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Volumn 56, Issue 3, 2013, Pages 1301-1310

Selective inhibition of extracellular thioredoxin by asymmetric disulfides

Author keywords

[No Author keywords available]

Indexed keywords

1 METHYL 1 PROPYL 2 IMIDAZOLYL DISULFIDE; 2 (CYCLOHEXYLDISULFANYL) 1H BENZO[D]IMIDAZOLE; 2 (CYCLOHEXYLDISULFANYL) 5 ETHOXY 1H BENZO[D]IMIDAZOLE; 2 (CYCLOHEXYLDISULFANYL) 5 NITRO 1H BENZO[D]IMIDAZOLE; 2 (CYCLOHEXYLDISULFANYL)BENZO[D]OXAZOLE; 2 (CYCLOHEXYLDISULFANYL)BENZO[D]THIAZOLE; 2 (CYCLOPENTYLDISULFANYL) 1H BENZO[D]IMIDAZOLE; 2 (ETHYLDISULFANYL) 1H BENZO[D]IMIDAZOLE; 2 (ISOPROPYLDISULFANYL) 1H BENZO[D]IMIDAZOLE; 2 (SEC BUTYLDISULFANYL) 1H BENZO[D]IMIDAZOLE; 2 (SEC BUTYLDISULFANYL) 3H IMIDAZO[4,5 C]PYRIDINE; 2 (SEC BUTYLDISULFANYL) 5 NITRO 1H BENZO[D]IMIDAZOLE; 2 (SEC BUTYLDISULFANYL) 6 CHLORO 5 FLUORO 1H BENZO[D]IMIDAZOLE; 2 (SEC BUTYLDISULFANYL) 6 CHLOROBENZO[D]THIAZOLE; 2 (SEC BUTYLDISULFANYL) 6 FLUOROBENZO[D]THIAZOLE; 2 (SEC BUTYLDISULFANYL) 6 IODOBENZO[D]THIAZOLE; 2 (SEC BUTYLDISULFANYL) 6 NITROBENZO[D]THIAZOLE; 2 (SEC BUTYLDISULFANYL)BENZO[D]THIAZOLE; 2 (SEC BUTYLDISULFANYL)PYRIDINE; 2 (SEC BUTYLDISULFANYL)THIAZOLE; 2 (TERT BUTYLDISULFANYL) 1H BENZO[D]IMIDAZOLE; 4 BROMO 2 (SEC BUTYLDISULFANYL)BENZO[D]THIAZOLE; 5 BROMO 2 (SEC BUTYLDISULFANYL)BENZO[D]THIAZOLE; 6 CHLORO 2 (CYCLOHEXYLDISULFANYL) 5 FLUORO 1H BENZO[D]IMIDAZOLE; [2 (CYCLOHEXYLDISULFANYL) 1H BENZO[D]IMIDAZOL 6 YL](PHENYL)METHANONE; DISULFIDE; FIBRONECTIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; THIOREDOXIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84873917904     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm301775s     Document Type: Article
Times cited : (52)

References (37)
  • 1
    • 77952311188 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
    • Holmgren, A.; Lu, J. Thioredoxin and thioredoxin reductase: Current research with special reference to human disease Biochem. Biophys. Res. Commun. 2010, 396, 120-124
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 120-124
    • Holmgren, A.1    Lu, J.2
  • 2
    • 0242277285 scopus 로고    scopus 로고
    • The thioredoxin system-From science to clinic
    • Gromer, S.; Urig, S.; Becker, K. The thioredoxin system-From science to clinic Med. Res. Rev. 2004, 24, 40-89
    • (2004) Med. Res. Rev. , vol.24 , pp. 40-89
    • Gromer, S.1    Urig, S.2    Becker, K.3
  • 3
    • 33845428642 scopus 로고    scopus 로고
    • Thioredoxin and related molecules-From biology to health and disease
    • Lillig, C. H.; Holmgren, A. Thioredoxin and related molecules-From biology to health and disease Antioxid. Redox Signal. 2007, 9, 25-47
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 25-47
    • Lillig, C.H.1    Holmgren, A.2
  • 4
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • Rubartelli, A.; Bajetto, A.; Allavena, G.; Wollman, E.; Sitia, R. Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway J. Biol. Chem. 1992, 267, 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
  • 5
    • 0346690291 scopus 로고    scopus 로고
    • Thioredoxin as a key molecule in redox signaling
    • Nakamura, H. Thioredoxin as a key molecule in redox signaling Antioxid. Redox Signal. 2004, 6, 15-17
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 15-17
    • Nakamura, H.1
  • 7
    • 78650057571 scopus 로고    scopus 로고
    • Disulfide bond that constrains the HIV-1 gp120 V3 domain is cleaved by thioredoxin
    • Azimi, I.; Matthias, L. J.; Center, R. J.; Wong, J. W. H.; Hogg, P. J. Disulfide bond that constrains the HIV-1 gp120 V3 domain is cleaved by thioredoxin J. Biol. Chem. 2010, 285, 40072-40080
    • (2010) J. Biol. Chem. , vol.285 , pp. 40072-40080
    • Azimi, I.1    Matthias, L.J.2    Center, R.J.3    Wong, J.W.H.4    Hogg, P.J.5
  • 8
    • 57649149732 scopus 로고    scopus 로고
    • Identification of human thioredoxin as a novel IFN-gamma induced factor: Mechanism of induction and its role in cytokine production
    • Kim, S.; Oh, J.; Choi, J.; Jang, J.; Kang, M. Identification of human thioredoxin as a novel IFN-gamma induced factor: Mechanism of induction and its role in cytokine production BMC Immunol. 2008, 9, 1-15
    • (2008) BMC Immunol. , vol.9 , pp. 1-15
    • Kim, S.1    Oh, J.2    Choi, J.3    Jang, J.4    Kang, M.5
  • 11
    • 0032528813 scopus 로고    scopus 로고
    • Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity
    • van de Wal, Y.; Kooy, Y.; van Veelen, P.; Peña, S.; Mearin, L.; Papadopoulos, G.; Koning, F. Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity J. Immunol. 1998, 161, 1585-1588
    • (1998) J. Immunol. , vol.161 , pp. 1585-1588
    • Van De Wal, Y.1    Kooy, Y.2    Van Veelen, P.3    Peña, S.4    Mearin, L.5    Papadopoulos, G.6    Koning, F.7
  • 12
    • 46749147598 scopus 로고    scopus 로고
    • Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury
    • Siegel, M.; Strnad, P.; Watts, R. E.; Choi, K.; Jabri, B.; Omary, M. B.; Khosla, C. Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury PLoS ONE 2008, 3, e1861
    • (2008) PLoS ONE , vol.3 , pp. 1861
    • Siegel, M.1    Strnad, P.2    Watts, R.E.3    Choi, K.4    Jabri, B.5    Omary, M.B.6    Khosla, C.7
  • 13
    • 0028828948 scopus 로고
    • Gluten specific, HLA-DQ restricted T cells from coeliac mucosa produce cytokines with Th1 or Th0 profile dominated by interferon gamma
    • Nilsen, E. M.; Lundin, K. E.; Krajci, P.; Scott, H.; Sollid, L. M.; Brandtzaeg, P. Gluten specific, HLA-DQ restricted T cells from coeliac mucosa produce cytokines with Th1 or Th0 profile dominated by interferon gamma Gut 1995, 37, 766-776
    • (1995) Gut , vol.37 , pp. 766-776
    • Nilsen, E.M.1    Lundin, K.E.2    Krajci, P.3    Scott, H.4    Sollid, L.M.5    Brandtzaeg, P.6
  • 14
  • 16
    • 0031466528 scopus 로고    scopus 로고
    • Cell line-directed screening assay for inhibitors of thioredoxin reductase signaling as potential anti-cancer drugs
    • Kunkel, M. W.; Kirkpatrick, D. L.; Johnson, J. I.; Powis, G. Cell line-directed screening assay for inhibitors of thioredoxin reductase signaling as potential anti-cancer drugs Anticancer Drugs 1997, 12, 659-670
    • (1997) Anticancer Drugs , vol.12 , pp. 659-670
    • Kunkel, M.W.1    Kirkpatrick, D.L.2    Johnson, J.I.3    Powis, G.4
  • 18
    • 79953784421 scopus 로고    scopus 로고
    • A randomized phase II study of PX-12, an inhibitor of thioredoxin in patients with advanced cancer of the pancreas following progression after a gemcitabine-containing combination
    • Ramanathan, R. K.; Abbruzzese, J.; Dragovich, T.; Kirkpatrick, L.; Guillen, J. M.; Baker, A. F.; Pestano, L. A.; Green, S.; Hoff, D. D. A randomized phase II study of PX-12, an inhibitor of thioredoxin in patients with advanced cancer of the pancreas following progression after a gemcitabine-containing combination Cancer Chemother. Pharmacol. 2011, 67, 503-509
    • (2011) Cancer Chemother. Pharmacol. , vol.67 , pp. 503-509
    • Ramanathan, R.K.1    Abbruzzese, J.2    Dragovich, T.3    Kirkpatrick, L.4    Guillen, J.M.5    Baker, A.F.6    Pestano, L.A.7    Green, S.8    Hoff, D.D.9
  • 20
    • 84858643071 scopus 로고    scopus 로고
    • Interferon-γ activates transglutaminase 2 via a phosphatidylinositol-3-kinase-dependent pathway: Implications for celiac sprue therapy
    • Diraimondo, T. R.; Klöck, C.; Khosla, C. Interferon-γ activates transglutaminase 2 via a phosphatidylinositol-3-kinase-dependent pathway: Implications for celiac sprue therapy J. Pharmacol. Exp. Ther. 2012, 341, 104-114
    • (2012) J. Pharmacol. Exp. Ther. , vol.341 , pp. 104-114
    • Diraimondo, T.R.1    Klöck, C.2    Khosla, C.3
  • 21
    • 33845501601 scopus 로고    scopus 로고
    • Structure-activity relationship analysis of the selective inhibition of transglutaminase 2 by dihydroisoxazoles
    • Watts, R. E.; Siegel, M.; Khosla, C. Structure-activity relationship analysis of the selective inhibition of transglutaminase 2 by dihydroisoxazoles J. Med. Chem. 2006, 49, 7493-7501
    • (2006) J. Med. Chem. , vol.49 , pp. 7493-7501
    • Watts, R.E.1    Siegel, M.2    Khosla, C.3
  • 22
    • 0001494424 scopus 로고
    • Structure-reactivity correlations for the thiol-disulfide interchange reaction
    • Wilson, J.; Bayer, R.; Hupe, D. Structure-reactivity correlations for the thiol-disulfide interchange reaction J. Am. Chem. Soc. 1977, 99, 7922-7926
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 7922-7926
    • Wilson, J.1    Bayer, R.2    Hupe, D.3
  • 23
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione
    • Szajewski, R.; Whitesides, G. Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione J. Am. Chem. Soc. 1980, 102, 2011-2026
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2011-2026
    • Szajewski, R.1    Whitesides, G.2
  • 24
    • 33845283266 scopus 로고
    • Structure-reactivity relations for thiol-disulfide interchange
    • Houk, J.; Whitesides, G. Structure-reactivity relations for thiol-disulfide interchange J. Am. Chem. Soc. 1987, 109, 6825-6836
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6825-6836
    • Houk, J.1    Whitesides, G.2
  • 25
    • 0347719283 scopus 로고    scopus 로고
    • Theoretical insights into the mechanism for thiol/disulfide exchange
    • Fernandes, P. A.; Ramos, M. J. Theoretical insights into the mechanism for thiol/disulfide exchange Chemistry 2004, 10, 257-266
    • (2004) Chemistry , vol.10 , pp. 257-266
    • Fernandes, P.A.1    Ramos, M.J.2
  • 28
    • 0025865875 scopus 로고
    • Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis
    • Krause, G.; Holmgren, A. Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis J. Biol. Chem. 1991, 266, 4056-4066
    • (1991) J. Biol. Chem. , vol.266 , pp. 4056-4066
    • Krause, G.1    Holmgren, A.2
  • 30
    • 84870359579 scopus 로고    scopus 로고
    • Regulation of the activities of the mammalian transglutaminase family of enzymes
    • Klöck, C.; Khosla, C. Regulation of the activities of the mammalian transglutaminase family of enzymes Protein Sci. 2012, 21, 1781-1791
    • (2012) Protein Sci. , vol.21 , pp. 1781-1791
    • Klöck, C.1    Khosla, C.2
  • 32
    • 82955250010 scopus 로고    scopus 로고
    • Celiac disease and transglutaminase 2: A model for posttranslational modification of antigens and HLA association in the pathogenesis of autoimmune disorders
    • Sollid, L. M.; Jabri, B. Celiac disease and transglutaminase 2: A model for posttranslational modification of antigens and HLA association in the pathogenesis of autoimmune disorders Curr. Opin. Immunol. 2011, 23, 732-738
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 732-738
    • Sollid, L.M.1    Jabri, B.2
  • 33
    • 0026602786 scopus 로고
    • Synthesis and evaluation of imidazolyl disulfides for selective cytotoxicity to hypoxic EMT6 tumor cells in vitro
    • Kirkpatrick, D.; Jimale, M.; King, K.; Chen, T. Synthesis and evaluation of imidazolyl disulfides for selective cytotoxicity to hypoxic EMT6 tumor cells in vitro Eur. J. Med. Chem. 1992, 27, 33-37
    • (1992) Eur. J. Med. Chem. , vol.27 , pp. 33-37
    • Kirkpatrick, D.1    Jimale, M.2    King, K.3    Chen, T.4
  • 34
    • 77249179133 scopus 로고    scopus 로고
    • Selective benzimidazole inhibitors of the antigen receptor-mediated NF-κB activation pathway
    • Okolotowicz, K. J.; Shi, R.; Zheng, X.; MacDonald, M.; Reed, J. C.; Cashman, J. R. Selective benzimidazole inhibitors of the antigen receptor-mediated NF-κB activation pathway Bioorg. Med. Chem. 2010, 18, 1918-1924
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 1918-1924
    • Okolotowicz, K.J.1    Shi, R.2    Zheng, X.3    MacDonald, M.4    Reed, J.C.5    Cashman, J.R.6
  • 35
    • 0006895581 scopus 로고    scopus 로고
    • Measurement of thioredoxin and thioredoxin reductase
    • Arnér, E. S.; Holmgren, A. Measurement of thioredoxin and thioredoxin reductase Curr. Protoc. Toxicol. 2001, 24, 7.4.1-7.4.14
    • (2001) Curr. Protoc. Toxicol. , vol.24 , pp. 741-7414
    • Arnér, E.S.1    Holmgren, A.2
  • 36
    • 79960029361 scopus 로고    scopus 로고
    • SwissDock, a protein-small molecule docking web service based on EADock DSS
    • Grosdidier, A.; Zoete, V.; Michielin, O. SwissDock, a protein-small molecule docking web service based on EADock DSS Nucleic Acids Res. 2011, 39, W270-W277
    • (2011) Nucleic Acids Res. , vol.39
    • Grosdidier, A.1    Zoete, V.2    Michielin, O.3


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