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Volumn 19, Issue 4, 1999, Pages 2650-2656

Differential protein S-thiolation of glyceraldehyde-3-phosphate dehydrogenase isoenzymes influences sensitivity to oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; ISOENZYME;

EID: 0032956855     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.4.2650     Document Type: Article
Times cited : (140)

References (49)
  • 1
    • 0028985640 scopus 로고
    • Differential synthesis of glyceraldehyde-3-phosphate dehydrogenase polypeptides in stressed yeast cells
    • Boucherie, H., N. Bataille, I. T. Fitch, M. Perrot, and M. F. Tuite. 1995. Differential synthesis of glyceraldehyde-3-phosphate dehydrogenase polypeptides in stressed yeast cells. FEMS Microbiol. Lett. 125:127-134.
    • (1995) FEMS Microbiol. Lett. , vol.125 , pp. 127-134
    • Boucherie, H.1    Bataille, N.2    Fitch, I.T.3    Perrot, M.4    Tuite, M.F.5
  • 2
    • 0030919274 scopus 로고    scopus 로고
    • Purification of a dichlorophenol-indophenol oxidoreductase from rat and bovine synaptic membranes: Tight complex association of a glyceraldehyde-3-phosphate dehydrogenase isoform, TOAD64, enolase-γ and aldolase C
    • Bulliard, C., R. Zurbiggen, J. Tornare, M. Faty, Z. Dastoor, and J.-L. Dreyer. 1997. Purification of a dichlorophenol-indophenol oxidoreductase from rat and bovine synaptic membranes: tight complex association of a glyceraldehyde-3-phosphate dehydrogenase isoform, TOAD64, enolase-γ and aldolase C. Biochem. J. 324:555-563.
    • (1997) Biochem. J. , vol.324 , pp. 555-563
    • Bulliard, C.1    Zurbiggen, R.2    Tornare, J.3    Faty, M.4    Dastoor, Z.5    Dreyer, J.-L.6
  • 3
    • 0028298361 scopus 로고
    • S-thiolation of individual neutrophil proteins including actin by stimulation of the respiratory burst: Evidence against a role for glutathione disulphide
    • Chai, Y.-C., S. Hendrich, and A. J. Thomas. 1994. S-thiolation of individual neutrophil proteins including actin by stimulation of the respiratory burst: evidence against a role for glutathione disulphide. Arch. Biochem. Biophys. 310:273-281.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 273-281
    • Chai, Y.-C.1    Hendrich, S.2    Thomas, A.J.3
  • 4
    • 0026011118 scopus 로고
    • Identification of an S-thiolated rat liver protein as carbonic anhydrase III: Characterization of S-thiolation and dethiolation reactions
    • Chai, Y.-C., C.-H. Jung, C. K. Lii, S. S. Ashraf, S. Hendrich, B. Wolf, H. Sies, and J. A. Thomas. 1991. Identification of an S-thiolated rat liver protein as carbonic anhydrase III: characterization of S-thiolation and dethiolation reactions. Arch. Biochem. Biophys. 284:270-278.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 270-278
    • Chai, Y.-C.1    Jung, C.-H.2    Lii, C.K.3    Ashraf, S.S.4    Hendrich, S.5    Wolf, B.6    Sies, H.7    Thomas, J.A.8
  • 5
    • 0031028059 scopus 로고    scopus 로고
    • apd1 +, a gene required for red pigment formation in ade6 mutants of Schizosaccharomyces pombe, encodes an enzyme required for glutathione biosynthesis: A role for glutathione and a glutathione-conjugate pump
    • Chaudhuri, B., S. Ingavale, and A. K. Bachhawat. 1997. apd1 +, a gene required for red pigment formation in ade6 mutants of Schizosaccharomyces pombe, encodes an enzyme required for glutathione biosynthesis: a role for glutathione and a glutathione-conjugate pump. Genetics 145:75-83.
    • (1997) Genetics , vol.145 , pp. 75-83
    • Chaudhuri, B.1    Ingavale, S.2    Bachhawat, A.K.3
  • 6
    • 0026773311 scopus 로고
    • Protein sulfhydryls are protected from irreversible oxidation by conversion to mixed disulfides
    • Coan, C., J.-Y. Ji, K. Hideg, and R. J. Mehlhorn. 1992. Protein sulfhydryls are protected from irreversible oxidation by conversion to mixed disulfides. Arch. Biochem. Biophys. 295:369-378.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 369-378
    • Coan, C.1    Ji, J.-Y.2    Hideg, K.3    Mehlhorn, R.J.4
  • 7
    • 3042744558 scopus 로고
    • Cellular injury by oxidants
    • Cochrane, C. G. 1991. Cellular injury by oxidants. Am. J. Med. 91(Suppl. 3C):23S-30S.
    • (1991) Am. J. Med. , vol.91 , Issue.SUPPL. 3C
    • Cochrane, C.G.1
  • 8
    • 0023235798 scopus 로고
    • S-thiolation of cytoplasmic cardiac creatine kinase in heart cells treated with diamide
    • Collison, M., and J. A. Thomas. 1987. S-thiolation of cytoplasmic cardiac creatine kinase in heart cells treated with diamide. Biochim. Biophys. Acta 928:121-129.
    • (1987) Biochim. Biophys. Acta , vol.928 , pp. 121-129
    • Collison, M.1    Thomas, J.A.2
  • 9
    • 0017199048 scopus 로고
    • Selective inhibition of protein synthesis initiation in Saccharomyces cerevisiae by low concentrations of cycloheximide
    • Cooper, T. G., and J. Bossinger. 1976. Selective inhibition of protein synthesis initiation in Saccharomyces cerevisiae by low concentrations of cycloheximide. J. Biol. Chem. 251:7278-7286.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7278-7286
    • Cooper, T.G.1    Bossinger, J.2
  • 10
    • 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 R. G. Gerdes. 1998. Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem. Biophys. Res. Commun. 242: 1-9.
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 11
    • 0030851732 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro
    • Davis, D. A., F. M. Newcomb, D. W. Starke, D. E. Ott, J. J. Mieyal, and R. Yarchoan. 1997. Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. J. Biol. Chem. 272:25935-25940.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25935-25940
    • Davis, D.A.1    Newcomb, F.M.2    Starke, D.W.3    Ott, D.E.4    Mieyal, J.J.5    Yarchoan, R.6
  • 12
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean, R. T., S. Fu, R. Stocker, and M. J. Davies. 1997. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324:1-18.
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 13
    • 10544227752 scopus 로고    scopus 로고
    • Assay of plasma homocysteine - Light sensitivity of the fluorescent 7-benzo-2-oxa-1,3,diazole-4-sulfonic acid derivative, and use of appropriate calibrators
    • Dudman, N. P. B., X. W. Guo, R. Crooks, L. J. Xie, and J. S. Silverberg. 1996. Assay of plasma homocysteine - light sensitivity of the fluorescent 7-benzo-2-oxa-1,3,diazole-4-sulfonic acid derivative, and use of appropriate calibrators. Clin. Chem. 42:2028-2032.
    • (1996) Clin. Chem. , vol.42 , pp. 2028-2032
    • Dudman, N.P.B.1    Guo, X.W.2    Crooks, R.3    Xie, L.J.4    Silverberg, J.S.5
  • 14
    • 0031888539 scopus 로고    scopus 로고
    • Toxicity of linoleic acid hydroperoxide to Saccharomyces cerevisiae: Involvement of a respiration-related process for maximal sensitivity and adaptive response
    • Evans, M. V., H. E. Turton, C. M. Grant, and I. W. Dawes. 1997. Toxicity of linoleic acid hydroperoxide to Saccharomyces cerevisiae: Involvement of a respiration-related process for maximal sensitivity and adaptive response. J. Bacteriol. 180:483-490.
    • (1997) J. Bacteriol. , vol.180 , pp. 483-490
    • Evans, M.V.1    Turton, H.E.2    Grant, C.M.3    Dawes, I.W.4
  • 15
    • 0030016469 scopus 로고    scopus 로고
    • Yeast glutathione reductase is required for protection against oxidative stress and is a target gene for yAP-1 transcriptional regulation
    • Grant, C. M., L. P. Collinson, J.-H. Roe, and I. W. Dawes. 1996. Yeast glutathione reductase is required for protection against oxidative stress and is a target gene for yAP-1 transcriptional regulation. Mol. Microbiol. 21: 171-179.
    • (1996) Mol. Microbiol. , vol.21 , pp. 171-179
    • Grant, C.M.1    Collinson, L.P.2    Roe, J.-H.3    Dawes, I.W.4
  • 16
    • 0001549254 scopus 로고    scopus 로고
    • Synthesis and role of glutathione in protection against oxidative stress in yeast
    • Grant, C. M., and I. W. Dawes. 1996. Synthesis and role of glutathione in protection against oxidative stress in yeast. Redox Rep. 2:223-229.
    • (1996) Redox Rep. , vol.2 , pp. 223-229
    • Grant, C.M.1    Dawes, I.W.2
  • 17
    • 0032583570 scopus 로고    scopus 로고
    • Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae
    • Grant, C. M., G. Perrone, and I. W. Dawes. 1998. Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 253:893-898.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 893-898
    • Grant, C.M.1    Perrone, G.2    Dawes, I.W.3
  • 18
    • 0030004354 scopus 로고    scopus 로고
    • Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae
    • Grant, C. M., F. H. MacIver, and I. W. Dawes. 1996. Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae. Curr. Genet. 29:511-515.
    • (1996) Curr. Genet. , vol.29 , pp. 511-515
    • Grant, C.M.1    MacIver, F.H.2    Dawes, I.W.3
  • 19
    • 0030747207 scopus 로고    scopus 로고
    • Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide gamma-glutamylcysteine
    • Grant, C. M., F. H. MacIver, and I. W. Dawes. 1997. Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide gamma-glutamylcysteine. Mol. Biol. Cell 8:1699-1707.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1699-1707
    • Grant, C.M.1    MacIver, F.H.2    Dawes, I.W.3
  • 20
    • 0029834918 scopus 로고    scopus 로고
    • Stationary phase induction of GLR1 expression is mediated by the yAP-1 transcriptional protein in Saccharomyces cerevisiae
    • Grant, C. M., F. M. MacIver, and I. W. Dawes. 1996. Stationary phase induction of GLR1 expression is mediated by the yAP-1 transcriptional protein in Saccharomyces cerevisiae. Mol. Microbiol. 22:739-746.
    • (1996) Mol. Microbiol. , vol.22 , pp. 739-746
    • Grant, C.M.1    MacIver, F.M.2    Dawes, I.W.3
  • 21
    • 0024603334 scopus 로고
    • The simultaneous determination of oxidized and reduced glutathione in liver tissues by ion pairing reverse phase high performance liquid chromatography with a coulometric electrochemical detector
    • Harvey, P. R. C., R. G. Ilson, and S. M. Strasberg. 1989. The simultaneous determination of oxidized and reduced glutathione in liver tissues by ion pairing reverse phase high performance liquid chromatography with a coulometric electrochemical detector. Clin. Chim. Acta 180:203-212.
    • (1989) Clin. Chim. Acta , vol.180 , pp. 203-212
    • Harvey, P.R.C.1    Ilson, R.G.2    Strasberg, S.M.3
  • 22
    • 0028364445 scopus 로고
    • NADPH binding and control of catalase compound II formation: Comparison of bovine, yeast, and Escherichia coli enzymes
    • Hillar, A., P. Nicholls, J. Switala, and P. C. Loewen. 1994. NADPH binding and control of catalase compound II formation: comparison of bovine, yeast, and Escherichia coli enzymes. Biochem. J. 300:531-539.
    • (1994) Biochem. J. , vol.300 , pp. 531-539
    • Hillar, A.1    Nicholls, P.2    Switala, J.3    Loewen, P.C.4
  • 23
    • 0018942072 scopus 로고
    • Structural comparison of two non-tandemly repeated glyceraldehyde-3-phosphate dehydrogenase genes
    • Holland, J. P., and M. J. Holland. 1980. Structural comparison of two non-tandemly repeated glyceraldehyde-3-phosphate dehydrogenase genes. J. Biol. Chem. 255:2596-2605.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2596-2605
    • Holland, J.P.1    Holland, M.J.2
  • 24
    • 0032559297 scopus 로고    scopus 로고
    • The eS-Sence of -SH in the ER
    • Huppa, J. B., and H. L. Ploegh. 1998. The eS-Sence of -SH in the ER. Cell 92:145-148.
    • (1998) Cell , vol.92 , pp. 145-148
    • Huppa, J.B.1    Ploegh, H.L.2
  • 25
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., A. J. Sinskey, and H. F. Lodish. 1992. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257:1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 27
    • 0029844594 scopus 로고    scopus 로고
    • Importance of catalase in the adaptive response to hydrogen peroxide: Analysis of acatalasaemic Saccharomyces cerevisae
    • Izawa, S., Y. Inoue, and A. Kimura. 1996. Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisae. Biochem. J. 320:61-67.
    • (1996) Biochem. J. , vol.320 , pp. 61-67
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3
  • 28
    • 0029042565 scopus 로고
    • Oxidative stress in yeast: Effect of glutathione on adaption to hydrogen peroxide stress in Saccharomyces cerevisiae
    • Izawa, S., Y. Inoue, and A. Kimura. 1995. Oxidative stress in yeast: effect of glutathione on adaption to hydrogen peroxide stress in Saccharomyces cerevisiae. FEBS Lett. 368:73-76.
    • (1995) FEBS Lett. , vol.368 , pp. 73-76
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3
  • 30
    • 0030296409 scopus 로고    scopus 로고
    • S-Glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione
    • Jung, C.-H., and J. A. Thomas. 1996. S-Glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione. Arch. Biochem. Biophys. 335:61-72.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 61-72
    • Jung, C.-H.1    Thomas, J.A.2
  • 32
    • 0031719952 scopus 로고    scopus 로고
    • The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species
    • Luikenhuis, S., I. W. Dawes, and C. M. Grant. 1997. The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol. Biol. Cell 9:1081-1091.
    • (1997) Mol. Biol. Cell , vol.9 , pp. 1081-1091
    • Luikenhuis, S.1    Dawes, I.W.2    Grant, C.M.3
  • 33
    • 0022385984 scopus 로고
    • Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes
    • McAlister, L., and M. J. Holland. 1985. Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes. J. Biol. Chem. 260: 15019-15027.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15019-15027
    • McAlister, L.1    Holland, M.J.2
  • 34
    • 0022412541 scopus 로고
    • Isolation and characterization of yeast strains carrying mutations in the glyceraldehyde-3-phosphate dehydrogenase genes
    • McAlister, L., and M. J. Holland. 1985. Isolation and characterization of yeast strains carrying mutations in the glyceraldehyde-3-phosphate dehydrogenase genes. J. Biol. Chem. 260:15013-15018.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15013-15018
    • McAlister, L.1    Holland, M.J.2
  • 35
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister, A. 1988. Glutathione metabolism and its selective modification. J. Biol. Chem. 263:17205-17208.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 37
    • 0029948308 scopus 로고    scopus 로고
    • A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth
    • Muller, E. G. D. 1996. A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth. Mol. Biol. Cell 7:1805-1813.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1805-1813
    • Muller, E.G.D.1
  • 38
    • 0023867498 scopus 로고
    • S-thiolation of creatine kinase and glycogen phosphorylase b initiated by partially reduced oxygen species
    • Park, E. M., and J. A. Thomas. 1988. S-thiolation of creatine kinase and glycogen phosphorylase b initiated by partially reduced oxygen species. Biochem. Biophys. Acta 964:151-160.
    • (1988) Biochem. Biophys. Acta , vol.964 , pp. 151-160
    • Park, E.M.1    Thomas, J.A.2
  • 39
    • 0027412924 scopus 로고
    • Metabolism and functions of glutathione in micro-organisms
    • Penninckx, M. J., and M. T. Elskens. 1993. Metabolism and functions of glutathione in micro-organisms. Adv. Microb. Physiol. 34:239-301.
    • (1993) Adv. Microb. Physiol. , vol.34 , pp. 239-301
    • Penninckx, M.J.1    Elskens, M.T.2
  • 40
    • 0028170673 scopus 로고
    • S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes
    • Ravichandran, V., T. Seres, T. Moriguchi, J. A. Thomas, and R. B. Johnston. 1994. S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. J. Biol. Chem. 269:25010-25015.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25010-25015
    • Ravichandran, V.1    Seres, T.2    Moriguchi, T.3    Thomas, J.A.4    Johnston, R.B.5
  • 41
    • 0026004924 scopus 로고
    • Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages
    • Rokutan, K., J. A. Thomas, and R. B. Johnson. 1991. Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages. J. Immunol. 147:260-264.
    • (1991) J. Immunol. , vol.147 , pp. 260-264
    • Rokutan, K.1    Thomas, J.A.2    Johnson, R.B.3
  • 42
    • 0026459935 scopus 로고
    • Protein-specific S-thiolation in human endothelial cells during oxidative stress
    • Schuppe, I., P. Moldeus, and I. A. Cotgreave. 1992. Protein-specific S-thiolation in human endothelial cells during oxidative stress. Biochem. Pharmacol. 44:1757-1764.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1757-1764
    • Schuppe, I.1    Moldeus, P.2    Cotgreave, I.A.3
  • 43
    • 0028204459 scopus 로고
    • S-thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment
    • Schuppe-Koistinen, I., P. Moldeus, T. Bergman, and I. A. Cotgreave. 1994. S-thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment. Eur. J. Biochem. 221:1033-1037.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 1033-1037
    • Schuppe-Koistinen, I.1    Moldeus, P.2    Bergman, T.3    Cotgreave, I.A.4
  • 44
  • 45
    • 0027209389 scopus 로고
    • Strategies of antioxidant defense
    • Sies, H. 1993. Strategies of antioxidant defense. Eur. J. Biochem. 215:213-219.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 213-219
    • Sies, H.1
  • 46
    • 0029691198 scopus 로고    scopus 로고
    • Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • Sirover, M. A. 1996. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. Life Sci. 58: 2271-2277.
    • (1996) Life Sci. , vol.58 , pp. 2271-2277
    • Sirover, M.A.1
  • 48
    • 0029015864 scopus 로고
    • Protein sulphydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas, J. A., B. Poland, and R. Honzatko. 1995. Protein sulphydryls and their role in the antioxidant function of protein S-thiolation. Arch. Biochem. Biophys. 319:1-9.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 49
    • 0031039492 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae exhibits a yAP-1-mediated adaptive response to malondialdehyde
    • Turton, H. E., I. W. Dawes, and C. M. Grant. 1997. Saccharomyces cerevisiae exhibits a yAP-1-mediated adaptive response to malondialdehyde. J. Bacteriol. 179:1096-1101.
    • (1997) J. Bacteriol. , vol.179 , pp. 1096-1101
    • Turton, H.E.1    Dawes, I.W.2    Grant, C.M.3


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