메뉴 건너뛰기




Volumn 92, Issue , 2013, Pages 204-215

Non-enzymatic modifications in metallothioneins connected to lipid membrane damages: Structural and biomimetic studies under reductive radical stress

Author keywords

Gamma irradiation; Metal binding; Metallothioneins; Radical damage; Raman spectroscopy; Trans lipids

Indexed keywords

METALLOTHIONEIN; TRANS FATTY ACID;

EID: 84886950912     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.02.005     Document Type: Article
Times cited : (16)

References (64)
  • 1
    • 0025314685 scopus 로고
    • Role of oxygen free radicals in carcinogenesis and brain ischemia
    • Floyd R.A. Role of oxygen free radicals in carcinogenesis and brain ischemia. FASEB J 1990, 4(9):2587-2597.
    • (1990) FASEB J , vol.4 , Issue.9 , pp. 2587-2597
    • Floyd, R.A.1
  • 2
    • 0001883969 scopus 로고
    • Raven Press, New York, J.I. Gallin, I.M. Goldestein, R. Snyderman (Eds.)
    • Klebanoff S.F. Inflammation: Basic Principles and Clinical Correlates 1988, vol. 391:391-443. Raven Press, New York. J.I. Gallin, I.M. Goldestein, R. Snyderman (Eds.).
    • (1988) Inflammation: Basic Principles and Clinical Correlates , vol.391 , pp. 391-443
    • Klebanoff, S.F.1
  • 3
    • 0025238543 scopus 로고
    • Free radicals: their involvement in disease processes
    • Lunec J. Free radicals: their involvement in disease processes. Ann Clin Biochem 1990, 27(Pt3):173-182.
    • (1990) Ann Clin Biochem , vol.27 , Issue.PART 3 , pp. 173-182
    • Lunec, J.1
  • 5
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • Hawkins C.L., Davies M.J. Generation and propagation of radical reactions on proteins. Biochim Biophys Acta 2001, 1504(2-3):196-219.
    • (2001) Biochim Biophys Acta , vol.1504 , Issue.2-3 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 6
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • Garrison W.M. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem Rev 1987, 87(2):381-398.
    • (1987) Chem Rev , vol.87 , Issue.2 , pp. 381-398
    • Garrison, W.M.1
  • 7
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn C.C., Hampton M.B. Thiol chemistry and specificity in redox signaling. Free Radic Biol Med 2008, 45:549-561.
    • (2008) Free Radic Biol Med , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 9
    • 57649198018 scopus 로고    scopus 로고
    • Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability
    • Janssen-Heininger
    • Janssen-Heininger, Paige J.S., Xu G., Stancevic B., Jaffrey S.R. Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability. Chem Biol 2008, 15:307-316.
    • (2008) Chem Biol , vol.15 , pp. 307-316
    • Paige, J.S.1    Xu, G.2    Stancevic, B.3    Jaffrey, S.R.4
  • 11
    • 0036160119 scopus 로고    scopus 로고
    • Evidence in support of a concept or reductive stress
    • Lipinski B. Evidence in support of a concept or reductive stress. Br J Nutr 2002, 87(1):93-94.
    • (2002) Br J Nutr , vol.87 , Issue.1 , pp. 93-94
    • Lipinski, B.1
  • 12
    • 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. Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics. Mass Spectrom Rev 2005, 24(1):55-99.
    • (2005) Mass Spectrom Rev , vol.24 , Issue.1 , pp. 55-99
    • Dalle-Donne, I.1    Scaloni, A.2    Giustarini, D.3    Cavarra, E.4    Tell, G.5    Lungarella, G.6
  • 13
    • 0026448524 scopus 로고
    • Failla memorial lecture. Redox, radiation, and reductive bioactivation
    • Adams G.E. Failla memorial lecture. Redox, radiation, and reductive bioactivation. Radiat Res 1992, 132(2):129-139.
    • (1992) Radiat Res , vol.132 , Issue.2 , pp. 129-139
    • Adams, G.E.1
  • 14
    • 77953125913 scopus 로고    scopus 로고
    • Involvement of reductive stress in the cardiomyopathy in transgenic mice with cardiac-specific overexpression of heat shock protein 27
    • Zhang X., Min X., Li C., Benjamin I.J., Qian B., Zhang X., et al. Involvement of reductive stress in the cardiomyopathy in transgenic mice with cardiac-specific overexpression of heat shock protein 27. Hypertension 2010, 55:1412-1417.
    • (2010) Hypertension , vol.55 , pp. 1412-1417
    • Zhang, X.1    Min, X.2    Li, C.3    Benjamin, I.J.4    Qian, B.5    Zhang, X.6
  • 16
    • 0035036447 scopus 로고    scopus 로고
    • Electrophilic methyl groups present in the diet ameliorate pathological states induced by reductive and oxidative stress: an hypothesis
    • Ghyczy M., Boros M. Electrophilic methyl groups present in the diet ameliorate pathological states induced by reductive and oxidative stress: an hypothesis. Br J Nutr 2001, 85(4):409-414.
    • (2001) Br J Nutr , vol.85 , Issue.4 , pp. 409-414
    • Ghyczy, M.1    Boros, M.2
  • 17
    • 0030787354 scopus 로고    scopus 로고
    • +, free radicals, and vascular dysfunction in early diabetes mellitus
    • +, free radicals, and vascular dysfunction in early diabetes mellitus. Diabetologia 1997, 40(2):S115-S117.
    • (1997) Diabetologia , vol.40 , Issue.2
    • Ido, Y.1    Kilo, C.2    Williamson, J.R.3
  • 18
    • 0026448524 scopus 로고
    • Redox, radiation, and reductive bioactivation
    • Adams G.E. Redox, radiation, and reductive bioactivation. Radiat Res 1992, 132:129-139.
    • (1992) Radiat Res , vol.132 , pp. 129-139
    • Adams, G.E.1
  • 19
    • 34547681313 scopus 로고    scopus 로고
    • Human αB-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice
    • Rajasekaran N.S., Connell P., Christians E.S., Yan L.J., Taylor R.P., Orosz A., et al. Human αB-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice. Cell 2007, 130:427-439.
    • (2007) Cell , vol.130 , pp. 427-439
    • Rajasekaran, N.S.1    Connell, P.2    Christians, E.S.3    Yan, L.J.4    Taylor, R.P.5    Orosz, A.6
  • 23
    • 52049096677 scopus 로고    scopus 로고
    • The reductive desulfurization of Met and Cys residues in bovine RNase A is associated with trans lipids formation in a mimetic model of biological membranes
    • Ferreri C., Chatgilialoglu C., Torreggiani A., Salzano A.M., Renzone G., Scaloni A. The reductive desulfurization of Met and Cys residues in bovine RNase A is associated with trans lipids formation in a mimetic model of biological membranes. J Proteome Res 2008, 7(5):2007-2015.
    • (2008) J Proteome Res , vol.7 , Issue.5 , pp. 2007-2015
    • Ferreri, C.1    Chatgilialoglu, C.2    Torreggiani, A.3    Salzano, A.M.4    Renzone, G.5    Scaloni, A.6
  • 25
    • 0034679015 scopus 로고    scopus 로고
    • Cis-trans isomerization of monounsaturated fatty acid residues in phospholipids by thiyl radicals
    • Chatgilialoglu C., Ferreri C., Ballestri M., Mulazzani Q.G., Landi L. Cis-trans isomerization of monounsaturated fatty acid residues in phospholipids by thiyl radicals. J Am Chem Soc 2000, 122(19):4593-4601.
    • (2000) J Am Chem Soc , vol.122 , Issue.19 , pp. 4593-4601
    • Chatgilialoglu, C.1    Ferreri, C.2    Ballestri, M.3    Mulazzani, Q.G.4    Landi, L.5
  • 26
    • 0028269651 scopus 로고
    • Steady-state fluorescence polarization study of structurally defined phospholipids from liver mitochondria of rats fed elaidic acid
    • Wolff R.L., Entressangles B. Steady-state fluorescence polarization study of structurally defined phospholipids from liver mitochondria of rats fed elaidic acid. Biochem Biophys Acta 1994, 1211(2):198-206.
    • (1994) Biochem Biophys Acta , vol.1211 , Issue.2 , pp. 198-206
    • Wolff, R.L.1    Entressangles, B.2
  • 27
    • 66349121915 scopus 로고    scopus 로고
    • Zinc and cadmium complexes of a plant metallothionein under radical stress: desulfurisation reactions associated with the formation of trans-lipids in model membranes
    • Torreggiani A., Domènech J., Orihuela R., Ferreri C., Atrian S., Capdevila M., et al. Zinc and cadmium complexes of a plant metallothionein under radical stress: desulfurisation reactions associated with the formation of trans-lipids in model membranes. Chem Eur J 2009, 15(24):6015-6024.
    • (2009) Chem Eur J , vol.15 , Issue.24 , pp. 6015-6024
    • Torreggiani, A.1    Domènech, J.2    Orihuela, R.3    Ferreri, C.4    Atrian, S.5    Capdevila, M.6
  • 28
    • 82355169735 scopus 로고    scopus 로고
    • State-of-the-art of metallothioneins at the beginning of the 21st century
    • Capdevila M., Bofill R., Palacios O., Atrian S. State-of-the-art of metallothioneins at the beginning of the 21st century. Coordin Chem Rev 2012, 256(1-2):46-62.
    • (2012) Coordin Chem Rev , vol.256 , Issue.1-2 , pp. 46-62
    • Capdevila, M.1    Bofill, R.2    Palacios, O.3    Atrian, S.4
  • 29
    • 80755152510 scopus 로고    scopus 로고
    • Zn- and Cu-thioneins: a functional classification for metallothioneins?
    • Palacios O., Atrian S., Capdevila M. Zn- and Cu-thioneins: a functional classification for metallothioneins?. J Biol Inorg Chem 2011, 16(7):991-1009.
    • (2011) J Biol Inorg Chem , vol.16 , Issue.7 , pp. 991-1009
    • Palacios, O.1    Atrian, S.2    Capdevila, M.3
  • 31
    • 39149113167 scopus 로고    scopus 로고
    • Metallothioneins with unusual residues: histidines as modulators of zinc affinity and reactivity
    • Blindauer C.A. Metallothioneins with unusual residues: histidines as modulators of zinc affinity and reactivity. J Inorg Biochem 2008, 102(3):507-521.
    • (2008) J Inorg Biochem , vol.102 , Issue.3 , pp. 507-521
    • Blindauer, C.A.1
  • 32
    • 0033571671 scopus 로고    scopus 로고
    • Nitric oxide induces Zn2+ release from metallothionein by destroying zinc-sulphur clusters without concomitant formation of S-nitrosothiol
    • Aravindakumar C.T., Ceulemans J., De Ley M. Nitric oxide induces Zn2+ release from metallothionein by destroying zinc-sulphur clusters without concomitant formation of S-nitrosothiol. Biochem J 1999, 344(Pt1):253-258.
    • (1999) Biochem J , vol.344 , Issue.PART 1 , pp. 253-258
    • Aravindakumar, C.T.1    Ceulemans, J.2    De Ley, M.3
  • 33
    • 0033816949 scopus 로고    scopus 로고
    • Copper-release from yeast Cu(I)-metallothionein by nitric oxide (NO)
    • Hartmann H.J., Weser U. Copper-release from yeast Cu(I)-metallothionein by nitric oxide (NO). Biometals 2000, 13(2):153-156.
    • (2000) Biometals , vol.13 , Issue.2 , pp. 153-156
    • Hartmann, H.J.1    Weser, U.2
  • 34
    • 0031954785 scopus 로고    scopus 로고
    • Metallothionein and apoptosis in primary human hepatocellular carcinoma and metastatic adenocarcinoma
    • Deng D.X., Chakrabarti S., Waalkes M.P., Cherian M.G. Metallothionein and apoptosis in primary human hepatocellular carcinoma and metastatic adenocarcinoma. Histopathology 1998, 32(4):340-347.
    • (1998) Histopathology , vol.32 , Issue.4 , pp. 340-347
    • Deng, D.X.1    Chakrabarti, S.2    Waalkes, M.P.3    Cherian, M.G.4
  • 35
    • 0035031486 scopus 로고    scopus 로고
    • Inhibition of hypoxia/reoxygenation-induced apoptosis in metallothionein-overexpressing cardiomyocytes
    • Wang G.W., Zhou Z., Klein J.B., Kang Y.J. Inhibition of hypoxia/reoxygenation-induced apoptosis in metallothionein-overexpressing cardiomyocytes. Am J Physiol Heart Circ Physiol 2001, 280(5):H2292-H2299.
    • (2001) Am J Physiol Heart Circ Physiol , vol.280 , Issue.5
    • Wang, G.W.1    Zhou, Z.2    Klein, J.B.3    Kang, Y.J.4
  • 36
    • 0035282221 scopus 로고    scopus 로고
    • Nitric oxide-dependent pro-oxidant and pro-apoptotic effect of metallothioneins in HL-60 cells challenged with cupric nitrilotriacetate
    • Liu A., Kawai K., Tyurin V.A., Tyurina Y.Y., Borisenko G.G., Fabisiak J.P., et al. Nitric oxide-dependent pro-oxidant and pro-apoptotic effect of metallothioneins in HL-60 cells challenged with cupric nitrilotriacetate. Biochem J 2001, 354(Pt2):397-406.
    • (2001) Biochem J , vol.354 , Issue.PART 2 , pp. 397-406
    • Liu, A.1    Kawai, K.2    Tyurin, V.A.3    Tyurina, Y.Y.4    Borisenko, G.G.5    Fabisiak, J.P.6
  • 37
    • 11144281841 scopus 로고    scopus 로고
    • A plant type 2 metallothionein (MT) from cork tissue responds to oxidative stress
    • Mir G., Domènech J., Huguet G., Guo W., Goldsbrough P., Atrian S., et al. A plant type 2 metallothionein (MT) from cork tissue responds to oxidative stress. J Exp Bot 2004, 55(408):2483-2493.
    • (2004) J Exp Bot , vol.55 , Issue.408 , pp. 2483-2493
    • Mir, G.1    Domènech, J.2    Huguet, G.3    Guo, W.4    Goldsbrough, P.5    Atrian, S.6
  • 38
    • 33745940302 scopus 로고    scopus 로고
    • Plant metallothionein domains: functional insight into physiological metal binding and protein folding
    • Domènech J., Mir G., Huguet G., Capdevila M., Molinas M., Atrian S. Plant metallothionein domains: functional insight into physiological metal binding and protein folding. Biochimie 2006, 88(6):583-593.
    • (2006) Biochimie , vol.88 , Issue.6 , pp. 583-593
    • Domènech, J.1    Mir, G.2    Huguet, G.3    Capdevila, M.4    Molinas, M.5    Atrian, S.6
  • 39
    • 34547430481 scopus 로고    scopus 로고
    • The Cd(II)-binding abilities of recombinant Quercus suber metallothionein, QsMT: bridging the gap between phytochelatins and metallothioneins
    • Domenech J., Orihuela R., Mir G., Molinas M., Atrian S., Capdevila M. The Cd(II)-binding abilities of recombinant Quercus suber metallothionein, QsMT: bridging the gap between phytochelatins and metallothioneins. J Biol Inorg Chem 2007, 12(6):867-882.
    • (2007) J Biol Inorg Chem , vol.12 , Issue.6 , pp. 867-882
    • Domenech, J.1    Orihuela, R.2    Mir, G.3    Molinas, M.4    Atrian, S.5    Capdevila, M.6
  • 40
    • 34250317473 scopus 로고    scopus 로고
    • Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: insights by vibrational spectroscopy
    • Domènech J., Tinti A., Capdevila M., Atrian S., Torreggiani A. Structural study of the zinc and cadmium complexes of a type 2 plant (Quercus suber) metallothionein: insights by vibrational spectroscopy. Biopolymers 2007, 86(3):240-248.
    • (2007) Biopolymers , vol.86 , Issue.3 , pp. 240-248
    • Domènech, J.1    Tinti, A.2    Capdevila, M.3    Atrian, S.4    Torreggiani, A.5
  • 41
    • 84873868531 scopus 로고    scopus 로고
    • The sea urchin metallothionein system: comparative evaluation of the SpMTA and SpMTB metal-binding preferences
    • Tomas M., Domènech J., Capdevila M., Bofill R., Atrian S. The sea urchin metallothionein system: comparative evaluation of the SpMTA and SpMTB metal-binding preferences. FEBS Open Bio 2013, 3:89-100.
    • (2013) FEBS Open Bio , vol.3 , pp. 89-100
    • Tomas, M.1    Domènech, J.2    Capdevila, M.3    Bofill, R.4    Atrian, S.5
  • 42
    • 70449719117 scopus 로고    scopus 로고
    • Caenorhabditis elegans metallothionein isoform specificity-metal binding abilities and the role of histidine in CeMT1 and CeMT2
    • Bofill R., Orihuela R., Romagosa M., Domenech J., Atrian S., Capdevila M. Caenorhabditis elegans metallothionein isoform specificity-metal binding abilities and the role of histidine in CeMT1 and CeMT2. FEBS J 2009, 276(23):7040-7056.
    • (2009) FEBS J , vol.276 , Issue.23 , pp. 7040-7056
    • Bofill, R.1    Orihuela, R.2    Romagosa, M.3    Domenech, J.4    Atrian, S.5    Capdevila, M.6
  • 43
    • 40849117969 scopus 로고    scopus 로고
    • Comparative insight into the Zn(II)-, Cd(II)- and Cu(I)-binding features of the protozoan Tetrahymena pyriformis MT1 metallothionein
    • Domènech J., Bofill R., Tinti A., Torreggiani A., Atrian S., Capdevila M. Comparative insight into the Zn(II)-, Cd(II)- and Cu(I)-binding features of the protozoan Tetrahymena pyriformis MT1 metallothionein. Biochim Biophys Acta 2008, 1784(4):693-704.
    • (2008) Biochim Biophys Acta , vol.1784 , Issue.4 , pp. 693-704
    • Domènech, J.1    Bofill, R.2    Tinti, A.3    Torreggiani, A.4    Atrian, S.5    Capdevila, M.6
  • 46
    • 0024289505 scopus 로고
    • Micromolar protein concentrations and metalloprotein stoichiometries obtained by inductively coupled plasma atomic emission spectrometric determination of sulfur
    • Bongers J., Walton C.D., Richardson D.E., Bell J.U. Micromolar protein concentrations and metalloprotein stoichiometries obtained by inductively coupled plasma atomic emission spectrometric determination of sulfur. Anal Chem 1988, 60(24):2683-2686.
    • (1988) Anal Chem , vol.60 , Issue.24 , pp. 2683-2686
    • Bongers, J.1    Walton, C.D.2    Richardson, D.E.3    Bell, J.U.4
  • 48
    • 77953659540 scopus 로고    scopus 로고
    • Raman spectroscopy a promising technique for investigations of metallothioneins
    • Torreggiani A., Tinti A. Raman spectroscopy a promising technique for investigations of metallothioneins. Metallomics 2010, 2(4):246-260.
    • (2010) Metallomics , vol.2 , Issue.4 , pp. 246-260
    • Torreggiani, A.1    Tinti, A.2
  • 49
    • 0002546264 scopus 로고    scopus 로고
    • Free radical scavenging actions of metallothionein isoforms I and II
    • Kumari M.V., Hiramatsu M., Ebadi M. Free radical scavenging actions of metallothionein isoforms I and II. Free Radic Res 1998, 29(2):93-101.
    • (1998) Free Radic Res , vol.29 , Issue.2 , pp. 93-101
    • Kumari, M.V.1    Hiramatsu, M.2    Ebadi, M.3
  • 50
    • 34548753956 scopus 로고    scopus 로고
    • Toward a property/function relationship for metallothioneins: histidine coordination and unusual cluster composition in a zinc-metallothionein from plants
    • Leszczyszyn O.I., Schmid R., Blindauer C.A. Toward a property/function relationship for metallothioneins: histidine coordination and unusual cluster composition in a zinc-metallothionein from plants. Proteins 2007, 68(4):922-935.
    • (2007) Proteins , vol.68 , Issue.4 , pp. 922-935
    • Leszczyszyn, O.I.1    Schmid, R.2    Blindauer, C.A.3
  • 51
    • 13544268437 scopus 로고    scopus 로고
    • Influence of chloride ligands on the structure of Zn- and Cd-metallothionein species
    • Villarreal L., Tio L., Atrian S., Capdevila M. Influence of chloride ligands on the structure of Zn- and Cd-metallothionein species. Arch Biochem Biophys 2005, 435(2):331-335.
    • (2005) Arch Biochem Biophys , vol.435 , Issue.2 , pp. 331-335
    • Villarreal, L.1    Tio, L.2    Atrian, S.3    Capdevila, M.4
  • 52
    • 58149340121 scopus 로고    scopus 로고
    • Raman study of in vivo synthesized Zn(II)-metallothionein complexes: structural insight into metal clusters and protein folding
    • Torreggiani A., Domènech J., Atrian S., Capdevila M., Tinti A. Raman study of in vivo synthesized Zn(II)-metallothionein complexes: structural insight into metal clusters and protein folding. Biopolymers 2008, 89(12):1114-1124.
    • (2008) Biopolymers , vol.89 , Issue.12 , pp. 1114-1124
    • Torreggiani, A.1    Domènech, J.2    Atrian, S.3    Capdevila, M.4    Tinti, A.5
  • 53
    • 78651382056 scopus 로고    scopus 로고
    • Torreggiani A Research progress on metallothioneins: insights into structure, metal binding properties and molecular function by spectroscopic investigations
    • Nova Science Publishers Inc, NY, T.S. Nemeth (Ed.)
    • Domenech J., Tinti A. Torreggiani A Research progress on metallothioneins: insights into structure, metal binding properties and molecular function by spectroscopic investigations. Biopolymer research trends 2008, 11-48. Nova Science Publishers Inc, NY. T.S. Nemeth (Ed.).
    • (2008) Biopolymer research trends , pp. 11-48
    • Domenech, J.1    Tinti, A.2
  • 54
    • 70450186865 scopus 로고    scopus 로고
    • Structural modifications in metal complexes of a plant metallothionein caused by reductive radical stress: a Raman study
    • Torreggiani A., Domènech J., Tinti A. Structural modifications in metal complexes of a plant metallothionein caused by reductive radical stress: a Raman study. J Raman Spectrosc 2009, 40(11):1687-1693.
    • (2009) J Raman Spectrosc , vol.40 , Issue.11 , pp. 1687-1693
    • Torreggiani, A.1    Domènech, J.2    Tinti, A.3
  • 56
    • 84896578618 scopus 로고    scopus 로고
    • Free radicals and proteins, research progress on sulfur-containing proteins under radical stress: an helpful contribute from Raman spectroscopy
    • Nova Science Publisher, D. Kozyrev, V. Slutsky (Eds.)
    • Torreggiani A. Free radicals and proteins, research progress on sulfur-containing proteins under radical stress: an helpful contribute from Raman spectroscopy. Handbok of free radicals: formation, types and effects 2009, 377-441. Nova Science Publisher. D. Kozyrev, V. Slutsky (Eds.).
    • (2009) Handbok of free radicals: formation, types and effects , pp. 377-441
    • Torreggiani, A.1
  • 58
    • 0002916557 scopus 로고    scopus 로고
    • Wiley, Chichester, Z.B. Alfassi (Ed.)
    • Wardman P. S-centered radicals 1999, 289-309. Wiley, Chichester. Z.B. Alfassi (Ed.).
    • (1999) S-centered radicals , pp. 289-309
    • Wardman, P.1
  • 59
    • 0033230043 scopus 로고    scopus 로고
    • Glutathione and its role in cellular functions
    • Sies H. Glutathione and its role in cellular functions. Free Radical Biol Med 1999, 27(9-10):916-921.
    • (1999) Free Radical Biol Med , vol.27 , Issue.9-10 , pp. 916-921
    • Sies, H.1
  • 60
    • 80052606544 scopus 로고    scopus 로고
    • Combined Raman and IR spectroscopic study on the radical-based modifications of methionine
    • Torreggiani A., Barata-Vallejo S., Chatgilialoglu C. Combined Raman and IR spectroscopic study on the radical-based modifications of methionine. Anal Bioanal Chem 2011, 401:1231-1239.
    • (2011) Anal Bioanal Chem , vol.401 , pp. 1231-1239
    • Torreggiani, A.1    Barata-Vallejo, S.2    Chatgilialoglu, C.3
  • 61
    • 34249669851 scopus 로고    scopus 로고
    • The sulfhydryl radical (HS(.)/S(.-)): a contender for the isomerization of double bonds in membrane lipids
    • Lykakis I.N., Ferreri C., Chatgilialoglu C. The sulfhydryl radical (HS(.)/S(.-)): a contender for the isomerization of double bonds in membrane lipids. Angew Chem Int Ed 2007, 46(11):1914-1916.
    • (2007) Angew Chem Int Ed , vol.46 , Issue.11 , pp. 1914-1916
    • Lykakis, I.N.1    Ferreri, C.2    Chatgilialoglu, C.3
  • 62
    • 61549100406 scopus 로고
    • The inactivation of some enzymes in aqueous solution by atomic hydrogen
    • Academic Press, London, G.O. Phillips (Ed.)
    • Stein G. The inactivation of some enzymes in aqueous solution by atomic hydrogen. Energetic and Mechanisms in Radiation Biology 1968, 467-477. Academic Press, London. G.O. Phillips (Ed.).
    • (1968) Energetic and Mechanisms in Radiation Biology , pp. 467-477
    • Stein, G.1
  • 63
    • 0022978990 scopus 로고
    • Raman, infrared, and circular-dichroism spectroscopic studies on metallothionein - a predominantly turn-containing protein
    • Pande J., Pande C., Gilg D., Vasak M., Callender R., Kägi J.H.R. Raman, infrared, and circular-dichroism spectroscopic studies on metallothionein - a predominantly turn-containing protein. Biochemistry 1986, 25:5526.
    • (1986) Biochemistry , vol.25 , pp. 5526
    • Pande, J.1    Pande, C.2    Gilg, D.3    Vasak, M.4    Callender, R.5    Kägi, J.H.R.6
  • 64
    • 79958177298 scopus 로고    scopus 로고
    • Use of Raman spectroscopy for the identification of radical-mediated damages in human serum albumin
    • Jurasekova Z., Tinti A., Torreggiani A. Use of Raman spectroscopy for the identification of radical-mediated damages in human serum albumin. Anal Bioanal Chem 2011, 400:2921-2931.
    • (2011) Anal Bioanal Chem , vol.400 , pp. 2921-2931
    • Jurasekova, Z.1    Tinti, A.2    Torreggiani, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.