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Volumn 42, Issue 4, 2014, Pages 971-978

Intermolecular disulfide-dependent redox signalling

Author keywords

Cysteine oxidation; Forkhead box O transcription factor (FOXO transcription factor); Intermolecular disulfide; Redox signalling

Indexed keywords

APOPTOTIC SIGNALLING KINASE 1; ATM PROTEIN; CGMP ACTIVATED PROTEIN TYPE 1ALPHA; CYSTEINE; DISULFIDE; E1A ASSOCIATED P300 PROTEIN; HISTONE ACETYLTRANSFERASE PCAF; NUCLEOPORIN; PROTEIN; SUMO PROTEIN; TRANSCRIPTION FACTOR FOXO4; TRANSPORTIN 1; UNCLASSIFIED DRUG; FORKHEAD TRANSCRIPTION FACTOR;

EID: 84905823043     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140097     Document Type: Conference Paper
Times cited : (20)

References (31)
  • 1
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel, T. (2011) Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7-15
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 2
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • Dickinson, B.C. and Chang, C.J. (2011) Chemistry and biology of reactive oxygen species in signaling or stress responses. Nat. Chem. Biol. 7, 504-511
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 3
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. Cerevisiae sulphiredoxin
    • Biteau, B., Labarre, J. and Toledano, M.B. (2003) ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425, 980-984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 4
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
    • Chang, T.S., Jeong, W., Woo, H.A., Lee, S.M., Park, S. and Rhee, S.G. (2004) Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J. Biol. Chem. 279, 50994-51001
    • (2004) J. Biol. Chem. , vol.279 , pp. 50994-51001
    • Chang, T.S.1    Jeong, W.2    Woo, H.A.3    Lee, S.M.4    Park, S.5    Rhee, S.G.6
  • 5
    • 77956140082 scopus 로고    scopus 로고
    • Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding
    • Rehder, D.S. and Borges, C.R. (2010) Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding. Biochemistry 49, 7748-7755
    • (2010) Biochemistry , vol.49 , pp. 7748-7755
    • Rehder, D.S.1    Borges, C.R.2
  • 6
    • 84884197445 scopus 로고    scopus 로고
    • Oxidant sensing by reversible disulfide bond formation
    • Cremers, C.M. and Jakob, U. (2013) Oxidant sensing by reversible disulfide bond formation. J. Biol. Chem. 288, 26489-26496
    • (2013) J. Biol. Chem. , vol.288 , pp. 26489-26496
    • Cremers, C.M.1    Jakob, U.2
  • 7
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren, A. (1995) Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 3, 239-243
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 8
    • 84875720244 scopus 로고    scopus 로고
    • Glutaredoxins in thiol/disulfide exchange
    • Lillig, C.H. and Berndt, C. (2013) Glutaredoxins in thiol/disulfide exchange. Antioxid. Redox Signal. 18, 1654-1665
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 1654-1665
    • Lillig, C.H.1    Berndt, C.2
  • 9
    • 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
  • 10
    • 20744438779 scopus 로고    scopus 로고
    • Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide
    • Bozonet, S.M., Findlay, V.J., Day, A.M., Cameron, J., Veal, E.A. and Morgan, B.A. (2005) Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide. J. Biol. Chem. 280, 23319-23327
    • (2005) J. Biol. Chem. , vol.280 , pp. 23319-23327
    • Bozonet, S.M.1    Findlay, V.J.2    Day, A.M.3    Cameron, J.4    Veal, E.A.5    Morgan, B.A.6
  • 11
    • 84866357593 scopus 로고    scopus 로고
    • Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells
    • Jarvis, R.M., Hughes, S.M. and Ledgerwood, E.C. (2012) Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells. Free Radic. Biol. Med. 53, 1522-1530
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1522-1530
    • Jarvis, R.M.1    Hughes, S.M.2    Ledgerwood, E.C.3
  • 12
    • 84856940017 scopus 로고    scopus 로고
    • Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
    • Rhee, S.G., Woo, H.A., Kil, I.S. and Bae, S.H. (2012) Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides. J. Biol. Chem. 287, 4403-4410
    • (2012) J. Biol. Chem. , vol.287 , pp. 4403-4410
    • Rhee, S.G.1    Woo, H.A.2    Kil, I.S.3    Bae, S.H.4
  • 14
    • 0032504189 scopus 로고    scopus 로고
    • Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-alpha signal transduction
    • Gotoh, Y. and Cooper, J.A. (1998) Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-alpha signal transduction. J. Biol. Chem. 273, 17477-17482
    • (1998) J. Biol. Chem. , vol.273 , pp. 17477-17482
    • Gotoh, Y.1    Cooper, J.A.2
  • 15
    • 34948845017 scopus 로고    scopus 로고
    • Disulfide bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H2O2-induced c-Jun NH2-terminal kinase activation and apoptosis
    • Nadeau, P.J., Charette, S.J., Toledano, M.B. and Landry, J. (2007) Disulfide bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H2O2-induced c-Jun NH2-terminal kinase activation and apoptosis. Mol. Biol. Cell 18, 3903-3913
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3903-3913
    • Nadeau, P.J.1    Charette, S.J.2    Toledano, M.B.3    Landry, J.4
  • 16
    • 4744363388 scopus 로고    scopus 로고
    • Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis
    • Brennan, J.P., Wait, R., Begum, S., Bell, J.R., Dunn, M.J. and Eaton, P. (2004) Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis. J. Biol. Chem. 279, 41352-41360
    • (2004) J. Biol. Chem. , vol.279 , pp. 41352-41360
    • Brennan, J.P.1    Wait, R.2    Begum, S.3    Bell, J.R.4    Dunn, M.J.5    Eaton, P.6
  • 18
  • 19
    • 84874041662 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling by protein kinases in the cardiovascular system
    • Burgoyne, J.R., Oka, S., Ale-Agha, N. and Eaton, P. (2013) Hydrogen peroxide sensing and signaling by protein kinases in the cardiovascular system. Antioxid. Redox Signal. 18, 1042-1052
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 1042-1052
    • Burgoyne, J.R.1    Oka, S.2    Ale-Agha, N.3    Eaton, P.4
  • 21
    • 84856701189 scopus 로고    scopus 로고
    • Single atom substitution in mouse protein kinase G eliminates oxidant sensing to cause hypertension
    • Prysyazhna, O., Rudyk, O. and Eaton, P. (2012) Single atom substitution in mouse protein kinase G eliminates oxidant sensing to cause hypertension. Nat. Methods 18, 286-290
    • (2012) Nat. Methods , vol.18 , pp. 286-290
    • Prysyazhna, O.1    Rudyk, O.2    Eaton, P.3
  • 23
    • 84878944582 scopus 로고    scopus 로고
    • SUMOylation: A regulatory protein modification in health and disease
    • Flotho, A. and Melchior, F. (2013) SUMOylation: a regulatory protein modification in health and disease. Annu. Rev. Biochem. 82, 357-385
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 24
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes
    • Bossis, G. and Melchior, F. (2006) Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes. Mol. Cell 21, 349-357
    • (2006) Mol. Cell , vol.21 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 25
    • 84880666472 scopus 로고    scopus 로고
    • Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport
    • Yoshimura, S.H., Otsuka, S., Kumeta, M., Taga, M. and Takeyasu, K. (2013) Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport. J. Cell Sci. 126, 3141-3150
    • (2013) J. Cell Sci. , vol.126 , pp. 3141-3150
    • Yoshimura, S.H.1    Otsuka, S.2    Kumeta, M.3    Taga, M.4    Takeyasu, K.5
  • 26
    • 79951887419 scopus 로고    scopus 로고
    • Forkhead box o as a sensor, mediator, and regulator of redox signaling
    • de Keizer, P.L., Burgering, B.M. and Dansen, T.B. (2011) Forkhead box o as a sensor, mediator, and regulator of redox signaling. Antioxid. Redox Signal. 14, 1093-1106
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1093-1106
    • De Keizer, P.L.1    Burgering, B.M.2    Dansen, T.B.3
  • 28
    • 73649087930 scopus 로고    scopus 로고
    • Synergistic interplay between promoter recognition and CBP/p300 coactivator recruitment by FOXO3a
    • Wang, F., Marshall, C.B., Li, G.Y., Yamamoto, K., Mak, T.W. and Ikura, M. (2009) Synergistic interplay between promoter recognition and CBP/p300 coactivator recruitment by FOXO3a. ACS Chem. Biol. 4, 1017-1027
    • (2009) ACS Chem. Biol. , vol.4 , pp. 1017-1027
    • Wang, F.1    Marshall, C.B.2    Li, G.Y.3    Yamamoto, K.4    Mak, T.W.5    Ikura, M.6
  • 29
    • 24344499875 scopus 로고    scopus 로고
    • The coactivator p300 directly acetylates the forkhead transscription factor Foxo1 and stimulates Foxo1-induced transcription
    • Perrot, V. and Rechler, M.M. (2005) The coactivator p300 directly acetylates the forkhead transscription factor Foxo1 and stimulates Foxo1-induced transcription. Mol. Endocrinol. 19, 2283-2298
    • (2005) Mol. Endocrinol. , vol.19 , pp. 2283-2298
    • Perrot, V.1    Rechler, M.M.2
  • 31
    • 84865826148 scopus 로고    scopus 로고
    • Diagonal electrophoresis for the detection of protein disulfides
    • McDonagh, B. (2012) Diagonal electrophoresis for the detection of protein disulfides. Methods Mol. Biol. 869, 309-315
    • (2012) Methods Mol. Biol. , vol.869 , pp. 309-315
    • McDonagh, B.1


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