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Volumn 49, Issue 43, 2010, Pages 9269-9279

Structural and biochemical studies of a fluoroacetyl-CoA-specific thioesterase reveal a molecular basis for fluorine selectivity

Author keywords

[No Author keywords available]

Indexed keywords

[CARBONYL; ACETYL-COA; ACTIVE SITE; BIOCHEMICAL STUDIES; CATALYTIC RESIDUE; COENZYME A; DRIVING FORCES; ENZYMATIC SYSTEM; FLUORINE SUBSTITUTION; FLUOROACETATE; HYDROPHOBIC BINDING; IN-VIVO; MOLECULAR BASIS; MOLECULAR INSIGHTS; ORGANOFLUORINE; STRUCTURAL STUDIES; SUBSTRATE BINDING; SUBSTRATE SELECTIVITY; THIOESTERASES; THIOESTERS;

EID: 78049301731     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101102u     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 84988231301 scopus 로고    scopus 로고
    • The diversity of naturally produced organohalogens
    • Gribble, G. W. (2003) The diversity of naturally produced organohalogens Handb. Environ. Chem. 3, 1-15
    • (2003) Handb. Environ. Chem. , vol.3 , pp. 1-15
    • Gribble, G.W.1
  • 2
    • 0000362773 scopus 로고    scopus 로고
    • Fluorine-containing natural products
    • O'Hagan, D. and Harper, D. (1999) Fluorine-containing natural products J. Fluorine Chem. 100, 127-133
    • (1999) J. Fluorine Chem. , vol.100 , pp. 127-133
    • O'Hagan, D.1    Harper, D.2
  • 3
    • 33747139649 scopus 로고    scopus 로고
    • Naturally occuring organofluorines
    • Gribble, G. (2002) Naturally occuring organofluorines Handb. Environ. Chem. 3, 121-136
    • (2002) Handb. Environ. Chem. , vol.3 , pp. 121-136
    • Gribble, G.1
  • 4
    • 0038413902 scopus 로고    scopus 로고
    • Fluorinated natural products: The biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya
    • Murphy, C. D., Schaffrath, C., and O'Hagan, D. (2003) Fluorinated natural products: The biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya Chemosphere 52, 455-461
    • (2003) Chemosphere , vol.52 , pp. 455-461
    • Murphy, C.D.1    Schaffrath, C.2    O'Hagan, D.3
  • 5
    • 11144334620 scopus 로고    scopus 로고
    • Fluorometabolite biosynthesis and the fluorinase from Streptomyces cattleya
    • Deng, H., O'Hagan, D., and Schaffrath, C. (2004) Fluorometabolite biosynthesis and the fluorinase from Streptomyces cattleya Nat. Prod. Rep. 21, 773-784
    • (2004) Nat. Prod. Rep. , vol.21 , pp. 773-784
    • Deng, H.1    O'Hagan, D.2    Schaffrath, C.3
  • 7
    • 0034926661 scopus 로고    scopus 로고
    • Fluorine substituent effects (on bioactivity)
    • Smart, B. (2001) Fluorine substituent effects (on bioactivity) J. Fluorine Chem. 109, 3-11
    • (2001) J. Fluorine Chem. , vol.109 , pp. 3-11
    • Smart, B.1
  • 8
    • 34848848499 scopus 로고    scopus 로고
    • Fluorine in pharmaceuticals: Looking beyond intuition
    • Muller, K., Faeh, C., and Diederich, F. (2007) Fluorine in pharmaceuticals: Looking beyond intuition Science 317, 1881-1886
    • (2007) Science , vol.317 , pp. 1881-1886
    • Muller, K.1    Faeh, C.2    Diederich, F.3
  • 10
    • 38149016915 scopus 로고    scopus 로고
    • Understanding organofluorine chemistry. An introduction to the C-F bond
    • O'Hagan, D. (2008) Understanding organofluorine chemistry. An introduction to the C-F bond Chem. Soc. Rev. 37, 308-319
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 308-319
    • O'Hagan, D.1
  • 11
    • 4544316921 scopus 로고    scopus 로고
    • The polar hydrophobicity of fluorinated compounds
    • Biffinger, J. C., Kim, H. W., and DiMagno, S. G. (2004) The polar hydrophobicity of fluorinated compounds ChemBioChem 5, 622-627
    • (2004) ChemBioChem , vol.5 , pp. 622-627
    • Biffinger, J.C.1    Kim, H.W.2    Dimagno, S.G.3
  • 12
    • 0029809541 scopus 로고    scopus 로고
    • Gemcitabine: Preclinical pharmacology and mechanisms of action
    • Plunkett, W., Huang, P., Searcy, C. E., and Gandhi, V. (1996) Gemcitabine: Preclinical pharmacology and mechanisms of action Semin. Oncol. 23, 3-15
    • (1996) Semin. Oncol. , vol.23 , pp. 3-15
    • Plunkett, W.1    Huang, P.2    Searcy, C.E.3    Gandhi, V.4
  • 13
    • 0030036601 scopus 로고    scopus 로고
    • Inactivation of ribonucleotide reductase by (E)-2′-fluoromethylene- 2′-deoxycytidine-5′-diphosphate: A paradigm for nucleotide mechanism-based inhibitors
    • van der Donk, W. A., Yu, G., Silva, D. J., Stubbe, J., McCarthy, J. R., Jarvi, E. T., Matthews, D. P., Resvick, R. J., and Wagner, E. (1996) Inactivation of ribonucleotide reductase by (E)-2′-fluoromethylene- 2′-deoxycytidine-5′-diphosphate: A paradigm for nucleotide mechanism-based inhibitors Biochemistry 35, 8381-8391
    • (1996) Biochemistry , vol.35 , pp. 8381-8391
    • Van Der Donk, W.A.1    Yu, G.2    Silva, D.J.3    Stubbe, J.4    McCarthy, J.R.5    Jarvi, E.T.6    Matthews, D.P.7    Resvick, R.J.8    Wagner, E.9
  • 15
    • 0025611018 scopus 로고
    • Metabolism and mechanism of action of 5-fluorouracil
    • Parker, W. B. and Cheng, Y. C. (1990) Metabolism and mechanism of action of 5-fluorouracil Pharmacol. Ther. 48, 381-395
    • (1990) Pharmacol. Ther. , vol.48 , pp. 381-395
    • Parker, W.B.1    Cheng, Y.C.2
  • 16
    • 0038387494 scopus 로고    scopus 로고
    • 5-Fluorouracil: Mechanisms of action and clinical strategies
    • Longley, D. B., Harkin, D. P., and Johnston, P. G. (2003) 5-Fluorouracil: Mechanisms of action and clinical strategies Nat. Rev. Cancer 3, 330-338
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 330-338
    • Longley, D.B.1    Harkin, D.P.2    Johnston, P.G.3
  • 17
    • 0000899141 scopus 로고
    • Monofluoroacetic acid and related compounds
    • Chenoweth, M. B. (1949) Monofluoroacetic acid and related compounds J. Pharmacol. Exp. Ther. 97, 383-423
    • (1949) J. Pharmacol. Exp. Ther. , vol.97 , pp. 383-423
    • Chenoweth, M.B.1
  • 19
    • 76549206177 scopus 로고
    • The in vivo formation of citrate induced by fluoroacetate and its signficance
    • Buffa, P. and Peters, R. A. (1950) The in vivo formation of citrate induced by fluoroacetate and its signficance J. Physiol. 110, 488-500
    • (1950) J. Physiol. , vol.110 , pp. 488-500
    • Buffa, P.1    Peters, R.A.2
  • 20
    • 76549260760 scopus 로고
    • Biochemistry of fluoroacetate poisoning. Isolation of an active tricarboxylic acid fraction from poisoned kidney homogenates
    • Buffa, P., Peters, R. A., and Wakelin, R. W. (1951) Biochemistry of fluoroacetate poisoning. Isolation of an active tricarboxylic acid fraction from poisoned kidney homogenates Biochem. J. 48, 467-477
    • (1951) Biochem. J. , vol.48 , pp. 467-477
    • Buffa, P.1    Peters, R.A.2    Wakelin, R.W.3
  • 21
    • 0000744922 scopus 로고
    • Biochemistry of fluoroacetate poisoning: The effect of fluorocitrate on purified aconitase
    • Morrison, J. F. and Peters, R. A. (1954) Biochemistry of fluoroacetate poisoning: The effect of fluorocitrate on purified aconitase Biochem. J. 58, 473-479
    • (1954) Biochem. J. , vol.58 , pp. 473-479
    • Morrison, J.F.1    Peters, R.A.2
  • 22
    • 0025936333 scopus 로고
    • Fluoroacetate and fluorocitrate: Mechanism of action
    • Clarke, D. D. (1991) Fluoroacetate and fluorocitrate: Mechanism of action Neurochem. Res. 16, 1055-1058
    • (1991) Neurochem. Res. , vol.16 , pp. 1055-1058
    • Clarke, D.D.1
  • 23
    • 0015621219 scopus 로고
    • Fluorocitrate inhibition of aconitate hydratase and the tricarboxylate carrier of rat liver mitochondria
    • Brandt, M., Evans, S., Mendes-Morao, J., and Chappell, B. (1973) Fluorocitrate inhibition of aconitate hydratase and the tricarboxylate carrier of rat liver mitochondria Biochem. J. 134, 217-224
    • (1973) Biochem. J. , vol.134 , pp. 217-224
    • Brandt, M.1    Evans, S.2    Mendes-Morao, J.3    Chappell, B.4
  • 24
    • 0015766610 scopus 로고
    • Fluorocitrate inhibition of aconitase. Reversibility of the inactivation
    • Villafranca, J. J. and Platus, E. (1973) Fluorocitrate inhibition of aconitase. Reversibility of the inactivation Biochem. Biophys. Res. Commun. 55, 1197-1207
    • (1973) Biochem. Biophys. Res. Commun. , vol.55 , pp. 1197-1207
    • Villafranca, J.J.1    Platus, E.2
  • 25
    • 0015973545 scopus 로고
    • Inhibition of liver aconitase isozymes by (-)-erythro-fluorocitrate
    • Eanes, R. Z. and Kun, E. (1974) Inhibition of liver aconitase isozymes by (-)-erythro-fluorocitrate Mol. Pharmacol. 10, 130-139
    • (1974) Mol. Pharmacol. , vol.10 , pp. 130-139
    • Eanes, R.Z.1    Kun, E.2
  • 26
    • 0021893322 scopus 로고
    • Mossbauer studies of aconitase. Substrate and inhibitor binding, reaction intermediates, and hyperfine interactions of reduced 3Fe and 4Fe clusters
    • Kent, T. A., Emptage, M. H., Merkle, H., Kennedy, M. C., Beinert, H., and Munck, E. (1985) Mossbauer studies of aconitase. Substrate and inhibitor binding, reaction intermediates, and hyperfine interactions of reduced 3Fe and 4Fe clusters J. Biol. Chem. 260, 6871-6881
    • (1985) J. Biol. Chem. , vol.260 , pp. 6871-6881
    • Kent, T.A.1    Emptage, M.H.2    Merkle, H.3    Kennedy, M.C.4    Beinert, H.5    Munck, E.6
  • 27
    • 0030447979 scopus 로고    scopus 로고
    • The reaction of fluorocitrate with aconitase and the crystal structure of the enzyme-inhibitor complex
    • Lauble, H., Kennedy, M. C., Emptage, M. H., Beinert, H., and Stout, C. D. (1996) The reaction of fluorocitrate with aconitase and the crystal structure of the enzyme-inhibitor complex Proc. Natl. Acad. Sci. U.S.A. 93, 13699-13703
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13699-13703
    • Lauble, H.1    Kennedy, M.C.2    Emptage, M.H.3    Beinert, H.4    Stout, C.D.5
  • 28
    • 0001518602 scopus 로고
    • Isolation of the toxic principle "k cymonate" from "gifblaar" Dichapetalum cymosum
    • Marais, J. (1943) Isolation of the toxic principle "K cymonate" from "Gifblaar" Dichapetalum cymosum J. Vet. Sci. Anim. Ind. 18, 203-206
    • (1943) J. Vet. Sci. Anim. Ind. , vol.18 , pp. 203-206
    • Marais, J.1
  • 29
    • 0011368731 scopus 로고
    • Fluoride metabolism in Dichapetalum toxicarium
    • Vickery, B. and Vickery, M. (1972) Fluoride metabolism in Dichapetalum toxicarium Phytochemistry 11, 1905-1909
    • (1972) Phytochemistry , vol.11 , pp. 1905-1909
    • Vickery, B.1    Vickery, M.2
  • 30
    • 84981633071 scopus 로고
    • The distribution of organic fluorine in some toxic tropical plants
    • Hall, R. (1972) The distribution of organic fluorine in some toxic tropical plants New Phytol. 71, 855-871
    • (1972) New Phytol. , vol.71 , pp. 855-871
    • Hall, R.1
  • 31
    • 0026272716 scopus 로고
    • The impact of fluoroacetate-bearing vegetation on native Australian fauna: A review
    • Twigg, L. and King, D. (1991) The impact of fluoroacetate-bearing vegetation on native Australian fauna: A review Oikos 61, 412-430
    • (1991) Oikos , vol.61 , pp. 412-430
    • Twigg, L.1    King, D.2
  • 32
    • 0028011352 scopus 로고
    • The fluorinated natural products
    • Harper, D. B. and O'Hagan, D. (1994) The fluorinated natural products Nat. Prod. Rep. 11, 123-133
    • (1994) Nat. Prod. Rep. , vol.11 , pp. 123-133
    • Harper, D.B.1    O'Hagan, D.2
  • 35
    • 0242711908 scopus 로고
    • Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria
    • Benveniste, R. and Davies, J. (1973) Aminoglycoside antibiotic- inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria Proc. Natl. Acad. Sci. U.S.A. 70, 2276-2280
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 2276-2280
    • Benveniste, R.1    Davies, J.2
  • 36
    • 0017885225 scopus 로고
    • Mechanism of resistance to thiostrepton in the producing-organism Streptomyces azureus
    • Cundliffe, E. (1978) Mechanism of resistance to thiostrepton in the producing-organism Streptomyces azureus Nature 272, 792-795
    • (1978) Nature , vol.272 , pp. 792-795
    • Cundliffe, E.1
  • 37
    • 0023704995 scopus 로고
    • Involvement of cell impermeability in resistance to macrolides in some producer streptomycetes
    • Fierro, J. F., Hardisson, C., and Salas, J. A. (1988) Involvement of cell impermeability in resistance to macrolides in some producer streptomycetes J. Antibiot. (Tokyo) 41, 142-144
    • (1988) J. Antibiot. (Tokyo) , vol.41 , pp. 142-144
    • Fierro, J.F.1    Hardisson, C.2    Salas, J.A.3
  • 38
    • 0024039558 scopus 로고
    • Cloning and characterization of a DNA gyrase B gene from Streptomyces sphaeroides that confers resistance to novobiocin
    • Thiara, A. S. and Cundliffe, E. (1988) Cloning and characterization of a DNA gyrase B gene from Streptomyces sphaeroides that confers resistance to novobiocin EMBO J. 7, 2255-2259
    • (1988) EMBO J. , vol.7 , pp. 2255-2259
    • Thiara, A.S.1    Cundliffe, E.2
  • 39
    • 0024459873 scopus 로고
    • How antibiotic-producing organisms avoid suicide
    • Cundliffe, E. (1989) How antibiotic-producing organisms avoid suicide Annu. Rev. Microbiol. 43, 207-233
    • (1989) Annu. Rev. Microbiol. , vol.43 , pp. 207-233
    • Cundliffe, E.1
  • 40
    • 0031910748 scopus 로고    scopus 로고
    • ABC transporters in antibiotic-producing actinomycetes
    • Mendez, C. and Salas, J. A. (1998) ABC transporters in antibiotic-producing actinomycetes FEMS Microbiol. Lett. 158, 1-8
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 1-8
    • Mendez, C.1    Salas, J.A.2
  • 41
    • 33646568459 scopus 로고    scopus 로고
    • The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: A thioesterase confers resistance to fluoroacetyl-coenzyme A
    • Huang, F., Haydock, S. F., Spiteller, D., Mironenko, T., Li, T. L., O'Hagan, D., Leadlay, P. F., and Spencer, J. B. (2006) The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: A thioesterase confers resistance to fluoroacetyl-coenzyme A Chem. Biol. 13, 475-484
    • (2006) Chem. Biol. , vol.13 , pp. 475-484
    • Huang, F.1    Haydock, S.F.2    Spiteller, D.3    Mironenko, T.4    Li, T.L.5    O'Hagan, D.6    Leadlay, P.F.7    Spencer, J.B.8
  • 44
    • 84934444524 scopus 로고    scopus 로고
    • Expression and purification of soluble His(6)-tagged TEV protease
    • Tropea, J. E., Cherry, S., and Waugh, D. S. (2009) Expression and purification of soluble His(6)-tagged TEV protease Methods Mol. Biol. 498, 297-307
    • (2009) Methods Mol. Biol. , vol.498 , pp. 297-307
    • Tropea, J.E.1    Cherry, S.2    Waugh, D.S.3
  • 45
    • 0000311119 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallogr. 212, 916-924
    • (1993) J. Appl. Crystallogr. , vol.212 , pp. 916-924
    • Kabsch, W.1
  • 48
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement Nat. Struct. Biol. 6, 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 49
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 50
    • 0242290213 scopus 로고    scopus 로고
    • The structure of 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU
    • Thoden, J. B., Zhuang, Z., Dunaway-Mariano, D., and Holden, H. M. (2003) The structure of 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU J. Biol. Chem. 278, 43709-43716
    • (2003) J. Biol. Chem. , vol.278 , pp. 43709-43716
    • Thoden, J.B.1    Zhuang, Z.2    Dunaway-Mariano, D.3    Holden, H.M.4
  • 54
    • 64349123693 scopus 로고    scopus 로고
    • The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis
    • Cao, J., Xu, H., Zhao, H., Gong, W., and Dunaway-Mariano, D. (2009) The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis Biochemistry 48, 1293-1304
    • (2009) Biochemistry , vol.48 , pp. 1293-1304
    • Cao, J.1    Xu, H.2    Zhao, H.3    Gong, W.4    Dunaway-Mariano, D.5
  • 55
    • 59249107241 scopus 로고    scopus 로고
    • In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH
    • Chen, D., Wu, R., Bryan, T. L., and Dunaway-Mariano, D. (2009) In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH Biochemistry 48, 511-513
    • (2009) Biochemistry , vol.48 , pp. 511-513
    • Chen, D.1    Wu, R.2    Bryan, T.L.3    Dunaway-Mariano, D.4
  • 57
    • 33846199962 scopus 로고    scopus 로고
    • Structure-activity analysis of base and enzyme-catalyzed 4-hydroxybenzoyl coenzyme A hydrolysis
    • Song, F., Zhuang, Z., and Dunaway-Mariano, D. (2007) Structure-activity analysis of base and enzyme-catalyzed 4-hydroxybenzoyl coenzyme A hydrolysis Bioorg. Chem. 35, 1-10
    • (2007) Bioorg. Chem. , vol.35 , pp. 1-10
    • Song, F.1    Zhuang, Z.2    Dunaway-Mariano, D.3
  • 58
    • 67349094267 scopus 로고    scopus 로고
    • Structure and function of a Campylobacter jejuni thioesterase Cj0915, a hexameric hot dog fold enzyme
    • Yokoyama, T., Choi, K. J., Bosch, A. M., and Yeo, H. J. (2009) Structure and function of a Campylobacter jejuni thioesterase Cj0915, a hexameric hot dog fold enzyme Biochim. Biophys. Acta 1794, 1073-1081
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1073-1081
    • Yokoyama, T.1    Choi, K.J.2    Bosch, A.M.3    Yeo, H.J.4
  • 60
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 61
    • 0030590426 scopus 로고    scopus 로고
    • How good is fluorine as a hydrogen bond acceptor?
    • Howard, J., Hoy, V., O'Hagan, D., and Smith, G. (1996) How good is fluorine as a hydrogen bond acceptor? Tetrahedron 52, 12613-12622
    • (1996) Tetrahedron , vol.52 , pp. 12613-12622
    • Howard, J.1    Hoy, V.2    O'Hagan, D.3    Smith, G.4
  • 62
    • 0030937244 scopus 로고    scopus 로고
    • Organic fluorine hardly ever accepts hydrogen bonds
    • Dunitz, J. and Taylor, R. (1997) Organic fluorine hardly ever accepts hydrogen bonds Chem.-Eur. J. 3, 89-98
    • (1997) Chem.-Eur. J. , vol.3 , pp. 89-98
    • Dunitz, J.1    Taylor, R.2
  • 63
    • 70350515927 scopus 로고    scopus 로고
    • Fluorine bonding-How does it work in protein ligand interactions?
    • Zhou, P., Zou, J., Tian, F., and Shang, Z. (2009) Fluorine bonding-How does it work in protein ligand interactions? J. Chem. Inf. Model. 49, 2344-2355
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 2344-2355
    • Zhou, P.1    Zou, J.2    Tian, F.3    Shang, Z.4
  • 64
    • 1842736537 scopus 로고    scopus 로고
    • A sensitive and robust method for quantification of intracellular short-chain coenzyme A esters
    • Shimazu, M., Vetcher, L., Galazzo, J. L., Licari, P., and Santi, D. V. (2004) A sensitive and robust method for quantification of intracellular short-chain coenzyme A esters Anal. Biochem. 328, 51-59
    • (2004) Anal. Biochem. , vol.328 , pp. 51-59
    • Shimazu, M.1    Vetcher, L.2    Galazzo, J.L.3    Licari, P.4    Santi, D.V.5


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