메뉴 건너뛰기




Volumn 15, Issue 2-3, 2015, Pages 287-299

Thiol-based redox proteomics in cancer research

Author keywords

Biomedicine; Cancer biomarkers; Comparative proteomics; Mass spectrometry; Qxidative stress; Signal transduction

Indexed keywords

APOPTOSIS SIGNAL REGULATING KINASE 1; ATM PROTEIN; COFILIN; CYCLIC GMP DEPENDENT PROTEIN KINASE; FAS ANTIGEN; GLUTATHIONE PEROXIDASE; HIGH MOBILITY GROUP B1 PROTEIN; HOMEODOMAIN INTERACTING PROTEIN KINASE 2; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; LIPOCORTIN 2; PROTEIN KINASE LYN; PYRUVATE KINASE; PYRUVATE KINASE M2; SUMO 3 PROTEIN; THIOL; TRANSCRIPTION FACTOR FOXO; TRANSCRIPTION FACTOR FOXO4; UNCLASSIFIED DRUG; VASCULOTROPIN RECEPTOR 2; PROTEIN; REACTIVE OXYGEN METABOLITE; THIOL DERIVATIVE;

EID: 84921372345     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400164     Document Type: Review
Times cited : (24)

References (132)
  • 1
    • 84864367909 scopus 로고    scopus 로고
    • Global cancer transitions according to the Human Development Index (2008-2030): a population-based study
    • Bray, F., Jemal, A., Grey, N., Ferlay, J. et al., Global cancer transitions according to the Human Development Index (2008-2030): a population-based study. Lancet Oncol. 2012, 13, 790-801.
    • (2012) Lancet Oncol. , vol.13 , pp. 790-801
    • Bray, F.1    Jemal, A.2    Grey, N.3    Ferlay, J.4
  • 3
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. the prototypic redox-based signaling mechanism
    • Stamler, J. S., Lamas, S., Fang, F. C., Nitrosylation. the prototypic redox-based signaling mechanism. Cell 2001, 106, 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 5
    • 0342723791 scopus 로고    scopus 로고
    • Nitric oxide in the pathogenesis of vascular disease
    • Li, H., Forstermann, U., Nitric oxide in the pathogenesis of vascular disease. J. Pathol. 2000, 190, 244-254.
    • (2000) J. Pathol. , vol.190 , pp. 244-254
    • Li, H.1    Forstermann, U.2
  • 6
    • 0028155913 scopus 로고
    • Effects of a nitric oxide synthase inhibitor in humans with septic shock
    • Petros, A., Lamb, G., Leone, A., Moncada, S. et al., Effects of a nitric oxide synthase inhibitor in humans with septic shock. Cardiovasc. Res. 1994, 28, 34-39.
    • (1994) Cardiovasc. Res. , vol.28 , pp. 34-39
    • Petros, A.1    Lamb, G.2    Leone, A.3    Moncada, S.4
  • 7
    • 0029958972 scopus 로고    scopus 로고
    • Pathogenesis of influenza virus-induced pneumonia: involvement of both nitric oxide and oxygen radicals
    • Akaike, T., Noguchi, Y., Ijiri, S., Setoguchi, K. et al., Pathogenesis of influenza virus-induced pneumonia: involvement of both nitric oxide and oxygen radicals. Proc. Natl. Acad. Sci. USA 1996, 93, 2448-2453.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2448-2453
    • Akaike, T.1    Noguchi, Y.2    Ijiri, S.3    Setoguchi, K.4
  • 8
    • 0030959410 scopus 로고    scopus 로고
    • Suppression of herpes simplex virus type 1 (HSV-1)-induced pneumonia in mice by inhibition of inducible nitric oxide synthase (iNOS, NOS2)
    • Adler, H., Beland, J. L., Del-Pan, N. C., Kobzik, L. et al., Suppression of herpes simplex virus type 1 (HSV-1)-induced pneumonia in mice by inhibition of inducible nitric oxide synthase (iNOS, NOS2). J. Exp. Med. 1997, 185, 1533-1540.
    • (1997) J. Exp. Med. , vol.185 , pp. 1533-1540
    • Adler, H.1    Beland, J.L.2    Del-Pan, N.C.3    Kobzik, L.4
  • 9
    • 0037090069 scopus 로고    scopus 로고
    • Role of NADPH oxidase in the mechanism of lung neutrophil sequestration and microvessel injury induced by Gram-negative sepsis: studies in p47phox-/- and gp91phox-/- mice
    • Gao, X. P., Standiford, T. J., Rahman, A., Newstead, M. et al., Role of NADPH oxidase in the mechanism of lung neutrophil sequestration and microvessel injury induced by Gram-negative sepsis: studies in p47phox-/- and gp91phox-/- mice. J. Immunol. 2002, 168, 3974-3982.
    • (2002) J. Immunol. , vol.168 , pp. 3974-3982
    • Gao, X.P.1    Standiford, T.J.2    Rahman, A.3    Newstead, M.4
  • 10
    • 0031041884 scopus 로고    scopus 로고
    • Absence of respiratory burst in X-linked chronic granulomatous disease mice leads to abnormalities in both host defense and inflammatory response to Aspergillus fumigatus
    • Morgenstern, D. E., Gifford, M. A., Li, L. L., Doerschuk, C. M. et al., Absence of respiratory burst in X-linked chronic granulomatous disease mice leads to abnormalities in both host defense and inflammatory response to Aspergillus fumigatus. J. Exp. Med. 1997, 185, 207-218.
    • (1997) J. Exp. Med. , vol.185 , pp. 207-218
    • Morgenstern, D.E.1    Gifford, M.A.2    Li, L.L.3    Doerschuk, C.M.4
  • 11
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach
    • Trachootham, D., Alexandre, J., Huang, P., Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Nat. Rev. Drug Discov. 2009, 8, 579-591.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 12
    • 84889575198 scopus 로고    scopus 로고
    • Modulation of oxidative stress as an anticancer strategy
    • Gorrini, C., Harris, I. S., Mak, T. W., Modulation of oxidative stress as an anticancer strategy. Nat. Rev. Drug Discov. 2013, 12, 931-947.
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 931-947
    • Gorrini, C.1    Harris, I.S.2    Mak, T.W.3
  • 13
    • 33748146888 scopus 로고    scopus 로고
    • Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by beta-phenylethyl isothiocyanate
    • Trachootham, D., Zhou, Y., Zhang, H., Demizu, Y. et al., Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by beta-phenylethyl isothiocyanate. Cancer Cell 2006, 10, 241-252.
    • (2006) Cancer Cell , vol.10 , pp. 241-252
    • Trachootham, D.1    Zhou, Y.2    Zhang, H.3    Demizu, Y.4
  • 14
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani, S., Takeshita, M., Grollman, A. P., Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature 1991, 349, 431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 15
    • 79951906200 scopus 로고    scopus 로고
    • Thiol-based redox switches and gene regulation
    • Antelmann, H., Helmann, J. D., Thiol-based redox switches and gene regulation. Antioxid. Redox Signal. 2011, 14, 1049-1063.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1049-1063
    • Antelmann, H.1    Helmann, J.D.2
  • 16
    • 84891511098 scopus 로고    scopus 로고
    • Redox proteomics: from protein modifications to cellular dysfunction and disease
    • Butterfield, D. A., Dalle-Donne, I., Redox proteomics: from protein modifications to cellular dysfunction and disease. Mass Spectrom. Rev. 2014, 33, 1-6.
    • (2014) Mass Spectrom. Rev. , vol.33 , pp. 1-6
    • Butterfield, D.A.1    Dalle-Donne, I.2
  • 17
    • 84901340994 scopus 로고    scopus 로고
    • Determination of oxidative protein modifications using mass spectrometry
    • Raftery, M. J., Determination of oxidative protein modifications using mass spectrometry. Redox Rep. 2014, 19, 140-147.
    • (2014) Redox Rep. , vol.19 , pp. 140-147
    • Raftery, M.J.1
  • 18
    • 84898812067 scopus 로고    scopus 로고
    • Redox proteomics analysis of HNE-modified proteins in Down syndrome brain: clues for understanding the development of Alzheimer disease
    • Di Domenico, F., Pupo, G., Tramutola, A., Giorgi, A. et al., Redox proteomics analysis of HNE-modified proteins in Down syndrome brain: clues for understanding the development of Alzheimer disease. Free Radic. Biol. Med. 2014, 71, 270-280.
    • (2014) Free Radic. Biol. Med. , vol.71 , pp. 270-280
    • Di Domenico, F.1    Pupo, G.2    Tramutola, A.3    Giorgi, A.4
  • 19
    • 84892463241 scopus 로고    scopus 로고
    • Redox proteomics and the dynamic molecular landscape of the aging brain
    • Perluigi, M., Swomley, A. M., Butterfield, D. A., Redox proteomics and the dynamic molecular landscape of the aging brain. Ageing Res. Rev. 2014, 13, 75-89.
    • (2014) Ageing Res. Rev. , vol.13 , pp. 75-89
    • Perluigi, M.1    Swomley, A.M.2    Butterfield, D.A.3
  • 20
    • 84893509799 scopus 로고    scopus 로고
    • Unraveling the complexity of neurodegeneration in brains of subjects with Down syndrome: insights from proteomics
    • Perluigi, M., Di Domenico, F., Buttterfield, D. A., Unraveling the complexity of neurodegeneration in brains of subjects with Down syndrome: insights from proteomics. Proteomics Clin. Appl. 2014, 8, 73-85.
    • (2014) Proteomics Clin. Appl. , vol.8 , pp. 73-85
    • Perluigi, M.1    Di Domenico, F.2    Buttterfield, D.A.3
  • 21
    • 84899900734 scopus 로고    scopus 로고
    • Redox proteomic identification of HNE-bound mitochondrial proteins in cardiac tissues reveals a systemic effect on energy metabolism after doxorubicin treatment
    • Zhao, Y., Miriyala, S., Miao, L., Mitov, M. et al., Redox proteomic identification of HNE-bound mitochondrial proteins in cardiac tissues reveals a systemic effect on energy metabolism after doxorubicin treatment. Free Radic. Biol. Med. 2014, 72, 55-65.
    • (2014) Free Radic. Biol. Med. , vol.72 , pp. 55-65
    • Zhao, Y.1    Miriyala, S.2    Miao, L.3    Mitov, M.4
  • 22
    • 84887917839 scopus 로고    scopus 로고
    • Redox proteomics gives insights into the role of oxidative stress in alkaptonuria
    • Braconi, D., Millucci, L., Ghezzi, L., Santucci, A., Redox proteomics gives insights into the role of oxidative stress in alkaptonuria. Expert Rev. Proteomics 2013, 10, 521-535.
    • (2013) Expert Rev. Proteomics , vol.10 , pp. 521-535
    • Braconi, D.1    Millucci, L.2    Ghezzi, L.3    Santucci, A.4
  • 23
    • 84887045134 scopus 로고    scopus 로고
    • 2D DIGE based proteomics study of erythrocyte cytosol in sickle cell disease: altered proteostasis and oxidative stress
    • Basu, A., Saha, S., Karmakar, S., Chakravarty, S. et al., 2D DIGE based proteomics study of erythrocyte cytosol in sickle cell disease: altered proteostasis and oxidative stress. Proteomics 2013, 13, 3233-3242.
    • (2013) Proteomics , vol.13 , pp. 3233-3242
    • Basu, A.1    Saha, S.2    Karmakar, S.3    Chakravarty, S.4
  • 24
    • 84866663422 scopus 로고    scopus 로고
    • Redox proteomics analyses of the influence of co-expression of wild-type or mutated LRRK2 and Tau on C. elegans protein expression and oxidative modification: relevance to Parkinson disease
    • Di Domenico, F., Sultana, R., Ferree, A., Smith, K. et al., Redox proteomics analyses of the influence of co-expression of wild-type or mutated LRRK2 and Tau on C. elegans protein expression and oxidative modification: relevance to Parkinson disease. Antioxid. Redox Signal. 2012, 17, 1490-1506.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1490-1506
    • Di Domenico, F.1    Sultana, R.2    Ferree, A.3    Smith, K.4
  • 25
    • 84872254434 scopus 로고    scopus 로고
    • Redox proteomics: chemical principles, methodological approaches and biological/biomedical promises
    • Bachi, A., Dalle-Donne, I., Scaloni, A., Redox proteomics: chemical principles, methodological approaches and biological/biomedical promises. Chem. Rev. 2013, 113, 596-698.
    • (2013) Chem. Rev. , vol.113 , pp. 596-698
    • Bachi, A.1    Dalle-Donne, I.2    Scaloni, A.3
  • 26
    • 84878240943 scopus 로고    scopus 로고
    • Targeting allosteric disulphide bonds in cancer
    • Hogg, P. J., Targeting allosteric disulphide bonds in cancer. Nat. Rev. Cancer 2013, 13, 425-431.
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 425-431
    • Hogg, P.J.1
  • 27
    • 79952279293 scopus 로고    scopus 로고
    • Simultaneous analysis of relative protein expression levels across multiple samples using iTRAQ isobaric tags with 2D nano LC-MS/MS
    • Unwin, R. D., Griffiths, J. R., Whetton, A. D., Simultaneous analysis of relative protein expression levels across multiple samples using iTRAQ isobaric tags with 2D nano LC-MS/MS. Nat. Protoc. 2010, 5, 1574-1582.
    • (2010) Nat. Protoc. , vol.5 , pp. 1574-1582
    • Unwin, R.D.1    Griffiths, J.R.2    Whetton, A.D.3
  • 28
    • 67650564834 scopus 로고    scopus 로고
    • Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma
    • Addona, T. A., Abbatiello, S. E., Schilling, B., Skates, S. J. et al., Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma. Nat. Biotechnol. 2009, 27, 633-641.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 633-641
    • Addona, T.A.1    Abbatiello, S.E.2    Schilling, B.3    Skates, S.J.4
  • 29
    • 76649109590 scopus 로고    scopus 로고
    • An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers
    • Whiteaker, J. R., Zhao, L., Anderson, L., Paulovich, A. G., An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers. Mol. Cell. Proteomics 2010, 9, 184-196.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 184-196
    • Whiteaker, J.R.1    Zhao, L.2    Anderson, L.3    Paulovich, A.G.4
  • 30
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert, L. I., Jakob, U., Protein thiol modifications visualized in vivo. PLoS Biol. 2004, 2, e333.
    • (2004) PLoS Biol. , vol.2 , pp. e333
    • Leichert, L.I.1    Jakob, U.2
  • 31
    • 46149125288 scopus 로고    scopus 로고
    • Quantifying changes in the thiol redox proteome upon oxidative stress in vivo
    • Leichert, L. I., Gehrke, F., Gudiseva, H. V., Blackwell, T. et al., Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proc. Natl. Acad. Sci. USA 2008, 105, 8197-8202.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8197-8202
    • Leichert, L.I.1    Gehrke, F.2    Gudiseva, H.V.3    Blackwell, T.4
  • 32
    • 33747180294 scopus 로고    scopus 로고
    • A suite of algorithms for the comprehensive analysis of complex protein mixtures using high-resolution LC-MS
    • Bellew, M., Coram, M., Fitzgibbon, M., Igra, M. et al., A suite of algorithms for the comprehensive analysis of complex protein mixtures using high-resolution LC-MS. Bioinformatics 2006, 22, 1902-1909.
    • (2006) Bioinformatics , vol.22 , pp. 1902-1909
    • Bellew, M.1    Coram, M.2    Fitzgibbon, M.3    Igra, M.4
  • 33
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson, A., Schafer, J., Kuhn, K., Kienle, S. et al., Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal. Chem. 2003, 75, 1895-1904.
    • (2003) Anal. Chem. , vol.75 , pp. 1895-1904
    • Thompson, A.1    Schafer, J.2    Kuhn, K.3    Kienle, S.4
  • 34
    • 74849138649 scopus 로고    scopus 로고
    • Combining low- and high-energy tandem mass spectra for optimized peptide quantification with isobaric tags
    • Dayon, L., Pasquarello, C., Hoogland, C., Sanchez, J. C. et al., Combining low- and high-energy tandem mass spectra for optimized peptide quantification with isobaric tags. J. Proteomics 2010, 73, 769-777.
    • (2010) J. Proteomics , vol.73 , pp. 769-777
    • Dayon, L.1    Pasquarello, C.2    Hoogland, C.3    Sanchez, J.C.4
  • 35
    • 33745315287 scopus 로고    scopus 로고
    • S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara, T., Nakamura, T., Yao, D., Shi, Z. Q. et al., S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 2006, 441, 513-517.
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4
  • 36
    • 84856717563 scopus 로고    scopus 로고
    • Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay
    • M111 013441
    • Murray, C. I., Uhrigshardt, H., O'Meally, R. N., Cole, R. N. et al., Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay. Mol. Cell. Proteomics 2012, 11, M111 013441.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Murray, C.I.1    Uhrigshardt, H.2    O'Meally, R.N.3    Cole, R.N.4
  • 37
    • 78650078496 scopus 로고    scopus 로고
    • Quantitative reactivity profiling predicts functional cysteines in proteomes
    • Weerapana, E., Wang, C., Simon, G. M., Richter, F. et al., Quantitative reactivity profiling predicts functional cysteines in proteomes. Nature 2010, 468, 790-795.
    • (2010) Nature , vol.468 , pp. 790-795
    • Weerapana, E.1    Wang, C.2    Simon, G.M.3    Richter, F.4
  • 38
    • 84875182792 scopus 로고    scopus 로고
    • Proteome-wide quantification and characterization of oxidation-sensitive cysteines in pathogenic bacteria
    • Deng, X., Weerapana, E., Ulanovskaya, O., Sun, F. et al., Proteome-wide quantification and characterization of oxidation-sensitive cysteines in pathogenic bacteria. Cell Host Microbe 2013, 13, 358-370.
    • (2013) Cell Host Microbe , vol.13 , pp. 358-370
    • Deng, X.1    Weerapana, E.2    Ulanovskaya, O.3    Sun, F.4
  • 39
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • Rostovtsev, V. V., Green, L. G., Fokin, V. V., Sharpless, K. B., A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew. Chem. Int. Ed. Engl. 2002, 41, 2596-2599.
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 40
    • 0037012920 scopus 로고    scopus 로고
    • Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(i)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides
    • Tornoe, C. W., Christensen, C., Meldal, M., Peptidotriazoles on solid phase: [1, 2, 3]-triazoles by regiospecific copper(i)-catalyzed 1, 3-dipolar cycloadditions of terminal alkynes to azides. J. Org. Chem. 2002, 67, 3057-3064.
    • (2002) J. Org. Chem. , vol.67 , pp. 3057-3064
    • Tornoe, C.W.1    Christensen, C.2    Meldal, M.3
  • 41
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast:tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., McDonald, W. H., Yates, J. R., 3rd, DTASelect and Contrast:tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 2002, 1, 21-26.
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates 3rd, J.R.3
  • 42
    • 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., Soito, L. et al., Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods Enzymol. 2010, 473, 77-94.
    • (2010) Methods Enzymol. , vol.473 , pp. 77-94
    • Klomsiri, C.1    Nelson, K.J.2    Bechtold, E.3    Soito, L.4
  • 43
    • 70349482669 scopus 로고    scopus 로고
    • Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies
    • Seo, Y. H., Carroll, K. S., Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies. Proc. Natl. Acad. Sci. USA 2009, 106, 16163-16168.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16163-16168
    • Seo, Y.H.1    Carroll, K.S.2
  • 44
    • 80052290597 scopus 로고    scopus 로고
    • Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome"
    • Karisch, R., Fernandez, M., Taylor, P., Virtanen, C. et al., Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome". Cell 2011, 146, 826-840.
    • (2011) Cell , vol.146 , pp. 826-840
    • Karisch, R.1    Fernandez, M.2    Taylor, P.3    Virtanen, C.4
  • 45
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee, S. G., Bae, Y. S., Lee, S. R., Kwon, J., Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE 2000, 2000, pe1.
    • (2000) Sci. STKE , vol.2000 , pp. pe1
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 46
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T. C. et al., Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 2003, 423, 769-773.
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4
  • 47
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort, R. L., Congreve, M., Tisi, D., Carr, R. et al., Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 2003, 423, 773-777.
    • (2003) Nature , vol.423 , pp. 773-777
    • van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4
  • 48
    • 64349117191 scopus 로고    scopus 로고
    • Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines
    • Chen, C. Y., Willard, D., Rudolph, J., Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines. Biochemistry 2009, 48, 1399-1409.
    • (2009) Biochemistry , vol.48 , pp. 1399-1409
    • Chen, C.Y.1    Willard, D.2    Rudolph, J.3
  • 49
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: revisiting PTPs and the control of cell signaling
    • Tonks, N. K., Redox redux: revisiting PTPs and the control of cell signaling. Cell 2005, 121, 667-670.
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 50
    • 10644275378 scopus 로고    scopus 로고
    • An antibody-based method for monitoring in vivo oxidation of protein tyrosine phosphatases
    • Persson, C., Kappert, K., Engstrom, U., Ostman, A. et al., An antibody-based method for monitoring in vivo oxidation of protein tyrosine phosphatases. Methods 2005, 35, 37-43.
    • (2005) Methods , vol.35 , pp. 37-43
    • Persson, C.1    Kappert, K.2    Engstrom, U.3    Ostman, A.4
  • 51
    • 15444374584 scopus 로고    scopus 로고
    • Differential oxidation of protein-tyrosine phosphatases
    • Groen, A., Lemeer, S., van der Wijk, T., Overvoorde, J. et al., Differential oxidation of protein-tyrosine phosphatases. J. Biol. Chem. 2005, 280, 10298-10304.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10298-10304
    • Groen, A.1    Lemeer, S.2    van der Wijk, T.3    Overvoorde, J.4
  • 52
    • 1242342002 scopus 로고    scopus 로고
    • Preferential oxidation of the second phosphatase domain of receptor-like PTP-alpha revealed by an antibody against oxidized protein tyrosine phosphatases
    • Persson, C., Sjoblom, T., Groen, A., Kappert, K. et al., Preferential oxidation of the second phosphatase domain of receptor-like PTP-alpha revealed by an antibody against oxidized protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 2004, 101, 1886-1891.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1886-1891
    • Persson, C.1    Sjoblom, T.2    Groen, A.3    Kappert, K.4
  • 53
    • 34249870112 scopus 로고    scopus 로고
    • Oxidation sensitivity of the catalytic cysteine of the protein-tyrosine phosphatases SHP-1 and SHP-2
    • Weibrecht, I., Bohmer, S. A., Dagnell, M., Kappert, K. et al., Oxidation sensitivity of the catalytic cysteine of the protein-tyrosine phosphatases SHP-1 and SHP-2. Free Radic. Biol. Med. 2007, 43, 100-110.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 100-110
    • Weibrecht, I.1    Bohmer, S.A.2    Dagnell, M.3    Kappert, K.4
  • 54
    • 0031022433 scopus 로고    scopus 로고
    • Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate
    • Huyer, G., Liu, S., Kelly, J., Moffat, J. et al., Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J. Biol. Chem. 1997, 272, 843-851.
    • (1997) J. Biol. Chem. , vol.272 , pp. 843-851
    • Huyer, G.1    Liu, S.2    Kelly, J.3    Moffat, J.4
  • 55
    • 68949206409 scopus 로고    scopus 로고
    • Applying mass spectrometry-based proteomics to genetics, genomics and network biology
    • Gstaiger, M., Aebersold, R., Applying mass spectrometry-based proteomics to genetics, genomics and network biology. Nat. Rev. Genet. 2009, 10, 617-627.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 617-627
    • Gstaiger, M.1    Aebersold, R.2
  • 56
    • 77955876447 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics in cell biology
    • Walther, T. C., Mann, M., Mass spectrometry-based proteomics in cell biology. J. Cell Biol. 2010, 190, 491-500.
    • (2010) J. Cell Biol. , vol.190 , pp. 491-500
    • Walther, T.C.1    Mann, M.2
  • 57
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: approaches, advances, and applications
    • Yates, J. R., Ruse, C. I., Nakorchevsky, A., Proteomics by mass spectrometry: approaches, advances, and applications. Annu. Rev. Biomed. Eng. 2009, 11, 49-79.
    • (2009) Annu. Rev. Biomed. Eng. , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 58
    • 78751675280 scopus 로고    scopus 로고
    • Targeted proteomics by selected reaction monitoring mass spectrometry: applications to systems biology and biomarker discovery
    • Elschenbroich, S., Kislinger, T., Targeted proteomics by selected reaction monitoring mass spectrometry: applications to systems biology and biomarker discovery. Mol. Biosyst. 2011, 7, 292-303.
    • (2011) Mol. Biosyst. , vol.7 , pp. 292-303
    • Elschenbroich, S.1    Kislinger, T.2
  • 59
    • 34247153458 scopus 로고    scopus 로고
    • Analytical methodology for TEX86 paleothermometry by high-performance liquid chromatography/atmospheric pressure chemical ionization-mass spectrometry
    • Schouten, S., Huguet, C., Hopmans, E. C., Kienhuis, M. V. et al., Analytical methodology for TEX86 paleothermometry by high-performance liquid chromatography/atmospheric pressure chemical ionization-mass spectrometry. Anal. Chem. 2007, 79, 2940-2944.
    • (2007) Anal. Chem. , vol.79 , pp. 2940-2944
    • Schouten, S.1    Huguet, C.2    Hopmans, E.C.3    Kienhuis, M.V.4
  • 60
    • 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. 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
  • 61
    • 0029737618 scopus 로고    scopus 로고
    • Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution
    • Yeh, J. I., Claiborne, A., Hol, W. G., Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution. Biochemistry 1996, 35, 9951-9957.
    • (1996) Biochemistry , vol.35 , pp. 9951-9957
    • Yeh, J.I.1    Claiborne, A.2    Hol, W.G.3
  • 62
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • Reddie, K. G., Carroll, K. S., Expanding the functional diversity of proteins through cysteine oxidation. Curr. Opin. Chem. Biol. 2008, 12, 746-754.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 63
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • Paulsen, C. E., Carroll, K. S., Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem. Biol. 2010, 5, 47-62.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 65
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson, G. L., Lapadat, R., Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 2002, 298, 1911-1912.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 66
    • 14444281569 scopus 로고    scopus 로고
    • Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways
    • Ichijo, H., Nishida, E., Irie, K., ten Dijke, P. et al., Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 1997, 275, 90-94.
    • (1997) Science , vol.275 , pp. 90-94
    • Ichijo, H.1    Nishida, E.2    Irie, K.3    ten Dijke, P.4
  • 67
    • 0032504189 scopus 로고    scopus 로고
    • Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-alpha signal transduction
    • Gotoh, Y., Cooper, J. A., Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-alpha signal transduction. J. Biol. Chem. 1998, 273, 17477-17482.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17477-17482
    • Gotoh, Y.1    Cooper, J.A.2
  • 68
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K. et al., Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J. 1998, 17, 2596-2606.
    • (1998) EMBO J. , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3    Takeda, K.4
  • 69
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • Ray, P. D., Huang, B. W., Tsuji, Y., Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell. Signal. 2012, 24, 981-990.
    • (2012) Cell. Signal. , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 70
    • 84877957225 scopus 로고    scopus 로고
    • A role for Hipk in the Hippo pathway
    • Heidary Arash, E., Attisano, L., A role for Hipk in the Hippo pathway. Sci. Signal. 2013, 6, pe18.
    • (2013) Sci. Signal. , vol.6 , pp. pe18
    • Heidary Arash, E.1    Attisano, L.2
  • 71
    • 77955470408 scopus 로고    scopus 로고
    • Regulation of p53 activity by HIPK2: molecular mechanisms and therapeutical implications in human cancer cells
    • Puca, R., Nardinocchi, L., Givol, D., D'Orazi, G., Regulation of p53 activity by HIPK2: molecular mechanisms and therapeutical implications in human cancer cells. Oncogene 2010, 29, 4378-4387.
    • (2010) Oncogene , vol.29 , pp. 4378-4387
    • Puca, R.1    Nardinocchi, L.2    Givol, D.3    D'Orazi, G.4
  • 72
  • 73
    • 84861452914 scopus 로고    scopus 로고
    • A redox-regulated SUMO/acetylation switch of HIPK2 controls the survival threshold to oxidative stress
    • de la Vega, L., Grishina, I., Moreno, R., Kruger, M. et al., A redox-regulated SUMO/acetylation switch of HIPK2 controls the survival threshold to oxidative stress. Mol. Cell 2012, 46, 472-483.
    • (2012) Mol. Cell , vol.46 , pp. 472-483
    • de la Vega, L.1    Grishina, I.2    Moreno, R.3    Kruger, M.4
  • 74
    • 34247536682 scopus 로고    scopus 로고
    • The CD95 receptor: apoptosis revisited
    • Peter, M. E., Budd, R. C., Desbarats, J., Hedrick, S. M. et al., The CD95 receptor: apoptosis revisited. Cell 2007, 129, 447-450.
    • (2007) Cell , vol.129 , pp. 447-450
    • Peter, M.E.1    Budd, R.C.2    Desbarats, J.3    Hedrick, S.M.4
  • 75
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: more than a paradigm
    • Wajant, H., The Fas signaling pathway: more than a paradigm. Science 2002, 296, 1635-1636.
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 76
    • 60849086193 scopus 로고    scopus 로고
    • Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas
    • Anathy, V., Aesif, S. W., Guala, A. S., Havermans, M. et al., Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas. J. Cell Biol. 2009, 184, 241-252.
    • (2009) J. Cell Biol. , vol.184 , pp. 241-252
    • Anathy, V.1    Aesif, S.W.2    Guala, A.S.3    Havermans, M.4
  • 77
    • 80051995190 scopus 로고    scopus 로고
    • Fas-mediated neutrophil apoptosis is accelerated by Bid, Bak, and Bax and inhibited by Bcl-2 and Mcl-1
    • Croker, B. A., O'Donnell, J. A., Nowell, C. J., Metcalf, D. et al., Fas-mediated neutrophil apoptosis is accelerated by Bid, Bak, and Bax and inhibited by Bcl-2 and Mcl-1. Proc. Natl. Acad. Sci. USA 2011, 108, 13135-13140.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 13135-13140
    • Croker, B.A.1    O'Donnell, J.A.2    Nowell, C.J.3    Metcalf, D.4
  • 78
    • 84866378556 scopus 로고    scopus 로고
    • Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release
    • Venereau, E., Casalgrandi, M., Schiraldi, M., Antoine, D. J. et al., Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release. J. Exp. Med. 2012, 209, 1519-1528.
    • (2012) J. Exp. Med. , vol.209 , pp. 1519-1528
    • Venereau, E.1    Casalgrandi, M.2    Schiraldi, M.3    Antoine, D.J.4
  • 79
    • 77957106729 scopus 로고    scopus 로고
    • HMGB1 release and redox regulates autophagy and apoptosis in cancer cells
    • Tang, D., Kang, R., Cheh, C. W., Livesey, K. M. et al., HMGB1 release and redox regulates autophagy and apoptosis in cancer cells. Oncogene 2010, 29, 5299-5310.
    • (2010) Oncogene , vol.29 , pp. 5299-5310
    • Tang, D.1    Kang, R.2    Cheh, C.W.3    Livesey, K.M.4
  • 80
    • 33845951211 scopus 로고    scopus 로고
    • DAMPs, PAMPs and alarmins: all we need to know about danger
    • Bianchi, M. E., DAMPs, PAMPs and alarmins: all we need to know about danger. J. Leukoc. Biol. 2007, 81, 1-5.
    • (2007) J. Leukoc. Biol. , vol.81 , pp. 1-5
    • Bianchi, M.E.1
  • 81
    • 84860862890 scopus 로고    scopus 로고
    • Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1)
    • Yang, H., Lundback, P., Ottosson, L., Erlandsson-Harris, H. et al., Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1). Mol. Med. 2012, 18, 250-259.
    • (2012) Mol. Med. , vol.18 , pp. 250-259
    • Yang, H.1    Lundback, P.2    Ottosson, L.3    Erlandsson-Harris, H.4
  • 82
    • 0344668558 scopus 로고    scopus 로고
    • Mitochondrial translocation of cofilin is an early step in apoptosis induction
    • Chua, B. T., Volbracht, C., Tan, K. O., Li, R. et al., Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nat. Cell Biol. 2003, 5, 1083-1089.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1083-1089
    • Chua, B.T.1    Volbracht, C.2    Tan, K.O.3    Li, R.4
  • 83
    • 33749017960 scopus 로고    scopus 로고
    • Prohibitin and cofilin are intracellular effectors of transforming growth factor beta signaling in human prostate cancer cells
    • Zhu, B., Fukada, K., Zhu, H., Kyprianou, N., Prohibitin and cofilin are intracellular effectors of transforming growth factor beta signaling in human prostate cancer cells. Cancer Res. 2006, 66, 8640-8647.
    • (2006) Cancer Res. , vol.66 , pp. 8640-8647
    • Zhu, B.1    Fukada, K.2    Zhu, H.3    Kyprianou, N.4
  • 84
    • 16244370745 scopus 로고    scopus 로고
    • Activated cofilin colocalises with Arp2/3 complex in apoptotic blebs during programmed cell death
    • Mannherz, H. G., Gonsior, S. M., Gremm, D., Wu, X. et al., Activated cofilin colocalises with Arp2/3 complex in apoptotic blebs during programmed cell death. Eur. J. Cell Biol. 2005, 84, 503-515.
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 503-515
    • Mannherz, H.G.1    Gonsior, S.M.2    Gremm, D.3    Wu, X.4
  • 85
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli, M., Demol, H., Puype, M., Casagrande, S. et al., Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc. Natl. Acad. Sci. USA 2002, 99, 3505-3510.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4
  • 86
    • 70349651926 scopus 로고    scopus 로고
    • Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
    • Klamt, F., Zdanov, S., Levine, R. L., Pariser, A. et al., Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nat. Cell Biol. 2009, 11, 1241-1246.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1241-1246
    • Klamt, F.1    Zdanov, S.2    Levine, R.L.3    Pariser, A.4
  • 87
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: the metabolic requirements of cell proliferation
    • Vander Heiden, M. G., Cantley, L. C., Thompson, C. B., Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 2009, 324, 1029-1033.
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 88
    • 40749163248 scopus 로고    scopus 로고
    • The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
    • Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A. et al., The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature 2008, 452, 230-233.
    • (2008) Nature , vol.452 , pp. 230-233
    • Christofk, H.R.1    Vander Heiden, M.G.2    Harris, M.H.3    Ramanathan, A.4
  • 89
    • 75149150660 scopus 로고    scopus 로고
    • HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer
    • David, C. J., Chen, M., Assanah, M., Canoll, P. et al., HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer. Nature 2010, 463, 364-368.
    • (2010) Nature , vol.463 , pp. 364-368
    • David, C.J.1    Chen, M.2    Assanah, M.3    Canoll, P.4
  • 90
    • 82755166890 scopus 로고    scopus 로고
    • Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses
    • Anastasiou, D., Poulogiannis, G., Asara, J. M., Boxer, M. B. et al., Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses. Science 2011, 334, 1278-1283.
    • (2011) Science , vol.334 , pp. 1278-1283
    • Anastasiou, D.1    Poulogiannis, G.2    Asara, J.M.3    Boxer, M.B.4
  • 91
    • 40749099894 scopus 로고    scopus 로고
    • Pyruvate kinase M2 is a phosphotyrosine-binding protein
    • Christofk, H. R., Vander Heiden, M. G., Wu, N., Asara, J. M. et al., Pyruvate kinase M2 is a phosphotyrosine-binding protein. Nature 2008, 452, 181-186.
    • (2008) Nature , vol.452 , pp. 181-186
    • Christofk, H.R.1    Vander Heiden, M.G.2    Wu, N.3    Asara, J.M.4
  • 92
    • 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. 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
  • 93
    • 0242330206 scopus 로고    scopus 로고
    • Physiology and pathophysiology of vascular signaling controlled by guanosine 3',5'-cyclic monophosphate-dependent protein kinase [corrected]
    • Munzel, T., Feil, R., Mulsch, A., Lohmann, S. M. et al., Physiology and pathophysiology of vascular signaling controlled by guanosine 3', 5'-cyclic monophosphate-dependent protein kinase [corrected]. Circulation 2003, 108, 2172-2183.
    • (2003) Circulation , vol.108 , pp. 2172-2183
    • Munzel, T.1    Feil, R.2    Mulsch, A.3    Lohmann, S.M.4
  • 94
    • 41149096647 scopus 로고    scopus 로고
    • Expression of cyclic guanosine monophosphate-dependent protein kinase in metastatic colon carcinoma cells blocks tumor angiogenesis
    • Kwon, I. K., Schoenlein, P. V., Delk, J., Liu, K. et al., Expression of cyclic guanosine monophosphate-dependent protein kinase in metastatic colon carcinoma cells blocks tumor angiogenesis. Cancer 2008, 112, 1462-1470.
    • (2008) Cancer , vol.112 , pp. 1462-1470
    • Kwon, I.K.1    Schoenlein, P.V.2    Delk, J.3    Liu, K.4
  • 95
    • 34548695863 scopus 로고    scopus 로고
    • Cysteine redox sensor in PKGIa enables oxidant-induced activation
    • Burgoyne, J. R., Madhani, M., Cuello, F., Charles, R. L. et al., Cysteine redox sensor in PKGIa enables oxidant-induced activation. Science 2007, 317, 1393-1397.
    • (2007) Science , vol.317 , pp. 1393-1397
    • Burgoyne, J.R.1    Madhani, M.2    Cuello, F.3    Charles, R.L.4
  • 96
    • 67749111502 scopus 로고    scopus 로고
    • The LKB1-AMPK pathway: metabolism and growth control in tumour suppression
    • Shackelford, D. B., Shaw, R. J., The LKB1-AMPK pathway: metabolism and growth control in tumour suppression. Nat. Rev. Cancer 2009, 9, 563-575.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 563-575
    • Shackelford, D.B.1    Shaw, R.J.2
  • 97
    • 33745213627 scopus 로고    scopus 로고
    • AMPK and cell proliferation-AMPK as a therapeutic target for atherosclerosis and cancer
    • Motoshima, H., Goldstein, B. J., Igata, M., Araki, E., AMPK and cell proliferation-AMPK as a therapeutic target for atherosclerosis and cancer. J. Physiol. 2006, 574, 63-71.
    • (2006) J. Physiol. , vol.574 , pp. 63-71
    • Motoshima, H.1    Goldstein, B.J.2    Igata, M.3    Araki, E.4
  • 98
    • 77958501463 scopus 로고    scopus 로고
    • Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase
    • Zmijewski, J. W., Banerjee, S., Bae, H., Friggeri, A. et al., Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase. J. Biol. Chem. 2010, 285, 33154-33164.
    • (2010) J. Biol. Chem. , vol.285 , pp. 33154-33164
    • Zmijewski, J.W.1    Banerjee, S.2    Bae, H.3    Friggeri, A.4
  • 99
    • 84893432818 scopus 로고    scopus 로고
    • A redox-dependent mechanism for regulation of AMPK activation by thioredoxin1 during energy starvation
    • Shao, D., Oka, S., Liu, T., Zhai, P. et al., A redox-dependent mechanism for regulation of AMPK activation by thioredoxin1 during energy starvation. Cell Metab. 2014, 19, 232-245.
    • (2014) Cell Metab. , vol.19 , pp. 232-245
    • Shao, D.1    Oka, S.2    Liu, T.3    Zhai, P.4
  • 100
    • 0034641724 scopus 로고    scopus 로고
    • Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro
    • Matsuoka, S., Rotman, G., Ogawa, A., Shiloh, Y. et al., Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro. Proc. Natl. Acad. Sci. USA 2000, 97, 10389-10394.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10389-10394
    • Matsuoka, S.1    Rotman, G.2    Ogawa, A.3    Shiloh, Y.4
  • 101
    • 0032508608 scopus 로고    scopus 로고
    • Activation of the ATM kinase by ionizing radiation and phosphorylation of p53
    • Canman, C. E., Lim, D. S., Cimprich, K. A., Taya, Y. et al., Activation of the ATM kinase by ionizing radiation and phosphorylation of p53. Science 1998, 281, 1677-1679.
    • (1998) Science , vol.281 , pp. 1677-1679
    • Canman, C.E.1    Lim, D.S.2    Cimprich, K.A.3    Taya, Y.4
  • 102
    • 0035848819 scopus 로고    scopus 로고
    • The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis
    • Falck, J., Mailand, N., Syljuasen, R. G., Bartek, J. et al., The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis. Nature 2001, 410, 842-847.
    • (2001) Nature , vol.410 , pp. 842-847
    • Falck, J.1    Mailand, N.2    Syljuasen, R.G.3    Bartek, J.4
  • 103
    • 0035834693 scopus 로고    scopus 로고
    • ATM phosphorylates histone H2AX in response to DNA double-strand breaks
    • Burma, S., Chen, B. P., Murphy, M., Kurimasa, A. et al., ATM phosphorylates histone H2AX in response to DNA double-strand breaks. J. Biol. Chem. 2001, 276, 42462-42467.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42462-42467
    • Burma, S.1    Chen, B.P.2    Murphy, M.3    Kurimasa, A.4
  • 104
    • 77958191599 scopus 로고    scopus 로고
    • ATM activation by oxidative stress
    • Guo, Z., Kozlov, S., Lavin, M. F., Person, M. D. et al., ATM activation by oxidative stress. Science 2010, 330, 517-521.
    • (2010) Science , vol.330 , pp. 517-521
    • Guo, Z.1    Kozlov, S.2    Lavin, M.F.3    Person, M.D.4
  • 105
    • 61849152775 scopus 로고    scopus 로고
    • Multiple roles of Lyn kinase in myeloid cell signaling and function
    • Scapini, P., Pereira, S., Zhang, H., Lowell, C. A., Multiple roles of Lyn kinase in myeloid cell signaling and function. Immunol. Rev. 2009, 228, 23-40.
    • (2009) Immunol. Rev. , vol.228 , pp. 23-40
    • Scapini, P.1    Pereira, S.2    Zhang, H.3    Lowell, C.A.4
  • 106
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: challenges and opportunities
    • Nathan, C., Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 2006, 6, 173-182.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 173-182
    • Nathan, C.1
  • 107
    • 0022891340 scopus 로고
    • Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing
    • Dvorak, H. F., Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing. N. Engl. J. Med. 1986, 315, 1650-1659.
    • (1986) N. Engl. J. Med. , vol.315 , pp. 1650-1659
    • Dvorak, H.F.1
  • 108
    • 0029846531 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced chemotaxis of mouse peritoneal neutrophils
    • Klyubin, I. V., Kirpichnikova, K. M., Gamaley, I. A., Hydrogen peroxide-induced chemotaxis of mouse peritoneal neutrophils. Eur. J. Cell Biol. 1996, 70, 347-351.
    • (1996) Eur. J. Cell Biol. , vol.70 , pp. 347-351
    • Klyubin, I.V.1    Kirpichnikova, K.M.2    Gamaley, I.A.3
  • 109
    • 78650447229 scopus 로고    scopus 로고
    • Live imaging of innate immune cell sensing of transformed cells in zebrafish larvae: parallels between tumor initiation and wound inflammation
    • Feng, Y., Santoriello, C., Mione, M., Hurlstone, A. et al., Live imaging of innate immune cell sensing of transformed cells in zebrafish larvae: parallels between tumor initiation and wound inflammation. PLoS Biol. 2010, 8, e1000562.
    • (2010) PLoS Biol. , vol.8 , pp. e1000562
    • Feng, Y.1    Santoriello, C.2    Mione, M.3    Hurlstone, A.4
  • 110
    • 77649181715 scopus 로고    scopus 로고
    • Prioritization of competing damage and developmental signals by migrating macrophages in the Drosophila embryo
    • Moreira, S., Stramer, B., Evans, I., Wood, W. et al., Prioritization of competing damage and developmental signals by migrating macrophages in the Drosophila embryo. Curr. Biol. 2010, 20, 464-470.
    • (2010) Curr. Biol. , vol.20 , pp. 464-470
    • Moreira, S.1    Stramer, B.2    Evans, I.3    Wood, W.4
  • 111
    • 67649255876 scopus 로고    scopus 로고
    • A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
    • Niethammer, P., Grabher, C., Look, A. T., Mitchison, T. J., A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish. Nature 2009, 459, 996-999.
    • (2009) Nature , vol.459 , pp. 996-999
    • Niethammer, P.1    Grabher, C.2    Look, A.T.3    Mitchison, T.J.4
  • 112
    • 82555168190 scopus 로고    scopus 로고
    • Lyn is a redox sensor that mediates leukocyte wound attraction in vivo
    • Yoo, S. K., Starnes, T. W., Deng, Q., Huttenlocher, A., Lyn is a redox sensor that mediates leukocyte wound attraction in vivo. Nature 2011, 480, 109-112.
    • (2011) Nature , vol.480 , pp. 109-112
    • Yoo, S.K.1    Starnes, T.W.2    Deng, Q.3    Huttenlocher, A.4
  • 113
    • 6344270258 scopus 로고    scopus 로고
    • Identification of a novel putative non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx) essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells
    • Utomo, A., Jiang, X., Furuta, S., Yun, J. et al., Identification of a novel putative non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx) essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells. J. Biol. Chem. 2004, 279, 43522-43529.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43522-43529
    • Utomo, A.1    Jiang, X.2    Furuta, S.3    Yun, J.4
  • 114
    • 40949159866 scopus 로고    scopus 로고
    • Oxidative stress is inherent in prostate cancer cells and is required for aggressive phenotype
    • Kumar, B., Koul, S., Khandrika, L., Meacham, R. B. et al., Oxidative stress is inherent in prostate cancer cells and is required for aggressive phenotype. Cancer Res. 2008, 68, 1777-1785.
    • (2008) Cancer Res. , vol.68 , pp. 1777-1785
    • Kumar, B.1    Koul, S.2    Khandrika, L.3    Meacham, R.B.4
  • 115
    • 80052000670 scopus 로고    scopus 로고
    • Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities
    • Lubos, E., Loscalzo, J., Handy, D. E., Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxid. Redox Signal. 2011, 15, 1957-1997.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 1957-1997
    • Lubos, E.1    Loscalzo, J.2    Handy, D.E.3
  • 116
    • 84870877138 scopus 로고    scopus 로고
    • Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic disease
    • Wei, P. C., Hsieh, Y. H., Su, M. I., Jiang, X. et al., Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic disease. Mol. Cell 2012, 48, 747-759.
    • (2012) Mol. Cell , vol.48 , pp. 747-759
    • Wei, P.C.1    Hsieh, Y.H.2    Su, M.I.3    Jiang, X.4
  • 117
    • 34548257176 scopus 로고    scopus 로고
    • HIF-dependent antitumorigenic effect of antioxidants in vivo
    • Gao, P., Zhang, H., Dinavahi, R., Li, F. et al., HIF-dependent antitumorigenic effect of antioxidants in vivo. Cancer Cell 2007, 12, 230-238.
    • (2007) Cancer Cell , vol.12 , pp. 230-238
    • Gao, P.1    Zhang, H.2    Dinavahi, R.3    Li, F.4
  • 118
    • 36348938884 scopus 로고    scopus 로고
    • Reactive oxygen species regulate angiogenesis and tumor growth through vascular endothelial growth factor
    • Xia, C., Meng, Q., Liu, L. Z., Rojanasakul, Y. et al., Reactive oxygen species regulate angiogenesis and tumor growth through vascular endothelial growth factor. Cancer Res. 2007, 67, 10823-10830.
    • (2007) Cancer Res. , vol.67 , pp. 10823-10830
    • Xia, C.1    Meng, Q.2    Liu, L.Z.3    Rojanasakul, Y.4
  • 119
    • 37849022071 scopus 로고    scopus 로고
    • Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis
    • Guzy, R. D., Sharma, B., Bell, E., Chandel, N. S. et al., Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis. Mol. Cell. Biol. 2008, 28, 718-731.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 718-731
    • Guzy, R.D.1    Sharma, B.2    Bell, E.3    Chandel, N.S.4
  • 120
    • 70349213234 scopus 로고    scopus 로고
    • SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation
    • Huang, C., Han, Y., Wang, Y., Sun, X. et al., SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation. EMBO J. 2009, 28, 2748-2762.
    • (2009) EMBO J. , vol.28 , pp. 2748-2762
    • Huang, C.1    Han, Y.2    Wang, Y.3    Sun, X.4
  • 121
    • 78449275359 scopus 로고    scopus 로고
    • Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90
    • Yan, S., Sun, X., Xiang, B., Cang, H. et al., Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90. EMBO J. 2010, 29, 3773-3786.
    • (2010) EMBO J. , vol.29 , pp. 3773-3786
    • Yan, S.1    Sun, X.2    Xiang, B.3    Cang, H.4
  • 123
    • 81355150904 scopus 로고    scopus 로고
    • Peroxiredoxin II is an essential antioxidant enzyme that prevents the oxidative inactivation of VEGF receptor-2 in vascular endothelial cells
    • Kang, D. H., Lee, D. J., Lee, K. W., Park, Y. S. et al., Peroxiredoxin II is an essential antioxidant enzyme that prevents the oxidative inactivation of VEGF receptor-2 in vascular endothelial cells. Mol. Cell 2011, 44, 545-558.
    • (2011) Mol. Cell , vol.44 , pp. 545-558
    • Kang, D.H.1    Lee, D.J.2    Lee, K.W.3    Park, Y.S.4
  • 124
    • 41849150779 scopus 로고    scopus 로고
    • FOXOs, cancer and regulation of apoptosis
    • Fu, Z., Tindall, D. J., FOXOs, cancer and regulation of apoptosis. Oncogene 2008, 27, 2312-2319.
    • (2008) Oncogene , vol.27 , pp. 2312-2319
    • Fu, Z.1    Tindall, D.J.2
  • 125
    • 2342496712 scopus 로고    scopus 로고
    • FoxOs at the crossroads of cellular metabolism, differentiation, and transformation
    • Accili, D., Arden, K. C., FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell 2004, 117, 421-426.
    • (2004) Cell , vol.117 , pp. 421-426
    • Accili, D.1    Arden, K.C.2
  • 126
    • 75149115329 scopus 로고    scopus 로고
    • FoxO1 is a positive regulator of bone formation by favoring protein synthesis and resistance to oxidative stress in osteoblasts
    • Rached, M. T., Kode, A., Xu, L., Yoshikawa, Y. et al., FoxO1 is a positive regulator of bone formation by favoring protein synthesis and resistance to oxidative stress in osteoblasts. Cell Metab. 2010, 11, 147-160.
    • (2010) Cell Metab. , vol.11 , pp. 147-160
    • Rached, M.T.1    Kode, A.2    Xu, L.3    Yoshikawa, Y.4
  • 127
    • 69249229450 scopus 로고    scopus 로고
    • Redox-sensitive cysteines bridge p300/CBP-mediated acetylation and FoxO4 activity
    • Dansen, T. B., Smits, L. M., van Triest, M. H., de Keizer, P. L. et al., Redox-sensitive cysteines bridge p300/CBP-mediated acetylation and FoxO4 activity. Nat. Chem. Biol. 2009, 5, 664-672.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 664-672
    • Dansen, T.B.1    Smits, L.M.2    van Triest, M.H.3    de Keizer, P.L.4
  • 129
    • 84863004520 scopus 로고    scopus 로고
    • Annexin A2 is a novel cellular redox regulatory protein involved in tumorigenesis
    • Madureira, P. A., Hill, R., Miller, V. A., Giacomantonio, C. et al., Annexin A2 is a novel cellular redox regulatory protein involved in tumorigenesis. Oncotarget 2011, 2, 1075-1093.
    • (2011) Oncotarget , vol.2 , pp. 1075-1093
    • Madureira, P.A.1    Hill, R.2    Miller, V.A.3    Giacomantonio, C.4
  • 130
    • 84875107066 scopus 로고    scopus 로고
    • Annexin A2: the importance of being redox sensitive
    • Madureira, P. A., Waisman, D. M., Annexin A2: the importance of being redox sensitive. Int. J. Mol. Sci. 2013, 14, 3568-3594.
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 3568-3594
    • Madureira, P.A.1    Waisman, D.M.2
  • 132
    • 26944462004 scopus 로고    scopus 로고
    • Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis
    • Hochgrafe, F., Mostertz, J., Albrecht, D., Hecker, M., Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis. Mol. Microbiol. 2005, 58, 409-425.
    • (2005) Mol. Microbiol. , vol.58 , pp. 409-425
    • Hochgrafe, F.1    Mostertz, J.2    Albrecht, D.3    Hecker, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.