메뉴 건너뛰기




Volumn 288, Issue 31, 2013, Pages 22777-22789

Mechanisms of nitrosylation and denitrosylation of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; GLUTATHIONES; GLUTATHIONYLATION; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; NITROSYLATION; THIOREDOXINS;

EID: 84881253817     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.475467     Document Type: Article
Times cited : (90)

References (94)
  • 1
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: A current perspective
    • Foster, M. W., Hess, D. T., and Stamler, J. S. (2009) Protein S-nitrosylation in health and disease: a current perspective. Trends Mol. Med. 15, 391-404
    • (2009) Trends Mol. Med. , vol.15 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 2
    • 71849114694 scopus 로고    scopus 로고
    • Oxidative stress and human diseases: Origin, link, measurement, mechanisms, and biomarkers
    • Giustarini, D., Dalle-Donne, I., Tsikas, D., and Rossi, R. (2009) Oxidative stress and human diseases: origin, link, measurement, mechanisms, and biomarkers. Crit. Rev. Clin. Lab. Sci. 46, 241-281
    • (2009) Crit. Rev. Clin. Lab. Sci. , vol.46 , pp. 241-281
    • Giustarini, D.1    Dalle-Donne, I.2    Tsikas, D.3    Rossi, R.4
  • 3
    • 34247158550 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases
    • Trushina, E., and McMurray, C. T. (2007) Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases. Neuroscience 145, 1233-1248
    • (2007) Neuroscience , vol.145 , pp. 1233-1248
    • Trushina, E.1    McMurray, C.T.2
  • 4
    • 79954599366 scopus 로고    scopus 로고
    • S-Glutathionylation: From molecular mechanisms to health outcomes
    • Xiong, Y., Uys, J. D., Tew, K. D., and Townsend, D. M. (2011) S-Glutathionylation: From molecular mechanisms to health outcomes. Antioxid. Redox Signal. 15, 233-270
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 233-270
    • Xiong, Y.1    Uys, J.D.2    Tew, K.D.3    Townsend, D.M.4
  • 5
    • 45249088541 scopus 로고    scopus 로고
    • Redox signal integration: From stimulus to networks and genes
    • Dietz, K. J. (2008) Redox signal integration: from stimulus to networks and genes. Physiol. Plant. 133, 459-468
    • (2008) Physiol. Plant. , vol.133 , pp. 459-468
    • Dietz, K.J.1
  • 6
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • Forman, H. J., Maiorino, M., and Ursini, F. (2010) Signaling functions of reactive oxygen species. Biochemistry 49, 835-842
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 7
    • 60749136076 scopus 로고    scopus 로고
    • Redox regulation in photosynthetic organisms: Signaling, acclimation, and practical implications
    • Foyer, C. H., and Noctor, G. (2009) Redox regulation in photosynthetic organisms: signaling, acclimation, and practical implications. Antioxid. Redox Signal. 11, 861-905
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 861-905
    • Foyer, C.H.1    Noctor, G.2
  • 8
    • 70350564926 scopus 로고    scopus 로고
    • The role of redox mechanisms in cell signalling
    • Hancock, J. T. (2009) The role of redox mechanisms in cell signalling. Mol. Biotechnol. 43, 162-166
    • (2009) Mol. Biotechnol. , vol.43 , pp. 162-166
    • Hancock, J.T.1
  • 9
    • 46149098907 scopus 로고    scopus 로고
    • Oxygen-regulated isoforms of cytochrome c oxidase have differential effects on its nitric oxide production and on hypoxic signaling
    • Castello, P. R., Woo, D. K., Ball, K., Wojcik, J., Liu, L., and Poyton, R. O. (2008) Oxygen-regulated isoforms of cytochrome c oxidase have differential effects on its nitric oxide production and on hypoxic signaling. Proc. Natl. Acad. Sci. U.S.A. 105, 8203-8208
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 8203-8208
    • Castello, P.R.1    Woo, D.K.2    Ball, K.3    Wojcik, J.4    Liu, L.5    Poyton, R.O.6
  • 10
    • 77952077940 scopus 로고    scopus 로고
    • The redox switch: Dynamic regulation of protein function by cysteine modifications
    • Spadaro, D., Yun, B. W., Spoel, S. H., Chu, C., Wang, Y. Q., and Loake, G. J. (2010) The redox switch: dynamic regulation of protein function by cysteine modifications. Physiol. Plant. 138, 360-371
    • (2010) Physiol. Plant. , vol.138 , pp. 360-371
    • Spadaro, D.1    Yun, B.W.2    Spoel, S.H.3    Chu, C.4    Wang, Y.Q.5    Loake, G.J.6
  • 11
    • 76349119210 scopus 로고    scopus 로고
    • Protein S-nitrosylation and cardioprotection
    • Sun, J., and Murphy, E. (2010) Protein S-nitrosylation and cardioprotection. Circ. Res. 106, 285-296
    • (2010) Circ. Res. , vol.106 , pp. 285-296
    • Sun, J.1    Murphy, E.2
  • 14
    • 79851512689 scopus 로고    scopus 로고
    • The SNO-proteome: Causation and classifications
    • Seth, D., and Stamler, J. S. (2011) The SNO-proteome: causation and classifications. Curr. Opin. Chem. Biol. 15, 129-136
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 129-136
    • Seth, D.1    Stamler, J.S.2
  • 15
    • 84866253155 scopus 로고    scopus 로고
    • Redox regulation of protein function via cysteine S-nitrosylation and its relevance to neurodegenerative diseases
    • Akhtar, M. W., Sunico, C. R., Nakamura, T., and Lipton, S. A. (2012) Redox regulation of protein function via cysteine S-nitrosylation and its relevance to neurodegenerative diseases. Int. J. Cell Biol. 2012, 463756
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 463756
    • Akhtar, M.W.1    Sunico, C.R.2    Nakamura, T.3    Lipton, S.A.4
  • 16
    • 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. 90, 233-244
    • (2012) J. Mol. Med. , vol.90 , pp. 233-244
    • Anand, P.1    Stamler, J.S.2
  • 17
    • 77949370996 scopus 로고    scopus 로고
    • S-Nitrosylation in cardiovascular signaling
    • Lima, B., Forrester, M. T., Hess, D. T., and Stamler, J. S. (2010) S-Nitrosylation in cardiovascular signaling. Circ. Res. 106, 633-646
    • (2010) Circ. Res. , vol.106 , pp. 633-646
    • Lima, B.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 18
    • 77952075913 scopus 로고    scopus 로고
    • NO synthesis and signaling in plants-where do we stand?
    • Moreau, M., Lindermayr, C., Durner, J., and Klessig, D. F. (2010) NO synthesis and signaling in plants-where do we stand? Physiol. Plant. 138, 372-383
    • (2010) Physiol. Plant. , vol.138 , pp. 372-383
    • Moreau, M.1    Lindermayr, C.2    Durner, J.3    Klessig, D.F.4
  • 20
    • 70349977142 scopus 로고    scopus 로고
    • S-Nitrosylation in plants: Pattern and function
    • Lindermayr, C., and Durner, J. (2009) S-Nitrosylation in plants: pattern and function. J. Proteomics 73, 1-9
    • (2009) J. Proteomics , vol.73 , pp. 1-9
    • Lindermayr, C.1    Durner, J.2
  • 21
    • 84864526136 scopus 로고    scopus 로고
    • A sleigh ride through the SNO: Regulation of plant immune function by protein Snitrosylation
    • 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 Snitrosylation. 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
  • 22
    • 84866853296 scopus 로고    scopus 로고
    • Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ ATPase CDC48, a target for S-nitrosylation in cryptogein signalling in tobacco cells
    • Astier, J., Besson-Bard, A., Lamotte, O., Bertoldo, J., Bourque, S., Terenzi, H., and Wendehenne, D. (2012) Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ ATPase CDC48, a target for S-nitrosylation in cryptogein signalling in tobacco cells. Biochem. J. 447, 249-260
    • (2012) Biochem. J. , vol.447 , pp. 249-260
    • Astier, J.1    Besson-Bard, A.2    Lamotte, O.3    Bertoldo, J.4    Bourque, S.5    Terenzi, H.6    Wendehenne, D.7
  • 23
    • 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
  • 24
    • 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., Zuo, J., and Dong, X. (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    Zuo, J.7    Dong, X.8
  • 28
    • 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
  • 29
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-Nitrosothiols
    • Hogg, N. (2002) The biochemistry and physiology of S-Nitrosothiols. Annu. Rev. Pharmacol. Toxicol. 42, 585-600
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 585-600
    • Hogg, N.1
  • 30
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • Pawloski, J. R., Hess, D. T., and Stamler, J. S. (2001) Export by red blood cells of nitric oxide bioactivity. Nature 409, 622-626
    • (2001) Nature , vol.409 , pp. 622-626
    • Pawloski, J.R.1    Hess, D.T.2    Stamler, J.S.3
  • 31
    • 33644818614 scopus 로고    scopus 로고
    • Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine
    • Mitchell, D. A., and Marletta, M. A. (2005) Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. Nat. Chem. Biol. 1, 154-158
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 154-158
    • Mitchell, D.A.1    Marletta, M.A.2
  • 32
    • 34547427294 scopus 로고    scopus 로고
    • Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells
    • Mitchell, D. A., Morton, S. U., Fernhoff, N. B., and Marletta, M. A. (2007) Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells. Proc. Natl. Acad. Sci. U.S.A. 104, 11609-11614
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 11609-11614
    • Mitchell, D.A.1    Morton, S.U.2    Fernhoff, N.B.3    Marletta, M.A.4
  • 35
    • 80052150240 scopus 로고    scopus 로고
    • S-Nitrosylation activates Cdk5 and contributes to synaptic spine loss induced by-amyloid peptide
    • Qu, J., Nakamura, T., Cao, G., Holland, E. A., McKercher, S. R., and Lipton, S. A. (2011) S-Nitrosylation activates Cdk5 and contributes to synaptic spine loss induced by-amyloid peptide. Proc. Natl. Acad. Sci. U.S.A. 108, 14330-14335
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14330-14335
    • Qu, J.1    Nakamura, T.2    Cao, G.3    Holland, E.A.4    McKercher, S.R.5    Lipton, S.A.6
  • 39
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J., and Stamler, J. S. (2001) A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410, 490-494
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 40
    • 81055143827 scopus 로고    scopus 로고
    • Detection and quantification of S-nitrosoglutathione (GSNO) in pepper (Capsicum annuum L.) plant organs by LC-ES/MS
    • Airaki, M., Sanchez-Moreno, L., Leterrier, M., Barroso, J. B., Palma, J. M., and Corpas, F. J. (2011) Detection and quantification of S-nitrosoglutathione (GSNO) in pepper (Capsicum annuum L.) plant organs by LC-ES/MS. Plant Cell Physiol. 52, 2006-2015
    • (2011) Plant Cell Physiol. , vol.52 , pp. 2006-2015
    • Airaki, M.1    Sanchez-Moreno, L.2    Leterrier, M.3    Barroso, J.B.4    Palma, J.M.5    Corpas, F.J.6
  • 41
    • 15744403464 scopus 로고    scopus 로고
    • Characterization of the Sdenitrosation activity of protein-disulfide isomerase
    • Sliskovic, I., Raturi, A., and Mutus, B. (2005) Characterization of the Sdenitrosation activity of protein-disulfide isomerase. J. Biol. Chem. 280, 8733-8741
    • (2005) J. Biol. Chem. , vol.280 , pp. 8733-8741
    • Sliskovic, I.1    Raturi, A.2    Mutus, B.3
  • 42
    • 0029764601 scopus 로고    scopus 로고
    • S-Nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide
    • Nikitovic, D., and Holmgren, A. (1996) S-Nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide. J. Biol. Chem. 271, 19180-19185
    • (1996) J. Biol. Chem. , vol.271 , pp. 19180-19185
    • Nikitovic, D.1    Holmgren, A.2
  • 46
    • 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. (2009) 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
  • 48
    • 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
  • 49
    • 62849091792 scopus 로고    scopus 로고
    • Intracellular glutathione mediates the denitrosylation of protein nitrosothiols in the rat spinal cord
    • Romero, J. M., and Bizzozero, O. A. (2009) Intracellular glutathione mediates the denitrosylation of protein nitrosothiols in the rat spinal cord. J. Neurosci. Res. 87, 701-709
    • (2009) J. Neurosci. Res. , vol.87 , pp. 701-709
    • Romero, J.M.1    Bizzozero, O.A.2
  • 50
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar, M., Forrester, M. T., Hess, D. T., and Stamler, J. S. (2008) Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320, 1050-1054
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 51
    • 77955576782 scopus 로고    scopus 로고
    • Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach
    • Benhar, M., Thompson, J. W., Moseley, M. A., and Stamler, J. S. (2010) Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach. Biochemistry 49, 6963-6969
    • (2010) Biochemistry , vol.49 , pp. 6963-6969
    • Benhar, M.1    Thompson, J.W.2    Moseley, M.A.3    Stamler, J.S.4
  • 53
    • 80054870283 scopus 로고    scopus 로고
    • Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach
    • Wu, C., Parrott, A. M., Liu, T., Jain, M. R., Yang, Y., Sadoshima, J., and Li, H. (2011) Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach. J. Proteomics 74, 2498-2509
    • (2011) J. Proteomics , vol.74 , pp. 2498-2509
    • Wu, C.1    Parrott, A.M.2    Liu, T.3    Jain, M.R.4    Yang, Y.5    Sadoshima, J.6    Li, H.7
  • 54
    • 84870715491 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase in relation to reversible S-nitrosylation
    • Sengupta, R., and Holmgren, A. (2013) Thioredoxin and thioredoxin reductase in relation to reversible S-nitrosylation. Antioxid. Redox Signal. 18, 259-269
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 259-269
    • Sengupta, R.1    Holmgren, A.2
  • 55
    • 79959226194 scopus 로고    scopus 로고
    • On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control
    • Sirover, M. A. (2011) On the functional diversity of glyceraldehyde-3- phosphate dehydrogenase: biochemical mechanisms and regulatory control. Biochim. Biophys. Acta 1810, 741-751
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 741-751
    • Sirover, M.A.1
  • 56
    • 78649842470 scopus 로고    scopus 로고
    • The diverse functions of GAPDH: Views from different subcellular compartments
    • Tristan, C., Shahani, N., Sedlak, T. W., and Sawa, A. (2011) The diverse functions of GAPDH: views from different subcellular compartments. Cell. Signal. 23, 317-323
    • (2011) Cell. Signal. , vol.23 , pp. 317-323
    • Tristan, C.1    Shahani, N.2    Sedlak, T.W.3    Sawa, A.4
  • 60
    • 84864327019 scopus 로고    scopus 로고
    • Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro
    • Bedhomme, M., Adamo, M., Marchand, C. H., Couturier, J., Rouhier, N., Lemaire, S. D., Zaffagnini, M., and Trost, P. (2012) Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro. Biochem. J. 445, 337-347
    • (2012) Biochem. J. , vol.445 , pp. 337-347
    • Bedhomme, M.1    Adamo, M.2    Marchand, C.H.3    Couturier, J.4    Rouhier, N.5    Lemaire, S.D.6    Zaffagnini, M.7    Trost, P.8
  • 62
    • 77952955260 scopus 로고    scopus 로고
    • Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: Kinetics and specificity in deglutathionylation reactions
    • Gao, X. H., Zaffagnini, M., Bedhomme, M., Michelet, L., Cassier-Chauvat, C., Decottignies, P., and Lemaire, S. D. (2010) Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: kinetics and specificity in deglutathionylation reactions. FEBS Lett. 584, 2242-2248
    • (2010) FEBS Lett. , vol.584 , pp. 2242-2248
    • Gao, X.H.1    Zaffagnini, M.2    Bedhomme, M.3    Michelet, L.4    Cassier-Chauvat, C.5    Decottignies, P.6    Lemaire, S.D.7
  • 63
    • 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
  • 66
    • 0028354036 scopus 로고
    • Arabidopsis thaliana NADPH thioredoxin reductase cDNA characterization and expression of the recombinant protein in Escherichia coli
    • Jacquot, J. P., Rivera-Madrid, R., Marinho, P., Kollarova, M., Le Marechal, P., Miginiac-Maslow, M., and Meyer, Y. (1994) Arabidopsis thaliana NADPHthioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli. J. Mol. Biol. 235, 1357-1363
    • (1994) J. Mol. Biol. , vol.235 , pp. 1357-1363
    • Jacquot, J.P.1    Rivera-Madrid, R.2    Marinho, P.3    Kollarova, M.4    Le Marechal, P.5    Miginiac-Maslow, M.6    Meyer, Y.7
  • 67
    • 0346366724 scopus 로고    scopus 로고
    • Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction
    • Gelhaye, E., Rouhier, N., and Jacquot, J. P. (2003) Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction. FEBS Lett. 555, 443-448
    • (2003) FEBS Lett. , vol.555 , pp. 443-448
    • Gelhaye, E.1    Rouhier, N.2    Jacquot, J.P.3
  • 70
    • 4544325179 scopus 로고    scopus 로고
    • Thioredoxin Ch1 of Chlamydomonas reinhardtii displays an unusual resistance toward one-electron oxidation
    • Sicard-Roselli, C., Lemaire, S., Jacquot, J. P., Favaudon, V., Marchand, C., and Houee-Levin, C. (2004) Thioredoxin Ch1 of Chlamydomonas reinhardtii displays an unusual resistance toward one-electron oxidation. Eur. J. Biochem. 271, 3481-3487
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3481-3487
    • Sicard-Roselli, C.1    Lemaire, S.2    Jacquot, J.P.3    Favaudon, V.4    Marchand, C.5    Houee-Levin, C.6
  • 71
    • 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, p11
    • (2001) Sci. STKE 2001 , pp. 11
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 72
    • 0017576456 scopus 로고
    • Sequence and structure of D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Biesecker, G., Harris, J. I., Thierry, J. C., Walker, J. E., and Wonacott, A. J. (1977) Sequence and structure of D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Nature 266, 328-333
    • (1977) Nature , vol.266 , pp. 328-333
    • Biesecker, G.1    Harris, J.I.2    Thierry, J.C.3    Walker, J.E.4    Wonacott, A.J.5
  • 73
    • 0032521628 scopus 로고    scopus 로고
    • Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis
    • Talfournier, F., Colloc'h, N., Mornon, J. P., and Branlant, G. (1998) Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis. Eur. J. Biochem. 252, 447-457
    • (1998) Eur. J. Biochem. , vol.252 , pp. 447-457
    • Talfournier, F.1    Colloc'H, N.2    Mornon, J.P.3    Branlant, G.4
  • 74
    • 0038617423 scopus 로고    scopus 로고
    • Decomposition of protein nitrosothiols in matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry
    • Kaneko, R., and Wada, Y. (2003) Decomposition of protein nitrosothiols in matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry. J. Mass Spectrom. 38, 526-530
    • (2003) J. Mass Spectrom. , vol.38 , pp. 526-530
    • Kaneko, R.1    Wada, Y.2
  • 75
    • 0031000775 scopus 로고    scopus 로고
    • PH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • Srinivasan, U., Mieyal, P. A., and Mieyal, J. J. (1997) pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry 36, 3199-3206
    • (1997) Biochemistry , vol.36 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 76
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • Gallogly, M. M., and Mieyal, J. J. (2007) Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr. Opin. Pharmacol. 7, 381-391
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 80
    • 71949124535 scopus 로고    scopus 로고
    • Proteomics reveals the overlapping roles of hydrogen peroxide and nitric oxide in the acclimation of citrus plants to salinity
    • Tanou, G., Job, C., Rajjou, L., Arc, E., Belghazi, M., Diamantidis, G., Molassiotis, A., and Job, D. (2009) Proteomics reveals the overlapping roles of hydrogen peroxide and nitric oxide in the acclimation of citrus plants to salinity. Plant J. 60, 795-804
    • (2009) Plant J. , vol.60 , pp. 795-804
    • Tanou, G.1    Job, C.2    Rajjou, L.3    Arc, E.4    Belghazi, M.5    Diamantidis, G.6    Molassiotis, A.7    Job, D.8
  • 81
    • 84868503178 scopus 로고    scopus 로고
    • Oxidative and nitrosative-based signaling and associated post-translational modifications orchestrate the acclimation of citrus plants to salinity stress
    • Tanou, G., Filippou, P., Belghazi, M., Job, D., Diamantidis, G., Fotopoulos, V., and Molassiotis, A. (2012) Oxidative and nitrosative-based signaling and associated post-translational modifications orchestrate the acclimation of citrus plants to salinity stress. Plant J. 72, 585-599
    • (2012) Plant J. , vol.72 , pp. 585-599
    • Tanou, G.1    Filippou, P.2    Belghazi, M.3    Job, D.4    Diamantidis, G.5    Fotopoulos, V.6    Molassiotis, A.7
  • 82
    • 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
  • 84
    • 1242323413 scopus 로고    scopus 로고
    • Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus
    • Anderson, L. E., Ringenberg, M. R., and Carol, A. A. (2004) Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus. Protoplasma 223, 33-43
    • (2004) Protoplasma , vol.223 , pp. 33-43
    • Anderson, L.E.1    Ringenberg, M.R.2    Carol, A.A.3
  • 85
    • 84877044940 scopus 로고    scopus 로고
    • Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots
    • Vescovi, M., Zaffagnini, M., Festa, M., Trost, P., Lo Schiavo, F., and Costa, A. (2013) Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots. Plant Physiol. 162, 333-346
    • (2013) Plant Physiol. , vol.162 , pp. 333-346
    • Vescovi, M.1    Zaffagnini, M.2    Festa, M.3    Trost, P.4    Lo Schiavo, F.5    Costa, A.6
  • 86
    • 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
  • 87
    • 0034209724 scopus 로고    scopus 로고
    • Modification of creatine kinase by S-nitrosothiols: S-nitrosation versus S-thiolation
    • Konorev, E. A., Kalyanaraman, B., and Hogg, N. (2000) Modification of creatine kinase by S-nitrosothiols: S-nitrosation versus S-thiolation. Free Radic. Biol. Med. 28, 1671-1678
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1671-1678
    • Konorev, E.A.1    Kalyanaraman, B.2    Hogg, N.3
  • 88
    • 59249105149 scopus 로고    scopus 로고
    • S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation
    • Coles, S. J., Easton, P., Sharrod, H., Hutson, S. M., Hancock, J., Patel, V. B., and Conway, M. E. (2009) S-Nitrosoglutathione inactivation of the mitochondrial and cytosolic BCAT proteins: S-nitrosation and S-thiolation. Biochemistry 48, 645-656
    • (2009) Biochemistry , vol.48 , pp. 645-656
    • Coles, S.J.1    Easton, P.2    Sharrod, H.3    Hutson, S.M.4    Hancock, J.5    Patel, V.B.6    Conway, M.E.7
  • 89
    • 84860875546 scopus 로고    scopus 로고
    • Thioredoxin-1 regulates cellular heme insertion by controlling S-nitrosation of glyceraldehyde-3-phosphate dehydrogenase
    • Chakravarti, R., and Stuehr, D. J. (2012) Thioredoxin-1 regulates cellular heme insertion by controlling S-nitrosation of glyceraldehyde-3- phosphate dehydrogenase. J. Biol. Chem. 287, 16179-16186
    • (2012) J. Biol. Chem. , vol.287 , pp. 16179-16186
    • Chakravarti, R.1    Stuehr, D.J.2
  • 90
    • 0037438118 scopus 로고    scopus 로고
    • Subcellular alteration of glyceraldehyde-3-phosphate dehydrogenase in Alzheimer's disease fibroblasts
    • Mazzola, J. L., and Sirover, M. A. (2003) Subcellular alteration of glyceraldehyde-3-phosphate dehydrogenase in Alzheimer's disease fibroblasts. J. Neurosci. Res. 71, 279-285
    • (2003) J. Neurosci. Res. , vol.71 , pp. 279-285
    • Mazzola, J.L.1    Sirover, M.A.2
  • 91
    • 0033566144 scopus 로고    scopus 로고
    • Pea chloroplast glyceraldehyde-3-phosphate dehydrogenase has uracil glycosylase activity
    • Wang, X., Sirover, M. A., and Anderson, L. E. (1999) Pea chloroplast glyceraldehyde-3-phosphate dehydrogenase has uracil glycosylase activity. Arch. Biochem. Biophys. 367, 348-353
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 348-353
    • Wang, X.1    Sirover, M.A.2    Anderson, L.E.3
  • 93
    • 65249135989 scopus 로고    scopus 로고
    • Prompt and easy activation by specific thioredoxins of Calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex
    • Marri, L., Zaffagnini, M., Collin, V., Issakidis-Bourguet, E., Lemaire, S. D., Pupillo, P., Sparla, F., Miginiac-Maslow, M., and Trost, P. (2009) Prompt and easy activation by specific thioredoxins of Calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex. Mol. Plant 2, 259-269
    • (2009) Mol. Plant , vol.2 , pp. 259-269
    • Marri, L.1    Zaffagnini, M.2    Collin, V.3    Issakidis-Bourguet, E.4    Lemaire, S.D.5    Pupillo, P.6    Sparla, F.7    Miginiac-Maslow, M.8    Trost, P.9
  • 94
    • 84862274751 scopus 로고    scopus 로고
    • Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly
    • Fermani, S., Trivelli, X., Sparla, F., Thumiger, A., Calvaresi, M., Marri, L., Falini, G., Zerbetto, F., and Trost, P. (2012) Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. J. Biol. Chem. 287, 21372-21383
    • (2012) J. Biol. Chem. , vol.287 , pp. 21372-21383
    • Fermani, S.1    Trivelli, X.2    Sparla, F.3    Thumiger, A.4    Calvaresi, M.5    Marri, L.6    Falini, G.7    Zerbetto, F.8    Trost, P.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.