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Volumn 15, Issue 4, 2006, Pages 761-773

Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: A special subgroup of the type III extradiol dioxygenases

Author keywords

2 His 1 carboxylate facial triad; 3 hydroxyanthranilic acid 3,4 dioxygenase; Cupin superfamily; Extradiol dioxygenase; Kynurenine pathway; MAD; X ray crystallography

Indexed keywords

3 HYDROXYANTHRANILATE 3,4 DIOXYGENASE; DIOXYGENASE; HOMODIMER; KYNURENINE; METAL ION; N METHYL DEXTRO ASPARTIC ACID; NICKEL; QUINOLINIC ACID;

EID: 33645502064     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051967906     Document Type: Article
Times cited : (30)

References (48)
  • 1
    • 0037129976 scopus 로고    scopus 로고
    • Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 Å resolution
    • Anand, R., Dorrestein, P.C., Kinsland, C., Begley, T.P., and Ealick, S.E. 2002. Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 Å resolution. Biochemistry 41: 7659-7669.
    • (2002) Biochemistry , vol.41 , pp. 7659-7669
    • Anand, R.1    Dorrestein, P.C.2    Kinsland, C.3    Begley, T.P.4    Ealick, S.E.5
  • 2
    • 0035822094 scopus 로고    scopus 로고
    • Solving the riddle of the intradiol and extradiol catechol dioxygenases: How do enzymes control hydroperoxide rearrangements?
    • Bugg, T.D.H. and Lin, G. 2001. Solving the riddle of the intradiol and extradiol catechol dioxygenases: How do enzymes control hydroperoxide rearrangements? Chem. Commun. 2001: 941-952.
    • (2001) Chem. Commun. , vol.2001 , pp. 941-952
    • Bugg, T.D.H.1    Lin, G.2
  • 3
    • 0031057367 scopus 로고    scopus 로고
    • Exploring the catalytic mechanism of the extradiol catechol dioxygenases
    • Bugg, T.D., Sanvoisin, J., and Spence, E.L. 1997. Exploring the catalytic mechanism of the extradiol catechol dioxygenases. Biochem. Soc. Trans. 25: 81-85.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 81-85
    • Bugg, T.D.1    Sanvoisin, J.2    Spence, E.L.3
  • 6
    • 0033198415 scopus 로고    scopus 로고
    • Error estimation and bias correction in phase-improvement calculations
    • Cowtan, K. 1999. Error estimation and bias correction in phase-improvement calculations. Acta Crystallogr. D Biol. Crystallogr. 55: 1555-1567.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1555-1567
    • Cowtan, K.1
  • 7
    • 0003292939 scopus 로고    scopus 로고
    • SHARP: A smaximum-likelihood heavy-atom parameter refinement and phasing program for the MIR and MAD methods
    • eds. P. Bourne and K. Watenpaugh, IUCR, Oxford, UK
    • de la Fortelle, E., Irwin, J.J., and Bricogne, G. 1997. SHARP: A smaximum-likelihood heavy-atom parameter refinement and phasing program for the MIR and MAD methods. In Crystallographic computing (eds. P. Bourne and K. Watenpaugh), pp. 250-262. IUCR, Oxford, UK.
    • (1997) Crystallographic Computing , pp. 250-262
    • De La Fortelle, E.1    Irwin, J.J.2    Bricogne, G.3
  • 9
    • 0742287185 scopus 로고    scopus 로고
    • Cupins: The most functionally diverse protein superfamily?
    • Dunwell, J.M., Purvis, A., and Khuri, S. 2004. Cupins: The most functionally diverse protein superfamily? Phytochemistry 65: 7-17.
    • (2004) Phytochemistry , vol.65 , pp. 7-17
    • Dunwell, J.M.1    Purvis, A.2    Khuri, S.3
  • 10
    • 1942437656 scopus 로고    scopus 로고
    • The crystal structures of Zea mays and Arabidopsis 4- hydroxyphenylpyruvate dioxygenase
    • Fritze, I.M., Linden, L., Freigang, J., Auerbach, G., Huber, R., and Steinbacher, S. 2004. The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase. Plant Physiol. 134: 1388-1400.
    • (2004) Plant Physiol. , vol.134 , pp. 1388-1400
    • Fritze, I.M.1    Linden, L.2    Freigang, J.3    Auerbach, G.4    Huber, R.5    Steinbacher, S.6
  • 11
    • 11844304935 scopus 로고    scopus 로고
    • The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s)
    • Gopal, B., Madan, L.L., Betz, S.F., and Kossiakoff, A.A. 2005. The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s). Biochemistry 44: 193-201.
    • (2005) Biochemistry , vol.44 , pp. 193-201
    • Gopal, B.1    Madan, L.L.2    Betz, S.F.3    Kossiakoff, A.A.4
  • 12
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D.I., and Metoz, F. 1999. ESPript: Multiple sequence alignments in PostScript. Bioinformatics 15: 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 13
    • 9644270316 scopus 로고    scopus 로고
    • Neostriatal and cortical quinolinate levels are increased in early grade Huntington's disease
    • Guidetti, P., Luthi-Carter, R.E., Augood, S.J., and Schwarcz, R. 2004. Neostriatal and cortical quinolinate levels are increased in early grade Huntington's disease. Neurobiol. Dis. 17: 455-461.
    • (2004) Neurobiol. Dis. , vol.17 , pp. 455-461
    • Guidetti, P.1    Luthi-Carter, R.E.2    Augood, S.J.3    Schwarcz, R.4
  • 14
    • 0034666543 scopus 로고    scopus 로고
    • A novel degradative pathway of 2-nitrobenzoate via 3-hydroxyanthranilate in Pseudomonas fuorescens strain KU-7
    • Hasegawa, Y., Muraki, T., Tokuyama, T., Iwaki, H., Tatsuno, M., and Lau, P.C.K. 2000. A novel degradative pathway of 2-nitrobenzoate via 3-hydroxyanthranilate in Pseudomonas fuorescens strain KU-7. FEMS Microbiol. Lett. 190: 185-190.
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 185-190
    • Hasegawa, Y.1    Muraki, T.2    Tokuyama, T.3    Iwaki, H.4    Tatsuno, M.5    Lau, P.C.K.6
  • 15
    • 0026663065 scopus 로고
    • Poliovirus induces indoleamine-2,3-dioxygenase and quinolinic acid synthesis in macaque brain
    • Heyes, M.P., Saito, K., Jacobowitz, D., Markey, S.P., Takikawa, O., and Vickers, J.H. 1992. Poliovirus induces indoleamine-2,3-dioxygenase and quinolinic acid synthesis in macaque brain. FASEB J. 6: 2977-2989.
    • (1992) FASEB J. , vol.6 , pp. 2977-2989
    • Heyes, M.P.1    Saito, K.2    Jacobowitz, D.3    Markey, S.P.4    Takikawa, O.5    Vickers, J.H.6
  • 16
    • 0029960647 scopus 로고    scopus 로고
    • Human microglia convert L-tryptophan into the neurotoxin quinolinic acid
    • Heyes, M.P., Achim, C.L., Wiley, C.A., Major, E.O., Saito, K., and Markey, S.P. 1996. Human microglia convert L-tryptophan into the neurotoxin quinolinic acid. Biochem. J. 320: 595-597.
    • (1996) Biochem. J. , vol.320 , pp. 595-597
    • Heyes, M.P.1    Achim, C.L.2    Wiley, C.A.3    Major, E.O.4    Saito, K.5    Markey, S.P.6
  • 17
    • 17644413773 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
    • Koehntop, K.D., Emerson, J.P., and Que Jr., L. 2005. The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J. Biol. Inorg. Chem. 10: 87-93.
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 87-93
    • Koehntop, K.D.1    Emerson, J.P.2    Que Jr., L.3
  • 18
    • 0032513122 scopus 로고    scopus 로고
    • The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis
    • Kucharczyk, R., Zagulskia, M., Rytkaa, J., and Herbertb, C.J. 1998. The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis. FEBS Lett. 424: 127-130.
    • (1998) FEBS Lett. , vol.424 , pp. 127-130
    • Kucharczyk, R.1    Zagulskia, M.2    Rytkaa, J.3    Herbertb, C.J.4
  • 20
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 21
    • 0029858048 scopus 로고    scopus 로고
    • 2-Aminophenol 1,6-dioxygenase: A novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45
    • Lendenmann, U. and Spain, J.C. 1996. 2-Aminophenol 1,6-dioxygenase: A novel aromatic ring cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45. J. Bacteriol. 178: 6227-6232.
    • (1996) J. Bacteriol. , vol.178 , pp. 6227-6232
    • Lendenmann, U.1    Spain, J.C.2
  • 22
    • 6344291632 scopus 로고    scopus 로고
    • Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: Site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)
    • Mendel, S., Arndt, A., and Bugg, T.D.H. 2004. Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: Site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB). Biochemistry 43: 13390-13396.
    • (2004) Biochemistry , vol.43 , pp. 13390-13396
    • Mendel, S.1    Arndt, A.2    Bugg, T.D.H.3
  • 23
    • 0347004630 scopus 로고    scopus 로고
    • Cloning of a gene encoding 4-amino-3-hydroxybenzoate 2,3-dioxygenase from Bordetella sp. 10d
    • Murakami, S., Sawami, Y., Takenaka, S., and Aoki, K. 2004. Cloning of a gene encoding 4-amino-3-hydroxybenzoate 2,3-dioxygenase from Bordetella sp. 10d. Biochem. Biophys. Res. Commun. 314: 489-494.
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 489-494
    • Murakami, S.1    Sawami, Y.2    Takenaka, S.3    Aoki, K.4
  • 24
    • 0037338581 scopus 로고    scopus 로고
    • Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7
    • Muraki, T., Taki, M., Hasegawa, Y., Iwaki, H., and Lau, P.C.K. 2003. Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7. Appl. Environ. Microbiol. 69: 1564-1572.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1564-1572
    • Muraki, T.1    Taki, M.2    Hasegawa, Y.3    Iwaki, H.4    Lau, P.C.K.5
  • 26
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., and Chothia, C. 1995. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247: 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 28
    • 27444438472 scopus 로고    scopus 로고
    • Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440: The prototype of a new subgroup of extradiol dioxygenases
    • Nogales, J., Canales, Á., Jiménez-Barbero, J., García, J.L., and Díaz, E. 2005. Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440: The prototype of a new subgroup of extradiol dioxygenases. J. Biol. Chem. 280: 35382-35390.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35382-35390
    • Nogales, J.1    Canales, Á.2    Jiménez-Barbero, J.3    García, J.L.4    Díaz, E.5
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276A: 307-326.
    • (1997) Methods Enzymol. , vol.276 A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0346849871 scopus 로고    scopus 로고
    • Branching of o-nitrobenzoate degradation pathway in Arthrobacter protophormiae RKJ100: Identification of new intermediates
    • Pandey, J., Paul, D., and Jain, R.K. 2003. Branching of o-nitrobenzoate degradation pathway in Arthrobacter protophormiae RKJ100: Identification of new intermediates. FEMS Microbiol. Lett. 229: 231-236.
    • (2003) FEMS Microbiol. Lett. , vol.229 , pp. 231-236
    • Pandey, J.1    Paul, D.2    Jain, R.K.3
  • 31
    • 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
  • 32
    • 0036895878 scopus 로고    scopus 로고
    • Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae
    • Pochapsky, T.C., Pochapsky, S.S., Ju, T.T., Mo, H.P., Al-Mjeni, F., and Maroney, M.J. 2002. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 9: 966-972.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 966-972
    • Pochapsky, T.C.1    Pochapsky, S.S.2    Ju, T.T.3    Mo, H.P.4    Al-Mjeni, F.5    Maroney, M.J.6
  • 34
    • 0036784518 scopus 로고    scopus 로고
    • Manipulation of brain kynurenines: Glial targets, neuronal effects, and clinical opportunities
    • Schwarcz, R. and Pellicciari, R. 2002. Manipulation of brain kynurenines: Glial targets, neuronal effects, and clinical opportunities. J. Pharmacol. Exp. Ther. 303: 1-10.
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 1-10
    • Schwarcz, R.1    Pellicciari, R.2
  • 35
    • 0020702374 scopus 로고
    • Quinolinic acid: An endogenous metabolite that produces axon-sparing lesions in rat brain
    • Schwarcz, R., Whetsell, W.O., and Mangano, R.M. 1983. Quinolinic acid: An endogenous metabolite that produces axon-sparing lesions in rat brain. Science 219: 316-318.
    • (1983) Science , vol.219 , pp. 316-318
    • Schwarcz, R.1    Whetsell, W.O.2    Mangano, R.M.3
  • 36
    • 0024024251 scopus 로고
    • 3-Hydroxyanthranilate oxygenase activity is increased in the brains of Huntington disease victims
    • Schwarcz, R., Okuno, E., White, R.J., Bird, E.D., and Whetsell Jr., W.O. 1988. 3-Hydroxyanthranilate oxygenase activity is increased in the brains of Huntington disease victims. Proc. Nat. Acad. Sci. 85: 4079-4081.
    • (1988) Proc. Nat. Acad. Sci. , vol.85 , pp. 4079-4081
    • Schwarcz, R.1    Okuno, E.2    White, R.J.3    Bird, E.D.4    Whetsell Jr., W.O.5
  • 37
    • 3242811958 scopus 로고    scopus 로고
    • Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases
    • Siegbahn, P.E.M. and Haeffner, F. 2004. Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases. J. Am. Chem. Soc. 126: 8919-8932.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8919-8932
    • Siegbahn, P.E.M.1    Haeffner, F.2
  • 39
    • 0029789393 scopus 로고    scopus 로고
    • Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): Sequence analysis and biochemical properties of a third family of extradiol dioxygenases
    • Spence, E.L., Kawamukai, M., Sanvoisin, J., Braven, H., and Bugg, T.D.H. 1996. Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): Sequence analysis and biochemical properties of a third family of extradiol dioxygenases. J. Bacteriol. 178:5249-5256.
    • (1996) J. Bacteriol. , vol.178 , pp. 5249-5256
    • Spence, E.L.1    Kawamukai, M.2    Sanvoisin, J.3    Braven, H.4    Bugg, T.D.H.5
  • 40
    • 0036690151 scopus 로고    scopus 로고
    • Endogenous kynurenines as targets for drug discovery and development
    • Stone, T.W. and Darlington, L.G. 2002. Endogenous kynurenines as targets for drug discovery and development. Nat. Rev. Drug Discov. 1: 609-620.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 609-620
    • Stone, T.W.1    Darlington, L.G.2
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 43
    • 0037139492 scopus 로고    scopus 로고
    • Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography
    • Vaillancourt, F.H., Barbosa, C.J., Spiro, T.G., Bolin, J.T., Blades, M.W., Turner, R.F., and Eltis, L.D. 2002. Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography. J. Am. Chem. Soc. 124: 2485-2496.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2485-2496
    • Vaillancourt, F.H.1    Barbosa, C.J.2    Spiro, T.G.3    Bolin, J.T.4    Blades, M.W.5    Turner, R.F.6    Eltis, L.D.7
  • 44
    • 1642264726 scopus 로고    scopus 로고
    • Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases
    • Vetting, M.W., Wackett Jr., L.P., Que, L., Lipscomb, J.D., and Ohlendorf, D.H. 2004. Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. J. Bacteriol. 186: 1945-1958.
    • (2004) J. Bacteriol. , vol.186 , pp. 1945-1958
    • Vetting, M.W.1    Wackett Jr., L.P.2    Que, L.3    Lipscomb, J.D.4    Ohlendorf, D.H.5
  • 45
    • 10344235266 scopus 로고    scopus 로고
    • The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1
    • Viggiani, A., Siani, L., Notomista, E., Birolo, L., Pucci, P., and Donato, A.D. 2004. The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1. J. Biol. Chem. 279: 48630-48639.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48630-48639
    • Viggiani, A.1    Siani, L.2    Notomista, E.3    Birolo, L.4    Pucci, P.5    Donato, A.D.6
  • 46
    • 0033766314 scopus 로고    scopus 로고
    • Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities
    • Woo, E.J., Dunwell, J.M., Goodenough, P.W., Marvier, A.C., and Pickersgill, R.W. 2000. Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nat. Struct. Biol. 7: 1036-1040.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1036-1040
    • Woo, E.J.1    Dunwell, J.M.2    Goodenough, P.W.3    Marvier, A.C.4    Pickersgill, R.W.5
  • 48
    • 19644363211 scopus 로고    scopus 로고
    • Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: The catalytic mechanism of a complex oxidation involved in NAD biosynthesis
    • Zhang, Y., Colabroy, K.L., Begley, T.P., and Ealick, S.E. 2005. Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: The catalytic mechanism of a complex oxidation involved in NAD biosynthesis. Biochemistry 44: 7632-7643.
    • (2005) Biochemistry , vol.44 , pp. 7632-7643
    • Zhang, Y.1    Colabroy, K.L.2    Begley, T.P.3    Ealick, S.E.4


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