메뉴 건너뛰기




Volumn 268, Issue 5, 1997, Pages 869-885

The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9 Å resolution

Author keywords

Crystal structure; Glutathione peroxidase; Human plasma; Patterson search; Selenoprotein

Indexed keywords

GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROPEROXIDE; SELENOCYSTEINE; THIOREDOXIN;

EID: 0031584269     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1005     Document Type: Article
Times cited : (148)

References (67)
  • 1
    • 0024496830 scopus 로고
    • Antihuman plasma glutathione peroxidase antibodies: Immunologic investigation to determine plasma glutathione peroxidase protein and selenium content in plasma
    • Avissar N., Whitin J. C., Allen P. Z., Plamer I. S., Cohen H. J. Antihuman plasma glutathione peroxidase antibodies: immunologic investigation to determine plasma glutathione peroxidase protein and selenium content in plasma. Blood. 73:1989a;318-323.
    • (1989) Blood , vol.73 , pp. 318-323
    • Avissar, N.1    Whitin, J.C.2    Allen, P.Z.3    Plamer, I.S.4    Cohen, H.J.5
  • 2
  • 3
    • 0026326603 scopus 로고
    • Partial sequence of human plasma glutathione peroxidase and immunologic identification of milk glutathione peroxidase as the plasma enzyme
    • Avissar N., Slemmon J. R., Palmer I. S., Cohen H. J. Partial sequence of human plasma glutathione peroxidase and immunologic identification of milk glutathione peroxidase as the plasma enzyme. J. Nutr. 121:1991;1243-1249.
    • (1991) J. Nutr. , vol.121 , pp. 1243-1249
    • Avissar, N.1    Slemmon, J.R.2    Palmer, I.S.3    Cohen, H.J.4
  • 4
    • 0028232438 scopus 로고
    • Extracellular glutathione peroxidase mRNA and protein in human cell lines
    • Avissar N., Kerl E. A., Baker S. S., Cohen H. J. Extracellular glutathione peroxidase mRNA and protein in human cell lines. Arch. Biochem. Biophys. 309:1994;239-246.
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 239-246
    • Avissar, N.1    Kerl, E.A.2    Baker, S.S.3    Cohen, H.J.4
  • 5
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G. J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 6
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Björnstedt M., Xue J., Huang W., Åkesson B., Holmgren A. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J. Biol. Chem. 269:1994;29382-29384.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29382-29384
    • Björnstedt, M.1    Xue, J.2    Huang, W.3    Åkesson, B.4    Holmgren, A.5
  • 7
    • 0023390076 scopus 로고
    • Properties of glutathione peroxidase isolated from human plasma
    • Broderick D. J., Deagen J. T., Whanger P. D. Properties of glutathione peroxidase isolated from human plasma. J. Inorg. Biochem. 30:1987;299-308.
    • (1987) J. Inorg. Biochem. , vol.30 , pp. 299-308
    • Broderick, D.J.1    Deagen, J.T.2    Whanger, P.D.3
  • 8
    • 0024279342 scopus 로고
    • Crystallographic refinement by simulated annealing. Application to a 2.8 Å resolution structure of aspartate aminotransferase
    • Brünger A. T. Crystallographic refinement by simulated annealing. Application to a 2.8 Å resolution structure of aspartate aminotransferase. J. Mol. Biol. 203:1988;803-816.
    • (1988) J. Mol. Biol. , vol.203 , pp. 803-816
    • Brünger, A.T.1
  • 9
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on Patterson correlation refinement
    • Brünger A. T. Extension of molecular replacement: a new search strategy based on Patterson correlation refinement. Acta Crystallog. sect. A. 46:1990;46-57.
    • (1990) Acta Crystallog. Sect. A , vol.46 , pp. 46-57
    • Brünger, A.T.1
  • 11
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A. T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992b;472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 12
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione peroxidase gene: The selenocysteine in the active site is encoded by the "termination" codon, TGA
    • Chambers I., Frampton J., Goldfarb P., Affara N., McBain W., Harrison P. R. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the "termination" codon, TGA. EMBO J. 5:1986;1221-1227.
    • (1986) EMBO J. , vol.5 , pp. 1221-1227
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    McBain, W.5    Harrison, P.R.6
  • 13
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou P. Y., Fasman F. D. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47:1978;251-276.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, F.D.2
  • 14
    • 0026773732 scopus 로고
    • Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents
    • Chu F.-F., Esworthy R. S., Doroshow J. H., Doan K., Liu X.-F. Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood. 79:1992;3233-3238.
    • (1992) Blood , vol.79 , pp. 3233-3238
    • Chu, F.-F.1    Esworthy, R.S.2    Doroshow, J.H.3    Doan, K.4    Liu, X.-F.5
  • 15
    • 0027536023 scopus 로고
    • Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI
    • Chu F.-F., Doroshow J. H., Esworthy R. S. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J. Biol. Chem. 268:1993;2571-2576.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2571-2576
    • Chu, F.-F.1    Doroshow, J.H.2    Esworthy, R.S.3
  • 16
    • 0000546402 scopus 로고
    • Accurate bond and angle parameters for X-ray structure refinement
    • Engh R., Huber R. Accurate bond and angle parameters for X-ray structure refinement. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Engh, R.1    Huber, R.2
  • 17
    • 0020775636 scopus 로고
    • The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution
    • Epp O., Ladenstein R., Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur. J. Biochem. 133:1983;51-69.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 51-69
    • Epp, O.1    Ladenstein, R.2    Wendel, A.3
  • 18
    • 0025754084 scopus 로고
    • Characterization and partial amino acid sequence of human plasma glutathione peroxidase
    • Esworthy R. S., Chu F.-F., Paxton R., Akman S., Doroshow J. Characterization and partial amino acid sequence of human plasma glutathione peroxidase. Arch. Biochem. Biophys. 286:1991;330-336.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 330-336
    • Esworthy, R.S.1    Chu, F.-F.2    Paxton, R.3    Akman, S.4    Doroshow, J.5
  • 20
    • 0028122601 scopus 로고
    • Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase
    • Esworthy R. S., Doan K., Doroshow J. H., Chu F.-F. Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase. Gene. 144:1994;317-318.
    • (1994) Gene , vol.144 , pp. 317-318
    • Esworthy, R.S.1    Doan, K.2    Doroshow, J.H.3    Chu, F.-F.4
  • 21
    • 0000704119 scopus 로고
    • The selenoprotein glutathione peroxidase
    • New York: John Wiley & Sons
    • Flohé L. The selenoprotein glutathione peroxidase. Glutathione. 1989;John Wiley & Sons, New York.
    • (1989) Glutathione
    • Flohé, L.1
  • 23
    • 0018449709 scopus 로고
    • Rat liver cytosolic glutathione peroxidase: Reactivity with linoleic acid hydroperoxide and cumene hydroperoxide
    • Forstrom J. W., Stults F. H., Tappel A. L. Rat liver cytosolic glutathione peroxidase: reactivity with linoleic acid hydroperoxide and cumene hydroperoxide. Arch. Biochem. Biophys. 193:1978a;51-55.
    • (1978) Arch. Biochem. Biophys. , vol.193 , pp. 51-55
    • Forstrom, J.W.1    Stults, F.H.2    Tappel, A.L.3
  • 24
    • 0017889205 scopus 로고
    • Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine
    • Forstrom J. W., Zakowski J. J., Tappel A. L. Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine. Biochemistry. 17:1978b;2639-2644.
    • (1978) Biochemistry , vol.17 , pp. 2639-2644
    • Forstrom, J.W.1    Zakowski, J.J.2    Tappel, A.L.3
  • 25
    • 0026748829 scopus 로고
    • Selenium-dependent glutathione peroxidase from ovine and bovine erythrocytes occur as longer chain forms than previously recognized
    • Gettins P., Dyal D., Crews B. Selenium-dependent glutathione peroxidase from ovine and bovine erythrocytes occur as longer chain forms than previously recognized. Arch. Biochem. Biophys. 294:1992;511-518.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 511-518
    • Gettins, P.1    Dyal, D.2    Crews, B.3
  • 27
    • 0000980729 scopus 로고
    • Representation of phase probability distributions for simplified combination of independent phase information
    • Hendrickson W. A., Lattman E. E. Representation of phase probability distributions for simplified combination of independent phase information. Acta Crystallog. sect. B. 20:1970;136-143.
    • (1970) Acta Crystallog. Sect. B , vol.20 , pp. 136-143
    • Hendrickson, W.A.1    Lattman, E.E.2
  • 28
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson W., Horton J. R., LeMaster D. M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9:1990;1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.1    Horton, J.R.2    LeMaster, D.M.3
  • 29
    • 0027428117 scopus 로고
    • Radioimmunoassay of glutathione peroxidase in human serum
    • Huang W., Åkesson B. Radioimmunoassay of glutathione peroxidase in human serum. Clin. Chim. Acta. 219:1993;139-148.
    • (1993) Clin. Chim. Acta , vol.219 , pp. 139-148
    • Huang, W.1    Åkesson, B.2
  • 30
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF: A program to identify and analyze structural motifs in proteins
    • Hutchinson E. G., Thornton J. M. PROMOTIF: a program to identify and analyze structural motifs in proteins. Protein Sci. 5:1996;212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 31
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in the model
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in the model. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 32
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallog. 21:1988;916-924.
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 33
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopholymers. 22:1983;2577-2637.
    • (1983) Biopholymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0018801438 scopus 로고
    • Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 Å resolution
    • Ladenstein R., Epp O., Bartels K., Jones A., Huber R. Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 Å resolution. J. Mol. Biol. 134:1979;199-218.
    • (1979) J. Mol. Biol. , vol.134 , pp. 199-218
    • Ladenstein, R.1    Epp, O.2    Bartels, K.3    Jones, A.4    Huber, R.5
  • 36
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 37
    • 0001099937 scopus 로고
    • Traitements statistiques des erreurs dans la determination des structures cristallines
    • Luzzati P. V. Traitements statistiques des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 38
    • 0023522192 scopus 로고
    • Characterization of the major hydroperoxide-reducing activity of human plasma: Purification and properties of a selenium-dependent glutathione peroxidase
    • Maddipati K. R., Marnett L. K. Characterization of the major hydroperoxide-reducing activity of human plasma: purification and properties of a selenium-dependent glutathione peroxidase. J. Biol. Chem. 262:1987;17398-17403.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17398-17403
    • Maddipati, K.R.1    Marnett, L.K.2
  • 39
    • 0023199294 scopus 로고
    • Characterization of the hydroperoxide-reducing activity of human plasma
    • Maddipati K. R., Gasparski C., Marnett L. J. Characterization of the hydroperoxide-reducing activity of human plasma. Arch. Biochem. Biophys. 254:1987;9-17.
    • (1987) Arch. Biochem. Biophys. , vol.254 , pp. 9-17
    • Maddipati, K.R.1    Gasparski, C.2    Marnett, L.J.3
  • 40
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin J. L. Thioredoxin - a fold for all reasons. Structure. 3:1995;245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 41
    • 0027320750 scopus 로고
    • Cloning of the bovine plasma selenium-dependent glutathione peroxidase (GP) cDNA from the ocular cilliary epithelium: Expression of the plasma and cellular forms within the mammalian eye
    • Martin-Alonso J. M., Ghosh S., Coca-Prados M. Cloning of the bovine plasma selenium-dependent glutathione peroxidase (GP) cDNA from the ocular cilliary epithelium: expression of the plasma and cellular forms within the mammalian eye. J. Biochem. 114:1993;284-291.
    • (1993) J. Biochem. , vol.114 , pp. 284-291
    • Martin-Alonso, J.M.1    Ghosh, S.2    Coca-Prados, M.3
  • 42
    • 0027993038 scopus 로고
    • Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion
    • Master R. L., Magenheimer B. S., Calvet J. P. Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion. J. Biol. Chem. 269:1994;27066-27073.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27066-27073
    • Master, R.L.1    Magenheimer, B.S.2    Calvet, J.P.3
  • 43
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 44
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative damage
    • Mills G. C. Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative damage. J. Biol. Chem. 229:1957;189-197.
    • (1957) J. Biol. Chem. , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 45
    • 0023782187 scopus 로고
    • Selenocysteine's mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases
    • Mullenbach G. T., Tabrizi A., Irvine B. D., Bell G. I., Tainer J. A., Hallewell R. A. Selenocysteine's mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases. Protein Eng. 2:1988;239-246.
    • (1988) Protein Eng. , vol.2 , pp. 239-246
    • Mullenbach, G.T.1    Tabrizi, A.2    Irvine, B.D.3    Bell, G.I.4    Tainer, J.A.5    Hallewell, R.A.6
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 47
    • 0002790551 scopus 로고
    • Selenium biochemistry: Chemical and physical studies
    • Odom J. D. Selenium biochemistry: chemical and physical studies. Struct. Bond. 54:1983;1-26.
    • (1983) Struct. Bond. , vol.54 , pp. 1-26
    • Odom, J.D.1
  • 48
    • 0021065954 scopus 로고
    • Selenium and drug metabolism. I. Multiple modulations of mouse liver enzymes
    • Reiter R., Wendel A. Selenium and drug metabolism. I. Multiple modulations of mouse liver enzymes. Biochem. Pharmacol. 32:1983;3063-3067.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 3063-3067
    • Reiter, R.1    Wendel, A.2
  • 49
    • 0028796708 scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of glutathione peroxidase from human plasma
    • Ren B., Huang W., Åkesson B., Ladenstein R. Crystallization and preliminary X-ray diffraction analysis of glutathione peroxidase from human plasma. Acta Crystallog. sect. D. 51:1995;824-826.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 824-826
    • Ren, B.1    Huang, W.2    Åkesson, B.3    Ladenstein, R.4
  • 50
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson J. The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34:1981;167-339.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.1
  • 51
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossmann M. G., Blow D. M. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallog. 15:1962;24-31.
    • (1962) Acta Crystallog. , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 52
    • 0025744144 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase is a selenoenzyme distinct from the classical glutathione peroxidase as evident from cDNA and amino acid sequencing
    • Schuckelt R., Brigelius-Flohé R., Maiorino M., Roveri A., Reumkens J., Straβburger W., Ursini F., Wolf B., Flohé L. Phospholipid hydroperoxide glutathione peroxidase is a selenoenzyme distinct from the classical glutathione peroxidase as evident from cDNA and amino acid sequencing. Free Rad. Res. Commun. 14:1991;343-361.
    • (1991) Free Rad. Res. Commun. , vol.14 , pp. 343-361
    • Schuckelt, R.1    Brigelius-Flohé, R.2    Maiorino, M.3    Roveri, A.4    Reumkens, J.5    Straburger, W.6    Ursini, F.7    Wolf, B.8    Flohé, L.9
  • 53
    • 0029617643 scopus 로고
    • Cloning of the mouse gene encoding plasma glutathione peroxidase: Organization, sequence and chromosomal localization
    • Schwaab V., Band E., Ghyselinck N., Mattei M. G., Dufaure J. P., Drevet J. R. Cloning of the mouse gene encoding plasma glutathione peroxidase: organization, sequence and chromosomal localization. Gene. 167:1995;25-31.
    • (1995) Gene , vol.167 , pp. 25-31
    • Schwaab, V.1    Band, E.2    Ghyselinck, N.3    Mattei, M.G.4    Dufaure, J.P.5    Drevet, J.R.6
  • 55
    • 0023598337 scopus 로고
    • Specific occurence of selenium in enzymes and amino acid tRNAs
    • Stadtman T. C. Specific occurence of selenium in enzymes and amino acid tRNAs. FASEB J. 1:1987;375-379.
    • (1987) FASEB J. , vol.1 , pp. 375-379
    • Stadtman, T.C.1
  • 57
    • 0023186348 scopus 로고
    • Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzyme
    • Takahashi K., Avissar N., Whitin J., Cohen H. J. Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme. Arch. Biochem. Biophys. 256:1987;677-686.
    • (1987) Arch. Biochem. Biophys. , vol.256 , pp. 677-686
    • Takahashi, K.1    Avissar, N.2    Whitin, J.3    Cohen, H.J.4
  • 59
    • 0025060737 scopus 로고
    • Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation: In situ reduction of phospholipid and chlesterol hydroperoxides
    • Thomas J. P., Maiorino M., Ursini F., Girotti A. W. Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation: in situ reduction of phospholipid and chlesterol hydroperoxides. J. Biol. Chem. 265:1990;454-461.
    • (1990) J. Biol. Chem. , vol.265 , pp. 454-461
    • Thomas, J.P.1    Maiorino, M.2    Ursini, F.3    Girotti, A.W.4
  • 62
    • 0014347799 scopus 로고
    • Stereochemical criteria for polypeptides and proteins V. Conformation of a system of three linked peptide units
    • Venkatachalam C. M. Stereochemical criteria for polypeptides and proteins V. Conformation of a system of three linked peptide units. Biopolymers. 6:1968;1425-1436.
    • (1968) Biopolymers , vol.6 , pp. 1425-1436
    • Venkatachalam, C.M.1
  • 63
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • Von Heijne G. A new method for predicting signal sequence cleavage sites. Nucl. Acids Res. 14:1986;4683-4690.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 64
    • 0001210234 scopus 로고
    • The probability distribution of X-ray intensities
    • Wilson A. J. The probability distribution of X-ray intensities. Acta Crystallog. 2:1949;318-321.
    • (1949) Acta Crystallog. , vol.2 , pp. 318-321
    • Wilson, A.J.1
  • 65
    • 0027246660 scopus 로고
    • Glutathione peroxidase isolated from plasma reduces phospholipid hydroperoxides
    • Yamamoto Y., Takahashi K. Glutathione peroxidase isolated from plasma reduces phospholipid hydroperoxides. Arch. Biochem. Biophys. 305:1993;541-545.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 541-545
    • Yamamoto, Y.1    Takahashi, K.2
  • 67
    • 0001256080 scopus 로고
    • Nucleotide sequence and expression of selenocysteine-containing polypeptide of formate dehydrogenase (format-hydrogen-lyase-linked) fromEscherichia coli
    • Zinoni F., Birkmann A., Stadtman T. C., Böck A. Nucleotide sequence and expression of selenocysteine-containing polypeptide of formate dehydrogenase (format-hydrogen-lyase-linked) fromEscherichia coli. Proc. Natl Acad. Sci. USA. 83:1986;4650-4654.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Böck, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.