, R.L.3
  • 11
    • 63849086054 scopus 로고    scopus 로고
    • Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide
    • Bosworth, C. A., Toledo, J. C. Jr., Zmijewski, J. W., Li, Q., and Lancaster, J. R. (2009). Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide. Proc. Natl. Acad. Sci. U.S.A. 106, 4671-4676.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4671-4676
    • Bosworth, C.A.1    Toledo Jr., J.C.2    Zmijewski, J.W.3    Li, Q.4    Lancaster, J.R.5
  • 12
    • 0032400370 scopus 로고    scopus 로고
    • Regeneration of the ferrous heme of soluble guanylate cyclase from the nitric oxide complex: Acceleration by thiols and oxyhemoglobin
    • Brandish, P. E., Buechler, W., and Marletta, M. A. (1998). Regeneration of the ferrous heme of soluble guanylate cyclase from the nitric oxide complex: acceleration by thiols and oxyhemoglobin. Biochemistry 37, 16898-16907.
    • (1998) Biochemistry , vol.37 , pp. 16898-16907
    • Brandish, P.E.1    Buechler, W.2    Marletta, M.A.3
  • 13
    • 0037047414 scopus 로고    scopus 로고
    • The local electrostatic environment determines cysteine reactivity of tubulin
    • Britto, P. J., Knipling, L., and Wolff, J. (2002). The local electrostatic environment determines cysteine reactivity of tubulin. J. Biol. Chem. 277, 29018-29027.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29018-29027
    • Britto, P.J.1    Knipling, L.2    Wolff, J.3
  • 14
    • 84864579819 scopus 로고    scopus 로고
    • The chemical biology of S-nitrosothiols
    • Broniowska, K. A., and Hogg, N. (2012). The chemical biology of S-nitrosothiols. Antioxid. Redox Signal. 17, 969-980.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 969-980
    • Broniowska, K.A.1    Hogg, N.2
  • 16
    • 34548152584 scopus 로고    scopus 로고
    • A novel approach to identify proteins modified by nitric oxide: The HIS-TAG switch method
    • Camerini, S., Polci, M. L., Restuccia, U., Usuelli, V., Malgaroli, A., and Bachi, A. (2007). A novel approach to identify proteins modified by nitric oxide: the HIS-TAG switch method. J. Proteome Res. 6, 3224-3231.
    • (2007) J. Proteome Res. , vol.6 , pp. 3224-3231
    • Camerini, S.1    Polci, M.L.2    Restuccia, U.3    Usuelli, V.4    Malgaroli, A.5    Bachi, A.6
  • 18
    • 78649889548 scopus 로고    scopus 로고
    • S-alkylating labeling strategy for site-specific identification of the S-nitrosoproteome
    • Chen, Y. J., Ku, W. C., Lin, P. Y., Chou, H. C., Khoo, K. H., and Chen, Y. J. (2010). S-alkylating labeling strategy for site-specific identification of the S-nitrosoproteome. J. Proteome Res. 9, 6417-6439.
    • (2010) J. Proteome Res. , vol.9 , pp. 6417-6439
    • Chen, Y.J.1    Ku, W.C.2    Lin, P.Y.3    Chou, H.C.4    Khoo, K.H.5    Chen, Y.J.6
  • 19
    • 16544368902 scopus 로고    scopus 로고
    • Cellular and subcellular localization of endogenous nitric oxide in young and senescent pea plants
    • Corpas, F. J., Barroso, J. B., Carreras, A., Quiros, M., Leon, A. M., Romero-Puertas, M. C., et al. (2004). Cellular and subcellular localization of endogenous nitric oxide in young and senescent pea plants. Plant Physiol. 136, 2722-2733.
    • (2004) Plant Physiol. , vol.136 , pp. 2722-2733
    • Corpas, F.J.1    Barroso, J.B.2    Carreras, A.3    Quiros, M.4    Leon, A.M.5    Romero-Puertas, M.C.6
  • 20
    • 80052421534 scopus 로고    scopus 로고
    • Nitric oxide imbalance provokes a nitrosative response in plants under abiotic stress
    • Corpas, F. J., Leterrier, M., Valderrama, R., Airaki, M., Chaki, M., Palma, J. M., et al. (2011). Nitric oxide imbalance provokes a nitrosative response in plants under abiotic stress. Plant Sci. 181, 604-611.
    • (2011) Plant Sci. , vol.181 , pp. 604-611
    • Corpas, F.J.1    Leterrier, M.2    Valderrama, R.3    Airaki, M.4    Chaki, M.5    Palma, J.M.6
  • 21
    • 1942423166 scopus 로고    scopus 로고
    • Nitric oxide plays a central role in determining lateral root development in tomato
    • Correa-Aragunde, N., Graziano, M., and Lamattina, L. (2004). Nitric oxide plays a central role in determining lateral root development in tomato. Planta 218, 900-905.
    • (2004) Planta , vol.218 , pp. 900-905
    • Correa-Aragunde, N.1    Graziano, M.2    Lamattina, L.3
  • 22
    • 33744527052 scopus 로고    scopus 로고
    • Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite: Implications for the interaction of nitric oxide with mitochondria
    • Dahm, C. C., Moore, K., and Murphy, M. P. (2006). Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite: implications for the interaction of nitric oxide with mitochondria. J. Biol. Chem. 281, 10056-10065.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10056-10065
    • Dahm, C.C.1    Moore, K.2    Murphy, M.P.3
  • 23
    • 78049288138 scopus 로고    scopus 로고
    • Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation
    • Doulias, P. T., Greene, J. L., Greco, T. M., Tenopoulou, M., Seeholzer, S. H., Dunbrack, R. L., et al. (2010). Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation. Proc. Natl. Acad. Sci. U.S.A. 107, 16958-16963.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 16958-16963
    • Doulias, P.T.1    Greene, J.L.2    Greco, T.M.3    Tenopoulou, M.4    Seeholzer, S.H.5    Dunbrack, R.L.6
  • 24
    • 0032544005 scopus 로고    scopus 로고
    • Defense gene induction in tobacco by nitric oxide, cyclic GMP, and cyclic ADP-ribose
    • Durner, J., Wendehenne, D., and Klessig, D. F. (1998). Defense gene induction in tobacco by nitric oxide, cyclic GMP, and cyclic ADP-ribose. Proc. Natl. Acad. Sci. U.S.A. 95, 10328-10333.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 10328-10333
    • Durner, J.1    Wendehenne, D.2    Klessig, D.F.3
  • 25
    • 77955786575 scopus 로고    scopus 로고
    • Gold nanoparticle enrichment method for identifying S-nitrosylation and S-glutathionylation sites in proteins
    • Faccenda, A., Bonham, C. A., Vacratsis, P. O., Zhang, X., and Mutus, B. (2010). Gold nanoparticle enrichment method for identifying S-nitrosylation and S-glutathionylation sites in proteins. J. Am. Chem. Soc. 132, 11392-11394.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11392-11394
    • Faccenda, A.1    Bonham, C.A.2    Vacratsis, P.O.3    Zhang, X.4    Mutus, B.5
  • 26
    • 84855895599 scopus 로고    scopus 로고
    • Proteomics investigation of endogenous S-nitrosylation in Arabidopsis
    • Fares, A., Rossignol, M., and Peltier, J. B. (2011). Proteomics investigation of endogenous S-nitrosylation in Arabidopsis. Biochem. Biophys. Res. Commun. 416, 331-336.
    • (2011) Biochem. Biophys. Res. Commun. , vol.416 , pp. 331-336
    • Fares, A.1    Rossignol, M.2    Peltier, J.B.3
  • 27
    • 77955460024 scopus 로고    scopus 로고
    • Reactions of NO and nitrite with heme models and proteins
    • Ford, P. C. (2010). Reactions of NO and nitrite with heme models and proteins. Inorg. Chem. 49, 6226-6239.
    • (2010) Inorg. Chem. , vol.49 , pp. 6226-6239
    • Ford, P.C.1
  • 28
    • 58049124883 scopus 로고    scopus 로고
    • Detection of protein S-nitrosylation with the biotin-switch technique
    • Forrester, M. T., Foster, M. W., Benhar, M., and Stamler, J. S. (2009a). Detection of protein S-nitrosylation with the biotin-switch technique. Free Radic. Biol. Med. 46, 119-126.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 119-126
    • Forrester, M.T.1    Foster, M.W.2    Benhar, M.3    Stamler, J.S.4
  • 30
    • 34347268109 scopus 로고    scopus 로고
    • Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress
    • Forrester, M. T., Foster, M. W., and Stamler, J. S. (2007). Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress. J. Biol. Chem. 282, 13977-13983.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13977-13983
    • Forrester, M.T.1    Foster, M.W.2    Stamler, J.S.3
  • 31
    • 84860443646 scopus 로고    scopus 로고
    • Methodologies for the characterization, identification and quantification of S-nitrosylated proteins
    • Foster, M. W. (2012). Methodologies for the characterization, identification and quantification of S-nitrosylated proteins. Biochim. Biophys. Acta 1820, 675-683.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 675-683
    • Foster, M.W.1
  • 33
  • 34
    • 0029909954 scopus 로고    scopus 로고
    • Direct and indirect oxidations by peroxynitrite, neither involving the hydroxyl radical
    • Goldstein, S., Squadrito, G. L., Pryor, W. A., and Czapski, G. (1996). Direct and indirect oxidations by peroxynitrite, neither involving the hydroxyl radical. Free Radic. Biol. Med. 21, 965-974.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 965-974
    • Goldstein, S.1    Squadrito, G.L.2    Pryor, W.A.3    Czapski, G.4
  • 35
    • 0031029150 scopus 로고    scopus 로고
    • A novel reaction mechanism for the formation of S-nitrosothiol in vivo
    • Gow, A. J., Buerk, D. G., and Ischiropoulos, H. (1997). A novel reaction mechanism for the formation of S-nitrosothiol in vivo. J. Biol. Chem. 272, 2841-2845.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2841-2845
    • Gow, A.J.1    Buerk, D.G.2    Ischiropoulos, H.3
  • 36
    • 11844296696 scopus 로고    scopus 로고
    • Nitric oxide and iron in plants: An emerging and converging story
    • Graziano, M., and Lamattina, L. (2005). Nitric oxide and iron in plants: an emerging and converging story. Trends Plant Sci. 10, 4-8.
    • (2005) Trends Plant Sci. , vol.10 , pp. 4-8
    • Graziano, M.1    Lamattina, L.2
  • 37
    • 33646580362 scopus 로고    scopus 로고
    • Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells
    • Greco, T. M., Hodara, R., Parastatidis, I., Heijnen, H. F., Dennehy, M. K., Liebler, D. C., et al. (2006). Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells. Proc. Natl. Acad. Sci. U.S.A. 103, 7420-7425.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7420-7425
    • Greco, T.M.1    Hodara, R.2    Parastatidis, I.3    Heijnen, H.F.4    Dennehy, M.K.5    Liebler, D.C.6
  • 38
    • 17644413565 scopus 로고    scopus 로고
    • Chemical considerations and biological selectivity of protein nitrosation: Implications for NO-mediated signal transduction
    • Guikema, B., Lu, Q., and Jourd'heuil, D. (2005). Chemical considerations and biological selectivity of protein nitrosation: implications for NO-mediated signal transduction. Antioxid. Redox Signal. 7, 593-606.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 593-606
    • Guikema, B.1    Lu, Q.2    Jourd'heuil, D.3
  • 39
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999). Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 40
    • 42649106845 scopus 로고    scopus 로고
    • Detergent-free biotin switch combined with liquid chromatography/tandem mass spectrometry in the analysis of S-nitrosylated proteins
    • Han, P., and Chen, C. (2008). Detergent-free biotin switch combined with liquid chromatography/tandem mass spectrometry in the analysis of S-nitrosylated proteins. Rapid Commun. Mass Spectrom. 22, 1137-1145.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 1137-1145
    • Han, P.1    Chen, C.2
  • 41
    • 32244445145 scopus 로고    scopus 로고
    • SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures
    • Hao, G., Derakhshan, B., Shi, L., Campagne, F., and Gross, S. S. (2006). SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures. Proc. Natl. Acad. Sci. U.S.A. 103, 1012-1017.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 1012-1017
    • Hao, G.1    Derakhshan, B.2    Shi, L.3    Campagne, F.4    Gross, S.S.5
  • 42
    • 4644227523 scopus 로고    scopus 로고
    • Nitric oxide represses the Arabidopsis floral transition
    • He, Y., Tang, R. H., Hao, Y., Stevens, R. D., Cook, C. W., Ahn, S. M., et al. (2004). Nitric oxide represses the Arabidopsis floral transition. Science 305, 1968-1971.
    • (2004) Science , vol.305 , pp. 1968-1971
    • He, Y.1    Tang, R.H.2    Hao, Y.3    Stevens, R.D.4    Cook, C.W.5    Ahn, S.M.6
  • 45
    • 84856834347 scopus 로고    scopus 로고
    • Regulation by S-nitrosylation of protein post-translational modification
    • Hess, D. T., and Stamler, J. S. (2012). Regulation by S-nitrosylation of protein post-translational modification. J. Biol. Chem. 287, 4411-4418.
    • (2012) J. Biol. Chem. , vol.287 , pp. 4411-4418
    • Hess, D.T.1    Stamler, J.S.2
  • 46
    • 0034256633 scopus 로고    scopus 로고
    • Reaction of ascorbic acid with S-nitrosothiols: Clear evidence for two distinct reaction pathways
    • Holmes, A. J., and Williams, D. L. H. (2000). Reaction of ascorbic acid with S-nitrosothiols: clear evidence for two distinct reaction pathways. J. Chem. Soc. Perkin Trans. 2, 1639-1644.
    • (2000) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1639-1644
    • Holmes, A.J.1    Williams, D.L.H.2
  • 47
    • 43149119739 scopus 로고    scopus 로고
    • Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase isoforms by thiol modifications
    • Holtgrefe, S., Gohlke, J., Starmann, J., Druce, S., Klocke, S., Altmann, B., et al. (2008). Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase isoforms by thiol modifications. Physiol. Plant. 133, 211-228.
    • (2008) Physiol. Plant. , vol.133 , pp. 211-228
    • Holtgrefe, S.1    Gohlke, J.2    Starmann, J.3    Druce, S.4    Klocke, S.5    Altmann, B.6
  • 48
    • 33746070773 scopus 로고    scopus 로고
    • An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay
    • Huang, B., and Chen, C. (2006). An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay. Free Radic. Biol. Med. 41, 562-567.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 562-567
    • Huang, B.1    Chen, C.2
  • 49
    • 77954142212 scopus 로고    scopus 로고
    • Detection of protein S-nitrosation using irreversible biotinylation procedures (IBP)
    • Huang, B., and Chen, C. (2010). Detection of protein S-nitrosation using irreversible biotinylation procedures (IBP). Free Radic. Biol. Med. 49, 447-456.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 447-456
    • Huang, B.1    Chen, C.2
  • 50
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • Ignarro, L. J., Buga, G. M., Wood, K. S., Byrns, R. E., and Chaudhuri, G. (1987). Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc. Natl. Acad. Sci. U.S.A. 84, 9265-9269.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 51
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey, S. R., and Snyder, S. H. (2001). The biotin switch method for the detection of S-nitrosylated proteins. Sci. STKE 2001, pl1.
    • (2001) Sci. STKE , vol.2001
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 52
    • 0038182543 scopus 로고    scopus 로고
    • Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide. Evidence for a free radical mechanism
    • Jourd'heuil, D., Jourd'heuil, F. L., and Feelisch, M. (2003). Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide. Evidence for a free radical mechanism. J. Biol. Chem. 278, 15720-15726.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15720-15726
    • Jourd'heuil, D.1    Jourd'heuil, F.L.2    Feelisch, M.3
  • 53
    • 84879189969 scopus 로고    scopus 로고
    • Proteomic analysis of S-nitrosylated proteins in potato plant
    • doi: 10.1111/j.1399-3054.2012.01684.x [Epub ahead of print]
    • Kato, H., Takemoto, D., and Kawakita, K. (2012). Proteomic analysis of S-nitrosylated proteins in potato plant. Physiol Plant. doi: 10.1111/j.1399-3054.2012.01684.x [Epub ahead of print].
    • (2012) Physiol Plant.
    • Kato, H.1    Takemoto, D.2    Kawakita, K.3
  • 54
    • 74049084627 scopus 로고    scopus 로고
    • Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: How are S-nitrosothiols formed?
    • Keszler, A., Zhang, Y., and Hogg, N. (2010). Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: how are S-nitrosothiols formed? Free Radic. Biol. Med. 48, 55-64.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 55-64
    • Keszler, A.1    Zhang, Y.2    Hogg, N.3
  • 56
    • 52049105346 scopus 로고    scopus 로고
    • In-gel detection of S-nitrosated proteins using fluorescence methods
    • Kettenhofen, N. J., Wang, X., Gladwin, M. T., and Hogg, N. (2008). In-gel detection of S-nitrosated proteins using fluorescence methods. Methods Enzymol. 441, 53-71.
    • (2008) Methods Enzymol. , vol.441 , pp. 53-71
    • Kettenhofen, N.J.1    Wang, X.2    Gladwin, M.T.3    Hogg, N.4
  • 58
    • 29644434588 scopus 로고    scopus 로고
    • Ascorbic acid reduction of microtubule protein disulfides and its relevance to protein S-nitrosylation assays
    • Landino, L. M., Koumas, M. T., Mason, C. E., and Alston, J. A. (2006). Ascorbic acid reduction of microtubule protein disulfides and its relevance to protein S-nitrosylation assays. Biochem. Biophys. Res. Commun. 340, 347-352.
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , pp. 347-352
    • Landino, L.M.1    Koumas, M.T.2    Mason, C.E.3    Alston, J.A.4
  • 60
    • 79960305072 scopus 로고    scopus 로고
    • SNOSite: Exploiting maximal dependence decomposition to identify cysteine S-nitrosylation with substrate site specificity
    • doi: 10.1371/journal.pone.0021849
    • Lee, T. Y., Chen, Y. J., Lu, T. C., Huang, H. D., and Chen, Y. J. (2011). SNOSite: exploiting maximal dependence decomposition to identify cysteine S-nitrosylation with substrate site specificity. PLoS ONE 6:e21849. doi: 10.1371/journal.pone.0021849
    • (2011) PLoS ONE , vol.6
    • Lee, T.Y.1    Chen, Y.J.2    Lu, T.C.3    Huang, H.D.4    Chen, Y.J.5
  • 61
    • 0032212044 scopus 로고    scopus 로고
    • Evidence for the function of the free radical gas-nitric oxide (NO(center dot)-as an endogenous maturation and senescence regulating factor in higher plants
    • Leshem, Y. Y., Wills, R. B. H., and Ku, V. V. V. (1998). Evidence for the function of the free radical gas-nitric oxide (NO(center dot)-as an endogenous maturation and senescence regulating factor in higher plants. Plant Physiol. Biochem. 36, 825-833.
    • (1998) Plant Physiol. Biochem. , vol.36 , pp. 825-833
    • Leshem, Y.Y.1    Wills, R.B.H.2    Ku, V.V.V.3
  • 62
    • 84855263017 scopus 로고    scopus 로고
    • Nitric oxide and protein S-nitrosylation are integral to hydrogen peroxide-induced leaf cell death in rice
    • Lin, A., Wang, Y., Tang, J., Xue, P., Li, C., Liu, L., et al. (2012). Nitric oxide and protein S-nitrosylation are integral to hydrogen peroxide-induced leaf cell death in rice. Plant Physiol. 158, 451-464.
    • (2012) Plant Physiol. , vol.158 , pp. 451-464
    • Lin, A.1    Wang, Y.2    Tang, J.3    Xue, P.4    Li, C.5    Liu, L.6
  • 63
    • 33645240777 scopus 로고    scopus 로고
    • Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation
    • Lindermayr, C., Saalbach, G., Bahnweg, G., and Durner, J. (2006). Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation. J. Biol. Chem. 281, 4285-4291.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4285-4291
    • Lindermayr, C.1    Saalbach, G.2    Bahnweg, G.3    Durner, J.4
  • 64
    • 20344377809 scopus 로고    scopus 로고
    • Proteomic identification of S-nitrosylated proteins in Arabidopsis
    • Lindermayr, C., Saalbach, G., and Durner, J. (2005). Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant Physiol. 137, 921-930.
    • (2005) Plant Physiol. , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 65
    • 77957824005 scopus 로고    scopus 로고
    • Redox regulation of the NPR1-TGA1 system of Arabidopsis thaliana by nitric oxide
    • Lindermayr, C., Sell, S., Muller, B., Leister, D., and Durner, J. (2010). Redox regulation of the NPR1-TGA1 system of Arabidopsis thaliana by nitric oxide. Plant Cell 22, 2894-2907.
    • (2010) Plant Cell , vol.22 , pp. 2894-2907
    • Lindermayr, C.1    Sell, S.2    Muller, B.3    Leister, D.4    Durner, J.5
  • 66
    • 79851515520 scopus 로고    scopus 로고
    • Site-specific proteomics approach for study protein S-nitrosylation
    • Liu, M., Hou, J., Huang, L., Huang, X., Heibeck, T. H., Zhao, R., et al. (2010). Site-specific proteomics approach for study protein S-nitrosylation. Anal. Chem. 82, 7160-7168.
    • (2010) Anal. Chem. , vol.82 , pp. 7160-7168
    • Liu, M.1    Hou, J.2    Huang, L.3    Huang, X.4    Heibeck, T.H.5    Zhao, R.6
  • 67
    • 84862757844 scopus 로고    scopus 로고
    • Development and application of site-specific proteomic approach for study protein S-nitrosylation
    • Liu, M., Talmadge, J. E., and Ding, S. J. (2012). Development and application of site-specific proteomic approach for study protein S-nitrosylation. Amino Acids 42, 1541-1551.
    • (2012) Amino Acids , vol.42 , pp. 1541-1551
    • Liu, M.1    Talmadge, J.E.2    Ding, S.J.3
  • 68
    • 64849099434 scopus 로고    scopus 로고
    • Cyclic nucleotide gated channels and related signaling components in plant innate immunity
    • Ma, W., Smigel, A., Verma, R., and Berkowitz, G. A. (2009). Cyclic nucleotide gated channels and related signaling components in plant innate immunity. Plant Signal. Behav. 4, 277-282.
    • (2009) Plant Signal. Behav. , vol.4 , pp. 277-282
    • Ma, W.1    Smigel, A.2    Verma, R.3    Berkowitz, G.A.4
  • 69
    • 43849090222 scopus 로고    scopus 로고
    • Thiyl radicals react with nitric oxide to form S-nitrosothiols with rate constants near the diffusion-controlled limit
    • Madej, E., Folkes, L. K., Wardman, P., Czapski, G., and Goldstein, S. (2008). Thiyl radicals react with nitric oxide to form S-nitrosothiols with rate constants near the diffusion-controlled limit. Free Radic. Biol. Med. 44, 2013-2018.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 2013-2018
    • Madej, E.1    Folkes, L.K.2    Wardman, P.3    Czapski, G.4    Goldstein, S.5
  • 71
    • 73649121243 scopus 로고    scopus 로고
    • Structural analysis of cysteine S-nitrosylation: A modified acid-based motif and the emerging role of trans-nitrosylation
    • Marino, S. M., and Gladyshev, V. N. (2010). Structural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylation. J. Mol. Biol. 395, 844-859.
    • (2010) J. Mol. Biol. , vol.395 , pp. 844-859
    • Marino, S.M.1    Gladyshev, V.N.2
  • 73
    • 79957933470 scopus 로고    scopus 로고
    • Nitric oxide signaling: Classical, less classical, and nonclassical mechanisms
    • Martinez-Ruiz, A., Cadenas, S., and Lamas, S. (2011). Nitric oxide signaling: classical, less classical, and nonclassical mechanisms. Free Radic. Biol. Med. 51, 17-29.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 17-29
    • Martinez-Ruiz, A.1    Cadenas, S.2    Lamas, S.3
  • 75
    • 84870689957 scopus 로고    scopus 로고
    • Emerging role of protein-protein transnitrosylation in cell signaling pathways
    • Nakamura, T., and Lipton, S. A. (2013). Emerging role of protein-protein transnitrosylation in cell signaling pathways. Antioxid. Redox Signal. 18, 239-249.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 239-249
    • Nakamura, T.1    Lipton, S.A.2
  • 77
    • 85047684872 scopus 로고    scopus 로고
    • Nitric oxide is a novel component of abscisic acid signaling in stomatal guard cells
    • Neill, S. J., Desikan, R., Clarke, A., and Hancock, J. T. (2002). Nitric oxide is a novel component of abscisic acid signaling in stomatal guard cells. Plant Physiol. 128, 13-16.
    • (2002) Plant Physiol. , vol.128 , pp. 13-16
    • Neill, S.J.1    Desikan, R.2    Clarke, A.3    Hancock, J.T.4
  • 79
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher, P., Beckman, J. S., and Liaudet, L. (2007). Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 87, 315-424.
    • (2007) Physiol. Rev. , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 80
    • 57649198018 scopus 로고    scopus 로고
    • Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability
    • Paige, J. S., Xu, G., Stancevic, B., and Jaffrey, S. R. (2008). Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability. Chem. Biol. 15, 1307-1316.
    • (2008) Chem. Biol. , vol.15 , pp. 1307-1316
    • Paige, J.S.1    Xu, G.2    Stancevic, B.3    Jaffrey, S.R.4
  • 81
    • 0023912670 scopus 로고
    • Vascular endothelial cells synthesize nitric oxide from L-arginine
    • Palmer, R. M., Ashton, D. S., and Moncada, S. (1988). Vascular endothelial cells synthesize nitric oxide from L-arginine. Nature 333, 664-666.
    • (1988) Nature , vol.333 , pp. 664-666
    • Palmer, R.M.1    Ashton, D.S.2    Moncada, S.3
  • 82
    • 77949534774 scopus 로고    scopus 로고
    • Regulation of plant glycine decarboxylase by S-nitrosylation and glutathionylation
    • Palmieri, M. C., Lindermayr, C., Bauwe, H., Steinhauser, C., and Durner, J. (2010). Regulation of plant glycine decarboxylase by S-nitrosylation and glutathionylation. Plant Physiol. 152, 1514-1528.
    • (2010) Plant Physiol. , vol.152 , pp. 1514-1528
    • Palmieri, M.C.1    Lindermayr, C.2    Bauwe, H.3    Steinhauser, C.4    Durner, J.5
  • 83
    • 3042813441 scopus 로고    scopus 로고
    • Nitric oxide is involved in growth regulation and re-orientation of pollen tubes
    • Prado, A. M., Porterfield, D. M., and Feijo, J. A. (2004). Nitric oxide is involved in growth regulation and re-orientation of pollen tubes. Development 131, 2707-2714.
    • (2004) Development , vol.131 , pp. 2707-2714
    • Prado, A.M.1    Porterfield, D.M.2    Feijo, J.A.3
  • 84
    • 39149133106 scopus 로고    scopus 로고
    • S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration
    • Romero-Puertas, M. C., Laxa, M., Matte, A., Zaninotto, F., Finkemeier, I., Jones, A. M., et al. (2007). S-nitrosylation of peroxiredoxin II E promotes peroxynitrite-mediated tyrosine nitration. Plant Cell 19, 4120-4130.
    • (2007) Plant Cell , vol.19 , pp. 4120-4130
    • Romero-Puertas, M.C.1    Laxa, M.2    Matte, A.3    Zaninotto, F.4    Finkemeier, I.5    Jones, A.M.6
  • 86
    • 84860176878 scopus 로고    scopus 로고
    • Endogenous protein S-Nitrosylation in E. coli: Regulation by OxyR
    • Seth, D., Hausladen, A., Wang, Y. J., and Stamler, J. S. (2012). Endogenous protein S-Nitrosylation in E. coli: regulation by OxyR. Science 336, 470-473.
    • (2012) Science , vol.336 , pp. 470-473
    • Seth, D.1    Hausladen, A.2    Wang, Y.J.3    Stamler, J.S.4
  • 88
    • 84155181022 scopus 로고    scopus 로고
    • Exposure to nitric oxide increases the nitrosyl-iron complexes content in sorghum embryonic axes
    • Simontacchi, M., Buet, A., Lamattina, L., and Puntarulo, S. (2012). Exposure to nitric oxide increases the nitrosyl-iron complexes content in sorghum embryonic axes. Plant Sci. 183, 159-166.
    • (2012) Plant Sci. , vol.183 , pp. 159-166
    • Simontacchi, M.1    Buet, A.2    Lamattina, L.3    Puntarulo, S.4
  • 89
    • 0029780524 scopus 로고    scopus 로고
    • Mechanism of nitric oxide release from S-nitrosothiols
    • Singh, R. J., Hogg, N., Joseph, J., and Kalyanaraman, B. (1996). Mechanism of nitric oxide release from S-nitrosothiols. J. Biol. Chem. 271, 18596-18603.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18596-18603
    • Singh, R.J.1    Hogg, N.2    Joseph, J.3    Kalyanaraman, B.4
  • 90
    • 0034064525 scopus 로고    scopus 로고
    • Kinetics and mechanism of the decomposition of S-nitrosoglutathione by l-ascorbic acid and copper ions in aqueous solution to produce nitric oxide
    • Smith, J. N., and Dasgupta, T. P. (2000). Kinetics and mechanism of the decomposition of S-nitrosoglutathione by l-ascorbic acid and copper ions in aqueous solution to produce nitric oxide. Nitric Oxide 4, 57-66.
    • (2000) Nitric Oxide , vol.4 , pp. 57-66
    • Smith, J.N.1    Dasgupta, T.P.2
  • 91
    • 0030956929 scopus 로고    scopus 로고
    • SNO signals: Translocation, regulation, and a consensus motif
    • Stamler, J. S., Toone, E. J., Lipton, S. A., and Sucher, N. J. (1997). (S)NO signals: translocation, regulation, and a consensus motif. Neuron 18, 691-696.
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 92
    • 0033214985 scopus 로고    scopus 로고
    • Mechanism of S-nitrosothiol formation and degradation mediated by copper ions
    • Stubauer, G., Giuffre, A., and Sarti, P. (1999). Mechanism of S-nitrosothiol formation and degradation mediated by copper ions. J. Biol. Chem. 274, 28128-28133.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28128-28133
    • Stubauer, G.1    Giuffre, A.2    Sarti, P.3
  • 93
    • 49649112131 scopus 로고    scopus 로고
    • Plant immunity requires conformational changes [corrected] of NPR1 via S-nitrosylation and thioredoxins
    • Tada, Y., Spoel, S. H., Pajerowska-Mukhtar, K., Mou, Z., Song, J., Wang, C., et al. (2008). Plant immunity requires conformational changes [corrected] of NPR1 via S-nitrosylation and thioredoxins. Science 321, 952-956.
    • (2008) Science , vol.321 , pp. 952-956
    • Tada, Y.1    Spoel, S.H.2    Pajerowska-Mukhtar, K.3    Mou, Z.4    Song, J.5    Wang, C.6
  • 94
    • 73249139291 scopus 로고    scopus 로고
    • A "fluorescence switch" technique increases the sensitivity of proteomic detection and identification of S-nitrosylated proteins
    • Tello, D., Tarin, C., Ahicart, P., Breton-Romero, R., Lamas, S., and Martinez-Ruiz, A. (2009). A "fluorescence switch" technique increases the sensitivity of proteomic detection and identification of S-nitrosylated proteins. Proteomics 9, 5359-5370.
    • (2009) Proteomics , vol.9 , pp. 5359-5370
    • Tello, D.1    Tarin, C.2    Ahicart, P.3    Breton-Romero, R.4    Lamas, S.5    Martinez-Ruiz, A.6
  • 95
    • 84859597311 scopus 로고    scopus 로고
    • Nitric oxide influences auxin signaling through S-nitrosylation of the Arabidopsis TRANSPORT INHIBITOR RESPONSE 1 auxin receptor
    • Terrile, M. C., Paris, R., Calderon-Villalobos, L. I., Iglesias, M. J., Lamattina, L., Estelle, M., et al. (2012). Nitric oxide influences auxin signaling through S-nitrosylation of the Arabidopsis TRANSPORT INHIBITOR RESPONSE 1 auxin receptor. Plant J. 70, 492-500.
    • (2012) Plant J. , vol.70 , pp. 492-500
    • Terrile, M.C.1    Paris, R.2    Calderon-Villalobos, L.I.3    Iglesias, M.J.4    Lamattina, L.5    Estelle, M.6
  • 96
    • 84861321238 scopus 로고    scopus 로고
    • Connecting the chemical and biological properties of nitric oxide
    • Toledo, J. C. Jr., and Augusto, O. (2012). Connecting the chemical and biological properties of nitric oxide. Chem. Res. Toxicol. 25, 975-989.
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 975-989
    • Toledo Jr., J.C.1    Augusto, O.2
  • 97
    • 84864120813 scopus 로고    scopus 로고
    • Quantitative analysis of S-nitrosylated proteins
    • Torta, F., and Bachi, A. (2012). Quantitative analysis of S-nitrosylated proteins. Methods Mol. Biol. 893, 405-416.
    • (2012) Methods Mol. Biol. , vol.893 , pp. 405-416
    • Torta, F.1    Bachi, A.2
  • 98
    • 55849097315 scopus 로고    scopus 로고
    • Proteomic analysis of protein S-nitrosylation
    • Torta, F., Usuelli, V., Malgaroli, A., and Bachi, A. (2008). Proteomic analysis of protein S-nitrosylation. Proteomics 8, 4484-4494.
    • (2008) Proteomics , vol.8 , pp. 4484-4494
    • Torta, F.1    Usuelli, V.2    Malgaroli, A.3    Bachi, A.4
  • 100
    • 15144349362 scopus 로고    scopus 로고
    • Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide
    • van der Vliet, A., Hoen, P. A., Wong, P. S., Bast, A., and Cross, C. E. (1998). Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide. J. Biol. Chem. 273, 30255-30262.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30255-30262
    • van der Vliet, A.1    Hoen, P.A.2    Wong, P.S.3    Bast, A.4    Cross, C.E.5
  • 101
    • 0031417313 scopus 로고    scopus 로고
    • Iron catalyzes both decomposition and synthesis of S-nitrosothiols: Optical and electron paramagnetic resonance studies
    • Vanin, A. F., Malenkova, I. V., and Serezhenkov, V. A. (1997). Iron catalyzes both decomposition and synthesis of S-nitrosothiols: optical and electron paramagnetic resonance studies. Nitric Oxide 1, 191-203.
    • (1997) Nitric Oxide , vol.1 , pp. 191-203
    • Vanin, A.F.1    Malenkova, I.V.2    Serezhenkov, V.A.3
  • 102
    • 40949098241 scopus 로고    scopus 로고
    • Copper dependence of the biotin switch assay: Modified assay for measuring cellular and blood nitrosated proteins
    • Wang, X., Kettenhofen, N. J., Shiva, S., Hogg, N., and Gladwin, M. T. (2008). Copper dependence of the biotin switch assay: modified assay for measuring cellular and blood nitrosated proteins. Free Radic. Biol. Med. 44, 1362-1372.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1362-1372
    • Wang, X.1    Kettenhofen, N.J.2    Shiva, S.3    Hogg, N.4    Gladwin, M.T.5
  • 103
    • 59049098945 scopus 로고    scopus 로고
    • S-nitrosylation of AtSABP3 antagonizes the expression of plant immunity
    • Wang, Y. Q., Feechan, A., Yun, B. W., Shafiei, R., Hofmann, A., Taylor, P., et al. (2009). S-nitrosylation of AtSABP3 antagonizes the expression of plant immunity. J. Biol. Chem. 284, 2131-2137.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2131-2137
    • Wang, Y.Q.1    Feechan, A.2    Yun, B.W.3    Shafiei, R.4    Hofmann, A.5    Taylor, P.6
  • 104
    • 79959423082 scopus 로고    scopus 로고
    • Quantification of cysteinyl S-nitrosylation by fluorescence in unbiased proteomic studies
    • Wiktorowicz, J. E., Stafford, S., Rea, H., Urvil, P., Soman, K., Kurosky, A., et al. (2011). Quantification of cysteinyl S-nitrosylation by fluorescence in unbiased proteomic studies. Biochemistry 50, 5601-5614.
    • (2011) Biochemistry , vol.50 , pp. 5601-5614
    • Wiktorowicz, J.E.1    Stafford, S.2    Rea, H.3    Urvil, P.4    Soman, K.5    Kurosky, A.6
  • 105
    • 41849130604 scopus 로고    scopus 로고
    • Nitric oxide synthesis and signalling in plants
    • Wilson, I. D., Neill, S. J., and Hancock, J. T. (2008). Nitric oxide synthesis and signalling in plants. Plant Cell Environ. 31, 622-631.
    • (2008) Plant Cell Environ. , vol.31 , pp. 622-631
    • Wilson, I.D.1    Neill, S.J.2    Hancock, J.T.3
  • 106
    • 0028015989 scopus 로고
    • Reaction kinetics for nitrosation of cysteine and glutathione in aerobic nitric oxide solutions at neutral pH. Insights into the fate and physiological effects of intermediates generated in the NO/O2 reaction
    • Wink, D. A., Nims, R. W., Darbyshire, J. F., Christodoulou, D., Hanbauer, I., Cox, G. W., et al. (1994). Reaction kinetics for nitrosation of cysteine and glutathione in aerobic nitric oxide solutions at neutral pH. Insights into the fate and physiological effects of intermediates generated in the NO/O2 reaction. Chem. Res. Toxicol. 7, 519-525.
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 519-525
    • Wink, D.A.1    Nims, R.W.2    Darbyshire, J.F.3    Christodoulou, D.4    Hanbauer, I.5    Cox, G.W.6
  • 107
    • 84873575437 scopus 로고    scopus 로고
    • ISNO-PseAAC: Predict cysteine S-nitrosylation sites in proteins by incorporating position specific amino acid propensity into pseudo amino acid composition
    • doi: 10.1371/journal.pone.0055844
    • Xu, Y., Ding, J., Wu, L. Y., and Chou, K. C. (2013). iSNO-PseAAC: predict cysteine S-nitrosylation sites in proteins by incorporating position specific amino acid propensity into pseudo amino acid composition. PLoS ONE 8:e55844. doi: 10.1371/journal.pone.0055844
    • (2013) PLoS ONE , vol.8
    • Xu, Y.1    Ding, J.2    Wu, L.Y.3    Chou, K.C.4
  • 108
    • 77955283497 scopus 로고    scopus 로고
    • GPS-SNO: Computational prediction of protein S-nitrosylation sites with a modified GPS algorithm
    • doi: 10.1371/journal.pone.0011290
    • Xue, Y., Liu, Z., Gao, X., Jin, C., Wen, L., Yao, X., et al. (2010). GPS-SNO: computational prediction of protein S-nitrosylation sites with a modified GPS algorithm. PLoS ONE 5:e11290. doi: 10.1371/journal.pone.0011290
    • (2010) PLoS ONE , vol.5
    • Xue, Y.1    Liu, Z.2    Gao, X.3    Jin, C.4    Wen, L.5    Yao, X.6
  • 109
    • 84864526136 scopus 로고    scopus 로고
    • A sleigh ride through the SNO: Regulation of plant immune function by protein S-nitrosylation
    • Yu, M., Yun, B. W., Spoel, S. H., and Loake, G. J. (2012). A sleigh ride through the SNO: regulation of plant immune function by protein S-nitrosylation. Curr. Opin. Plant Biol. 15, 424-430.
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 424-430
    • Yu, M.1    Yun, B.W.2    Spoel, S.H.3    Loake, G.J.4
  • 110
    • 80054013682 scopus 로고    scopus 로고
    • S-nitrosylation of NADPH oxidase regulates cell death in plant immunity
    • Yun, B. W., Feechan, A., Yin, M., Saidi, N. B., Le Bihan, T., Yu, M., et al. (2011). S-nitrosylation of NADPH oxidase regulates cell death in plant immunity. Nature 478, 264-268.
    • (2011) Nature , vol.478 , pp. 264-268
    • Yun, B.W.1    Feechan, A.2    Yin, M.3    Saidi, N.B.4    Le Bihan, T.5    Yu, M.6
  • 111
    • 84885944025 scopus 로고    scopus 로고
    • SNObase, a database for S-nitrosation modification
    • Zhang, X., Huang, B., Zhang, L., Zhang, Y., Zhao, Y., Guo, X., et al. (2012). SNObase, a database for S-nitrosation modification. Protein Cell 3, 929-933.
    • (2012) Protein Cell , vol.3 , pp. 929-933
    • Zhang, X.1    Huang, B.2    Zhang, L.3    Zhang, Y.4    Zhao, Y.5    Guo, X.6
  • 112
    • 14644423288 scopus 로고    scopus 로고
    • Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins
    • Zhang, Y., Keszler, A., Broniowska, K. A., and Hogg, N. (2005). Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins. Free Radic. Biol. Med. 38, 874-881.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 874-881
    • Zhang, Y.1    Keszler, A.2    Broniowska, K.A.3    Hogg, N.4
  • 113
    • 34548247715 scopus 로고    scopus 로고
    • Nitric oxide is involved in nitrate-induced inhibition of root elongation in Zea mays
    • Zhao, D. Y., Tian, Q. Y., Li, L. H., and Zhang, W. H. (2007). Nitric oxide is involved in nitrate-induced inhibition of root elongation in Zea mays. Ann. Bot. 100, 497-503.
    • (2007) Ann. Bot. , vol.100 , pp. 497-503
    • Zhao, D.Y.1    Tian, Q.Y.2    Li, L.H.3    Zhang, W.H.4
  • 114
    • 77956302110 scopus 로고    scopus 로고
    • ESNOQ, proteomic quantification of endogenous S-nitrosation
    • doi: 10.1371/journal.pone.0010015
    • Zhou, X., Han, P., Li, J., Zhang, X., Huang, B., Ruan, H. Q., et al. (2010). ESNOQ, proteomic quantification of endogenous S-nitrosation. PLoS ONE 5:e10015. doi: 10.1371/journal.pone.0010015
    • (2010) PLoS ONE , vol.5
    • Zhou, X.1    Han, P.2    Li, J.3    Zhang, X.4    Huang, B.5    Ruan, H.Q.6


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