메뉴 건너뛰기




Volumn 45, Issue 1, 2008, Pages 1-17

Redox-based regulation of signal transduction: Principles, pitfalls, and promises

Author keywords

Biotin switch; Cysteine; Free radicals; Glutaredoxin; Oxidant; Peroxiredoxin; S Glutathionylation; S Nitrosylation; Signal transduction; Sulfenic acid; Thioredoxin

Indexed keywords

CHAPERONE; CYSTEINE; HYDROGEN PEROXIDE; NITRIC OXIDE; OXIDIZING AGENT; PROTEIN TYROSINE PHOSPHATASE; PROTEINASE; S NITROSOTHIOL; TRANSCRIPTION FACTOR;

EID: 45049085873     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2008.03.011     Document Type: Review
Times cited : (663)

References (243)
  • 2
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel T. Oxidant signals and oxidative stress. Curr. Opin. Cell Biol. 15 (2003) 247-254
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 247-254
    • Finkel, T.1
  • 3
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling
    • 2, a necessary evil for cell signaling. Science 312 (2006) 1882-1883
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 4
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee S.G., Bae Y.S., Lee S.R., and Kwon J. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE 2000 (2000) PE1
    • (2000) Sci. STKE , vol.2000
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 5
    • 0028220671 scopus 로고
    • Nitric oxide directly activates calcium-dependent potassium channels in vascular smooth muscle
    • Bolotina V.M., Najibi S., Palacino J.J., Pagano P.J., and Cohen R.A. Nitric oxide directly activates calcium-dependent potassium channels in vascular smooth muscle. Nature 368 (1994) 850-853
    • (1994) Nature , vol.368 , pp. 850-853
    • Bolotina, V.M.1    Najibi, S.2    Palacino, J.J.3    Pagano, P.J.4    Cohen, R.A.5
  • 7
    • 33646529673 scopus 로고    scopus 로고
    • Nitric-oxide-induced vasodilatation: regulation by physiologic S-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase
    • Cohen R.A., and Adachi T. Nitric-oxide-induced vasodilatation: regulation by physiologic S-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc. Med. 16 (2006) 109-114
    • (2006) Trends Cardiovasc. Med. , vol.16 , pp. 109-114
    • Cohen, R.A.1    Adachi, T.2
  • 11
    • 0028132836 scopus 로고
    • Redox signaling: nitrosylation and related target interactions of nitric oxide
    • Stamler J.S. Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell 78 (1994) 931-936
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 12
  • 14
    • 0037155791 scopus 로고    scopus 로고
    • Basal and stimulated protein S-nitrosylation in multiple cell types and tissues
    • Gow A.J., Chen Q., Hess D.T., Day B.J., Ischiropoulos H., and Stamler J.S. Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. J. Biol. Chem. 277 (2002) 9637-9640
    • (2002) J. Biol. Chem. , vol.277 , pp. 9637-9640
    • Gow, A.J.1    Chen, Q.2    Hess, D.T.3    Day, B.J.4    Ischiropoulos, H.5    Stamler, J.S.6
  • 17
    • 0036193746 scopus 로고    scopus 로고
    • Oxidants painting the cysteine chapel: redox regulation of PTPs
    • Xu D., Rovira I.I., and Finkel T. Oxidants painting the cysteine chapel: redox regulation of PTPs. Dev. Cell 2 (2002) 251-252
    • (2002) Dev. Cell , vol.2 , pp. 251-252
    • Xu, D.1    Rovira, I.I.2    Finkel, T.3
  • 22
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: role in EGF receptor-mediated tyrosine phosphorylation
    • Bae Y.S., Kang S.W., Seo M.S., Baines I.C., Tekle E., Chock P.B., and Rhee S.G. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide: role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272 (1997) 217-221
    • (1997) J. Biol. Chem. , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 23
    • 0033529675 scopus 로고    scopus 로고
    • Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells
    • Ushio-Fukai M., Alexander R.W., Akers M., Yin Q., Fujio Y., Walsh K., and Griendling K.K. Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells. J. Biol. Chem. 274 (1999) 22699-22704
    • (1999) J. Biol. Chem. , vol.274 , pp. 22699-22704
    • Ushio-Fukai, M.1    Alexander, R.W.2    Akers, M.3    Yin, Q.4    Fujio, Y.5    Walsh, K.6    Griendling, K.K.7
  • 24
    • 2342482002 scopus 로고    scopus 로고
    • Nitric oxide in health and disease of the respiratory system
    • Ricciardolo F.L., Sterk P.J., Gaston B., and Folkerts G. Nitric oxide in health and disease of the respiratory system. Physiol. Rev. 84 (2004) 731-765
    • (2004) Physiol. Rev. , vol.84 , pp. 731-765
    • Ricciardolo, F.L.1    Sterk, P.J.2    Gaston, B.3    Folkerts, G.4
  • 25
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth J.D. NOX enzymes and the biology of reactive oxygen. Nat. Rev., Immunol. 4 (2004) 181-189
    • (2004) Nat. Rev., Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 28
    • 33745988574 scopus 로고    scopus 로고
    • Aquaporin-1 transports NO across cell membranes
    • Herrera M., Hong N.J., and Garvin J.L. Aquaporin-1 transports NO across cell membranes. Hypertension 48 (2006) 157-164
    • (2006) Hypertension , vol.48 , pp. 157-164
    • Herrera, M.1    Hong, N.J.2    Garvin, J.L.3
  • 29
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng T.C., Fukada T., and Tonks N.K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9 (2002) 387-399
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 31
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman H.J., Fukuto J.M., and Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am. J. Physiol., Cell Physiol. 287 (2004) C246-C256
    • (2004) Am. J. Physiol., Cell Physiol. , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 33
    • 0042314356 scopus 로고    scopus 로고
    • Sulfur and selenium: the role of oxidation state in protein structure and function
    • Jacob C., Giles G.I., Giles N.M., and Sies H. Sulfur and selenium: the role of oxidation state in protein structure and function. Angew. Chem., Int. Ed. Engl. 42 (2003) 4742-4758
    • (2003) Angew. Chem., Int. Ed. Engl. , vol.42 , pp. 4742-4758
    • Jacob, C.1    Giles, G.I.2    Giles, N.M.3    Sies, H.4
  • 34
    • 0034326826 scopus 로고    scopus 로고
    • Effect of S-nitrosothiols on cellular glutathione and reactive protein sulfhydryls
    • Mallis R.J., and Thomas J.A. Effect of S-nitrosothiols on cellular glutathione and reactive protein sulfhydryls. Arch. Biochem. Biophys. 383 (2000) 60-69
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 60-69
    • Mallis, R.J.1    Thomas, J.A.2
  • 35
    • 0033080394 scopus 로고    scopus 로고
    • S-Nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione
    • Ji Y., Akerboom T.P., Sies H., and Thomas J.A. S-Nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione. Arch. Biochem. Biophys. 362 (1999) 67-78
    • (1999) Arch. Biochem. Biophys. , vol.362 , pp. 67-78
    • Ji, Y.1    Akerboom, T.P.2    Sies, H.3    Thomas, J.A.4
  • 36
    • 19244365393 scopus 로고    scopus 로고
    • Stress, protein (mis)folding, and signaling: the redox connection
    • Sitia R., and Molteni S.N. Stress, protein (mis)folding, and signaling: the redox connection. Sci. STKE 2004 (2004) pe27
    • (2004) Sci. STKE , vol.2004
    • Sitia, R.1    Molteni, S.N.2
  • 37
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget M.S., and Buttner M.J. Thiol-based regulatory switches. Annu. Rev. Genet. 37 (2003) 91-121
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 91-121
    • Paget, M.S.1    Buttner, M.J.2
  • 38
    • 0037184525 scopus 로고    scopus 로고
    • How to flip the (redox) switch
    • Georgiou G. How to flip the (redox) switch. Cell 111 (2002) 607-610
    • (2002) Cell , vol.111 , pp. 607-610
    • Georgiou, G.1
  • 39
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee S.G., Chae H.Z., and Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 38 (2005) 1543-1552
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 40
    • 22544482619 scopus 로고    scopus 로고
    • Avicinylation (thioesterification): a protein modification that can regulate the response to oxidative and nitrosative stress
    • Haridas V., Kim S.O., Nishimura G., Hausladen A., Stamler J.S., and Gutterman J.U. Avicinylation (thioesterification): a protein modification that can regulate the response to oxidative and nitrosative stress. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 10088-10093
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 10088-10093
    • Haridas, V.1    Kim, S.O.2    Nishimura, G.3    Hausladen, A.4    Stamler, J.S.5    Gutterman, J.U.6
  • 41
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase
    • Rossi A., Kapahi P., Natoli G., Takahashi T., Chen Y., Karin M., and Santoro M.G. Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase. Nature 403 (2000) 103-108
    • (2000) Nature , vol.403 , pp. 103-108
    • Rossi, A.1    Kapahi, P.2    Natoli, G.3    Takahashi, T.4    Chen, Y.5    Karin, M.6    Santoro, M.G.7
  • 43
    • 34247590130 scopus 로고    scopus 로고
    • Palmitoylation of ligands, receptors, and intracellular signaling molecules
    • Resh M.D. Palmitoylation of ligands, receptors, and intracellular signaling molecules. Sci. STKE 2006 (2006) re14
    • (2006) Sci. STKE , vol.2006
    • Resh, M.D.1
  • 46
    • 34447513434 scopus 로고    scopus 로고
    • Regulation and specificity of S-nitrosylation and denitrosylation
    • Tannenbaum S.R., and White F.M. Regulation and specificity of S-nitrosylation and denitrosylation. ACS Chem. Biol. 1 (2006) 615-618
    • (2006) ACS Chem. Biol. , vol.1 , pp. 615-618
    • Tannenbaum, S.R.1    White, F.M.2
  • 47
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton M.D., Chock P.B., and Mieyal J.J. Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid. Redox signal. 7 (2005) 348-366
    • (2005) Antioxid. Redox signal. , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 48
    • 0028260177 scopus 로고
    • Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex
    • Watabe S., Kohno H., Kouyama H., Hiroi T., Yago N., and Nakazawa T. Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex. J. Biochem. 115 (1994) 648-654
    • (1994) J. Biochem. , vol.115 , pp. 648-654
    • Watabe, S.1    Kohno, H.2    Kouyama, H.3    Hiroi, T.4    Yago, N.5    Nakazawa, T.6
  • 49
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • Yang K.S., Kang S.W., Woo H.A., Hwang S.C., Chae H.Z., Kim K., and Rhee S.G. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J. Biol. Chem. 277 (2002) 38029-38036
    • (2002) J. Biol. Chem. , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5    Kim, K.6    Rhee, S.G.7
  • 50
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • Rhee S.G., Kang S.W., Jeong W., Chang T.S., Yang K.S., and Woo H.A. Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17 (2005) 183-189
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 51
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne A., Yeh J.I., Mallett T.C., Luba J., Crane III E.J., Charrier V., and Parsonage D. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38 (1999) 15407-15416
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1    Yeh, J.I.2    Mallett, T.C.3    Luba, J.4    Crane III, E.J.5    Charrier, V.6    Parsonage, D.7
  • 52
    • 33846934941 scopus 로고    scopus 로고
    • A classification scheme for redox-based modifications of proteins
    • Forrester M.T., and Stamler J.S. A classification scheme for redox-based modifications of proteins. Am. J. Respir. Cell Mol. Biol. 36 (2007) 135-137
    • (2007) Am. J. Respir. Cell Mol. Biol. , vol.36 , pp. 135-137
    • Forrester, M.T.1    Stamler, J.S.2
  • 55
    • 9644290748 scopus 로고    scopus 로고
    • In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: identification of Ran GTPase as a target for S-nitrosylation
    • Ckless K., Reynaert N.L., Taatjes D.J., Lounsbury K.M., van der Vliet A., and Janssen-Heininger Y. In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: identification of Ran GTPase as a target for S-nitrosylation. Nitric Oxide 11 (2004) 216-227
    • (2004) Nitric Oxide , vol.11 , pp. 216-227
    • Ckless, K.1    Reynaert, N.L.2    Taatjes, D.J.3    Lounsbury, K.M.4    van der Vliet, A.5    Janssen-Heininger, Y.6
  • 58
    • 29344465714 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2
    • Kim S.F., Huri D.A., and Snyder S.H. Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science 310 (2005) 1966-1970
    • (2005) Science , vol.310 , pp. 1966-1970
    • Kim, S.F.1    Huri, D.A.2    Snyder, S.H.3
  • 59
    • 0030238701 scopus 로고    scopus 로고
    • Nitric oxide-induced inhibition of lung endothelial cell nitric oxide synthase via interaction with allosteric thiols: role of thioredoxin in regulation of catalytic activity
    • Patel J.M., Zhang J., and Block E.R. Nitric oxide-induced inhibition of lung endothelial cell nitric oxide synthase via interaction with allosteric thiols: role of thioredoxin in regulation of catalytic activity. Am. J. Respir. Cell Mol. Biol. 15 (1996) 410-419
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.15 , pp. 410-419
    • Patel, J.M.1    Zhang, J.2    Block, E.R.3
  • 60
    • 1442330336 scopus 로고    scopus 로고
    • S-Nitrosylation of endothelial nitric oxide synthase is associated with monomerization and decreased enzyme activity
    • Ravi K., Brennan L.A., Levic S., Ross P.A., and Black S.M. S-Nitrosylation of endothelial nitric oxide synthase is associated with monomerization and decreased enzyme activity. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 2619-2624
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2619-2624
    • Ravi, K.1    Brennan, L.A.2    Levic, S.3    Ross, P.A.4    Black, S.M.5
  • 61
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood Z.A., Poole L.B., and Karplus P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300 (2003) 650-653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 63
    • 2142815107 scopus 로고    scopus 로고
    • Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD
    • Budanov A.V., Sablina A.A., Feinstein E., Koonin E.V., and Chumakov P.M. Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science 304 (2004) 596-600
    • (2004) Science , vol.304 , pp. 596-600
    • Budanov, A.V.1    Sablina, A.A.2    Feinstein, E.3    Koonin, E.V.4    Chumakov, P.M.5
  • 64
    • 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. 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 (2004) 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
  • 65
    • 33744919853 scopus 로고    scopus 로고
    • Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin
    • Jeong W., Park S.J., Chang T.S., Lee D.Y., and Rhee S.G. Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J. Biol. Chem. 281 (2006) 14400-14407
    • (2006) J. Biol. Chem. , vol.281 , pp. 14400-14407
    • Jeong, W.1    Park, S.J.2    Chang, T.S.3    Lee, D.Y.4    Rhee, S.G.5
  • 66
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau B., Labarre J., and Toledano M.B. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425 (2003) 980-984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 68
    • 0033607229 scopus 로고    scopus 로고
    • Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
    • Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T., and Hakoshima T. Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 12333-12338
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12333-12338
    • Hirotsu, S.1    Abe, Y.2    Okada, K.3    Nagahara, N.4    Hori, H.5    Nishino, T.6    Hakoshima, T.7
  • 69
    • 3042755716 scopus 로고    scopus 로고
    • A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase
    • Veal E.A., Findlay V.J., Day A.M., Bozonet S.M., Evans J.M., Quinn J., and Morgan B.A. A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase. Mol. Cell 15 (2004) 129-139
    • (2004) Mol. Cell , vol.15 , pp. 129-139
    • Veal, E.A.1    Findlay, V.J.2    Day, A.M.3    Bozonet, S.M.4    Evans, J.M.5    Quinn, J.6    Morgan, B.A.7
  • 72
    • 27644443951 scopus 로고    scopus 로고
    • Bovine mitochondrial peroxiredoxin III forms a two-ring catenane
    • Cao Z., Roszak A.W., Gourlay L.J., Lindsay J.G., and Isaacs N.W. Bovine mitochondrial peroxiredoxin III forms a two-ring catenane. Structure 13 (2005) 1661-1664
    • (2005) Structure , vol.13 , pp. 1661-1664
    • Cao, Z.1    Roszak, A.W.2    Gourlay, L.J.3    Lindsay, J.G.4    Isaacs, N.W.5
  • 74
    • 0347478188 scopus 로고    scopus 로고
    • Preferential elevation of Prx I and Trx expression in lung cancer cells following hypoxia and in human lung cancer tissues
    • Kim H.J., Chae H.Z., Kim Y.J., Kim Y.H., Hwangs T.S., Park E.M., and Park Y.M. Preferential elevation of Prx I and Trx expression in lung cancer cells following hypoxia and in human lung cancer tissues. Cell Biol. Toxicol. 19 (2003) 285-298
    • (2003) Cell Biol. Toxicol. , vol.19 , pp. 285-298
    • Kim, H.J.1    Chae, H.Z.2    Kim, Y.J.3    Kim, Y.H.4    Hwangs, T.S.5    Park, E.M.6    Park, Y.M.7
  • 75
    • 33846703755 scopus 로고    scopus 로고
    • Human prx1 gene is a target of Nrf2 and is up-regulated by hypoxia/reoxygenation: implication to tumor biology
    • Kim Y.J., Ahn J.Y., Liang P., Ip C., Zhang Y., and Park Y.M. Human prx1 gene is a target of Nrf2 and is up-regulated by hypoxia/reoxygenation: implication to tumor biology. Cancer Res. 67 (2007) 546-554
    • (2007) Cancer Res. , vol.67 , pp. 546-554
    • Kim, Y.J.1    Ahn, J.Y.2    Liang, P.3    Ip, C.4    Zhang, Y.5    Park, Y.M.6
  • 76
    • 0034872152 scopus 로고    scopus 로고
    • Induction of peroxiredoxin gene expression by oxygen in lungs of newborn primates
    • Das K.C., Pahl P.M., Guo X.L., and White C.W. Induction of peroxiredoxin gene expression by oxygen in lungs of newborn primates. Am. J. Respir. Cell Mol. Biol. 25 (2001) 226-232
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.25 , pp. 226-232
    • Das, K.C.1    Pahl, P.M.2    Guo, X.L.3    White, C.W.4
  • 77
    • 0036802653 scopus 로고    scopus 로고
    • Confirmation and high resolution mapping of an atherosclerosis susceptibility gene in mice on chromosome 1
    • Phelan S.A., Beier D.R., Higgins D.C., and Paigen B. Confirmation and high resolution mapping of an atherosclerosis susceptibility gene in mice on chromosome 1. Mamm. Genome 13 (2002) 548-553
    • (2002) Mamm. Genome , vol.13 , pp. 548-553
    • Phelan, S.A.1    Beier, D.R.2    Higgins, D.C.3    Paigen, B.4
  • 78
    • 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. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 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
  • 79
    • 0346654056 scopus 로고    scopus 로고
    • The role of a formaldehyde dehydrogenase-glutathione pathway in protein S-nitrosation in mammalian cells
    • Haqqani A.S., Do S.K., and Birnboim H.C. The role of a formaldehyde dehydrogenase-glutathione pathway in protein S-nitrosation in mammalian cells. Nitric Oxide 9 (2003) 172-181
    • (2003) Nitric Oxide , vol.9 , pp. 172-181
    • Haqqani, A.S.1    Do, S.K.2    Birnboim, H.C.3
  • 83
    • 33847746679 scopus 로고    scopus 로고
    • Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system
    • Berndt C., Lillig C.H., and Holmgren A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am. J. Physiol., Heart Circ. Physiol. 292 (2007) H1227-H1236
    • (2007) Am. J. Physiol., Heart Circ. Physiol. , vol.292
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 84
    • 20544433877 scopus 로고    scopus 로고
    • Roles of thioredoxin reductase 1 and APE/Ref-1 in the control of basal p53 stability and activity
    • Seemann S., and Hainaut P. Roles of thioredoxin reductase 1 and APE/Ref-1 in the control of basal p53 stability and activity. Oncogene 24 (2005) 3853-3863
    • (2005) Oncogene , vol.24 , pp. 3853-3863
    • Seemann, S.1    Hainaut, P.2
  • 85
    • 0034864796 scopus 로고    scopus 로고
    • Activation of nuclear factor-kappa B transcriptional activity in airway epithelial cells by thioredoxin but not by N-acetyl-cysteine and glutathione
    • Harper R., Wu K., Chang M.M., Yoneda K., Pan R., Reddy S.P., and Wu R. Activation of nuclear factor-kappa B transcriptional activity in airway epithelial cells by thioredoxin but not by N-acetyl-cysteine and glutathione. Am. J. Respir. Cell Mol. Biol. 25 (2001) 178-185
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.25 , pp. 178-185
    • Harper, R.1    Wu, K.2    Chang, M.M.3    Yoneda, K.4    Pan, R.5    Reddy, S.P.6    Wu, R.7
  • 86
    • 0027217531 scopus 로고
    • Oxidoreductive regulation of nuclear factor kappa B: involvement of a cellular reducing catalyst thioredoxin
    • Hayashi T., Ueno Y., and Okamoto T. Oxidoreductive regulation of nuclear factor kappa B: involvement of a cellular reducing catalyst thioredoxin. J. Biol. Chem. 268 (1993) 11380-11388
    • (1993) J. Biol. Chem. , vol.268 , pp. 11380-11388
    • Hayashi, T.1    Ueno, Y.2    Okamoto, T.3
  • 87
    • 10644245123 scopus 로고    scopus 로고
    • Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1
    • Hwang C.Y., Ryu Y.S., Chung M.S., Kim K.D., Park S.S., Chae S.K., Chae H.Z., and Kwon K.S. Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1. Oncogene 23 (2004) 8868-8875
    • (2004) Oncogene , vol.23 , pp. 8868-8875
    • Hwang, C.Y.1    Ryu, Y.S.2    Chung, M.S.3    Kim, K.D.4    Park, S.S.5    Chae, S.K.6    Chae, H.Z.7    Kwon, K.S.8
  • 88
    • 0030838711 scopus 로고    scopus 로고
    • Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator
    • Hayashi S., Hajiro-Nakanishi K., Makino Y., Eguchi H., Yodoi J., and Tanaka H. Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator. Nucleic Acids Res. 25 (1997) 4035-4040
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4035-4040
    • Hayashi, S.1    Hajiro-Nakanishi, K.2    Makino, Y.3    Eguchi, H.4    Yodoi, J.5    Tanaka, H.6
  • 89
    • 0033613871 scopus 로고    scopus 로고
    • Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function
    • Makino Y., Yoshikawa N., Okamoto K., Hirota K., Yodoi J., Makino I., and Tanaka H. Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J. Biol. Chem. 274 (1999) 3182-3188
    • (1999) J. Biol. Chem. , vol.274 , pp. 3182-3188
    • Makino, Y.1    Yoshikawa, N.2    Okamoto, K.3    Hirota, K.4    Yodoi, J.5    Makino, I.6    Tanaka, H.7
  • 91
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • Rubartelli A., Bajetto A., Allavena G., Wollman E., and Sitia R. Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J. Biol. Chem. 267 (1992) 24161-24164
    • (1992) J. Biol. Chem. , vol.267 , pp. 24161-24164
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia, R.5
  • 93
    • 13944266092 scopus 로고    scopus 로고
    • Elevated thioredoxin after angioplasty in peripheral arterial disease
    • Wahlgren C.M., and Pekkari K. Elevated thioredoxin after angioplasty in peripheral arterial disease. Eur. J. Vasc. Endovasc. Surg. 29 (2005) 281-286
    • (2005) Eur. J. Vasc. Endovasc. Surg. , vol.29 , pp. 281-286
    • Wahlgren, C.M.1    Pekkari, K.2
  • 95
    • 0346340023 scopus 로고    scopus 로고
    • Truncated thioredoxin: physiological functions and mechanism
    • Pekkari K., and Holmgren A. Truncated thioredoxin: physiological functions and mechanism. Antioxid. Redox Signal. 6 (2004) 53-61
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 53-61
    • Pekkari, K.1    Holmgren, A.2
  • 99
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes A.P., and Holmgren A. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 6 (2004) 63-74
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 101
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina S.A., and Mieyal J.J. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32 (1993) 3368-3376
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 106
    • 34347204123 scopus 로고    scopus 로고
    • Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity
    • Hashemy S.I., Johansson C., Berndt C., Lillig C.H., and Holmgren A. Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity. J. Biol. Chem. 282 (2007) 14428-14436
    • (2007) J. Biol. Chem. , vol.282 , pp. 14428-14436
    • Hashemy, S.I.1    Johansson, C.2    Berndt, C.3    Lillig, C.H.4    Holmgren, A.5
  • 107
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • Haendeler J., Hoffmann J., Tischler V., Berk B.C., Zeiher A.M., and Dimmeler S. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat. Cell Biol. 4 (2002) 743-749
    • (2002) Nat. Cell Biol. , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 108
    • 0038511319 scopus 로고    scopus 로고
    • S-Nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1
    • Sumbayev V.V. S-Nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1. Arch. Biochem. Biophys. 415 (2003) 133-136
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 133-136
    • Sumbayev, V.V.1
  • 111
    • 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. 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 (2007) 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
  • 112
    • 33644818614 scopus 로고    scopus 로고
    • Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine
    • Mitchell D.A., and Marletta M.A. Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. Nat. Chem. Biol. 1 (2005) 154-158
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 154-158
    • Mitchell, D.A.1    Marletta, M.A.2
  • 113
    • 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. S-Nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide. J. Biol. Chem. 271 (1996) 19180-19185
    • (1996) J. Biol. Chem. , vol.271 , pp. 19180-19185
    • Nikitovic, D.1    Holmgren, A.2
  • 114
    • 9444243245 scopus 로고    scopus 로고
    • Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control
    • Jones D.P., Go Y.M., Anderson C.L., Ziegler T.R., Kinkade Jr. J.M., and Kirlin W.G. Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control. FASEB J. 18 (2004) 1246-1248
    • (2004) FASEB J. , vol.18 , pp. 1246-1248
    • Jones, D.P.1    Go, Y.M.2    Anderson, C.L.3    Ziegler, T.R.4    Kinkade Jr., J.M.5    Kirlin, W.G.6
  • 116
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.R., Kwon K.S., Kim S.R., and Rhee S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273 (1998) 15366-15372
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 117
    • 9344259718 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
    • Kwon J., Lee S.R., Yang K.S., Ahn Y., Kim Y.J., Stadtman E.R., and Rhee S.G. Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 16419-16424
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16419-16424
    • Kwon, J.1    Lee, S.R.2    Yang, K.S.3    Ahn, Y.4    Kim, Y.J.5    Stadtman, E.R.6    Rhee, S.G.7
  • 118
    • 0034641689 scopus 로고    scopus 로고
    • Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation
    • Sullivan D.M., Wehr N.B., Fergusson M.M., Levine R.L., and Finkel T. Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation. Biochemistry 39 (2000) 11121-11128
    • (2000) Biochemistry , vol.39 , pp. 11121-11128
    • Sullivan, D.M.1    Wehr, N.B.2    Fergusson, M.M.3    Levine, R.L.4    Finkel, T.5
  • 120
    • 33745006817 scopus 로고    scopus 로고
    • Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B
    • Rinna A., Torres M., and Forman H.J. Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B. Free Radic. Biol. Med. 41 (2006) 86-91
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 86-91
    • Rinna, A.1    Torres, M.2    Forman, H.J.3
  • 121
    • 33847660853 scopus 로고    scopus 로고
    • 2 in studies of signal transduction
    • 2 in studies of signal transduction. Free Radic. Biol. Med. 42 (2007) 926-932
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 926-932
    • Forman, H.J.1
  • 122
    • 0037443130 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols
    • Li S., and Whorton A.R. 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
  • 123
  • 124
    • 33947250704 scopus 로고    scopus 로고
    • Phosphorylation of the survival kinase Akt by superoxide is dependent on an ascorbate-reversible oxidation of PTEN
    • Lim S., and Clement M.V. Phosphorylation of the survival kinase Akt by superoxide is dependent on an ascorbate-reversible oxidation of PTEN. Free Radic. Biol. Med. 42 (2007) 1178-1192
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 1178-1192
    • Lim, S.1    Clement, M.V.2
  • 125
    • 0141673128 scopus 로고    scopus 로고
    • Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms
    • Mikkelsen R.B., and Wardman P. Biological chemistry of reactive oxygen and nitrogen and radiation-induced signal transduction mechanisms. Oncogene 22 (2003) 5734-5754
    • (2003) Oncogene , vol.22 , pp. 5734-5754
    • Mikkelsen, R.B.1    Wardman, P.2
  • 126
    • 17644386593 scopus 로고    scopus 로고
    • Inhibition of protein-tyrosine phosphatases by mild oxidative stresses is dependent on S-nitrosylation
    • Barrett D.M., Black S.M., Todor H., Schmidt-Ullrich R.K., Dawson K.S., and Mikkelsen R.B. Inhibition of protein-tyrosine phosphatases by mild oxidative stresses is dependent on S-nitrosylation. J. Biol. Chem. 280 (2005) 14453-14461
    • (2005) J. Biol. Chem. , vol.280 , pp. 14453-14461
    • Barrett, D.M.1    Black, S.M.2    Todor, H.3    Schmidt-Ullrich, R.K.4    Dawson, K.S.5    Mikkelsen, R.B.6
  • 127
    • 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. Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress. J. Biol. Chem. 282 19 (2007) 13977-13983
    • (2007) J. Biol. Chem. , vol.282 , Issue.19 , pp. 13977-13983
    • Forrester, M.T.1    Foster, M.W.2    Stamler, J.S.3
  • 128
    • 33750620971 scopus 로고    scopus 로고
    • Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine
    • von Montfort C., Sharov V.S., Metzger S., Schoneich C., Sies H., and Klotz L.O. Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine. Biol. Chem. 387 (2006) 1399-1404
    • (2006) Biol. Chem. , vol.387 , pp. 1399-1404
    • von Montfort, C.1    Sharov, V.S.2    Metzger, S.3    Schoneich, C.4    Sies, H.5    Klotz, L.O.6
  • 129
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata H., Honda S., Maeda S., Chang L., Hirata H., and Karin M. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120 (2005) 649-661
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 130
    • 33746049192 scopus 로고    scopus 로고
    • Redox regulation of MAP kinase phosphatase 3
    • Seth D., and Rudolph J. Redox regulation of MAP kinase phosphatase 3. Biochemistry 45 (2006) 8476-8487
    • (2006) Biochemistry , vol.45 , pp. 8476-8487
    • Seth, D.1    Rudolph, J.2
  • 131
    • 14044277677 scopus 로고    scopus 로고
    • Reversible oxidation of ERK-directed protein phosphatases drives oxidative toxicity in neurons
    • Levinthal D.J., and Defranco D.B. Reversible oxidation of ERK-directed protein phosphatases drives oxidative toxicity in neurons. J. Biol. Chem. 280 (2005) 5875-5883
    • (2005) J. Biol. Chem. , vol.280 , pp. 5875-5883
    • Levinthal, D.J.1    Defranco, D.B.2
  • 134
    • 0033807445 scopus 로고    scopus 로고
    • Hydrogen peroxide inhibits activation, not activity, of cellular caspase-3 in vivo
    • Lee Y.J., and Shacter E. Hydrogen peroxide inhibits activation, not activity, of cellular caspase-3 in vivo. Free Radic. Biol. Med. 29 (2000) 684-692
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 684-692
    • Lee, Y.J.1    Shacter, E.2
  • 135
    • 33846809031 scopus 로고    scopus 로고
    • Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway
    • Pan S., and Berk B.C. Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway. Circ. Res. 100 (2007) 213-219
    • (2007) Circ. Res. , vol.100 , pp. 213-219
    • Pan, S.1    Berk, B.C.2
  • 136
    • 33846419151 scopus 로고    scopus 로고
    • GSH-dependent regulation of Fas-mediated caspase-8 activation by acrolein
    • Hristova M., Heuvelmans S., and van der Vliet A. GSH-dependent regulation of Fas-mediated caspase-8 activation by acrolein. FEBS Lett. 581 (2007) 361-367
    • (2007) FEBS Lett. , vol.581 , pp. 361-367
    • Hristova, M.1    Heuvelmans, S.2    van der Vliet, A.3
  • 138
    • 0035260351 scopus 로고    scopus 로고
    • Reactive oxygen species mediate tumor necrosis factor alpha-converting, enzyme-dependent ectodomain shedding induced by phorbol myristate acetate
    • Zhang Z., Oliver P., Lancaster J.J., Schwarzenberger P.O., Joshi M.S., Cork J., and Kolls J.K. Reactive oxygen species mediate tumor necrosis factor alpha-converting, enzyme-dependent ectodomain shedding induced by phorbol myristate acetate. FASEB J. 15 (2001) 303-305
    • (2001) FASEB J. , vol.15 , pp. 303-305
    • Zhang, Z.1    Oliver, P.2    Lancaster, J.J.3    Schwarzenberger, P.O.4    Joshi, M.S.5    Cork, J.6    Kolls, J.K.7
  • 139
    • 14144251241 scopus 로고    scopus 로고
    • Dual oxidase 1-dependent MUC5AC mucin expression in cultured human airway epithelial cells
    • Shao M.X., and Nadel J.A. Dual oxidase 1-dependent MUC5AC mucin expression in cultured human airway epithelial cells. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 767-772
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 767-772
    • Shao, M.X.1    Nadel, J.A.2
  • 140
    • 10044272802 scopus 로고    scopus 로고
    • Molecular mechanism for activation and regulation of matrix metalloproteinases during bacterial infections and respiratory inflammation
    • Okamoto T., Akuta T., Tamura F., van Der Vliet A., and Akaike T. Molecular mechanism for activation and regulation of matrix metalloproteinases during bacterial infections and respiratory inflammation. Biol. Chem. 385 (2004) 997-1006
    • (2004) Biol. Chem. , vol.385 , pp. 997-1006
    • Okamoto, T.1    Akuta, T.2    Tamura, F.3    van Der Vliet, A.4    Akaike, T.5
  • 141
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7): a mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu X., Kassim S.Y., Parks W.C., and Heinecke J.W. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7): a mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J. Biol. Chem. 276 (2001) 41279-41287
    • (2001) J. Biol. Chem. , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 142
    • 0042093741 scopus 로고    scopus 로고
    • Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation
    • Fu X., Kassim S.Y., Parks W.C., and Heinecke J.W. Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation. J. Biol. Chem. 278 (2003) 28403-28409
    • (2003) J. Biol. Chem. , vol.278 , pp. 28403-28409
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 143
    • 0026500717 scopus 로고
    • Different effects of hypochlorous acid on human neutrophil metalloproteinases: activation of collagenase and inactivation of collagenase and gelatinase
    • Michaelis J., Vissers M.C., and Winterbourn C.C. Different effects of hypochlorous acid on human neutrophil metalloproteinases: activation of collagenase and inactivation of collagenase and gelatinase. Arch. Biochem. Biophys. 292 (1992) 555-562
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 555-562
    • Michaelis, J.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 144
    • 11444262208 scopus 로고    scopus 로고
    • Beyond transcription-new mechanisms for the regulation of molecular chaperones
    • Winter J., and Jakob U. Beyond transcription-new mechanisms for the regulation of molecular chaperones. Crit. Rev. Biochem. Mol. Biol. 39 (2004) 297-317
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 297-317
    • Winter, J.1    Jakob, U.2
  • 146
    • 3142719113 scopus 로고    scopus 로고
    • Requirement of Hsp90 activity for IkappaB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-kappaB activation
    • Broemer M., Krappmann D., and Scheidereit C. Requirement of Hsp90 activity for IkappaB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-kappaB activation. Oncogene 23 (2004) 5378-5386
    • (2004) Oncogene , vol.23 , pp. 5378-5386
    • Broemer, M.1    Krappmann, D.2    Scheidereit, C.3
  • 147
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob U., Muse W., Eser M., and Bardwell J.C. Chaperone activity with a redox switch. Cell 96 (1999) 341-352
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 148
    • 0034623949 scopus 로고    scopus 로고
    • Redox switch of hsp33 has a novel zinc-binding motif
    • Jakob U., Eser M., and Bardwell J.C. Redox switch of hsp33 has a novel zinc-binding motif. J. Biol. Chem. 275 (2000) 38302-38310
    • (2000) J. Biol. Chem. , vol.275 , pp. 38302-38310
    • Jakob, U.1    Eser, M.2    Bardwell, J.C.3
  • 149
    • 13244279524 scopus 로고    scopus 로고
    • Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33
    • Winter J., Linke K., Jatzek A., and Jakob U. Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33. Mol. Cell 17 (2005) 381-392
    • (2005) Mol. Cell , vol.17 , pp. 381-392
    • Winter, J.1    Linke, K.2    Jatzek, A.3    Jakob, U.4
  • 151
    • 14044259324 scopus 로고    scopus 로고
    • Substitution of the unique cysteine residue of murine Hsp25 interferes with the protective activity of this stress protein through inhibition of dimer formation
    • Diaz-Latoud C., Buache E., Javouhey E., and Arrigo A.P. Substitution of the unique cysteine residue of murine Hsp25 interferes with the protective activity of this stress protein through inhibition of dimer formation. Antioxid. Redox Signal. 7 (2005) 436-445
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 436-445
    • Diaz-Latoud, C.1    Buache, E.2    Javouhey, E.3    Arrigo, A.P.4
  • 152
    • 1942423136 scopus 로고    scopus 로고
    • Protein S-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone
    • Hoppe G., Chai Y.C., Crabb J.W., and Sears J. Protein S-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone. Exp. Eye Res. 78 (2004) 1085-1092
    • (2004) Exp. Eye Res. , vol.78 , pp. 1085-1092
    • Hoppe, G.1    Chai, Y.C.2    Crabb, J.W.3    Sears, J.4
  • 156
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: substrate interactions and functional properties
    • Ellgaard L., and Ruddock L.W. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep. 6 (2005) 28-32
    • (2005) EMBO Rep. , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 158
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai B., Rodighiero C., Lencer W.I., and Rapoport T.A. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104 (2001) 937-948
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 159
    • 0037122001 scopus 로고    scopus 로고
    • Is protein disulfide isomerase a redox-dependent molecular chaperone?
    • Lumb R.A., and Bulleid N.J. Is protein disulfide isomerase a redox-dependent molecular chaperone?. EMBO J. 21 (2002) 6763-6770
    • (2002) EMBO J. , vol.21 , pp. 6763-6770
    • Lumb, R.A.1    Bulleid, N.J.2
  • 160
    • 0032939206 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide
    • Zai A., Rudd M.A., Scribner A.W., and Loscalzo J. Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide. J. Clin. Invest. 103 (1999) 393-399
    • (1999) J. Clin. Invest. , vol.103 , pp. 393-399
    • Zai, A.1    Rudd, M.A.2    Scribner, A.W.3    Loscalzo, J.4
  • 161
    • 0035859858 scopus 로고    scopus 로고
    • Mechanism of transfer of NO from extracellular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase
    • Ramachandran N., Root P., Jiang X.M., Hogg P.J., and Mutus B. Mechanism of transfer of NO from extracellular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 9539-9544
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9539-9544
    • Ramachandran, N.1    Root, P.2    Jiang, X.M.3    Hogg, P.J.4    Mutus, B.5
  • 162
    • 33745315287 scopus 로고    scopus 로고
    • S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara T., Nakamura T., Yao D., Shi Z.Q., Gu Z., Ma Y., Masliah E., Nomura Y., and Lipton S.A. S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 441 (2006) 513-517
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4    Gu, Z.5    Ma, Y.6    Masliah, E.7    Nomura, Y.8    Lipton, S.A.9
  • 163
    • 15744403464 scopus 로고    scopus 로고
    • Characterization of the S-denitrosation activity of protein disulfide isomerase
    • Sliskovic I., Raturi A., and Mutus B. Characterization of the S-denitrosation activity of protein disulfide isomerase. J. Biol. Chem. 280 (2005) 8733-8741
    • (2005) J. Biol. Chem. , vol.280 , pp. 8733-8741
    • Sliskovic, I.1    Raturi, A.2    Mutus, B.3
  • 164
    • 0344393408 scopus 로고    scopus 로고
    • Regulation of MAP kinase signaling modules by scaffold proteins in mammals
    • Morrison D.K., and Davis R.J. Regulation of MAP kinase signaling modules by scaffold proteins in mammals. Annu. Rev. Cell Dev. Biol. 19 (2003) 91-118
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 91-118
    • Morrison, D.K.1    Davis, R.J.2
  • 165
    • 0032422785 scopus 로고    scopus 로고
    • Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
    • Whitmarsh A.J., and Davis R.J. Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals. Trends Biochem. Sci. 23 (1998) 481-485
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 481-485
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 166
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • Liu H., Nishitoh H., Ichijo H., and Kyriakis J.M. Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol. Cell. Biol. 20 (2000) 2198-2208
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 169
    • 0037188936 scopus 로고    scopus 로고
    • Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner
    • Liu Y., and Min W. Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner. Circ. Res. 90 (2002) 1259-1266
    • (2002) Circ. Res. , vol.90 , pp. 1259-1266
    • Liu, Y.1    Min, W.2
  • 170
    • 0242582865 scopus 로고    scopus 로고
    • Hydrogen peroxide signaling through tumor necrosis factor receptor 1 leads to selective activation of c-Jun N-terminal kinase
    • Pantano C., Shrivastava P., McElhinney B., and Janssen-Heininger Y. Hydrogen peroxide signaling through tumor necrosis factor receptor 1 leads to selective activation of c-Jun N-terminal kinase. J. Biol. Chem. 278 (2003) 44091-44096
    • (2003) J. Biol. Chem. , vol.278 , pp. 44091-44096
    • Pantano, C.1    Shrivastava, P.2    McElhinney, B.3    Janssen-Heininger, Y.4
  • 172
    • 33845442925 scopus 로고    scopus 로고
    • Mechanistic studies of the Nrf2-Keap1 signaling pathway
    • Zhang D.D. Mechanistic studies of the Nrf2-Keap1 signaling pathway. Drug Metab. Rev. 38 (2006) 769-789
    • (2006) Drug Metab. Rev. , vol.38 , pp. 769-789
    • Zhang, D.D.1
  • 173
    • 1942455887 scopus 로고    scopus 로고
    • Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles
    • Itoh K., Tong K.I., and Yamamoto M. Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles. Free Radic. Biol. Med. 36 (2004) 1208-1213
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1208-1213
    • Itoh, K.1    Tong, K.I.2    Yamamoto, M.3
  • 176
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi A., Kang M.I., Okawa H., Ohtsuji M., Zenke Y., Chiba T., Igarashi K., and Yamamoto M. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell. Biol. 24 (2004) 7130-7139
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6    Igarashi, K.7    Yamamoto, M.8
  • 177
    • 33750613056 scopus 로고    scopus 로고
    • Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism
    • Tong K.I., Kobayashi A., Katsuoka F., and Yamamoto M. Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism. Biol. Chem. 387 (2006) 1311-1320
    • (2006) Biol. Chem. , vol.387 , pp. 1311-1320
    • Tong, K.I.1    Kobayashi, A.2    Katsuoka, F.3    Yamamoto, M.4
  • 180
    • 0041766297 scopus 로고    scopus 로고
    • Screening for nitric oxide-dependent protein-protein interactions
    • Matsumoto A., Comatas K.E., Liu L., and Stamler J.S. Screening for nitric oxide-dependent protein-protein interactions. Science 301 (2003) 657-661
    • (2003) Science , vol.301 , pp. 657-661
    • Matsumoto, A.1    Comatas, K.E.2    Liu, L.3    Stamler, J.S.4
  • 181
    • 0026453418 scopus 로고
    • Peroxynitrite formation from macrophage-derived nitric oxide
    • Ischiropoulos H., Zhu L., and Beckman J.S. Peroxynitrite formation from macrophage-derived nitric oxide. Arch. Biochem. Biophys. 298 (1992) 446-451
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 446-451
    • Ischiropoulos, H.1    Zhu, L.2    Beckman, J.S.3
  • 182
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher P., Beckman J.S., and Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 87 (2007) 315-424
    • (2007) Physiol. Rev. , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 183
    • 22144444152 scopus 로고    scopus 로고
    • A central role for S-nitrosylation in apoptosis
    • Benhar M., and Stamler J.S. A central role for S-nitrosylation in apoptosis. Nat. Cell Biol. 7 (2005) 645-646
    • (2005) Nat. Cell Biol. , vol.7 , pp. 645-646
    • Benhar, M.1    Stamler, J.S.2
  • 185
    • 33746445177 scopus 로고    scopus 로고
    • Nitric oxide-GAPDH-Siah: a novel cell death cascade
    • Hara M.R., and Snyder S.H. Nitric oxide-GAPDH-Siah: a novel cell death cascade. Cell. Mol. Neurobiol. 26 (2006) 527-538
    • (2006) Cell. Mol. Neurobiol. , vol.26 , pp. 527-538
    • Hara, M.R.1    Snyder, S.H.2
  • 186
    • 33646858497 scopus 로고    scopus 로고
    • The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-beta-catenin signalling through dishevelled
    • Funato Y., Michiue T., Asashima M., and Miki H. The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-beta-catenin signalling through dishevelled. Nat. Cell Biol. 8 (2006) 501-508
    • (2006) Nat. Cell Biol. , vol.8 , pp. 501-508
    • Funato, Y.1    Michiue, T.2    Asashima, M.3    Miki, H.4
  • 188
    • 0035877779 scopus 로고    scopus 로고
    • Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus
    • Wang T., Arifoglu P., Ronai Z., and Tew K.D. Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus. J. Biol. Chem. 276 (2001) 20999-21003
    • (2001) J. Biol. Chem. , vol.276 , pp. 20999-21003
    • Wang, T.1    Arifoglu, P.2    Ronai, Z.3    Tew, K.D.4
  • 190
    • 1542365411 scopus 로고    scopus 로고
    • Increased myeloproliferation in glutathione S-transferase Pi-deficient mice is associated with a deregulation of JNK and Janus kinase/STAT pathways
    • Gate L., Majumdar R.S., Lunk A., and Tew K.D. Increased myeloproliferation in glutathione S-transferase Pi-deficient mice is associated with a deregulation of JNK and Janus kinase/STAT pathways. J. Biol. Chem. 279 (2004) 8608-8616
    • (2004) J. Biol. Chem. , vol.279 , pp. 8608-8616
    • Gate, L.1    Majumdar, R.S.2    Lunk, A.3    Tew, K.D.4
  • 191
    • 1642326559 scopus 로고    scopus 로고
    • Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with Pi GST
    • Manevich Y., Feinstein S.I., and Fisher A.B. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with Pi GST. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 3780-3785
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3780-3785
    • Manevich, Y.1    Feinstein, S.I.2    Fisher, A.B.3
  • 192
    • 33744969804 scopus 로고    scopus 로고
    • Transcriptional regulation via cysteine thiol modification: a novel molecular strategy for chemoprevention and cytoprotection
    • Na H.K., and Surh Y.J. Transcriptional regulation via cysteine thiol modification: a novel molecular strategy for chemoprevention and cytoprotection. Mol. Carcinog. 45 (2006) 368-380
    • (2006) Mol. Carcinog. , vol.45 , pp. 368-380
    • Na, H.K.1    Surh, Y.J.2
  • 193
    • 0021930684 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium
    • Christman M.F., Morgan R.W., Jacobson F.S., and Ames B.N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 41 (1985) 753-762
    • (1985) Cell , vol.41 , pp. 753-762
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.N.4
  • 194
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi H., Kim S., Mukhopadhyay P., Cho S., Woo J., Storz G., and Ryu S. Structural basis of the redox switch in the OxyR transcription factor. Cell 105 (2001) 103-113
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5    Storz, G.6    Ryu, S.7
  • 196
    • 0030572708 scopus 로고    scopus 로고
    • Nitrosative stress: activation of the transcription factor OxyR
    • Hausladen A., Privalle C.T., Keng T., DeAngelo J., and Stamler J.S. Nitrosative stress: activation of the transcription factor OxyR. Cell 86 (1996) 719-729
    • (1996) Cell , vol.86 , pp. 719-729
    • Hausladen, A.1    Privalle, C.T.2    Keng, T.3    DeAngelo, J.4    Stamler, J.S.5
  • 199
    • 0035852845 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B by S-nitrosylation
    • Marshall H.E., and Stamler J.S. Inhibition of NF-kappa B by S-nitrosylation. Biochemistry 40 (2001) 1688-1693
    • (2001) Biochemistry , vol.40 , pp. 1688-1693
    • Marshall, H.E.1    Stamler, J.S.2
  • 201
    • 35649021739 scopus 로고    scopus 로고
    • NOS2 regulation of NF-kappa B by S-nitrosylation of p65*
    • Kelleher Z.T., Matsumoto A., Stamler J.S., and Marshall H.E. NOS2 regulation of NF-kappa B by S-nitrosylation of p65*. J. Biol. Chem. 282 42 (2007) 30667-30672
    • (2007) J. Biol. Chem. , vol.282 , Issue.42 , pp. 30667-30672
    • Kelleher, Z.T.1    Matsumoto, A.2    Stamler, J.S.3    Marshall, H.E.4
  • 204
    • 0036606407 scopus 로고    scopus 로고
    • Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277
    • Buzek J., Latonen L., Kurki S., Peltonen K., and Laiho M. Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277. Nucleic Acids Res. 30 (2002) 2340-2348
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2340-2348
    • Buzek, J.1    Latonen, L.2    Kurki, S.3    Peltonen, K.4    Laiho, M.5
  • 205
    • 0037472651 scopus 로고    scopus 로고
    • HIF-1 alpha protein as a target for S-nitrosation
    • Sumbayev V.V., Budde A., Zhou J., and Brune B. HIF-1 alpha protein as a target for S-nitrosation. FEBS Lett. 535 (2003) 106-112
    • (2003) FEBS Lett. , vol.535 , pp. 106-112
    • Sumbayev, V.V.1    Budde, A.2    Zhou, J.3    Brune, B.4
  • 206
    • 0042564792 scopus 로고    scopus 로고
    • S-Nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity
    • Yasinska I.M., and Sumbayev V.V. S-Nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity. FEBS Lett. 549 (2003) 105-109
    • (2003) FEBS Lett. , vol.549 , pp. 105-109
    • Yasinska, I.M.1    Sumbayev, V.V.2
  • 207
    • 0037442768 scopus 로고    scopus 로고
    • Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress
    • Ahn S.G., and Thiele D.J. Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress. Genes Dev. 17 (2003) 516-528
    • (2003) Genes Dev. , vol.17 , pp. 516-528
    • Ahn, S.G.1    Thiele, D.J.2
  • 209
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang F., Nguyen M., Qin F.X., and Tong Q. SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6 4 (2007) 505-514
    • (2007) Aging Cell , vol.6 , Issue.4 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 213
    • 4143070452 scopus 로고    scopus 로고
    • Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression
    • Rahman I., Marwick J., and Kirkham P. Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression. Biochem. Pharmacol. 68 (2004) 1255-1267
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1255-1267
    • Rahman, I.1    Marwick, J.2    Kirkham, P.3
  • 214
    • 0036066957 scopus 로고    scopus 로고
    • Oxidative stress and TNF-alpha induce histone acetylation and NF-kappaB/AP-1 activation in alveolar epithelial cells: potential mechanism in gene transcription in lung inflammation
    • Rahman I., Gilmour P.S., Jimenez L.A., and MacNee W. Oxidative stress and TNF-alpha induce histone acetylation and NF-kappaB/AP-1 activation in alveolar epithelial cells: potential mechanism in gene transcription in lung inflammation. Mol. Cell. Biochem. 234-235 (2002) 239-248
    • (2002) Mol. Cell. Biochem. , vol.234-235 , pp. 239-248
    • Rahman, I.1    Gilmour, P.S.2    Jimenez, L.A.3    MacNee, W.4
  • 215
    • 0842308109 scopus 로고    scopus 로고
    • Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: role of tyrosine nitration
    • Ito K., Hanazawa T., Tomita K., Barnes P.J., and Adcock I.M. Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: role of tyrosine nitration. Biochem. Biophys. Res. Commun. 315 (2004) 240-245
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 240-245
    • Ito, K.1    Hanazawa, T.2    Tomita, K.3    Barnes, P.J.4    Adcock, I.M.5
  • 217
    • 0032573507 scopus 로고    scopus 로고
    • 2 with fluorescein-conjugated iodoacetamide and antibodies to fluorescein
    • 2 with fluorescein-conjugated iodoacetamide and antibodies to fluorescein. FEBS Lett. 440 (1998) 111-115
    • (1998) FEBS Lett. , vol.440 , pp. 111-115
    • Wu, Y.1    Kwon, K.S.2    Rhee, S.G.3
  • 218
    • 0034255470 scopus 로고    scopus 로고
    • Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH
    • Kim J.R., Yoon H.W., Kwon K.S., Lee S.R., and Rhee S.G. Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Anal. Biochem. 283 (2000) 214-221
    • (2000) Anal. Biochem. , vol.283 , pp. 214-221
    • Kim, J.R.1    Yoon, H.W.2    Kwon, K.S.3    Lee, S.R.4    Rhee, S.G.5
  • 219
    • 0028126472 scopus 로고
    • Modification of cysteine residues within G(o) and other neuronal proteins by exposure to nitric oxide
    • Hess D.T., Lin L.H., Freeman J.A., and Norden J.J. Modification of cysteine residues within G(o) and other neuronal proteins by exposure to nitric oxide. Neuropharmacology 33 (1994) 1283-1292
    • (1994) Neuropharmacology , vol.33 , pp. 1283-1292
    • Hess, D.T.1    Lin, L.H.2    Freeman, J.A.3    Norden, J.J.4
  • 220
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert L.I., and Jakob U. Protein thiol modifications visualized in vivo. PLoS Biol. 2 (2004) e333
    • (2004) PLoS Biol. , vol.2
    • Leichert, L.I.1    Jakob, U.2
  • 221
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey S.R., and Snyder S.H. The biotin switch method for the detection of S-nitrosylated proteins. Sci. STKE 2001 (2001) PL1
    • (2001) Sci. STKE , vol.2001
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 222
    • 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. Ascorbic acid reduction of microtubule protein disulfides and its relevance to protein S-nitrosylation assays. Biochem. Biophys. Res. Commun. 340 (2006) 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
  • 223
    • 33746070773 scopus 로고    scopus 로고
    • An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay
    • Huang B., and Chen C. An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay. Free Radic. Biol. Med. 41 (2006) 562-567
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 562-567
    • Huang, B.1    Chen, C.2
  • 224
    • 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. Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins. Free Radic. Biol. Med. 38 (2005) 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
  • 225
    • 0035949671 scopus 로고    scopus 로고
    • Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
    • Sun J., Xin C., Eu J.P., Stamler J.S., and Meissner G. Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 11158-11162
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11158-11162
    • Sun, J.1    Xin, C.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 227
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • Lind C., Gerdes R., Hamnell Y., Schuppe-Koistinen I., von Lowenhielm H.B., Holmgren A., and Cotgreave I.A. Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch. Biochem. Biophys. 406 (2002) 229-240
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 229-240
    • Lind, C.1    Gerdes, R.2    Hamnell, Y.3    Schuppe-Koistinen, I.4    von Lowenhielm, H.B.5    Holmgren, A.6    Cotgreave, I.A.7
  • 228
    • 28444477354 scopus 로고    scopus 로고
    • S-Thiolation mimicry: quantitative and kinetic analysis of redox status of protein cysteines by glutathione-affinity chromatography
    • Niture S.K., Velu C.S., Bailey N.I., and Srivenugopal K.S. S-Thiolation mimicry: quantitative and kinetic analysis of redox status of protein cysteines by glutathione-affinity chromatography. Arch. Biochem. Biophys. 444 (2005) 174-184
    • (2005) Arch. Biochem. Biophys. , vol.444 , pp. 174-184
    • Niture, S.K.1    Velu, C.S.2    Bailey, N.I.3    Srivenugopal, K.S.4
  • 229
    • 12844254556 scopus 로고    scopus 로고
    • Detection of S-glutathionylated proteins by glutathione S-transferase overlay
    • Cheng G., Ikeda Y., Iuchi Y., and Fujii J. Detection of S-glutathionylated proteins by glutathione S-transferase overlay. Arch. Biochem. Biophys. 435 (2005) 42-49
    • (2005) Arch. Biochem. Biophys. , vol.435 , pp. 42-49
    • Cheng, G.1    Ikeda, Y.2    Iuchi, Y.3    Fujii, J.4
  • 230
    • 33646146488 scopus 로고    scopus 로고
    • Redox proteomics: identification and functional role of glutathionylated proteins
    • Fratelli M., Gianazza E., and Ghezzi P. Redox proteomics: identification and functional role of glutathionylated proteins. Expert Rev. Proteomics 1 (2004) 365-376
    • (2004) Expert Rev. Proteomics , vol.1 , pp. 365-376
    • Fratelli, M.1    Gianazza, E.2    Ghezzi, P.3
  • 231
    • 0032979438 scopus 로고    scopus 로고
    • Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation
    • Behrens A., Sibilia M., and Wagner E.F. Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation. Nat. Genet. 21 (1999) 326-329
    • (1999) Nat. Genet. , vol.21 , pp. 326-329
    • Behrens, A.1    Sibilia, M.2    Wagner, E.F.3
  • 232
    • 0034682264 scopus 로고    scopus 로고
    • Oncogenic transformation by ras and fos is mediated by c-Jun N-terminal phosphorylation
    • Behrens A., Jochum W., Sibilia M., and Wagner E.F. Oncogenic transformation by ras and fos is mediated by c-Jun N-terminal phosphorylation. Oncogene 19 (2000) 2657-2663
    • (2000) Oncogene , vol.19 , pp. 2657-2663
    • Behrens, A.1    Jochum, W.2    Sibilia, M.3    Wagner, E.F.4
  • 234
    • 34250370957 scopus 로고    scopus 로고
    • IRAK-4 kinase activity is required for IL-1 receptor- and Toll-like receptor 7-mediated signaling and gene expression
    • Koziczak-Holbro M., Joyce C., Gluck A., Kinzel B., Muller M., Tschopp C., Mathison J.C., Davis C.N., and Gram H. IRAK-4 kinase activity is required for IL-1 receptor- and Toll-like receptor 7-mediated signaling and gene expression. J. Biol. Chem. 282 18 (2007) 13552-13560
    • (2007) J. Biol. Chem. , vol.282 , Issue.18 , pp. 13552-13560
    • Koziczak-Holbro, M.1    Joyce, C.2    Gluck, A.3    Kinzel, B.4    Muller, M.5    Tschopp, C.6    Mathison, J.C.7    Davis, C.N.8    Gram, H.9
  • 236
    • 33845433364 scopus 로고    scopus 로고
    • Ser46 phosphorylation regulates p53-dependent apoptosis and replicative senescence
    • Feng L., Hollstein M., and Xu Y. Ser46 phosphorylation regulates p53-dependent apoptosis and replicative senescence. Cell Cycle 5 (2006) 2812-2819
    • (2006) Cell Cycle , vol.5 , pp. 2812-2819
    • Feng, L.1    Hollstein, M.2    Xu, Y.3
  • 238
    • 21644447832 scopus 로고    scopus 로고
    • Enhanced shutoff of phototransduction in transgenic mice expressing palmitoylation-deficient rhodopsin
    • Wang Z., Wen X.H., Ablonczy Z., Crouch R.K., Makino C.L., and Lem J. Enhanced shutoff of phototransduction in transgenic mice expressing palmitoylation-deficient rhodopsin. J. Biol. Chem. 280 (2005) 24293-24300
    • (2005) J. Biol. Chem. , vol.280 , pp. 24293-24300
    • Wang, Z.1    Wen, X.H.2    Ablonczy, Z.3    Crouch, R.K.4    Makino, C.L.5    Lem, J.6
  • 240
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S., Miao G., Wang F., Pan Y.C., and Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11 (1992) 3323-3335
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 241
    • 0038655553 scopus 로고    scopus 로고
    • Cysteine 64 of Ref-1 is not essential for redox regulation of AP-1 DNA binding
    • Ordway J.M., Eberhart D., and Curran T. Cysteine 64 of Ref-1 is not essential for redox regulation of AP-1 DNA binding. Mol. Cell. Biol. 23 (2003) 4257-4266
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4257-4266
    • Ordway, J.M.1    Eberhart, D.2    Curran, T.3
  • 242
    • 34250357205 scopus 로고    scopus 로고
    • Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of cysteines 93 and 310
    • Qu J., Liu G.H., Huang B., and Chen C. Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of cysteines 93 and 310. Nucleic Acids Res. 35 (2007) 2522-2532
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2522-2532
    • Qu, J.1    Liu, G.H.2    Huang, B.3    Chen, C.4
  • 243
    • 0037732635 scopus 로고    scopus 로고
    • Regulation of beta cell glucokinase by S-nitrosylation and association with nitric oxide synthase
    • Rizzo M.A., and Piston D.W. Regulation of beta cell glucokinase by S-nitrosylation and association with nitric oxide synthase. J. Cell Biol. 161 (2003) 243-248
    • (2003) J. Cell Biol. , vol.161 , pp. 243-248
    • Rizzo, M.A.1    Piston, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.