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Volumn 1850, Issue 9, 2015, Pages 1795-1805

Iron incorporation into MnSOD A (bacterial Mn-dependent superoxide dismutase) leads to the formation of a peroxidase/catalase implicated in oxidative damage to bacteria

Author keywords

Free radical; Iron; Manganese; Metal; Peroxidase; Superoxide dismutase (SOD)

Indexed keywords

FREE RADICAL; HYDROGEN PEROXIDE; IRON SUPEROXIDE DISMUTASE; MANGANESE SUPEROXIDE DISMUTASE; PEROXIDASE; BACTERIAL PROTEIN; CATALASE; IRON; SODA PROTEIN, BACTERIA; SODB PROTEIN, BACTERIA; SUPEROXIDE DISMUTASE;

EID: 84930507864     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2015.05.006     Document Type: Article
Times cited : (19)

References (60)
  • 1
    • 0014962945 scopus 로고
    • Superoxide dismutase from Escherichia coli B. A new manganese-containing enzyme
    • B.B. Keele Jr., J.M. McCord, and I. Fridovich Superoxide dismutase from Escherichia coli B. A new manganese-containing enzyme J. Biol. Chem. 245 1970 6176 6181
    • (1970) J. Biol. Chem. , vol.245 , pp. 6176-6181
    • Keele, B.B.1    McCord, J.M.2    Fridovich, I.3
  • 2
    • 0015903497 scopus 로고
    • An iron-containing superoxide dismutase from Escherichia coli
    • F.J. Yost Jr., and I. Fridovich An iron-containing superoxide dismutase from Escherichia coli J. Biol. Chem. 248 1973 4905 4908
    • (1973) J. Biol. Chem. , vol.248 , pp. 4905-4908
    • Yost, F.J.1    Fridovich, I.2
  • 3
    • 0021107035 scopus 로고
    • Biochemistry - dressing the SOD
    • R.H. Pain Biochemistry - dressing the SOD Nature 306 1983 228
    • (1983) Nature , vol.306 , pp. 228
    • Pain, R.H.1
  • 6
    • 0016860468 scopus 로고
    • Superoxide dismutase in photosynthetic organisms provides an evolutionary hypothesis
    • J. Lumsden, and D.O. Hall Superoxide dismutase in photosynthetic organisms provides an evolutionary hypothesis Nature 257 1975 670 671
    • (1975) Nature , vol.257 , pp. 670-671
    • Lumsden, J.1    Hall, D.O.2
  • 7
    • 0018472655 scopus 로고
    • Manganese-containing superoxide dismutase from Escherichia coli: Reversible resolution and metal replacements
    • D.E. Ose, and I. Fridovich Manganese-containing superoxide dismutase from Escherichia coli: reversible resolution and metal replacements Arch. Biochem. Biophys. 194 1979 360 364
    • (1979) Arch. Biochem. Biophys. , vol.194 , pp. 360-364
    • Ose, D.E.1    Fridovich, I.2
  • 8
    • 0026067789 scopus 로고
    • In vivo competition between iron and manganese for occupancy of the active-site region of the manganese-superoxide dismutase of Escherichia coli
    • W.F. Beyer, and I. Fridovich In vivo competition between iron and manganese for occupancy of the active-site region of the manganese-superoxide dismutase of Escherichia coli J. Biol. Chem. 266 1991 303 308
    • (1991) J. Biol. Chem. , vol.266 , pp. 303-308
    • Beyer, W.F.1    Fridovich, I.2
  • 9
    • 0024316116 scopus 로고
    • Differences between the manganese-containing and the iron-containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies
    • W.F. Beyer, J.A. Reynolds, and I. Fridovich Differences between the manganese-containing and the iron-containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies Biochemistry 28 1989 4403 4409
    • (1989) Biochemistry , vol.28 , pp. 4403-4409
    • Beyer, W.F.1    Reynolds, J.A.2    Fridovich, I.3
  • 10
    • 84857919018 scopus 로고    scopus 로고
    • Superoxide dismutases: Ancient enzymes and new insights
    • A.-F. Miller Superoxide dismutases: ancient enzymes and new insights FEBS Lett. 586 2012 585 595
    • (2012) FEBS Lett. , vol.586 , pp. 585-595
    • Miller, A.-F.1
  • 11
    • 0017760575 scopus 로고
    • Regulation of the synthesis of superoxide dismutase in Escherichia coli. Induction by methyl viologen
    • H.M. Hassan, and I. Fridovich Regulation of the synthesis of superoxide dismutase in Escherichia coli. Induction by methyl viologen J. Biol. Chem. 252 1977 7667 7672
    • (1977) J. Biol. Chem. , vol.252 , pp. 7667-7672
    • Hassan, H.M.1    Fridovich, I.2
  • 12
    • 84879422944 scopus 로고    scopus 로고
    • The molecular mechanisms and physiological consequences of oxidative stress: Lessons from a model bacterium
    • J.A. Imlay The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium Nat. Rev. Microbiol. 11 2013 443 454
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 443-454
    • Imlay, J.A.1
  • 13
    • 0024428198 scopus 로고
    • Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor
    • G.H.W. Wong, J.H. Elwell, L.W. Oberley, and D.V. Goeddel Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor Cell 58 1989 923 931
    • (1989) Cell , vol.58 , pp. 923-931
    • Wong, G.H.W.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.V.4
  • 14
    • 0025768952 scopus 로고
    • Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli
    • S.I. Liochev, and I. Fridovich Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli J. Biol. Chem. 266 1991 8747 8750
    • (1991) J. Biol. Chem. , vol.266 , pp. 8747-8750
    • Liochev, S.I.1    Fridovich, I.2
  • 16
    • 0033521006 scopus 로고    scopus 로고
    • Role of iron and superoxide for generation of hydroxyl radical, oxidative DNA lesions, and mutagenesis in Escherichia coli
    • T. Nunoshiba, F. Obata, A.C. Boss, S. Oikawa, T. Mori, S. Kawanishi, and K. Yamamoto Role of iron and superoxide for generation of hydroxyl radical, oxidative DNA lesions, and mutagenesis in Escherichia coli J. Biol. Chem. 274 1999 34832 34837
    • (1999) J. Biol. Chem. , vol.274 , pp. 34832-34837
    • Nunoshiba, T.1    Obata, F.2    Boss, A.C.3    Oikawa, S.4    Mori, T.5    Kawanishi, S.6    Yamamoto, K.7
  • 18
    • 0034011039 scopus 로고    scopus 로고
    • Manganese superoxide dismutase as a diagnostic marker for malignant pleural mesothelioma
    • K. Kahlos, P. Paakko, E. Kurttila, Y. Soini, and V.L. Kinnula Manganese superoxide dismutase as a diagnostic marker for malignant pleural mesothelioma Br. J. Cancer 82 2000 1022 1029
    • (2000) Br. J. Cancer , vol.82 , pp. 1022-1029
    • Kahlos, K.1    Paakko, P.2    Kurttila, E.3    Soini, Y.4    Kinnula, V.L.5
  • 20
    • 2442595951 scopus 로고    scopus 로고
    • Tumor suppressive effects of MnSOD overexpression may involve imbalance in peroxide generation versus peroxide removal
    • L.A. Ridnour, T.D. Oberley, and L.W. Oberley Tumor suppressive effects of MnSOD overexpression may involve imbalance in peroxide generation versus peroxide removal Antioxid. Redox Signal. 6 2004 501 512
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 501-512
    • Ridnour, L.A.1    Oberley, T.D.2    Oberley, L.W.3
  • 21
    • 0034938530 scopus 로고    scopus 로고
    • Potential mechanisms for the inhibition of tumor cell growth by manganese superoxide dismutase
    • K.-H. Kim, A.M. Rodriguez, P.M. Carrico, and J.A. Melendez Potential mechanisms for the inhibition of tumor cell growth by manganese superoxide dismutase Antioxid. Redox Signal. 3 2001 361 373
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 361-373
    • Kim, K.-H.1    Rodriguez, A.M.2    Carrico, P.M.3    Melendez, J.A.4
  • 22
    • 34247109461 scopus 로고    scopus 로고
    • The effects of superoxide dismutase on H2O2 formation
    • S.I. Liochev, and I. Fridovich The effects of superoxide dismutase on H2O2 formation Free Radic. Biol. Med. 42 2007 1465 1469
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 1465-1469
    • Liochev, S.I.1    Fridovich, I.2
  • 25
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • J.M. McCord, and I. Fridovich Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) J. Biol. Chem. 244 1969 6049 6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • Mccord, J.M.1    Fridovich, I.2
  • 26
    • 84879764625 scopus 로고    scopus 로고
    • Photooxidation of Amplex Red to resorufin: Implications of exposing the Amplex Red assay to light
    • F.A. Summers, B. Zhao, D. Ganini, and R.P. Mason Photooxidation of Amplex Red to resorufin: implications of exposing the Amplex Red assay to light Methods Enzymol. 526 2013 1 17
    • (2013) Methods Enzymol. , vol.526 , pp. 1-17
    • Summers, F.A.1    Zhao, B.2    Ganini, D.3    Mason, R.P.4
  • 27
    • 84864929834 scopus 로고    scopus 로고
    • Photooxidation of Amplex Red to resorufin: Implications of exposing the Amplex Red assay to light
    • B. Zhao, F.A. Summers, and R.P. Mason Photooxidation of Amplex Red to resorufin: implications of exposing the Amplex Red assay to light Free Radic. Biol. Med. 53 2012 1080 1087
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1080-1087
    • Zhao, B.1    Summers, F.A.2    Mason, R.P.3
  • 28
    • 84874714095 scopus 로고    scopus 로고
    • Immuno-spin trapping: Detection of protein-centered radicals
    • (Chapter 17, Unit 17.7.1-17.7.18)
    • D.C. Ramirez, and R.P. Mason Immuno-spin trapping: detection of protein-centered radicals Curr. Protoc. Toxicol. 2005 (Chapter 17, Unit 17.7.1-17.7.18)
    • (2005) Curr. Protoc. Toxicol.
    • Ramirez, D.C.1    Mason, R.P.2
  • 29
    • 1942520360 scopus 로고    scopus 로고
    • Using anti-5,5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping
    • R.P. Mason Using anti-5,5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping Free Radic. Biol. Med. 36 2004 1214 1223
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1214-1223
    • Mason, R.P.1
  • 31
    • 0034461764 scopus 로고    scopus 로고
    • Regulatable arabinose-inducible gene expression system with consistent control in all cells of a culture
    • A. Khlebnikov, O. Risa, T. Skaug, T.A. Carrier, and J.D. Keasling Regulatable arabinose-inducible gene expression system with consistent control in all cells of a culture J. Bacteriol. 182 2000 7029 7034
    • (2000) J. Bacteriol. , vol.182 , pp. 7029-7034
    • Khlebnikov, A.1    Risa, O.2    Skaug, T.3    Carrier, T.A.4    Keasling, J.D.5
  • 32
    • 0023231486 scopus 로고
    • The enzymatic oxidation of Desferal to a nitroxide free radical
    • K.M. Morehouse, W.D. Flitter, and R.P. Mason The enzymatic oxidation of Desferal to a nitroxide free radical FEBS Lett. 222 1987 246 250
    • (1987) FEBS Lett. , vol.222 , pp. 246-250
    • Morehouse, K.M.1    Flitter, W.D.2    Mason, R.P.3
  • 33
    • 46149116517 scopus 로고    scopus 로고
    • Manganese transport in eukaryotes: The role of DMT1
    • C. Au, A. Benedetto, and M. Aschner Manganese transport in eukaryotes: the role of DMT1 Neurotoxicology 29 2008 569 576
    • (2008) Neurotoxicology , vol.29 , pp. 569-576
    • Au, C.1    Benedetto, A.2    Aschner, M.3
  • 34
    • 0034572933 scopus 로고    scopus 로고
    • Iron homeostasis: Insights from genetics and animal models
    • N.C. Andrews Iron homeostasis: insights from genetics and animal models Nat. Rev. Genet. 1 2000 208 217
    • (2000) Nat. Rev. Genet. , vol.1 , pp. 208-217
    • Andrews, N.C.1
  • 35
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • M.W. Hentze, M.U. Muckenthaler, and N.C. Andrews Balancing acts: molecular control of mammalian iron metabolism Cell 117 2004 285 297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 37
    • 70350336540 scopus 로고    scopus 로고
    • In vitro metal uptake by recombinant human manganese superoxide dismutase
    • M.M. Whittaker, and J.W. Whittaker In vitro metal uptake by recombinant human manganese superoxide dismutase Arch. Biochem. Biophys. 491 2009 69 74
    • (2009) Arch. Biochem. Biophys. , vol.491 , pp. 69-74
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 38
    • 0023851488 scopus 로고
    • Iron superoxide dismutase - nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures
    • A. Carlioz, M.L. Ludwig, W.C. Stallings, J.A. Fee, H.M. Steinman, and D. Touati Iron superoxide dismutase - nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures J. Biol. Chem. 263 1988 1555 1562
    • (1988) J. Biol. Chem. , vol.263 , pp. 1555-1562
    • Carlioz, A.1    Ludwig, M.L.2    Stallings, W.C.3    Fee, J.A.4    Steinman, H.M.5    Touati, D.6
  • 39
    • 0032573845 scopus 로고    scopus 로고
    • Simple proposal that can explain the inactivity of metal-substituted superoxide dismutases
    • C.K. Vance, and A.-F. Miller Simple proposal that can explain the inactivity of metal-substituted superoxide dismutases J. Am. Chem. Soc. 120 1998 461 467
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 461-467
    • Vance, C.K.1    Miller, A.-F.2
  • 41
    • 0036646074 scopus 로고    scopus 로고
    • Mechanistic and molecular investigations on stabilization of horseradish peroxidase C
    • A. Schmidt, J.T. Schumacher, J. Reichelt, H.J. Hecht, and U. Bilitewski Mechanistic and molecular investigations on stabilization of horseradish peroxidase C Anal. Chem. 74 2002 3037 3045
    • (2002) Anal. Chem. , vol.74 , pp. 3037-3045
    • Schmidt, A.1    Schumacher, J.T.2    Reichelt, J.3    Hecht, H.J.4    Bilitewski, U.5
  • 42
    • 54849429128 scopus 로고    scopus 로고
    • Spin trapping investigation of peroxide- and isoniazid-induced radicals in Mycobacterium tuberculosis catalase-peroxidase
    • K. Ranguelova, J. Suarez, R.S. Magliozzo, and R.P. Mason Spin trapping investigation of peroxide- and isoniazid-induced radicals in Mycobacterium tuberculosis catalase-peroxidase Biochemistry 47 2008 11377 11385
    • (2008) Biochemistry , vol.47 , pp. 11377-11385
    • Ranguelova, K.1    Suarez, J.2    Magliozzo, R.S.3    Mason, R.P.4
  • 43
    • 77955096964 scopus 로고    scopus 로고
    • Conversion of the metal-specific activity of Escherichia coli Mn-SOD by site-directed mutagenesis of Gly165Thr
    • M. Osawa, F. Yamakura, M. Mihara, Y. Okubo, K. Yamada, and B.Y. Hiraoka Conversion of the metal-specific activity of Escherichia coli Mn-SOD by site-directed mutagenesis of Gly165Thr Biochim. Biophys. Acta 1804 2010 1775 1779
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1775-1779
    • Osawa, M.1    Yamakura, F.2    Mihara, M.3    Okubo, Y.4    Yamada, K.5    Hiraoka, B.Y.6
  • 44
    • 0042820012 scopus 로고    scopus 로고
    • Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site
    • F. Yamakura, S. Sugio, B.Y. Hiraoka, D. Ohmori, and T. Yokota Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site Biochemistry 42 2003 10790 10799
    • (2003) Biochemistry , vol.42 , pp. 10790-10799
    • Yamakura, F.1    Sugio, S.2    Hiraoka, B.Y.3    Ohmori, D.4    Yokota, T.5
  • 45
    • 0023124274 scopus 로고
    • Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia coli
    • W.F. Beyer, and I. Fridovich Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia coli Biochemistry 26 1987 1251 1257
    • (1987) Biochemistry , vol.26 , pp. 1251-1257
    • Beyer, W.F.1    Fridovich, I.2
  • 46
    • 69949143453 scopus 로고    scopus 로고
    • Mechanistic aspects of horseradish peroxidase elucidated through single-molecule studies
    • H.H. Gorris, and D.R. Walt Mechanistic aspects of horseradish peroxidase elucidated through single-molecule studies J. Am. Chem. Soc. 131 2009 6277 6282
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6277-6282
    • Gorris, H.H.1    Walt, D.R.2
  • 47
    • 84896719872 scopus 로고    scopus 로고
    • Transcriptional regulation by Ferric Uptake Regulator (Fur) in pathogenic bacteria
    • B. Troxell, and H.M. Hassan Transcriptional regulation by Ferric Uptake Regulator (Fur) in pathogenic bacteria Front. Cell. Infect. Microbiol. 3 2013 1 13
    • (2013) Front. Cell. Infect. Microbiol. , vol.3 , pp. 1-13
    • Troxell, B.1    Hassan, H.M.2
  • 48
    • 0026794023 scopus 로고
    • Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese-superoxide dismutase in Escherichia coli
    • C.T. Privalle, and I. Fridovich Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese-superoxide dismutase in Escherichia coli J. Biol. Chem. 267 1992 9140 9145
    • (1992) J. Biol. Chem. , vol.267 , pp. 9140-9145
    • Privalle, C.T.1    Fridovich, I.2
  • 49
    • 84880344474 scopus 로고    scopus 로고
    • Iron depletion increases manganese uptake and potentiates apoptosis through ER stress
    • Y.A. Seo, Y. Li, and M. Wessling-Resnick Iron depletion increases manganese uptake and potentiates apoptosis through ER stress Neurotoxicology 38 2013 67 73
    • (2013) Neurotoxicology , vol.38 , pp. 67-73
    • Seo, Y.A.1    Li, Y.2    Wessling-Resnick, M.3
  • 50
    • 84880390174 scopus 로고    scopus 로고
    • High blood manganese in iron-deficient children in Karachi
    • M.A. Rahman, B. Rahman, and N. Ahmed High blood manganese in iron-deficient children in Karachi Public Health Nutr. 16 2013 1677 1683
    • (2013) Public Health Nutr. , vol.16 , pp. 1677-1683
    • Rahman, M.A.1    Rahman, B.2    Ahmed, N.3
  • 51
    • 0030455852 scopus 로고    scopus 로고
    • Effects of iron deficiency and iron overload on manganese uptake and deposition in the brain and other organs of the rat
    • A.C.G. Chua, and E.H. Morgan Effects of iron deficiency and iron overload on manganese uptake and deposition in the brain and other organs of the rat Biol. Trace Elem. Res. 55 1996 39 54
    • (1996) Biol. Trace Elem. Res. , vol.55 , pp. 39-54
    • Chua, A.C.G.1    Morgan, E.H.2
  • 52
    • 84905828817 scopus 로고    scopus 로고
    • Investigating the role of transferrin in the distribution of iron, manganese, copper, and zinc
    • C. Herrera, M.A. Pettiglio, and T.B. Bartnikas Investigating the role of transferrin in the distribution of iron, manganese, copper, and zinc J. Biol. Inorg. Chem. 19 2014 869 877
    • (2014) J. Biol. Inorg. Chem. , vol.19 , pp. 869-877
    • Herrera, C.1    Pettiglio, M.A.2    Bartnikas, T.B.3
  • 53
    • 0014705297 scopus 로고
    • Modification of chronic manganese poisoning. Treatment with L-dopa or 5-OH tryptophane
    • I. Mena, J. Court, S. Fuenzalida, P.S. Papavasiliou, and G.C. Cotzias Modification of chronic manganese poisoning. Treatment with L-dopa or 5-OH tryptophane N. Engl. J. Med. 282 1970 5 10
    • (1970) N. Engl. J. Med. , vol.282 , pp. 5-10
    • Mena, I.1    Court, J.2    Fuenzalida, S.3    Papavasiliou, P.S.4    Cotzias, G.C.5
  • 56
    • 0036211994 scopus 로고    scopus 로고
    • The Haber-Weiss cycle - 70 years later: An alternative view
    • S.I. Liochev, and I. Fridovich The Haber-Weiss cycle - 70 years later: an alternative view Redox Rep. 7 2002 55 57
    • (2002) Redox Rep. , vol.7 , pp. 55-57
    • Liochev, S.I.1    Fridovich, I.2
  • 57
    • 0036204446 scopus 로고    scopus 로고
    • The Haber-Weiss cycle - 71 years later
    • W.H. Koppenol The Haber-Weiss cycle - 71 years later Redox Rep. 7 2002 59 60
    • (2002) Redox Rep. , vol.7 , pp. 59-60
    • Koppenol, W.H.1
  • 58
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • A. Anjem, S. Varghese, and J.A. Imlay Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli Mol. Microbiol. 72 2009 844 858
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 59
    • 34247472147 scopus 로고    scopus 로고
    • Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli
    • S. Varghese, A. Wu, S. Park, K.R. Imlay, and J.A. Imlay Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli Mol. Microbiol. 64 2007 822 830
    • (2007) Mol. Microbiol. , vol.64 , pp. 822-830
    • Varghese, S.1    Wu, A.2    Park, S.3    Imlay, K.R.4    Imlay, J.A.5


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