메뉴 건너뛰기




Volumn 25, Issue 3, 2012, Pages 588-604

Control of oxidative posttranslational cysteine modifications: From intricate chemistry to widespread biological and medical applications

Author keywords

[No Author keywords available]

Indexed keywords

1,2 DITHIOLE 3 THIONE DERIVATIVE; 5,5 DIMETHYL 1,3 CYCLOHEXANEDIONE; AJOENE; ALLICIN; ANETHOLE TRITHIONE; BENZOTHIAZINE DERIVATIVE; BETA TUBULIN; CHEMOSTERILANT; CLOPIDOGREL; CYSTEINE; DIALLYL DISULFIDE; DISULFIRAM; GLUTATHIONE PEROXIDASE; IODOACETAMIDE; MALEIMIDE; N ETHYLMALEIMIDE; NUCLEOPHILE; OLTIPRAZ; OMEPRAZOLE; PEROXIREDOXIN 2; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA 2; PESTICIDE; PROTEIN TYROSINE PHOSPHATASE 1B; REACTIVE OXYGEN METABOLITE; STREPTAVIDIN; SULFENAMIDE DERIVATIVE; SULFENIC ACID DERIVATIVE; THIOL; THIOREDOXIN; TRANSCRIPTION FACTOR NRF2;

EID: 84858678842     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx200342b     Document Type: Review
Times cited : (87)

References (122)
  • 1
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • DOI 10.1074/jbc.M111454200
    • Eaton, P., Byers, H. L., Leeds, N., et al. (2002) Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J. Biol. Chem. 277, 9806-9811. (Pubitemid 34968084)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 2
    • 33646745126 scopus 로고    scopus 로고
    • Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures
    • Eaton, P. (2006) Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures. Free Radical Biol. Med. 40, 1889-1899.
    • (2006) Free Radical Biol. Med. , vol.40 , pp. 1889-1899
    • Eaton, P.1
  • 3
    • 77956198091 scopus 로고    scopus 로고
    • A rapid approach for the detection, quantification, and discovery of novel sulfenic acid or S-nitrosothiol modified proteins using a biotin-switch method
    • Burgoyne, J. R., and Eaton, P. (2010) A rapid approach for the detection, quantification, and discovery of novel sulfenic acid or S-nitrosothiol modified proteins using a biotin-switch method. Methods Enzymol. 473, 281-303.
    • (2010) Methods Enzymol. , vol.473 , pp. 281-303
    • Burgoyne, J.R.1    Eaton, P.2
  • 4
    • 27944488351 scopus 로고    scopus 로고
    • Synthesis of chemical probes to map sulfenic acid modifications on proteins
    • DOI 10.1021/bc050257s
    • Poole, L. B., Zeng, B. B., Knaggs, S. A., et al. (2005) Synthesis of chemical probes to map sulfenic acid modifications on proteins. Bioconjugate Chem. 16, 1624-1628. (Pubitemid 41681531)
    • (2005) Bioconjugate Chemistry , vol.16 , Issue.6 , pp. 1624-1628
    • Poole, L.B.1    Zeng, B.-B.2    Knaggs, S.A.3    Yakubu, M.4    King, S.B.5
  • 6
    • 40849097418 scopus 로고    scopus 로고
    • Discovering mechanisms of signaling-mediated cysteine oxidation
    • Poole, L. B., and Nelson, K. J. (2008) Discovering mechanisms of signaling-mediated cysteine oxidation. Curr. Opin. Chem. Biol. 12, 18-24.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 18-24
    • Poole, L.B.1    Nelson, K.J.2
  • 7
    • 77956198422 scopus 로고    scopus 로고
    • Use of dimedone-based chemical probes for sulfenic acid detection: Evaluation of conditions affecting probe incorporation into redox-sensitive proteins
    • Klomsiri, C., Nelson, K. J., Bechtold, E., et al. (2010) Use of dimedone-based chemical probes for sulfenic acid detection: evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods Enzymol. 473, 77-94.
    • (2010) Methods Enzymol. , vol.473 , pp. 77-94
    • Klomsiri, C.1    Nelson, K.J.2    Bechtold, E.3
  • 8
    • 77956210622 scopus 로고    scopus 로고
    • Use of dimedone-based chemical probes for sulfenic acid detection: Methods to visualize and identify labeled proteins
    • Nelson, K. J., Klomsiri, C., Codreanu, S. G., et al. (2010) Use of dimedone-based chemical probes for sulfenic acid detection: methods to visualize and identify labeled proteins. Methods Enzymol. 473, 95-115.
    • (2010) Methods Enzymol. , vol.473 , pp. 95-115
    • Nelson, K.J.1    Klomsiri, C.2    Codreanu, S.G.3
  • 9
    • 58849148335 scopus 로고    scopus 로고
    • Quantifying the global cellular thiol-disulfide status
    • Hansen, R. E., Roth, D., and Winther, J. R. (2009) Quantifying the global cellular thiol-disulfide status. Proc. Natl. Acad. Sci. U.S.A. 106, 422-427.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 422-427
    • Hansen, R.E.1    Roth, D.2    Winther, J.R.3
  • 11
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells
    • Leonard, S. E., Reddie, K. G., and Carroll, K. S. (2009) Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem. Biol. 4, 783-799.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 12
    • 79551676040 scopus 로고    scopus 로고
    • Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone
    • Seo, Y. H., and Carroll, K. S. (2011) Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone. Angew. Chem., Int. Ed. 50, 1342-1345.
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 1342-1345
    • Seo, Y.H.1    Carroll, K.S.2
  • 13
    • 80051789102 scopus 로고    scopus 로고
    • Isotope-coded chemical reporter and acid-cleavable affinity reagents for monitoring protein sulfenic acids
    • Truong, T. H., Garcia, F. J., and Seo, Y. H. (2011) Isotope-coded chemical reporter and acid-cleavable affinity reagents for monitoring protein sulfenic acids. Bioorg. Med. Chem. Lett. 21, 5015-5020.
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 5015-5020
    • Truong, T.H.1    Garcia, F.J.2    Seo, Y.H.3
  • 14
    • 10644269917 scopus 로고    scopus 로고
    • Reactive sulphur species in oxidative signal transduction
    • DOI 10.1042/BST0321015
    • Jacob, C., Lancaster, J. R., and Giles, G. I. (2004) Reactive sulphur species in oxidative signal transduction. Biochem. Soc. Trans. 32, 1015-1017. (Pubitemid 39655531)
    • (2004) Biochemical Society Transactions , vol.32 , Issue.6 , pp. 1015-1017
    • Jacob, C.1    Lancaster Jr., J.R.2    Giles, G.I.3
  • 15
    • 0035385139 scopus 로고    scopus 로고
    • Chemistry of biologically important synthetic organoselenium compounds
    • DOI 10.1021/cr000426w
    • Mugesh, G., du Mont, W. W., and Sies, H. (2001) Chemistry of biologically important synthetic organoselenium compounds. Chem. Rev. 101, 2125-2179. (Pubitemid 35381674)
    • (2001) Chemical Reviews , vol.101 , Issue.7 , pp. 2125-2179
    • Mugesh, G.1    Du, M.W.-W.2    Sies, H.3
  • 16
    • 0042314356 scopus 로고    scopus 로고
    • Sulfur and Selenium: The Role of Oxidation State in Protein Structure and Function
    • DOI 10.1002/anie.200300573
    • Jacob, C., Giles, G. L., Giles, N. M., et al. (2003) Sulfur and selenium: The role of oxidation state in protein structure and function. Angew. Chem., Int. Ed. 42, 4742-4758. (Pubitemid 37314599)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.39 , pp. 4742-4758
    • Jacob, C.1    Giles, G.I.2    Giles, N.M.3    Sies, H.4
  • 17
    • 77956969973 scopus 로고    scopus 로고
    • Selenium- and Tellurium-Containing Multifunctional Redox Agents as Biochemical Redox Modulators with Selective Cytotoxicity
    • Jamier, V., Ba, L. A., and Jacob, C. (2010) Selenium- and Tellurium-Containing Multifunctional Redox Agents as Biochemical Redox Modulators with Selective Cytotoxicity. Chem. - Eur. J. 16, 10920-10928.
    • (2010) Chem. - Eur. J. , vol.16 , pp. 10920-10928
    • Jamier, V.1    Ba, L.A.2    Jacob, C.3
  • 18
    • 39949085437 scopus 로고    scopus 로고
    • Nonequilibrium thermodynamics of thiol/disulfide redox systems: A perspective on redox systems biology
    • Kemp, M., Go, Y. M., and Jones, D. P. (2008) Nonequilibrium thermodynamics of thiol/disulfide redox systems: A perspective on redox systems biology. Free Radical Biol. Med. 44, 921-937.
    • (2008) Free Radical Biol. Med. , vol.44 , pp. 921-937
    • Kemp, M.1    Go, Y.M.2    Jones, D.P.3
  • 19
    • 55949084077 scopus 로고    scopus 로고
    • Molecular transduction mechanisms of the redox network underlying the antiproliferative effects of allyl compounds from garlic
    • Filomeni, G., Rotilio, G., and Ciriolo, M. R. (2008) Molecular transduction mechanisms of the redox network underlying the antiproliferative effects of allyl compounds from garlic. J. Nutr. 138, 2053-2057.
    • (2008) J. Nutr. , vol.138 , pp. 2053-2057
    • Filomeni, G.1    Rotilio, G.2    Ciriolo, M.R.3
  • 20
    • 0027293791 scopus 로고
    • Determination of the reduction-oxidation potential of the thioredoxin- like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
    • Lundstrom, J., and Holmgren, A. (1993) Determination of the reduction oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32, 6649-6655. (Pubitemid 23217134)
    • (1993) Biochemistry , vol.32 , Issue.26 , pp. 6649-6655
    • Lundstrom, J.1    Holmgren, A.2
  • 21
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction by NADPH oxidase 4 localization
    • DOI 10.1083/jcb.200709049
    • Chen, K., Kirber, M. T., Xiao, H., et al. (2008) Regulation of ROS signal transduction by NADPH oxidase 4 localization. J. Cell Biol. 181, 1129-1139. (Pubitemid 351915488)
    • (2008) Journal of Cell Biology , vol.181 , Issue.7 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney Jr., J.F.5
  • 22
    • 35148881746 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanism of the hydrolysis of cysteine thiosulfinate ester
    • DOI 10.1021/tx700168z
    • Nagy, P., and Ashby, M. T. (2007) Reactive sulfur species: kinetics and mechanism of the hydrolysis of cysteine thiosulfinate ester. Chem. Res. Toxicol. 20, 1364-1372. (Pubitemid 47548305)
    • (2007) Chemical Research in Toxicology , vol.20 , Issue.9 , pp. 1364-1372
    • Nagy, P.1    Ashby, M.T.2
  • 23
    • 35948954266 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanisms of the reaction of cysteine thiosulfinate ester with cysteine to give cysteine sulfenic acid
    • DOI 10.1021/jo701813f
    • Nagy, P., Lemma, K., and Ashby, M. T. (2007) Reactive sulfur species: kinetics and mechanisms of the reaction of cysteine thiosulfinate ester with cysteine to give cysteine sulfenic acid. J. Org. Chem. 72, 8838-8846. (Pubitemid 350071714)
    • (2007) Journal of Organic Chemistry , vol.72 , Issue.23 , pp. 8838-8846
    • Nagy, P.1    Lemma, K.2    Ashby, M.T.3
  • 24
    • 33846868142 scopus 로고    scopus 로고
    • Kinetics and mechanism of the oxidation of the glutathione dimer by hypochlorous acid and catalytic reduction of the chloroamine product by glutathione reductase
    • DOI 10.1021/tx060184g
    • Nagy, P., and Ashby, M. T. (2007) Kinetics and mechanism of the oxidation of the glutathione dimer by hypochlorous acid and catalytic reduction of the chloroamine product by glutathione reductase. Chem. Res. Toxicol. 20, 79-87. (Pubitemid 46220157)
    • (2007) Chemical Research in Toxicology , vol.20 , Issue.1 , pp. 79-87
    • Nagy, P.1    Ashby, M.T.2
  • 25
    • 36148995826 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid
    • DOI 10.1021/ja0737218
    • Nagy, P., and Ashby, M. T. (2007) Reactive sulfur species: kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid. J. Am. Chem. Soc. 129, 14082-14091. (Pubitemid 350106102)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.45 , pp. 14082-14091
    • Nagy, P.1    Ashby, M.T.2
  • 26
    • 79951574562 scopus 로고    scopus 로고
    • Sulfenic acids as reactive intermediates in xenobiotic metabolism
    • Mansuy, D., and Dansette, P. M. (2011) Sulfenic acids as reactive intermediates in xenobiotic metabolism. Arch. Biochem. Biophys. 507, 174-185.
    • (2011) Arch. Biochem. Biophys. , vol.507 , pp. 174-185
    • Mansuy, D.1    Dansette, P.M.2
  • 27
    • 2442654043 scopus 로고    scopus 로고
    • Efficacy of allicin, the reactive molecule of garlic, in inhibiting Aspergillus spp. in vitro, and in a murine model of disseminated aspergillosis
    • DOI 10.1093/jac/dkh174
    • Shadkchan, Y., Shemesh, E., Mirelman, D., et al. (2004) Efficacy of allicin, the reactive molecule of garlic, in inhibiting Aspergillus spp. in vitro, and in a murine model of disseminated aspergillosis. J. Antimicrob. Chemother. 53, 832-836. (Pubitemid 38660287)
    • (2004) Journal of Antimicrobial Chemotherapy , vol.53 , Issue.5 , pp. 832-836
    • Shadkchan, Y.1    Shemesh, E.2    Mirelman, D.3    Miron, T.4    Rabinkov, A.5    Wilchek, M.6    Osherov, N.7
  • 29
    • 0037313425 scopus 로고    scopus 로고
    • A proton-pump inhibitor expedition: The case histories of omeprazole and esomeprazole
    • DOI 10.1038/nrd1010
    • Olbe, L., Carlsson, E., and Lindberg, P. (2003) A proton-pump inhibitor expedition: The case histories of omeprazole and esomeprazole. Nature Rev. Drug Discovery 2, 132-139. (Pubitemid 37361645)
    • (2003) Nature Reviews Drug Discovery , vol.2 , Issue.2 , pp. 132-139
    • Olbe, L.1    Carlsson, E.2    Lindberg, P.3
  • 30
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • DOI 10.1038/nature01680
    • Salmeen, A., Andersen, J. N., Myers, M. P., et al. (2003) Redox regulation of protein tyrosine phosphatase 1B involves a sulphenylamide intermediate. Nature 423, 769-773. (Pubitemid 36735701)
    • (2003) Nature , vol.423 , Issue.6941 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.-C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 31
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • DOI 10.1038/nature01681
    • van Montfort, R. L. M., Congreve, M., Tisi, D., et al. (2003) Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423, 773-777. (Pubitemid 36735702)
    • (2003) Nature , vol.423 , Issue.6941 , pp. 773-777
    • Van Montfort, R.L.M.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 32
    • 35148839162 scopus 로고    scopus 로고
    • Kinetics and mechanism of protein tyrosine phosphatase 1B inactivation by acrolein
    • DOI 10.1021/tx700213s
    • Seiner, D. R., LaButti, J. N., and Gates, K. S. (2007) Kinetics and mechanism of protein tyrosine phosphatase 1B inactivation by acrolein. Chem. Res. Toxicol. 20, 1315-1320. (Pubitemid 47548299)
    • (2007) Chemical Research in Toxicology , vol.20 , Issue.9 , pp. 1315-1320
    • Seiner, D.R.1    Labutti, J.N.2    Gates, K.S.3
  • 33
    • 0033678468 scopus 로고    scopus 로고
    • Identification and biological activity of the active metabolite of clopidogrel
    • Savi, P., Pereillo, J. M., Uzabiaga, M. F., et al. (2000) Identification and biological activity of the active metabolite of clopidogrel. Thromb. Hemostasis 84, 891-896.
    • (2000) Thromb. Hemostasis , vol.84 , pp. 891-896
    • Savi, P.1    Pereillo, J.M.2    Uzabiaga, M.F.3
  • 37
    • 75749102996 scopus 로고    scopus 로고
    • Metabolism and disposition of the thienopyridine antiplatelet drugs ticlopidine, clopidogrel, and prasugrel in humans
    • Farid, N. A., Kurihara, A., and Wrighton, S. A. (2010) Metabolism and disposition of the thienopyridine antiplatelet drugs ticlopidine, clopidogrel, and prasugrel in humans. J. Clin. Pharmacol. 50, 126-142.
    • (2010) J. Clin. Pharmacol. , vol.50 , pp. 126-142
    • Farid, N.A.1    Kurihara, A.2    Wrighton, S.A.3
  • 38
    • 62249112083 scopus 로고    scopus 로고
    • Metabolic oxidative cleavage of thioesters: Evidence for the formation of sulfenic acid intermediates in the bioactivation of the antithrombotic prodrugs ticlopidine and clopidogrel
    • Dansette, P. M., Libraire, J., Bertho, G., et al. (2009) Metabolic oxidative cleavage of thioesters: evidence for the formation of sulfenic acid intermediates in the bioactivation of the antithrombotic prodrugs ticlopidine and clopidogrel. Chem. Res. Toxicol. 22, 369-373.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 369-373
    • Dansette, P.M.1    Libraire, J.2    Bertho, G.3
  • 39
    • 29244484434 scopus 로고    scopus 로고
    • Diallyl trisulfide suppresses the proliferation and induces apoptosis of human colon cancer cells through oxidative modification of beta-tubulin
    • DOI 10.1074/jbc.M507127200
    • Hosono, T., Fukao, T., Ogihara, J., et al. (2005) Diallyl trisulfide suppresses the proliferation and induces apoptosis of human colon cancer cells through oxidative modification of beta-tubulin. J. Biol. Chem. 280, 41487-41493. (Pubitemid 41832209)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41487-41493
    • Hosono, T.1    Fukao, T.2    Ogihara, J.3    Ito, Y.4    Shiba, H.5    Seki, T.6    Ariga, T.7
  • 40
    • 5344220933 scopus 로고    scopus 로고
    • Induction of detoxifying enzymes by garlic organosulfur compounds through transcription factor Nrf2: Effect of chemical structure and stress signals
    • DOI 10.1016/j.freeradbiomed.2004.07.021, PII S0891584904005805
    • Chen, C., Pung, D., Leong, V., et al. (2004) Induction of detoxifying enzymes by garlic organosulfur compounds through transcription factor Nrf2: effect of chemical structure and stress signals. Free Radical Biol. Med. 37, 1578-1590. (Pubitemid 39349804)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.10 , pp. 1578-1590
    • Chen, C.1    Pung, D.2    Leong, V.3    Hebbar, V.4    Shen, G.5    Nair, S.6    Li, W.7    Tony, K.A.-N.8
  • 41
    • 23244464769 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by a persulfide (BnSSH)
    • DOI 10.1016/j.bmcl.2005.05.110, PII S0960894X05007341
    • Chatterji, T., Keerthi, K., and Gates, K. S. (2005) Generation of reactive oxygen species by a persulfide (BnSSH). Bioorg. Med. Chem. Lett. 15, 3921-3924. (Pubitemid 41095495)
    • (2005) Bioorganic and Medicinal Chemistry Letters , vol.15 , Issue.17 , pp. 3921-3924
    • Chatterji, T.1    Keerthi, K.2    Gates, K.S.3
  • 42
    • 84961986802 scopus 로고    scopus 로고
    • On the origin of cytotoxicity of the natural product varacin. A novel example of a pentathiepin reaction that provides evidence for a triatomic sulfur intermediate
    • Greer, A. (2001) On the origin of cytotoxicity of the natural product varacin. A novel example of a pentathiepin reaction that provides evidence for a triatomic sulfur intermediate. J. Am. Chem. Soc. 123, 10379-10386.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 10379-10386
    • Greer, A.1
  • 44
    • 63049105151 scopus 로고    scopus 로고
    • Hydrogen sulfide and the vasculature: A novel vasculoprotective entity and regulator of nitric oxide bioavailability?
    • Whiteman, M., and Moore, P. K. (2009) Hydrogen sulfide and the vasculature: a novel vasculoprotective entity and regulator of nitric oxide bioavailability? J. Cell Mol. Med. 13, 488-507.
    • (2009) J. Cell Mol. Med. , vol.13 , pp. 488-507
    • Whiteman, M.1    Moore, P.K.2
  • 45
    • 79952529632 scopus 로고    scopus 로고
    • Interactions of polysulfanes with components of red blood cells
    • Schneider, T., Ba, L. A., Khairan, K., et al. (2011) Interactions of polysulfanes with components of red blood cells. Med. Chem. Commun. 2, 196-200.
    • (2011) Med. Chem. Commun. , vol.2 , pp. 196-200
    • Schneider, T.1    Ba, L.A.2    Khairan, K.3
  • 47
    • 33751439570 scopus 로고    scopus 로고
    • A scent of therapy: Pharmacological implications of natural products containing redox-active sulfur atoms
    • Jacob, C. (2006) A scent of therapy: pharmacological implications of natural products containing redox-active sulfur atoms. Nat. Prod. Rep. 23, 851-863.
    • (2006) Nat. Prod. Rep. , vol.23 , pp. 851-863
    • Jacob, C.1
  • 48
    • 45249120583 scopus 로고    scopus 로고
    • The chemistry behind redox regulation with a focus on sulphur redox systems
    • DOI 10.1111/j.1399-3054.2008.01080.x
    • Jacob, C., and Anwar, A. (2008) The chemistry behind redox regulation with a focus on sulphur redox systems. Physiol. Plant. 133, 469-480. (Pubitemid 351841672)
    • (2008) Physiologia Plantarum , vol.133 , Issue.3 , pp. 469-480
    • Jacob, C.1    Anwar, A.2
  • 49
    • 0029660277 scopus 로고    scopus 로고
    • Inhibition of microbial growth by ajoene, a sulfur-containing compound derived from garlic
    • Naganawa, R., Iwata, N., Ishikawa, K., et al. (1996) Inhibition of microbial growth by ajoene, a sulfur-containing compound derived from garlic. Appl. Environ. Microbiol. 62, 4238-4242.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4238-4242
    • Naganawa, R.1    Iwata, N.2    Ishikawa, K.3
  • 51
    • 35648960217 scopus 로고
    • Treatment of alcoholism with a sensitising drug
    • Martensenlarsen, O. (1948) Treatment of alcoholism with a sensitising drug. Lancet 255, 1004-1005.
    • (1948) Lancet , vol.255 , pp. 1004-1005
    • Martensenlarsen, O.1
  • 52
    • 84875816744 scopus 로고
    • A preliminary report of antabuse therapy for alcoholism
    • Steckler, P. P., and Harris, L. (1951) A preliminary report of antabuse therapy for alcoholism. Psychiatr. Q. 25, 91-96.
    • (1951) Psychiatr. Q. , vol.25 , pp. 91-96
    • Steckler, P.P.1    Harris, L.2
  • 53
    • 79251473704 scopus 로고    scopus 로고
    • Disulfiram is a DNA demethylating agent and inhibits prostate cancer cell growth
    • Lin, J. Q., Haffner, M. C., Zhang, Y. G., et al. (2011) Disulfiram is a DNA demethylating agent and inhibits prostate cancer cell growth. Prostate 71, 333-343.
    • (2011) Prostate , vol.71 , pp. 333-343
    • Lin, J.Q.1    Haffner, M.C.2    Zhang, Y.G.3
  • 54
    • 79951688311 scopus 로고    scopus 로고
    • Targeting malignancies with disulfiram (antabuse): Multidrug resistance, angiogenesis, and proteasome
    • Cvek, B. (2011) Targeting malignancies with disulfiram (antabuse): multidrug resistance, angiogenesis, and proteasome. Curr. Cancer Drug Targets 11, 332-337.
    • (2011) Curr. Cancer Drug Targets , vol.11 , pp. 332-337
    • Cvek, B.1
  • 55
    • 77953789214 scopus 로고    scopus 로고
    • Synthesis, biological evaluation, and structure-activity relationships of dithiolethiones as inducers of cytoprotective phase 2 enzymes
    • Munday, R., Zhang, Y. S., Paonessa, J. D., et al. (2010) Synthesis, biological evaluation, and structure-activity relationships of dithiolethiones as inducers of cytoprotective phase 2 enzymes. J. Med. Chem. 53, 4761-4767.
    • (2010) J. Med. Chem. , vol.53 , pp. 4761-4767
    • Munday, R.1    Zhang, Y.S.2    Paonessa, J.D.3
  • 56
    • 77955469032 scopus 로고    scopus 로고
    • Inactivation of protein tyrosine phosphatases by oltipraz and other cancer chemopreventive 1,2-dithiole-3-thiones
    • Bhattacharyya, S., Zhou, H. Y., Seiner, D. R., et al. (2010) Inactivation of protein tyrosine phosphatases by oltipraz and other cancer chemopreventive 1,2-dithiole-3-thiones. Bioorg. Med. Chem. 18, 5945-5949.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 5945-5949
    • Bhattacharyya, S.1    Zhou, H.Y.2    Seiner, D.R.3
  • 57
    • 74049120454 scopus 로고    scopus 로고
    • Nrf2: Friend or foe for chemoprevention?
    • Kensler, T. W., and Wakabayashi, N. (2010) Nrf2: friend or foe for chemoprevention? Carcinogenesis 31, 90-99.
    • (2010) Carcinogenesis , vol.31 , pp. 90-99
    • Kensler, T.W.1    Wakabayashi, N.2
  • 58
    • 77649270763 scopus 로고    scopus 로고
    • Targeting NRF2 signaling for cancer chemoprevention
    • Kwak, M. K., and Kensler, T. W. (2010) Targeting NRF2 signaling for cancer chemoprevention. Toxicol. Appl. Pharmacol. 244, 66-76.
    • (2010) Toxicol. Appl. Pharmacol. , vol.244 , pp. 66-76
    • Kwak, M.K.1    Kensler, T.W.2
  • 59
    • 0034527831 scopus 로고    scopus 로고
    • Anethole dithiolethione regulates oxidant-induced tyrosine kinase activation in endothelial cells
    • Ben-Mahdi, M. H., Gozin, A., Driss, F., et al. (2000) Anethole dithiolethione regulates oxidant-induced tyrosine kinase activation in endothelial cells. Antioxid. Redox Signaling 2, 789-800.
    • (2000) Antioxid. Redox Signaling , vol.2 , pp. 789-800
    • Ben-Mahdi, M.H.1    Gozin, A.2    Driss, F.3
  • 60
    • 0030745630 scopus 로고    scopus 로고
    • Chemopreventive efficacy of anethole trithione, N-acetyl-L-cysteine, miconazole and phenethylisothiocyanate in the DMBA-induced rat mammary cancer model
    • DOI 10.1002/(SICI)1097-0215(19970703)72:1<95::AID-IJC14>3.0.CO;2-9
    • Lubet, R. A., Steele, V. E., Eto, I., et al. (1997) Chemopreventive efficacy of anethole trithione, N-acetyl-L-cysteine, miconazole and phenethylisothiocyanate in the DMBA-induced rat mammary cancer model. Int. J. Cancer 72, 95-101. (Pubitemid 27314645)
    • (1997) International Journal of Cancer , vol.72 , Issue.1 , pp. 95-101
    • Lubet, R.A.1    Steele, V.E.2    Eto, I.3    Margaret, J.M.4    Kelloff, G.J.5    Grubbs, C.J.6
  • 61
    • 50849114157 scopus 로고    scopus 로고
    • Effect of S-diclofenac, a novel hydrogen sulfide releasing derivative inhibit rat vascular smooth muscle cell proliferation
    • Baskar, R., Sparatore, A., Del Soldato, P., et al. (2008) Effect of S-diclofenac, a novel hydrogen sulfide releasing derivative inhibit rat vascular smooth muscle cell proliferation. Eur. J. Pharmacol. 594, 1-8.
    • (2008) Eur. J. Pharmacol. , vol.594 , pp. 1-8
    • Baskar, R.1    Sparatore, A.2    Del Soldato, P.3
  • 62
    • 0026022662 scopus 로고
    • Toward an understanding of the schistosomicidal effect of 4-methyl-5-(2-pyrazinyl)-1,2-dithiole-3-thione (oltipraz)
    • Fleury, M. B., Largeron, M., and Martens, T. (1991) Toward an understanding of the schistosomicidal effect of 4-methyl-5-(2-pyrazinyl)-1,2- dithiole-3-thione (oltipraz). Biochem. Pharmacol. 41, 361-367.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 361-367
    • Fleury, M.B.1    Largeron, M.2    Martens, T.3
  • 63
    • 3342944977 scopus 로고    scopus 로고
    • 1,2-Dithiole-3-ones as potent inhibitors of the bacterial 3-ketoacyl acyl carrier protein synthase III (FabH)
    • DOI 10.1128/AAC.48.8.3093-3102.2004
    • He, X., Reeve, A. M. E., Desai, U. R., et al. (2004) 1,2-Dithiole-3-ones as potent inhibitors of the bacterial 3-ketoacyl acyl carrier protein synthase III (FabH). Antimicrob. Agents Chemother. 48, 3093-3102. (Pubitemid 38989179)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.8 , pp. 3093-3102
    • He, X.1    Reeve, A.M.2    Desai, U.R.3    Kellogg, G.E.4    Reynolds, K.A.5
  • 64
    • 79954780467 scopus 로고    scopus 로고
    • Oltipraz therapy in patients with liver fibrosis or cirrhosis: A randomized, double-blind, placebo-controlled phase II trial
    • Kim, S. G., Kim, Y. M., Choi, J. Y., et al. (2011) Oltipraz therapy in patients with liver fibrosis or cirrhosis: a randomized, double-blind, placebo-controlled phase II trial. J. Pharm. Pharmacol. 63, 627-635.
    • (2011) J. Pharm. Pharmacol. , vol.63 , pp. 627-635
    • Kim, S.G.1    Kim, Y.M.2    Choi, J.Y.3
  • 65
    • 77954349231 scopus 로고    scopus 로고
    • Design, synthesis, and pharmacological evaluation of the aqueous prodrugs of desmethyl anethole trithione with hepatoprotective activity
    • Chen, P., Luo, Y., Hai, L., et al. (2010) Design, synthesis, and pharmacological evaluation of the aqueous prodrugs of desmethyl anethole trithione with hepatoprotective activity. Eur. J. Med. Chem. 45, 3005-3010.
    • (2010) Eur. J. Med. Chem. , vol.45 , pp. 3005-3010
    • Chen, P.1    Luo, Y.2    Hai, L.3
  • 66
    • 65649096556 scopus 로고    scopus 로고
    • Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis
    • Makarov, V., Manina, G., Mikusova, K., et al. (2009) Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis. Science 324, 801-804.
    • (2009) Science , vol.324 , pp. 801-804
    • Makarov, V.1    Manina, G.2    Mikusova, K.3
  • 67
    • 77957310736 scopus 로고    scopus 로고
    • Benzothiazinones: Prodrugs that covalently modify the decaprenylphosphoryl-beta-D-ribose 2′-epimerase DprE1 of Mycobacterium tuberculosis
    • Trefzer, C., Rengifo-Gonzalez, M., Hinner, M. J., et al. (2010) Benzothiazinones: prodrugs that covalently modify the decaprenylphosphoryl-beta- D-ribose 2′-epimerase DprE1 of Mycobacterium tuberculosis. J. Am. Chem. Soc. 132, 13663-13665.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13663-13665
    • Trefzer, C.1    Rengifo-Gonzalez, M.2    Hinner, M.J.3
  • 68
    • 0000927916 scopus 로고
    • Electrophilic intermediate in the reaction of glutathione and nitrosoarenes
    • Kazanis, S., and Mcclelland, R. A. (1992) Electrophilic intermediate in the reaction of glutathione and nitrosoarenes. J. Am. Chem. Soc. 114, 3052-3059.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3052-3059
    • Kazanis, S.1    Mcclelland, R.A.2
  • 69
    • 79851510345 scopus 로고    scopus 로고
    • Chemical 'omics' approaches for understanding protein cysteine oxidation in biology
    • Leonard, S. E., and Carroll, K. S. (2011) Chemical 'omics' approaches for understanding protein cysteine oxidation in biology. Curr. Opin. Chem. Biol. 15, 88-102.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 88-102
    • Leonard, S.E.1    Carroll, K.S.2
  • 70
    • 68349131632 scopus 로고    scopus 로고
    • Methods for the determination and quantification of the reactive thiol proteome
    • Hill, B. G., Reily, C., Oh, J. Y., et al. (2009) Methods for the determination and quantification of the reactive thiol proteome. Free Radical Biol. Med. 47, 675-683.
    • (2009) Free Radical Biol. Med. , vol.47 , pp. 675-683
    • Hill, B.G.1    Reily, C.2    Oh, J.Y.3
  • 71
    • 79251609052 scopus 로고    scopus 로고
    • A fluorescent dual labeling technique for the quantitative measurement of reduced and oxidized protein thiols in tissue samples
    • Armstrong, A. E., Zerbes, R., Fournier, P. A., et al. (2011) A fluorescent dual labeling technique for the quantitative measurement of reduced and oxidized protein thiols in tissue samples. Free Radical Biol. Med. 50, 510-517.
    • (2011) Free Radical Biol. Med. , vol.50 , pp. 510-517
    • Armstrong, A.E.1    Zerbes, R.2    Fournier, P.A.3
  • 72
    • 78650078496 scopus 로고    scopus 로고
    • Quantitative reactivity profiling predicts functional cysteines in proteomes
    • Weerapana, E., Wang, C., Simon, G. M., et al. (2010) Quantitative reactivity profiling predicts functional cysteines in proteomes. Nature 468, 790-795.
    • (2010) Nature , vol.468 , pp. 790-795
    • Weerapana, E.1    Wang, C.2    Simon, G.M.3
  • 73
    • 79958233011 scopus 로고    scopus 로고
    • Redox biology: Computational approaches to the investigation of functional cysteine residues
    • Marino, S. M., and Gladyshev, V. N. (2011) Redox biology: Computational approaches to the investigation of functional cysteine residues. Antioxid. Redox Signaling 15, 135-146.
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 135-146
    • Marino, S.M.1    Gladyshev, V.N.2
  • 74
    • 33846635882 scopus 로고    scopus 로고
    • High-throughput identification of catalytic redox-active cystein residues
    • DOI 10.1126/science.1133114
    • Fomenko, D. E., Xing, W. B., Adair, B. M., et al. (2007) High-throughput identification of catalytic redox-active cysteine residues. Science 315, 387-389. (Pubitemid 46175521)
    • (2007) Science , vol.315 , Issue.5810 , pp. 387-389
    • Fomenko, D.E.1    Xing, W.2    Adair, B.M.3    Thomas, D.J.4    Gladyshev, V.N.5
  • 75
    • 78649268193 scopus 로고    scopus 로고
    • Formation, reactivity, and detection of protein sulfenic acids
    • Kettenhofen, N. J., and Wood, M. J. (2010) Formation, reactivity, and detection of protein sulfenic acids. Chem. Res. Toxicol. 23, 1633-1646.
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1633-1646
    • Kettenhofen, N.J.1    Wood, M.J.2
  • 76
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • DOI 10.1021/bi973035t
    • Denu, J. M., and Tanner, K. G. (1998) Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37, 5633-5642. (Pubitemid 28241948)
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 78
    • 79955493857 scopus 로고    scopus 로고
    • Redox-based probes for protein tyrosine phosphatases
    • Leonard, S. E., Garcia, F. J., Goodsell, D. S., et al. (2011) Redox-based probes for protein tyrosine phosphatases. Angew. Chem., Int. Ed. 50, 4423-4427.
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 4423-4427
    • Leonard, S.E.1    Garcia, F.J.2    Goodsell, D.S.3
  • 79
    • 79958198412 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases: Structural and chemical aspects
    • Tanner, J. J., Parsons, Z. D., Cummings, A. H., et al. (2011) Redox regulation of protein tyrosine phosphatases: structural and chemical aspects. Antioxid. Redox Signaling 15, 77-97.
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 77-97
    • Tanner, J.J.1    Parsons, Z.D.2    Cummings, A.H.3
  • 81
    • 79953724030 scopus 로고    scopus 로고
    • Open season for hunting and trapping post-translational cysteine modifications in proteins and enzymes
    • Jacob, C., and Ba, L. A. (2011) Open season for hunting and trapping post-translational cysteine modifications in proteins and enzymes. ChemBioChem 12, 841-844.
    • (2011) ChemBioChem , vol.12 , pp. 841-844
    • Jacob, C.1    Ba, L.A.2
  • 82
    • 79251483598 scopus 로고    scopus 로고
    • Protocols for the detection of s-glutathionylated and s-nitrosylated proteins in situ
    • Aesif, S. W., Janssen-Heininger, Y. M., and Reynaert, N. L. (2010) Protocols for the detection of s-glutathionylated and s-nitrosylated proteins in situ. Methods Enzymol. 474, 289-296.
    • (2010) Methods Enzymol. , vol.474 , pp. 289-296
    • Aesif, S.W.1    Janssen-Heininger, Y.M.2    Reynaert, N.L.3
  • 84
    • 59449090185 scopus 로고    scopus 로고
    • Nitrofatty acid metabolome: Saturation, desaturation, beta-oxidation, and protein adduction
    • Rudolph, V., Schopfer, F. J., Khoo, N. K., et al. (2009) Nitrofatty acid metabolome: saturation, desaturation, beta-oxidation, and protein adduction. J. Biol. Chem. 284, 1461-1473.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1461-1473
    • Rudolph, V.1    Schopfer, F.J.2    Khoo, N.K.3
  • 85
    • 78149448121 scopus 로고    scopus 로고
    • Alkylation of the tumor suppressor PTEN activates Akt and beta-catenin signaling: A mechanism linking inflammation and oxidative stress with cancer
    • Covey, T. M., Edes, K., Coombs, G. S., et al. (2010) Alkylation of the tumor suppressor PTEN activates Akt and beta-catenin signaling: a mechanism linking inflammation and oxidative stress with cancer. PLoS One 5, e13545.
    • (2010) PLoS One , vol.5
    • Covey, T.M.1    Edes, K.2    Coombs, G.S.3
  • 86
    • 4344676781 scopus 로고    scopus 로고
    • Inactivation of protein disulfide isomerase by alkylators including alpha,beta-unsaturated aldehydes at low physiological pHs
    • Liu, X. W., and Sok, D. E. (2004) Inactivation of protein disulfide isomerase by alkylators including alpha,beta-unsaturated aldehydes at low physiological pHs. Biol. Chem. 385, 633-637.
    • (2004) Biol. Chem. , vol.385 , pp. 633-637
    • Liu, X.W.1    Sok, D.E.2
  • 87
    • 45849089850 scopus 로고    scopus 로고
    • SHP-1 inhibition by 4-hydroxynonenal activates Jun N-terminal kinase and glutamate cysteine ligase
    • DOI 10.1165/rcmb.2007-0371OC
    • Rinna, A., and Forman, H. J. (2008) SHP-1 inhibition by 4-hydroxynonenal activates Jun N-terminal kinase and glutamate cysteine ligase. Am. J. Respir. Cell Mol. Biol. 39, 97-104. (Pubitemid 351883963)
    • (2008) American Journal of Respiratory Cell and Molecular Biology , vol.39 , Issue.1 , pp. 97-104
    • Rinna, A.1    Forman, H.J.2
  • 88
    • 77953100764 scopus 로고    scopus 로고
    • Electrophilic tuning of the chemoprotective natural product sulforaphane
    • Ahn, Y. H., Hwang, Y., Liu, H., et al. (2010) Electrophilic tuning of the chemoprotective natural product sulforaphane. Proc. Natl. Acad. Sci. U.S.A. 107, 9590-9595.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9590-9595
    • Ahn, Y.H.1    Hwang, Y.2    Liu, H.3
  • 89
    • 77956205107 scopus 로고    scopus 로고
    • Proteome screens for cys residues oxidation: The redoxome
    • Chiappetta, G., Ndiaye, S., Igbaria, A., et al. (2010) Proteome screens for cys residues oxidation: The redoxome. Methods Enzymol. 473, 199-216.
    • (2010) Methods Enzymol. , vol.473 , pp. 199-216
    • Chiappetta, G.1    Ndiaye, S.2    Igbaria, A.3
  • 90
    • 79851510399 scopus 로고    scopus 로고
    • The redoxome: Proteomic analysis of cellular redox networks
    • Thamsen, M., and Jakob, U. (2011) The redoxome: Proteomic analysis of cellular redox networks. Curr. Opin. Chem. Biol. 15, 113-119.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 113-119
    • Thamsen, M.1    Jakob, U.2
  • 92
    • 80053376304 scopus 로고    scopus 로고
    • Redox signalling via the cellular thiolstat
    • Jacob, C. (2011) Redox signalling via the cellular thiolstat. Biochem. Soc. Trans. 39, 1247-1253.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1247-1253
    • Jacob, C.1
  • 93
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • DOI 10.1126/science.1080405
    • Wood, Z. A., Poole, L. B., and Karplus, P. A. (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653. (Pubitemid 36520591)
    • (2003) Science , vol.300 , Issue.5619 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 94
    • 3843064487 scopus 로고    scopus 로고
    • The sulfinic acid switch in proteins
    • Jacob, C., Holme, A. L., and Fry, F. H. (2004) The sulfinic acid switch in proteins. Org. Biomol. Chem. 2, 1953-1956.
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 1953-1956
    • Jacob, C.1    Holme, A.L.2    Fry, F.H.3
  • 96
    • 76749102420 scopus 로고    scopus 로고
    • 2accumulation for cell signaling
    • 2accumulation for cell signaling. Cell 140, 517-528.
    • (2010) Cell , vol.140 , pp. 517-528
    • Woo, H.A.1    Yim, S.H.2    Shin, D.H.3
  • 97
    • 0037222255 scopus 로고    scopus 로고
    • Structure, mechanism and regulation of peroxiredoxins
    • DOI 10.1016/S0968-0004(02)00003-8, PII S0968000402000038
    • Wood, Z. A., Schroder, E., Robin Harris, J., et al. (2003) Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28, 32-40. (Pubitemid 36051004)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 32-40
    • Wood, Z.A.1    Schroder, E.2    Harris, J.R.3    Poole, L.B.4
  • 98
    • 66649131702 scopus 로고    scopus 로고
    • Redox-regulated chaperones
    • Kumsta, C., and Jakob, U. (2009) Redox-regulated chaperones. Biochemistry 48, 4666-4676.
    • (2009) Biochemistry , vol.48 , pp. 4666-4676
    • Kumsta, C.1    Jakob, U.2
  • 99
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • DOI 10.1016/S0891-5849(01)00480-4, PII S0891584901004804
    • Schafer, F. Q., and Buettner, G. R. (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radical Biol. Med. 30, 1191-1212. (Pubitemid 32463931)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.11 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 100
    • 73149116849 scopus 로고    scopus 로고
    • Natural product derivative Bis(4-fluorobenzyl)trisulfide inhibits tumor growth by modification of beta-tubulin at Cys 12 and suppression of microtubule dynamics
    • Xu, W., Xi, B., Wu, J., et al. (2009) Natural product derivative Bis(4-fluorobenzyl)trisulfide inhibits tumor growth by modification of beta-tubulin at Cys 12 and suppression of microtubule dynamics. Mol. Cancer Ther. 8, 3318-3330.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 3318-3330
    • Xu, W.1    Xi, B.2    Wu, J.3
  • 101
    • 33947174588 scopus 로고    scopus 로고
    • Garlic compounds induced calpain and intrinsic caspase cascade for apoptosis in human malignant neuroblastoma SH-SY5Y cells
    • DOI 10.1007/s10495-006-0024-x
    • Karmakar, S., Banik, N. L., Patel, S. J., et al. (2007) Garlic compounds induced calpain and intrinsic caspase cascade for apoptosis in human malignant neuroblastoma SH-SY5Y cells. Apoptosis 12, 671-684. (Pubitemid 46411474)
    • (2007) Apoptosis , vol.12 , Issue.4 , pp. 671-684
    • Karmakar, S.1    Banik, N.L.2    Patel, S.J.3    Ray, S.K.4
  • 102
    • 0942288402 scopus 로고    scopus 로고
    • Diallyl disulfide (DADS) enhances gap-junctional intercellular communication by both direct and indirect mechanisms in rat liver cells
    • DOI 10.1093/carcin/bgg182
    • Huard, C., Druesne, N., Guyonnet, D., et al. (2004) Diallyl disulfide (DADS) enhances gap-junctional intercellular communication by both direct and indirect mechanisms in rat liver cells. Carcinogenesis 25, 91-98. (Pubitemid 38139227)
    • (2004) Carcinogenesis , vol.25 , Issue.1 , pp. 91-98
    • Huard, C.1    Druesne, N.2    Guyonnet, D.3    Thomas, M.4    Pagniez, A.5    Le, B.A.-M.6    Martel, P.7    Chaumontet, C.8
  • 103
    • 51849103354 scopus 로고    scopus 로고
    • Allyl mercaptan, a garlic-derived organosulfur compound, inhibits histone deacetylase and enhances Sp3 binding on the P21WAF1 promoter
    • Nian, H., Delage, B., Pinto, J. T., et al. (2008) Allyl mercaptan, a garlic-derived organosulfur compound, inhibits histone deacetylase and enhances Sp3 binding on the P21WAF1 promoter. Carcinogenesis 29, 1816-1824.
    • (2008) Carcinogenesis , vol.29 , pp. 1816-1824
    • Nian, H.1    Delage, B.2    Pinto, J.T.3
  • 104
    • 63049105405 scopus 로고    scopus 로고
    • Modulation of histone deacetylase activity by dietary isothiocyanates and allyl sulfides: Studies with sulforaphane and garlic organosulfur compounds
    • Nian, H., Delage, B., Ho, E., et al. (2009) Modulation of histone deacetylase activity by dietary isothiocyanates and allyl sulfides: studies with sulforaphane and garlic organosulfur compounds. Environ. Mol. Mutagen. 50, 213-221.
    • (2009) Environ. Mol. Mutagen. , vol.50 , pp. 213-221
    • Nian, H.1    Delage, B.2    Ho, E.3
  • 105
    • 33644869135 scopus 로고    scopus 로고
    • Diallyl trisulfide, a constituent of processed garlic, inactivates Akt to trigger mitochondrial translocation of BAD and caspase-mediated apoptosis in human prostate cancer cells
    • DOI 10.1093/carcin/bgi228
    • Xiao, D., and Singh, S. V. (2006) Diallyl trisulfide, a constituent of processed garlic, inactivates Akt to trigger mitochondrial translocation of BAD and caspase-mediated apoptosis in human prostate cancer cells. Carcinogenesis 27, 533-540. (Pubitemid 43372883)
    • (2006) Carcinogenesis , vol.27 , Issue.3 , pp. 533-540
    • Xiao, D.1    Singh, S.V.2
  • 106
    • 79952333387 scopus 로고    scopus 로고
    • Antiproliferative effect of natural tetrasulfides in human breast cancer cells is mediated through the inhibition of the cell division cycle 25 phosphatases
    • Viry, E., Anwar, A., Kirsch, G., et al. (2011) Antiproliferative effect of natural tetrasulfides in human breast cancer cells is mediated through the inhibition of the cell division cycle 25 phosphatases. Int. J. Oncol. 38, 1103-1111.
    • (2011) Int. J. Oncol. , vol.38 , pp. 1103-1111
    • Viry, E.1    Anwar, A.2    Kirsch, G.3
  • 107
    • 0037036460 scopus 로고    scopus 로고
    • Redox regulation of Cdc25C
    • DOI 10.1074/jbc.M201589200
    • Savitsky, P. A., and Finkel, T. (2002) Redox regulation of Cdc25C. J. Biol. Chem. 277, 20535-20540. (Pubitemid 34967353)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20535-20540
    • Savitsky, P.A.1    Finkel, T.2
  • 108
    • 63049105131 scopus 로고    scopus 로고
    • Diallyl trisulfide selectively causes Bax- and Bak-mediated apoptosis in human lung cancer cells
    • Xiao, D., Zeng, Y., Hahm, E. R., et al. (2009) Diallyl trisulfide selectively causes Bax- and Bak-mediated apoptosis in human lung cancer cells. Environ. Mol. Mutagen. 50, 201-212.
    • (2009) Environ. Mol. Mutagen. , vol.50 , pp. 201-212
    • Xiao, D.1    Zeng, Y.2    Hahm, E.R.3
  • 109
    • 0034734611 scopus 로고    scopus 로고
    • Effects of allyl sulfur compounds and garlic extract on the expression of Bcl-2, Bax, and p53 in non small cell lung cancer cell lines
    • Hong, Y. S., Ham, Y. A., Choi, J. H., et al. (2000) Effects of allyl sulfur compounds and garlic extract on the expression of Bcl-2, Bax, and p53 in non small cell lung cancer cell lines. Exp. Mol. Med. 32, 127-134.
    • (2000) Exp. Mol. Med. , vol.32 , pp. 127-134
    • Hong, Y.S.1    Ham, Y.A.2    Choi, J.H.3
  • 110
    • 77949568185 scopus 로고    scopus 로고
    • Diallyl sulfide induces growth inhibition and apoptosis of anaplastic thyroid cancer cells by mitochondrial signaling pathway
    • Shin, H. A., Cha, Y. Y., Park, M. S., et al. (2010) Diallyl sulfide induces growth inhibition and apoptosis of anaplastic thyroid cancer cells by mitochondrial signaling pathway. Oral Oncol. 46, 15-18.
    • (2010) Oral Oncol. , vol.46 , pp. 15-18
    • Shin, H.A.1    Cha, Y.Y.2    Park, M.S.3
  • 111
    • 79952043687 scopus 로고    scopus 로고
    • Effect of diallyl disulfide on Ca2+ movement and viability in PC3 human prostate cancer cells
    • Chen, W. C., Hsu, S. S., Chou, C. T., et al. (2011) Effect of diallyl disulfide on Ca2+ movement and viability in PC3 human prostate cancer cells. Toxicol. in Vitro 25, 636-643.
    • (2011) Toxicol. in Vitro , vol.25 , pp. 636-643
    • Chen, W.C.1    Hsu, S.S.2    Chou, C.T.3
  • 112
    • 67949088073 scopus 로고    scopus 로고
    • The garlic ingredient diallyl sulfide induces Ca(2+) mobilization in Madin-Darby canine kidney cells
    • Chen, C. H., Su, S. J., Chang, K. L., et al. (2009) The garlic ingredient diallyl sulfide induces Ca(2+) mobilization in Madin-Darby canine kidney cells. Food Chem. Toxicol. 47, 2344-2350.
    • (2009) Food Chem. Toxicol. , vol.47 , pp. 2344-2350
    • Chen, C.H.1    Su, S.J.2    Chang, K.L.3
  • 113
    • 55749083891 scopus 로고    scopus 로고
    • Diallyl disulfide (DADS) induces apoptosis in human cervical cancer Ca Ski cells via reactive oxygen species and Ca2+-dependent mitochondria-dependent pathway
    • Lin, Y. T., Yang, J. S., Lin, S. Y., et al. (2008) Diallyl disulfide (DADS) induces apoptosis in human cervical cancer Ca Ski cells via reactive oxygen species and Ca2+-dependent mitochondria-dependent pathway. Anticancer Res. 28, 2791-2799.
    • (2008) Anticancer Res. , vol.28 , pp. 2791-2799
    • Lin, Y.T.1    Yang, J.S.2    Lin, S.Y.3
  • 114
    • 0037205963 scopus 로고    scopus 로고
    • Role of Ca(2+) in diallyl disulfide-induced apoptotic cell death of HCT-15 cells
    • Park, E. K., Kwon, K. B., Park, K. I., et al. (2002) Role of Ca(2+) in diallyl disulfide-induced apoptotic cell death of HCT-15 cells. Exp. Mol. Med. 34, 250-257.
    • (2002) Exp. Mol. Med. , vol.34 , pp. 250-257
    • Park, E.K.1    Kwon, K.B.2    Park, K.I.3
  • 115
    • 70350313238 scopus 로고    scopus 로고
    • 1,2-Vinyidithiin from garlic inhibits differentiation and inflammation of human preadipocytes
    • Keophiphath, M., Priem, F., Jacquemond-Collet, I., et al. (2009) 1,2-Vinyidithiin from garlic inhibits differentiation and inflammation of human preadipocytes. J. Nutr. 139, 2055-2060.
    • (2009) J. Nutr. , vol.139 , pp. 2055-2060
    • Keophiphath, M.1    Priem, F.2    Jacquemond-Collet, I.3
  • 116
    • 68049084746 scopus 로고    scopus 로고
    • Evidence for trisulfide bonds in a recombinant variant of a human IgG2 monoclonal antibody
    • Pristatsky, P., Cohen, S. L., Krantz, D., et al. (2009) Evidence for trisulfide bonds in a recombinant variant of a human IgG2 monoclonal antibody. Anal. Chem. 81, 6148-6155.
    • (2009) Anal. Chem. , vol.81 , pp. 6148-6155
    • Pristatsky, P.1    Cohen, S.L.2    Krantz, D.3
  • 117
    • 77958122499 scopus 로고    scopus 로고
    • Chemistry of the cysteine sensors in Kelch-like ECH-associated protein 1
    • Holland, R., and Fishbein, J. C. (2010) Chemistry of the cysteine sensors in Kelch-like ECH-associated protein 1. Antioxid. Redox Signaling 13, 1749-1761.
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 1749-1761
    • Holland, R.1    Fishbein, J.C.2
  • 118
    • 79960427057 scopus 로고    scopus 로고
    • Selective killing of cancer cells by a small molecule targeting the stress response to ROS
    • Raj, L., Ide, T., Gurkar, A. U., et al. (2011) Selective killing of cancer cells by a small molecule targeting the stress response to ROS. Nature 475, 231-234.
    • (2011) Nature , vol.475 , pp. 231-234
    • Raj, L.1    Ide, T.2    Gurkar, A.U.3
  • 119
    • 79959362325 scopus 로고    scopus 로고
    • The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer
    • Tew, K. D., Manevich, Y., Grek, C., et al. (2011) The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer. Free Radical Biol. Med. 51, 299-313.
    • (2011) Free Radical Biol. Med. , vol.51 , pp. 299-313
    • Tew, K.D.1    Manevich, Y.2    Grek, C.3
  • 121
    • 68949157225 scopus 로고    scopus 로고
    • Identification of conoidin a as a covalent inhibitor of peroxiredoxin II
    • Haraldsen, J. D., Liu, G., Botting, C. H., et al. (2009) Identification of conoidin a as a covalent inhibitor of peroxiredoxin II. Org. Biomol. Chem. 7, 3040-3048.
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 3040-3048
    • Haraldsen, J.D.1    Liu, G.2    Botting, C.H.3
  • 122
    • 58149492821 scopus 로고    scopus 로고
    • Determination of thiols and disulfides via HPLC quantification of 5-thio-2-nitrobenzoic acid
    • Chen, W., Zhao, Y., Seefeldt, T., et al. (2008) Determination of thiols and disulfides via HPLC quantification of 5-thio-2-nitrobenzoic acid. J. Pharm. Biomed. Anal. 48, 1375-1380.
    • (2008) J. Pharm. Biomed. Anal. , vol.48 , pp. 1375-1380
    • Chen, W.1    Zhao, Y.2    Seefeldt, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.