메뉴 건너뛰기




Volumn 75, Issue 3, 2012, Pages 740-755

Effects of nitric oxide synthase-3 overexpression on post-translational modifications and cell survival in HepG2 cells

Author keywords

Carbonylation; Hepatocarcinoma; Nitration; Nitrosylation; Oxidative stress

Indexed keywords

CHAPERONE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SERINE PROTEINASE INHIBITOR;

EID: 84355162136     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.09.010     Document Type: Article
Times cited : (12)

References (87)
  • 2
    • 63449139593 scopus 로고    scopus 로고
    • Two decades of new concepts in nitric oxide signaling: from the discovery of a gas messenger to the mediation of nonenzymatic posttranslational modifications
    • Martinez-Ruiz A., Lamas S. Two decades of new concepts in nitric oxide signaling: from the discovery of a gas messenger to the mediation of nonenzymatic posttranslational modifications. IUBMB Life 2009, 61:91-98.
    • (2009) IUBMB Life , vol.61 , pp. 91-98
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 3
    • 47249122504 scopus 로고    scopus 로고
    • Post-translational modifications induced by nitric oxide (NO): implication in cancer cells apoptosis
    • Leon L., Jeannin J.F., Bettaieb A. Post-translational modifications induced by nitric oxide (NO): implication in cancer cells apoptosis. Nitric Oxide 2008, 19:77-83.
    • (2008) Nitric Oxide , vol.19 , pp. 77-83
    • Leon, L.1    Jeannin, J.F.2    Bettaieb, A.3
  • 4
    • 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., Stamler J.S. Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. J Biol Chem 2002, 277:9637-9640.
    • (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
  • 5
    • 12444296480 scopus 로고    scopus 로고
    • Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics
    • Dalle-Donne I., Scaloni A., Giustarini D., Cavarra E., Tell G., Lungarella G., et al. Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics. Mass Spectrom Rev 2005, 24:55-99.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 55-99
    • Dalle-Donne, I.1    Scaloni, A.2    Giustarini, D.3    Cavarra, E.4    Tell, G.5    Lungarella, G.6
  • 6
    • 46649090918 scopus 로고    scopus 로고
    • Protein tyrosine nitration - functional alteration or just a biomarker?
    • Souza J.M., Peluffo G., Radi R. Protein tyrosine nitration - functional alteration or just a biomarker?. Free Radic Biol Med 2008, 45:357-366.
    • (2008) Free Radic Biol Med , vol.45 , pp. 357-366
    • Souza, J.M.1    Peluffo, G.2    Radi, R.3
  • 8
    • 75149170936 scopus 로고    scopus 로고
    • Cell signaling by protein carbonylation and decarbonylation
    • Wong C.M., Marcocci L., Liu L., Suzuki Y.J. Cell signaling by protein carbonylation and decarbonylation. Antioxid Redox Signal 2010, 12:393-404.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 393-404
    • Wong, C.M.1    Marcocci, L.2    Liu, L.3    Suzuki, Y.J.4
  • 10
    • 0036244305 scopus 로고    scopus 로고
    • Nitric oxide and cell signaling pathways in mitochondrial-dependent apoptosis
    • Boyd C.S., Cadenas E. Nitric oxide and cell signaling pathways in mitochondrial-dependent apoptosis. Biol Chem 2002, 383:411-423.
    • (2002) Biol Chem , vol.383 , pp. 411-423
    • Boyd, C.S.1    Cadenas, E.2
  • 12
    • 14344258352 scopus 로고    scopus 로고
    • Expression of endothelial nitric oxide synthase and vascular endothelial growth factor in oral squamous cell carcinoma: its correlation with angiogenesis and disease progression
    • Shang Z.J., Li J.R. Expression of endothelial nitric oxide synthase and vascular endothelial growth factor in oral squamous cell carcinoma: its correlation with angiogenesis and disease progression. J Oral Pathol Med 2005, 34:134-139.
    • (2005) J Oral Pathol Med , vol.34 , pp. 134-139
    • Shang, Z.J.1    Li, J.R.2
  • 13
    • 0028929559 scopus 로고
    • Transfection with the inducible nitric oxide synthase gene suppresses tumorigenicity and abrogates metastasis by K-1735 murine melanoma cells
    • Xie K., Huang S., Dong Z., Juang S.H., Gutman M., Xie Q.W., et al. Transfection with the inducible nitric oxide synthase gene suppresses tumorigenicity and abrogates metastasis by K-1735 murine melanoma cells. J Exp Med 1995, 181:1333-1343.
    • (1995) J Exp Med , vol.181 , pp. 1333-1343
    • Xie, K.1    Huang, S.2    Dong, Z.3    Juang, S.H.4    Gutman, M.5    Xie, Q.W.6
  • 14
    • 0031904144 scopus 로고    scopus 로고
    • Effects of endothelial nitric oxide synthase gene expression on the tumor biology of human oral carcinoma SCC-25 cells
    • Liu R., Oberley T.D., Oberley L.W. Effects of endothelial nitric oxide synthase gene expression on the tumor biology of human oral carcinoma SCC-25 cells. Cell Growth Differ 1998, 9:239-246.
    • (1998) Cell Growth Differ , vol.9 , pp. 239-246
    • Liu, R.1    Oberley, T.D.2    Oberley, L.W.3
  • 15
    • 9944227667 scopus 로고    scopus 로고
    • ENOS, nNOS, cGMP and protein kinase G mediate the inhibitory effect of pancreastatin, a chromogranin A-derived peptide, on growth and proliferation of hepatoma cells
    • Diaz-Troya S., Najib S., Sanchez-Margalet V. eNOS, nNOS, cGMP and protein kinase G mediate the inhibitory effect of pancreastatin, a chromogranin A-derived peptide, on growth and proliferation of hepatoma cells. Regul Pept 2005, 125:41-46.
    • (2005) Regul Pept , vol.125 , pp. 41-46
    • Diaz-Troya, S.1    Najib, S.2    Sanchez-Margalet, V.3
  • 16
    • 47049091866 scopus 로고    scopus 로고
    • NO-donating NSAIDs and cancer: an overview with a note on whether NO is required for their action
    • Rigas B., Williams J.L. NO-donating NSAIDs and cancer: an overview with a note on whether NO is required for their action. Nitric Oxide 2008, 19:199-204.
    • (2008) Nitric Oxide , vol.19 , pp. 199-204
    • Rigas, B.1    Williams, J.L.2
  • 18
    • 67650702584 scopus 로고    scopus 로고
    • N-acetylcysteine, coenzyme Q10 and superoxide dismutase mimetic prevent mitochondrial cell dysfunction and cell death induced by d-galactosamine in primary culture of human hepatocytes
    • Gonzalez R., Ferrin G., Hidalgo A.B., Ranchal I., Lopez-Cillero P., Santos-Gonzalez M., et al. N-acetylcysteine, coenzyme Q10 and superoxide dismutase mimetic prevent mitochondrial cell dysfunction and cell death induced by d-galactosamine in primary culture of human hepatocytes. Chem Biol Interact 2009, 181:95-106.
    • (2009) Chem Biol Interact , vol.181 , pp. 95-106
    • Gonzalez, R.1    Ferrin, G.2    Hidalgo, A.B.3    Ranchal, I.4    Lopez-Cillero, P.5    Santos-Gonzalez, M.6
  • 19
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues
    • Tietze F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem 1969, 27:502-522.
    • (1969) Anal Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 20
    • 0025776627 scopus 로고
    • Preparative steps necessary for the accurate measurement of malondialdehyde by high-performance liquid chromatography
    • Lepage G., Munoz G., Champagne J., Roy C.C. Preparative steps necessary for the accurate measurement of malondialdehyde by high-performance liquid chromatography. Anal Biochem 1991, 197:277-283.
    • (1991) Anal Biochem , vol.197 , pp. 277-283
    • Lepage, G.1    Munoz, G.2    Champagne, J.3    Roy, C.C.4
  • 21
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • 2001:p.pl1.
    • Jaffrey S.R., Snyder S.H. The biotin switch method for the detection of S-nitrosylated proteins. Sci STKE 2001, 2001:p.pl1.
    • (2001) Sci STKE
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 22
    • 0033539683 scopus 로고    scopus 로고
    • Requirements for heme and thiols for the nonenzymatic modification of nitrotyrosine
    • Balabanli B., Kamisaki Y., Martin E., Murad F. Requirements for heme and thiols for the nonenzymatic modification of nitrotyrosine. Proc Natl Acad Sci U S A 1999, 96:13136-13141.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13136-13141
    • Balabanli, B.1    Kamisaki, Y.2    Martin, E.3    Murad, F.4
  • 23
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A., Aksenov M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R., et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 2002, 82:1524-1532.
    • (2002) J Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6
  • 24
    • 66749144065 scopus 로고    scopus 로고
    • Nitroproteomics of peripheral blood mononuclear cells from patients and a rat model of ALS
    • Nardo G., Pozzi S., Mantovani S., Garbelli S., Marinou K., Basso M., et al. Nitroproteomics of peripheral blood mononuclear cells from patients and a rat model of ALS. Antioxid Redox Signal 2009, 11:1559-1567.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1559-1567
    • Nardo, G.1    Pozzi, S.2    Mantovani, S.3    Garbelli, S.4    Marinou, K.5    Basso, M.6
  • 25
    • 23844458044 scopus 로고    scopus 로고
    • Inhibition of chaperone activity is a shared property of several Cu, Zn-superoxide dismutase mutants that cause amyotrophic lateral sclerosis
    • Tummala H., Jung C., Tiwari A., Higgins C.M., Hayward L.J., Xu Z. Inhibition of chaperone activity is a shared property of several Cu, Zn-superoxide dismutase mutants that cause amyotrophic lateral sclerosis. J Biol Chem 2005, 280:17725-17731.
    • (2005) J Biol Chem , vol.280 , pp. 17725-17731
    • Tummala, H.1    Jung, C.2    Tiwari, A.3    Higgins, C.M.4    Hayward, L.J.5    Xu, Z.6
  • 27
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine R.L., Williams J.A., Stadtman E.R., Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol 1994, 233:346-357.
    • (1994) Methods Enzymol , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 28
    • 0029682870 scopus 로고    scopus 로고
    • Oxidative damage and tyrosine nitration from peroxynitrite
    • Beckman J.S. Oxidative damage and tyrosine nitration from peroxynitrite. Chem Res Toxicol 1996, 9:836-844.
    • (1996) Chem Res Toxicol , vol.9 , pp. 836-844
    • Beckman, J.S.1
  • 29
    • 0038731081 scopus 로고    scopus 로고
    • Biological selectivity and functional aspects of protein tyrosine nitration
    • Ischiropoulos H. Biological selectivity and functional aspects of protein tyrosine nitration. Biochem Biophys Res Commun 2003, 305:776-783.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 776-783
    • Ischiropoulos, H.1
  • 31
    • 18144398928 scopus 로고    scopus 로고
    • Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: possible multifunctional role in the pathogenesis
    • Casoni F., Basso M., Massignan T., Gianazza E., Cheroni C., Salmona M., et al. Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: possible multifunctional role in the pathogenesis. J Biol Chem 2005, 280:16295-16304.
    • (2005) J Biol Chem , vol.280 , pp. 16295-16304
    • Casoni, F.1    Basso, M.2    Massignan, T.3    Gianazza, E.4    Cheroni, C.5    Salmona, M.6
  • 32
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal M.F. Oxidatively modified proteins in aging and disease. Free Radic Biol Med 2002, 32:797-803.
    • (2002) Free Radic Biol Med , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 33
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction
    • Greenacre S.A., Ischiropoulos H. Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction. Free Radic Res 2001, 34:541-581.
    • (2001) Free Radic Res , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 34
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos H. Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch Biochem Biophys 1998, 356:1-11.
    • (1998) Arch Biochem Biophys , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 35
    • 0034769477 scopus 로고    scopus 로고
    • Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway
    • Shang F., Nowell T.R., Taylor A. Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway. Exp Eye Res 2001, 73:229-238.
    • (2001) Exp Eye Res , vol.73 , pp. 229-238
    • Shang, F.1    Nowell, T.R.2    Taylor, A.3
  • 36
    • 79952036205 scopus 로고    scopus 로고
    • Protein misfolding and cellular stress: an overview
    • Gregersen N., Bross P. Protein misfolding and cellular stress: an overview. Methods Mol Biol 2010, 648:3-23.
    • (2010) Methods Mol Biol , vol.648 , pp. 3-23
    • Gregersen, N.1    Bross, P.2
  • 37
    • 78650338184 scopus 로고    scopus 로고
    • The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?
    • McLaughlin M., Vandenbroeck K. The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?. Br J Pharmacol 2011, 162:328-345.
    • (2011) Br J Pharmacol , vol.162 , pp. 328-345
    • McLaughlin, M.1    Vandenbroeck, K.2
  • 38
    • 4344604345 scopus 로고    scopus 로고
    • Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: a cell biochemical and proteomic investigation
    • Magi B., Ettorre A., Liberatori S., Bini L., Andreassi M., Frosali S., et al. Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: a cell biochemical and proteomic investigation. Cell Death Differ 2004, 11:842-852.
    • (2004) Cell Death Differ , vol.11 , pp. 842-852
    • Magi, B.1    Ettorre, A.2    Liberatori, S.3    Bini, L.4    Andreassi, M.5    Frosali, S.6
  • 39
    • 0032080377 scopus 로고    scopus 로고
    • Involvement of nitric oxide during phthalocyanine (Pc4) photodynamic therapy-mediated apoptosis
    • Gupta S., Ahmad N., Mukhtar H. Involvement of nitric oxide during phthalocyanine (Pc4) photodynamic therapy-mediated apoptosis. Cancer Res 1998, 58:1785-1788.
    • (1998) Cancer Res , vol.58 , pp. 1785-1788
    • Gupta, S.1    Ahmad, N.2    Mukhtar, H.3
  • 40
    • 56149106877 scopus 로고    scopus 로고
    • Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy
    • Cappello F., Conway de Macario E., Marasa L., Zummo G., Macario AJ. Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy. Cancer Biol Ther 2008, 7:801-809.
    • (2008) Cancer Biol Ther , vol.7 , pp. 801-809
    • Cappello, F.1    Conway de Macario, E.2    Marasa, L.3    Zummo, G.4    Macario, A.J.5
  • 41
    • 23744443565 scopus 로고    scopus 로고
    • Current progress in proteomic study of hepatitis C virus-related human hepatocellular carcinoma
    • Kuramitsu Y., Nakamura K. Current progress in proteomic study of hepatitis C virus-related human hepatocellular carcinoma. Expert Rev Proteomics 2005, 2:589-601.
    • (2005) Expert Rev Proteomics , vol.2 , pp. 589-601
    • Kuramitsu, Y.1    Nakamura, K.2
  • 42
    • 3843151554 scopus 로고    scopus 로고
    • Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction
    • Reverter-Branchat G., Cabiscol E., Tamarit J., Ros J. Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction. J Biol Chem 2004, 279:31983-31989.
    • (2004) J Biol Chem , vol.279 , pp. 31983-31989
    • Reverter-Branchat, G.1    Cabiscol, E.2    Tamarit, J.3    Ros, J.4
  • 44
    • 11144349225 scopus 로고    scopus 로고
    • Mortalin is over-expressed by colorectal adenocarcinomas and correlates with poor survival
    • Dundas S.R., Lawrie L.C., Rooney P.H., Murray G.I. Mortalin is over-expressed by colorectal adenocarcinomas and correlates with poor survival. J Pathol 2005, 205:74-81.
    • (2005) J Pathol , vol.205 , pp. 74-81
    • Dundas, S.R.1    Lawrie, L.C.2    Rooney, P.H.3    Murray, G.I.4
  • 46
    • 39749200037 scopus 로고    scopus 로고
    • Association of mortalin (HSPA9) with liver cancer metastasis and prediction for early tumor recurrence
    • Yi X., Luk J.M., Lee N.P., Peng J., Leng X., Guan X.Y., et al. Association of mortalin (HSPA9) with liver cancer metastasis and prediction for early tumor recurrence. Mol Cell Proteomics 2008, 7:315-325.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 315-325
    • Yi, X.1    Luk, J.M.2    Lee, N.P.3    Peng, J.4    Leng, X.5    Guan, X.Y.6
  • 47
    • 0032491426 scopus 로고    scopus 로고
    • Inactivation of tumor suppressor p53 by mot-2, a hsp70 family member
    • Wadhwa R., Takano S., Robert M., Yoshida A., Nomura H., Reddel R.R., et al. Inactivation of tumor suppressor p53 by mot-2, a hsp70 family member. J Biol Chem 1998, 273:29586-29591.
    • (1998) J Biol Chem , vol.273 , pp. 29586-29591
    • Wadhwa, R.1    Takano, S.2    Robert, M.3    Yoshida, A.4    Nomura, H.5    Reddel, R.R.6
  • 48
    • 0036346345 scopus 로고    scopus 로고
    • Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein
    • Wadhwa R., Yaguchi T., Hasan M.K., Mitsui Y., Reddel R.R., Kaul S.C. Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein. Exp Cell Res 2002, 274:246-253.
    • (2002) Exp Cell Res , vol.274 , pp. 246-253
    • Wadhwa, R.1    Yaguchi, T.2    Hasan, M.K.3    Mitsui, Y.4    Reddel, R.R.5    Kaul, S.C.6
  • 49
    • 70349970651 scopus 로고    scopus 로고
    • S-nitrosoproteome in endothelial cells revealed by a modified biotin switch approach coupled with Western blot-based two-dimensional gel electrophoresis
    • Huang B., Liao C.L., Lin Y.P., Chen S.C., Wang D.L. S-nitrosoproteome in endothelial cells revealed by a modified biotin switch approach coupled with Western blot-based two-dimensional gel electrophoresis. J Proteome Res 2009, 8:4835-4843.
    • (2009) J Proteome Res , vol.8 , pp. 4835-4843
    • Huang, B.1    Liao, C.L.2    Lin, Y.P.3    Chen, S.C.4    Wang, D.L.5
  • 51
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M.J., Sambrook J. Protein folding in the cell. Nature 1992, 355:33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 52
    • 0345624495 scopus 로고    scopus 로고
    • Two-dimensional gel analysis of human endometrial proteins: characterization of proteins with increased expression in hyperplasia and adenocarcinoma
    • Byrjalsen I., Mose Larsen P., Fey S.J., Nilas L., Larsen M.R., Christiansen C. Two-dimensional gel analysis of human endometrial proteins: characterization of proteins with increased expression in hyperplasia and adenocarcinoma. Mol Hum Reprod 1999, 5:748-756.
    • (1999) Mol Hum Reprod , vol.5 , pp. 748-756
    • Byrjalsen, I.1    Mose Larsen, P.2    Fey, S.J.3    Nilas, L.4    Larsen, M.R.5    Christiansen, C.6
  • 53
    • 3042646339 scopus 로고    scopus 로고
    • Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria
    • Koeck T., Fu X., Hazen S.L., Crabb J.W., Stuehr D.J., Aulak K.S. Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria. J Biol Chem 2004, 279:27257-27262.
    • (2004) J Biol Chem , vol.279 , pp. 27257-27262
    • Koeck, T.1    Fu, X.2    Hazen, S.L.3    Crabb, J.W.4    Stuehr, D.J.5    Aulak, K.S.6
  • 54
    • 0037105336 scopus 로고    scopus 로고
    • Signal transduction by protein tyrosine nitration: competition or cooperation with tyrosine phosphorylation-dependent signaling events?
    • Monteiro H.P. Signal transduction by protein tyrosine nitration: competition or cooperation with tyrosine phosphorylation-dependent signaling events?. Free Radic Biol Med 2002, 33:765-773.
    • (2002) Free Radic Biol Med , vol.33 , pp. 765-773
    • Monteiro, H.P.1
  • 55
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., et al. Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 2007, 131:1190-1203.
    • (2007) Cell , vol.131 , pp. 1190-1203
    • Rikova, K.1    Guo, A.2    Zeng, Q.3    Possemato, A.4    Yu, J.5    Haack, H.6
  • 56
    • 69549096143 scopus 로고    scopus 로고
    • Cell biology of the movement of breast cancer cells: intracellular signalling and the actin cytoskeleton
    • Jiang P., Enomoto A., Takahashi M. Cell biology of the movement of breast cancer cells: intracellular signalling and the actin cytoskeleton. Cancer Lett 2009, 284:122-130.
    • (2009) Cancer Lett , vol.284 , pp. 122-130
    • Jiang, P.1    Enomoto, A.2    Takahashi, M.3
  • 57
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins P.G. Serpin structure, mechanism, and function. Chem Rev 2002, 102:4751-4804.
    • (2002) Chem Rev , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 58
    • 0017762441 scopus 로고
    • Radioimmunoassay for tumor antigen of human cervical squamous cell carcinoma
    • Kato H., Torigoe T. Radioimmunoassay for tumor antigen of human cervical squamous cell carcinoma. Cancer 1977, 40:1621-1628.
    • (1977) Cancer , vol.40 , pp. 1621-1628
    • Kato, H.1    Torigoe, T.2
  • 59
    • 12144286943 scopus 로고    scopus 로고
    • Overexpression of squamous cell carcinoma antigen variants in hepatocellular carcinoma
    • Pontisso P., Calabrese F., Benvegnu L., Lise M., Belluco C., Ruvoletto M.G., et al. Overexpression of squamous cell carcinoma antigen variants in hepatocellular carcinoma. Br J Cancer 2004, 90:833-837.
    • (2004) Br J Cancer , vol.90 , pp. 833-837
    • Pontisso, P.1    Calabrese, F.2    Benvegnu, L.3    Lise, M.4    Belluco, C.5    Ruvoletto, M.G.6
  • 60
    • 23244459646 scopus 로고    scopus 로고
    • Clinical role of tissue and serum levels of SCCA antigen in hepatocellular carcinoma
    • Giannelli G., Marinosci F., Sgarra C., Lupo L., Dentico P., Antonaci S. Clinical role of tissue and serum levels of SCCA antigen in hepatocellular carcinoma. Int J Cancer 2005, 116:579-583.
    • (2005) Int J Cancer , vol.116 , pp. 579-583
    • Giannelli, G.1    Marinosci, F.2    Sgarra, C.3    Lupo, L.4    Dentico, P.5    Antonaci, S.6
  • 62
    • 70549100926 scopus 로고    scopus 로고
    • Role of squamous cell carcinoma antigen-1 on liver cells after partial hepatectomy in transgenic mice
    • Villano G., Quarta S., Ruvoletto M.G., Turato C., Vidalino L., Biasiolo A., et al. Role of squamous cell carcinoma antigen-1 on liver cells after partial hepatectomy in transgenic mice. Int J Mol Med 2010, 25:137-143.
    • (2010) Int J Mol Med , vol.25 , pp. 137-143
    • Villano, G.1    Quarta, S.2    Ruvoletto, M.G.3    Turato, C.4    Vidalino, L.5    Biasiolo, A.6
  • 64
    • 46249128955 scopus 로고    scopus 로고
    • S-nitrosation and thiol switching in the mitochondrion: a new paradigm for cardioprotection in ischaemic preconditioning
    • Hill B.G., Darley-Usmar V.M. S-nitrosation and thiol switching in the mitochondrion: a new paradigm for cardioprotection in ischaemic preconditioning. Biochem J 2008, 412:e11-e13.
    • (2008) Biochem J , vol.412
    • Hill, B.G.1    Darley-Usmar, V.M.2
  • 65
    • 33845327490 scopus 로고    scopus 로고
    • Nitric oxide regulation of mitochondrial oxygen consumption I: cellular physiology
    • Giulivi C., Kato K., Cooper C.E. Nitric oxide regulation of mitochondrial oxygen consumption I: cellular physiology. Am J Physiol Cell Physiol 2006, 291:C1225-C1231.
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Giulivi, C.1    Kato, K.2    Cooper, C.E.3
  • 66
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • Souza J.M., Giasson B.I., Chen Q., Lee V.M., Ischiropoulos H. Dityrosine cross-linking promotes formation of stable alpha-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J Biol Chem 2000, 275:18344-18349.
    • (2000) J Biol Chem , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 67
    • 33646144212 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease
    • Butterfield D.A., Poon H.F., St Clair D., Keller J.N., Pierce W.M., Klein J.B., et al. Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: insights into the development of Alzheimer's disease. Neurobiol Dis 2006, 22:223-232.
    • (2006) Neurobiol Dis , vol.22 , pp. 223-232
    • Butterfield, D.A.1    Poon, H.F.2    St Clair, D.3    Keller, J.N.4    Pierce, W.M.5    Klein, J.B.6
  • 68
    • 75149140183 scopus 로고    scopus 로고
    • Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid
    • Chavez J., Chung W.G., Miranda C.L., Singhal M., Stevens J.F., Maier C.S. Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid. Chem Res Toxicol 2010, 23:37-47.
    • (2010) Chem Res Toxicol , vol.23 , pp. 37-47
    • Chavez, J.1    Chung, W.G.2    Miranda, C.L.3    Singhal, M.4    Stevens, J.F.5    Maier, C.S.6
  • 69
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A., Aksenov M., Aksenova M., Thongboonkerd V., Klein J.B., Pierce W.M., et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic Biol Med 2002, 33:562-571.
    • (2002) Free Radic Biol Med , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6
  • 70
    • 37749052671 scopus 로고    scopus 로고
    • Glycolitic enzymes are targets of oxidation in aged human frontal cortex and oxidative damage of these proteins is increased in progressive supranuclear palsy
    • Martinez A., Dalfo E., Muntane G., Ferrer I. Glycolitic enzymes are targets of oxidation in aged human frontal cortex and oxidative damage of these proteins is increased in progressive supranuclear palsy. J Neural Transm 2008, 115:59-66.
    • (2008) J Neural Transm , vol.115 , pp. 59-66
    • Martinez, A.1    Dalfo, E.2    Muntane, G.3    Ferrer, I.4
  • 71
    • 33751003258 scopus 로고    scopus 로고
    • Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats
    • Moon K.H., Hood B.L., Kim B.J., Hardwick J.P., Conrads T.P., Veenstra T.D., et al. Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats. Hepatology 2006, 44:1218-1230.
    • (2006) Hepatology , vol.44 , pp. 1218-1230
    • Moon, K.H.1    Hood, B.L.2    Kim, B.J.3    Hardwick, J.P.4    Conrads, T.P.5    Veenstra, T.D.6
  • 73
    • 0027265259 scopus 로고
    • Biochemical factors in alcoholic liver disease
    • Lieber C.S. Biochemical factors in alcoholic liver disease. Semin Liver Dis 1993, 13:136-153.
    • (1993) Semin Liver Dis , vol.13 , pp. 136-153
    • Lieber, C.S.1
  • 74
    • 0029146749 scopus 로고
    • Characterisation of a novel enzyme of human fatty acid beta-oxidation: a matrix-associated, mitochondrial 2-enoyl-CoA hydratase
    • Jackson S., Schaefer J., Middleton B., Turnbull D.M. Characterisation of a novel enzyme of human fatty acid beta-oxidation: a matrix-associated, mitochondrial 2-enoyl-CoA hydratase. Biochem Biophys Res Commun 1995, 214:247-253.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 247-253
    • Jackson, S.1    Schaefer, J.2    Middleton, B.3    Turnbull, D.M.4
  • 75
    • 0031569376 scopus 로고    scopus 로고
    • Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3
    • Janssen U., Davis E.M., Le Beau M.M., Stoffel W. Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3. Genomics 1997, 40:470-475.
    • (1997) Genomics , vol.40 , pp. 470-475
    • Janssen, U.1    Davis, E.M.2    Le Beau, M.M.3    Stoffel, W.4
  • 76
    • 33644654215 scopus 로고    scopus 로고
    • Fatty acid metabolism pathway play an important role in carcinogenesis of human colorectal cancers by Microarray-Bioinformatics analysis
    • Yeh C.S., Wang J.Y., Cheng T.L., Juan C.H., Wu C.H., Lin S.R. Fatty acid metabolism pathway play an important role in carcinogenesis of human colorectal cancers by Microarray-Bioinformatics analysis. Cancer Lett 2006, 233:297-308.
    • (2006) Cancer Lett , vol.233 , pp. 297-308
    • Yeh, C.S.1    Wang, J.Y.2    Cheng, T.L.3    Juan, C.H.4    Wu, C.H.5    Lin, S.R.6
  • 78
    • 80052589230 scopus 로고    scopus 로고
    • Oxidative modifications of proteins by sodium arsenite in human umbilical vein endothelial cells
    • Lii C.K., Lin A.H., Lee S.L., Chen H.W., Wang T.S. Oxidative modifications of proteins by sodium arsenite in human umbilical vein endothelial cells. Environ Toxicol 2011, 26:459-471.
    • (2011) Environ Toxicol , vol.26 , pp. 459-471
    • Lii, C.K.1    Lin, A.H.2    Lee, S.L.3    Chen, H.W.4    Wang, T.S.5
  • 80
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver J.D., van der Wal F.J., Bulleid N.J., High S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 1997, 275:86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 81
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo J.J., Parodi A.J. Getting in and out from calnexin/calreticulin cycles. J Biol Chem 2008, 283:10221-10225.
    • (2008) J Biol Chem , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 82
    • 33744961082 scopus 로고    scopus 로고
    • Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules
    • Zhang Y., Baig E., Williams D.B. Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules. J Biol Chem 2006, 281:14622-14631.
    • (2006) J Biol Chem , vol.281 , pp. 14622-14631
    • Zhang, Y.1    Baig, E.2    Williams, D.B.3
  • 83
    • 33846044754 scopus 로고    scopus 로고
    • Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes
    • Garbi N., Hammerling G., Tanaka S. Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes. Curr Opin Immunol 2007, 19:99-105.
    • (2007) Curr Opin Immunol , vol.19 , pp. 99-105
    • Garbi, N.1    Hammerling, G.2    Tanaka, S.3
  • 84
    • 40949151469 scopus 로고    scopus 로고
    • Combining the antigen processing components TAP and Tapasin elicits enhanced tumor-free survival
    • Lou Y., Basha G., Seipp R.P., Cai B., Chen S.S., Moise A.R., et al. Combining the antigen processing components TAP and Tapasin elicits enhanced tumor-free survival. Clin Cancer Res 2008, 14:1494-1501.
    • (2008) Clin Cancer Res , vol.14 , pp. 1494-1501
    • Lou, Y.1    Basha, G.2    Seipp, R.P.3    Cai, B.4    Chen, S.S.5    Moise, A.R.6
  • 85
    • 0034666290 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
    • Chen J.W., Dodia C., Feinstein S.I., Jain M.K., Fisher A.B. 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. J Biol Chem 2000, 275:28421-28427.
    • (2000) J Biol Chem , vol.275 , pp. 28421-28427
    • Chen, J.W.1    Dodia, C.2    Feinstein, S.I.3    Jain, M.K.4    Fisher, A.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.