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Volumn 43, Issue 8, 2007, Pages 1099-1108

Thiol oxidation in signaling and response to stress: Detection and quantification of physiological and pathophysiological thiol modifications

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; CYSTEINE DERIVATIVE; GLUTATHIONE; ISOTOPE; THIOL;

EID: 34548507495     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.07.014     Document Type: Review
Times cited : (196)

References (50)
  • 1
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., and Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab. Rev. 30 (1998) 225-243
    • (1998) Drug Metab. Rev. , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 2
    • 0042164949 scopus 로고    scopus 로고
    • Redox proteomics: identification of oxidatively modified proteins
    • Ghezzi P., and Bonetto V. Redox proteomics: identification of oxidatively modified proteins. Proteomics 3 (2003) 1145-1153
    • (2003) Proteomics , vol.3 , pp. 1145-1153
    • Ghezzi, P.1    Bonetto, V.2
  • 3
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation?
    • Cotgreave I.A., and Gerdes R.G. Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation?. Biochem. Biophys. Res. Commun. 242 (1998) 1-9
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 4
    • 0028132836 scopus 로고
    • Redox signaling: nitrosylation and related target interactions of nitric oxide
    • Stamler J.S. Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell 78 (1994) 931-936
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 5
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P., and Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur. J. Biochem. 267 (2000) 4928-4944
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 6
    • 0036249836 scopus 로고    scopus 로고
    • Irreversible thiol oxidation in carbonic anhydrase III: protection by S-glutathiolation and detection in aging rats
    • Mallis R.J., Hamann M.J., Zhao W., Zhang T., Hendrich S., and Thomas J.A. Irreversible thiol oxidation in carbonic anhydrase III: protection by S-glutathiolation and detection in aging rats. Biol. Chem. 383 (2002) 649-662
    • (2002) Biol. Chem. , vol.383 , pp. 649-662
    • Mallis, R.J.1    Hamann, M.J.2    Zhao, W.3    Zhang, T.4    Hendrich, S.5    Thomas, J.A.6
  • 7
    • 3142663363 scopus 로고    scopus 로고
    • S-Glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • Adachi T., Pimentel D.R., Heibeck T., Hou X., Lee Y.J., Jiang B., Ido Y., and Cohen R.A. S-Glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J. Biol. Chem. 279 (2004) 29857-29862
    • (2004) J. Biol. Chem. , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 9
    • 33645806282 scopus 로고    scopus 로고
    • S-Glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells
    • Clavreul N., Adachi T., Pimental D.R., Ido Y., Schoneich C., and Cohen R.A. S-Glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells. FASEB J. 20 (2006) 518-520
    • (2006) FASEB J. , vol.20 , pp. 518-520
    • Clavreul, N.1    Adachi, T.2    Pimental, D.R.3    Ido, Y.4    Schoneich, C.5    Cohen, R.A.6
  • 10
    • 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., Hinks J.A., Tonks N.K., and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423 (2003) 769-773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 11
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.R., Kwon K.S., Kim S.R., and Rhee S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273 (1998) 15366-15372
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 12
    • 0034255470 scopus 로고    scopus 로고
    • Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH
    • Kim J.R., Yoon H.W., Kwon K.S., Lee S.R., and Rhee S.G. Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Anal. Biochem. 283 (2000) 214-221
    • (2000) Anal. Biochem. , vol.283 , pp. 214-221
    • Kim, J.R.1    Yoon, H.W.2    Kwon, K.S.3    Lee, S.R.4    Rhee, S.G.5
  • 13
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • Winterbourn C.C., and Metodiewa D. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic. Biol. Med. 27 (1999) 322-328
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 14
    • 33750953240 scopus 로고    scopus 로고
    • Redox signaling: bioinorganic chemistry at its best
    • Ullrich V., and Kissner R. Redox signaling: bioinorganic chemistry at its best. J. Inorg. Biochem. 100 (2006) 2079-2086
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 2079-2086
    • Ullrich, V.1    Kissner, R.2
  • 15
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins
    • Woo H.A., Jeong W., Chang T.S., Park K.J., Park S.J., Yang J.S., and Rhee S.G. Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. J. Biol. Chem. 280 (2005) 3125-3128
    • (2005) J. Biol. Chem. , vol.280 , pp. 3125-3128
    • Woo, H.A.1    Jeong, W.2    Chang, T.S.3    Park, K.J.4    Park, S.J.5    Yang, J.S.6    Rhee, S.G.7
  • 16
    • 4344672779 scopus 로고    scopus 로고
    • Direct determination of thiol pKa by isothermal titration microcalorimetry
    • Tajc S.G., Tolbert B.S., Basavappa R., and Miller B.L. Direct determination of thiol pKa by isothermal titration microcalorimetry. J. Am. Chem. Soc. 126 (2004) 10508-10509
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 10508-10509
    • Tajc, S.G.1    Tolbert, B.S.2    Basavappa, R.3    Miller, B.L.4
  • 17
    • 33847746679 scopus 로고    scopus 로고
    • Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system
    • Berndt C., Lillig C.H., and Holmgren A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am. J. Physiol. Heart Circ. Physiol. 292 (2007) H1227-H1236
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 19
    • 0026515446 scopus 로고
    • Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression
    • Rao G.N., and Berk B.C. Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression. Circ. Res. 70 (1992) 593-599
    • (1992) Circ. Res. , vol.70 , pp. 593-599
    • Rao, G.N.1    Berk, B.C.2
  • 20
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan M., Yu Z.X., Ferrans V.J., Irani K., and Finkel T. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 270 (1995) 296-299
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 21
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr S., Hallak H., de Boitte A., Lapetina E.G., and Brune B. Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 274 (1999) 9427-9430
    • (1999) J. Biol. Chem. , vol.274 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    de Boitte, A.3    Lapetina, E.G.4    Brune, B.5
  • 24
    • 0028223829 scopus 로고
    • S-Thiolation and irreversible oxidation of sulfhydryls on carbonic anhydrase III during oxidative stress: a method for studying protein modification in intact cells and tissues
    • Lii C.K., Chai Y.C., Zhao W., Thomas J.A., and Hendrich S. S-Thiolation and irreversible oxidation of sulfhydryls on carbonic anhydrase III during oxidative stress: a method for studying protein modification in intact cells and tissues. Arch. Biochem. Biophys. 308 (1994) 231-239
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 231-239
    • Lii, C.K.1    Chai, Y.C.2    Zhao, W.3    Thomas, J.A.4    Hendrich, S.5
  • 25
    • 33645009947 scopus 로고    scopus 로고
    • Quantitative mapping of oxidation-sensitive cysteine residues in SERCA in vivo and in vitro by HPLC-electrospray-tandem MS: selective protein oxidation during biological aging
    • Sharov V.S., Dremina E.S., Galeva N.A., Williams T.D., and Schoneich C. Quantitative mapping of oxidation-sensitive cysteine residues in SERCA in vivo and in vitro by HPLC-electrospray-tandem MS: selective protein oxidation during biological aging. Biochem. J. 394 (2006) 605-615
    • (2006) Biochem. J. , vol.394 , pp. 605-615
    • Sharov, V.S.1    Dremina, E.S.2    Galeva, N.A.3    Williams, T.D.4    Schoneich, C.5
  • 26
    • 0032573507 scopus 로고    scopus 로고
    • Probing cellular protein targets of H2O2 with fluorescein-conjugated iodoacetamide and antibodies to fluorescein
    • Wu Y., Kwon K.S., and Rhee S.G. Probing cellular protein targets of H2O2 with fluorescein-conjugated iodoacetamide and antibodies to fluorescein. FEBS Lett. 440 (1998) 111-115
    • (1998) FEBS Lett. , vol.440 , pp. 111-115
    • Wu, Y.1    Kwon, K.S.2    Rhee, S.G.3
  • 27
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey S.R., and Snyder S.H. The biotin switch method for the detection of S-nitrosylated proteins. Sci. STKE. 2001 (2001) PL1
    • (2001) Sci. STKE. , vol.2001
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 28
    • 34347268109 scopus 로고    scopus 로고
    • Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress
    • Forrester M.T., Foster M.W., and Stamler J.S. Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress. J. Biol. Chem. 282 (2007) 13977-13983
    • (2007) J. Biol. Chem. , vol.282 , pp. 13977-13983
    • Forrester, M.T.1    Foster, M.W.2    Stamler, J.S.3
  • 29
    • 0037155791 scopus 로고    scopus 로고
    • Basal and stimulated protein S-nitrosylation in multiple cell types and tissues
    • Gow A.J., Chen Q., Hess D.T., Day B.J., Ischiropoulos H., and Stamler J.S. Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. J. Biol. Chem. 277 (2002) 9637-9640
    • (2002) J. Biol. Chem. , vol.277 , pp. 9637-9640
    • Gow, A.J.1    Chen, Q.2    Hess, D.T.3    Day, B.J.4    Ischiropoulos, H.5    Stamler, J.S.6
  • 30
    • 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., Engstrom U., Hellman U., Heldin C.H., den Hertog J., and Ostman A. 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 101 (2004) 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    Engstrom, U.5    Hellman, U.6    Heldin, C.H.7    den Hertog, J.8    Ostman, A.9
  • 31
    • 33746445177 scopus 로고    scopus 로고
    • Nitric oxide-GAPDH-Siah: a novel cell death cascade
    • Hara M.R., and Snyder S.H. Nitric oxide-GAPDH-Siah: a novel cell death cascade. Cell. Mol. Neurobiol. 26 (2006) 527-538
    • (2006) Cell. Mol. Neurobiol. , vol.26 , pp. 527-538
    • Hara, M.R.1    Snyder, S.H.2
  • 32
    • 33845600791 scopus 로고    scopus 로고
    • Protein glutathiolation by nitric oxide: an intracellular mechanism regulating redox protein modification
    • West M.B., Hill B.G., Xuan Y.T., and Bhatnagar A. Protein glutathiolation by nitric oxide: an intracellular mechanism regulating redox protein modification. FASEB J. 20 (2006) 1715-1717
    • (2006) FASEB J. , vol.20 , pp. 1715-1717
    • West, M.B.1    Hill, B.G.2    Xuan, Y.T.3    Bhatnagar, A.4
  • 33
    • 0032401864 scopus 로고    scopus 로고
    • Evaluation of methods for the quantitation of cysteines in proteins
    • Wright S.K., and Viola R.E. Evaluation of methods for the quantitation of cysteines in proteins. Anal. Biochem. 265 (1998) 8-14
    • (1998) Anal. Biochem. , vol.265 , pp. 8-14
    • Wright, S.K.1    Viola, R.E.2
  • 35
    • 0029026649 scopus 로고
    • Noninvasive measurement of thiol levels in cells and isolated organs
    • Nohl H., Stolze K., and Weiner L.M. Noninvasive measurement of thiol levels in cells and isolated organs. Methods Enzymol. 251 (1995) 191-203
    • (1995) Methods Enzymol. , vol.251 , pp. 191-203
    • Nohl, H.1    Stolze, K.2    Weiner, L.M.3
  • 36
    • 0023131028 scopus 로고
    • Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. II. Site of labeling with iodoacetamide and its fluorescent derivative
    • Yamashita T., and Kawakita M. Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. II. Site of labeling with iodoacetamide and its fluorescent derivative. J. Biochem. (Tokyo) 101 (1987) 377-385
    • (1987) J. Biochem. (Tokyo) , vol.101 , pp. 377-385
    • Yamashita, T.1    Kawakita, M.2
  • 37
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • Baty J.W., Hampton M.B., and Winterbourn C.C. Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2 (2002) 1261-1266
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 38
    • 31344467471 scopus 로고    scopus 로고
    • A sensitive method for the quantitative measurement of protein thiol modification in response to oxidative stress
    • Landar A., Oh J.Y., Giles N.M., Isom A., Kirk M., Barnes S., and Darley-Usmar V.M. A sensitive method for the quantitative measurement of protein thiol modification in response to oxidative stress. Free Radic. Biol. Med. 40 (2006) 459-468
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 459-468
    • Landar, A.1    Oh, J.Y.2    Giles, N.M.3    Isom, A.4    Kirk, M.5    Barnes, S.6    Darley-Usmar, V.M.7
  • 39
    • 27744480272 scopus 로고    scopus 로고
    • Detection and characterization of protein nitrosothiols
    • Jaffrey S.R. Detection and characterization of protein nitrosothiols. Methods Enzymol. 396 (2005) 105-118
    • (2005) Methods Enzymol. , vol.396 , pp. 105-118
    • Jaffrey, S.R.1
  • 40
    • 11844295419 scopus 로고    scopus 로고
    • S-Nitrosoprotein formation and localization in endothelial cells
    • Yang Y., and Loscalzo J. S-Nitrosoprotein formation and localization in endothelial cells. Proc. Natl. Acad. Sci. USA 102 (2005) 117-122
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 117-122
    • Yang, Y.1    Loscalzo, J.2
  • 42
    • 33746070773 scopus 로고    scopus 로고
    • An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay
    • Huang B., and Chen C. An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay. Free Radic. Biol. Med. 41 (2006) 562-567
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 562-567
    • Huang, B.1    Chen, C.2
  • 43
    • 33746085196 scopus 로고    scopus 로고
    • Methodological vexation about thiol oxidation versus S-nitrosation-a commentary on "An ascorbate-dependent artifact that interferes with the interpretation of the biotin-switch assay"
    • Gladwin M.T., Wang X., and Hogg N. Methodological vexation about thiol oxidation versus S-nitrosation-a commentary on "An ascorbate-dependent artifact that interferes with the interpretation of the biotin-switch assay". Free Radic. Biol. Med. 41 (2006) 557-561
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 557-561
    • Gladwin, M.T.1    Wang, X.2    Hogg, N.3
  • 45
    • 0034641689 scopus 로고    scopus 로고
    • Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation
    • Sullivan D.M., Wehr N.B., Fergusson M.M., Levine R.L., and Finkel T. Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation. Biochemistry 39 (2000) 11121-11128
    • (2000) Biochemistry , vol.39 , pp. 11121-11128
    • Sullivan, D.M.1    Wehr, N.B.2    Fergusson, M.M.3    Levine, R.L.4    Finkel, T.5
  • 46
    • 34548511714 scopus 로고    scopus 로고
    • Detection and identification of S-glutathiolated proteins in endothelial cells exposed to oxidants by a biotin-labeling:liquid chromatographic and MS method
    • (ThP 560)
    • Clavreul N., Dauly C., Huang H., Sethuraman M., McComb M., Costello C.E., and Cohen R.A. Detection and identification of S-glutathiolated proteins in endothelial cells exposed to oxidants by a biotin-labeling:liquid chromatographic and MS method. J. Am. Soc. Mass Spectrom. 17 Suppl 1 (2006) 121S (ThP 560)
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , Issue.SUPPL. 1
    • Clavreul, N.1    Dauly, C.2    Huang, H.3    Sethuraman, M.4    McComb, M.5    Costello, C.E.6    Cohen, R.A.7
  • 47
    • 2642576571 scopus 로고    scopus 로고
    • Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols
    • Sethuraman M., McComb M.E., Heibeck T., Costello C.E., and Cohen R.A. Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols. Mol. Cell. Proteomics 3 (2004) 273-278
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 273-278
    • Sethuraman, M.1    McComb, M.E.2    Heibeck, T.3    Costello, C.E.4    Cohen, R.A.5
  • 48
    • 33847074105 scopus 로고    scopus 로고
    • Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotope-coded affinity tags and mass spectrometry
    • Sethuraman M., Clavreul N., Huang H., McComb M.E., Costello C.E., and Cohen R.A. Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotope-coded affinity tags and mass spectrometry. Free Radic. Biol. Med. 42 (2007) 823-829
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 823-829
    • Sethuraman, M.1    Clavreul, N.2    Huang, H.3    McComb, M.E.4    Costello, C.E.5    Cohen, R.A.6
  • 49
    • 11144252625 scopus 로고    scopus 로고
    • Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures
    • Sethuraman M., McComb M.E., Huang H., Huang S., Heibeck T., Costello C.E., and Cohen R.A. Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 3 (2004) 1228-1233
    • (2004) J. Proteome Res. , vol.3 , pp. 1228-1233
    • Sethuraman, M.1    McComb, M.E.2    Huang, H.3    Huang, S.4    Heibeck, T.5    Costello, C.E.6    Cohen, R.A.7
  • 50
    • 33746260272 scopus 로고    scopus 로고
    • Detailed map of oxidative post-translational modifications of human p21ras using fourier transform mass spectrometry
    • Zhao C., Sethuraman M., Clavreul N., Kaur P., Cohen R.A., and O'Connor P.B. Detailed map of oxidative post-translational modifications of human p21ras using fourier transform mass spectrometry. Anal. Chem. 78 (2006) 5134-5142
    • (2006) Anal. Chem. , vol.78 , pp. 5134-5142
    • Zhao, C.1    Sethuraman, M.2    Clavreul, N.3    Kaur, P.4    Cohen, R.A.5    O'Connor, P.B.6


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