메뉴 건너뛰기




Volumn 92, Issue 9, 2010, Pages 1227-1235

Efficient use and recycling of the micronutrient iodide in mammals

Author keywords

Deiodinase; Flavoprotein; Iodide metabolism; Reductive dehalogenation; Thyroid

Indexed keywords

CYSTEINE; IODIDE; IODOTYROSINE;

EID: 77955841663     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.02.013     Document Type: Review
Times cited : (59)

References (72)
  • 1
    • 77955846750 scopus 로고    scopus 로고
    • http://www.who.int/nutrition/topics/idd/en/index.html.
  • 4
    • 1942522635 scopus 로고
    • The metabolism of iodotyrosines. II. The metabolism of mono and diiodotyrosine in certain patients with familial goiter
    • Stanbury J.B., Meijer J.W.A., Kassenaar A.A.H. The metabolism of iodotyrosines. II. The metabolism of mono and diiodotyrosine in certain patients with familial goiter. J. Clin. Endocrinol. Metab. 1956, 16:848-868.
    • (1956) J. Clin. Endocrinol. Metab. , vol.16 , pp. 848-868
    • Stanbury, J.B.1    Meijer, J.W.A.2    Kassenaar, A.A.H.3
  • 9
    • 67649836744 scopus 로고    scopus 로고
    • The sodium-iodide symporter NIS and pendrin in iodide homeostasis of the thyroid
    • Bizhanova A., Kopp P. The sodium-iodide symporter NIS and pendrin in iodide homeostasis of the thyroid. Endocrinology 2009, 150:1084-1090.
    • (2009) Endocrinology , vol.150 , pp. 1084-1090
    • Bizhanova, A.1    Kopp, P.2
  • 11
    • 0036191639 scopus 로고    scopus 로고
    • Biochemistry, cellular and molecular biology and physiological roles of the iodothyronine selenodeiodinases
    • Bianco A.C., Salvatore D., Gereben B., Berry M.J., Larsen P.R. Biochemistry, cellular and molecular biology and physiological roles of the iodothyronine selenodeiodinases. Endocr. Rev. 2002, 23:38-89.
    • (2002) Endocr. Rev. , vol.23 , pp. 38-89
    • Bianco, A.C.1    Salvatore, D.2    Gereben, B.3    Berry, M.J.4    Larsen, P.R.5
  • 12
    • 67649842307 scopus 로고    scopus 로고
    • Minireview: defining the roles of the iodothyronine deiodinases: current concepts and challenges
    • St.Germain D.L., Galton V.A., Hernandez A. Minireview: defining the roles of the iodothyronine deiodinases: current concepts and challenges. Endocrinology 2009, 150:1097-1107.
    • (2009) Endocrinology , vol.150 , pp. 1097-1107
    • St.Germain, D.L.1    Galton, V.A.2    Hernandez, A.3
  • 14
    • 0025979337 scopus 로고
    • Type I iodothyronine deiodinase is a selenocysteine-containing enzyme
    • Berry M.J., Banu L., Larsen P.R. Type I iodothyronine deiodinase is a selenocysteine-containing enzyme. Nature 1991, 349:438-440.
    • (1991) Nature , vol.349 , pp. 438-440
    • Berry, M.J.1    Banu, L.2    Larsen, P.R.3
  • 15
    • 0026334925 scopus 로고
    • Selenocysteine confers the biochemical properties characteristic of the type I iodothyronine deiodinase
    • Berry M.J., Kieffer J.D., Harney J.W., Larsen P.R. Selenocysteine confers the biochemical properties characteristic of the type I iodothyronine deiodinase. J. Biol. Chem. 1991, 266:14155-14158.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14155-14158
    • Berry, M.J.1    Kieffer, J.D.2    Harney, J.W.3    Larsen, P.R.4
  • 16
    • 0025743489 scopus 로고
    • Recognition of a UGA as a selenocysteine codon in type 1 deiodinase requires sequences in the 3' untranslated region
    • Berry M.J., Banu L., Che Y., Mandel S.J., Kieffer J.D., Harney J.W., Larsen P.R. Recognition of a UGA as a selenocysteine codon in type 1 deiodinase requires sequences in the 3' untranslated region. Nature 1991, 353:273-276.
    • (1991) Nature , vol.353 , pp. 273-276
    • Berry, M.J.1    Banu, L.2    Che, Y.3    Mandel, S.J.4    Kieffer, J.D.5    Harney, J.W.6    Larsen, P.R.7
  • 17
    • 0030975820 scopus 로고    scopus 로고
    • Update on the human iodothyronine selenodeiodinases, the enzymes regulating activation and inactivation of thyroid hormone
    • Larsen P.R. Update on the human iodothyronine selenodeiodinases, the enzymes regulating activation and inactivation of thyroid hormone. Biochem. Soc. Trans. 1997, 25:588-592.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 588-592
    • Larsen, P.R.1
  • 18
    • 0041769723 scopus 로고    scopus 로고
    • Iodothyronine deiodinase mimics. Deiodination of o, o'-diiodophenols by selenium and tellurium reagents
    • Vasil'ev A.A., Engman L. Iodothyronine deiodinase mimics. Deiodination of o, o'-diiodophenols by selenium and tellurium reagents. J. Org. Chem. 1998, 63:3911-3917.
    • (1998) J. Org. Chem. , vol.63 , pp. 3911-3917
    • Vasil'ev, A.A.1    Engman, L.2
  • 19
    • 0003639939 scopus 로고
    • Prentice Hall, Englewood Cliffs, (Chapter 3)
    • McNabb F.M.A. Thyroid Hormones 1992, Prentice Hall, Englewood Cliffs, (Chapter 3).
    • (1992) Thyroid Hormones
    • McNabb, F.M.A.1
  • 21
    • 33646364583 scopus 로고    scopus 로고
    • Iodotyrosine deiodinase is the firs t mammalian member of the NADH oxidase/flavin reductase superfamily
    • Friedman J.E., Watson J.A., Lam D.W.-H., Rokita S.E. Iodotyrosine deiodinase is the firs t mammalian member of the NADH oxidase/flavin reductase superfamily. J. Biol. Chem. 2006, 281:2812-2819.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2812-2819
    • Friedman, J.E.1    Watson, J.A.2    Lam, D.W.-H.3    Rokita, S.E.4
  • 22
    • 0021284171 scopus 로고
    • Iodotyrosine deiodinase from bovine thyroid
    • Rosenberg I.N., Goswami A. Iodotyrosine deiodinase from bovine thyroid. Methods Enzymol. 1984, 107:488-500.
    • (1984) Methods Enzymol. , vol.107 , pp. 488-500
    • Rosenberg, I.N.1    Goswami, A.2
  • 23
    • 84941490882 scopus 로고
    • Über den Abbau von Dijotyrosin im Gewebe
    • Hartmann N. Über den Abbau von Dijotyrosin im Gewebe. Z. Physiol. Chem. 1950, 285:1-17.
    • (1950) Z. Physiol. Chem. , vol.285 , pp. 1-17
    • Hartmann, N.1
  • 24
    • 24444454608 scopus 로고
    • Sur la deshalogénation enzymatique des iodotyrosines par le corps thyroïde et sur son rôle physiologique. II
    • Roche J., Michel O., Michel R., Gorbman A., Lissitzky S. Sur la deshalogénation enzymatique des iodotyrosines par le corps thyroïde et sur son rôle physiologique. II. Biochim. Biophys. Acta 1953, 12:570-576.
    • (1953) Biochim. Biophys. Acta , vol.12 , pp. 570-576
    • Roche, J.1    Michel, O.2    Michel, R.3    Gorbman, A.4    Lissitzky, S.5
  • 25
    • 3042761364 scopus 로고    scopus 로고
    • Comparative kinetic characterization of rat thyroid iodotyrosine dehalogenase and iodothyronine deiodinase type 1
    • Solis-S J.C., Villalobos P., Valverde-R C. Comparative kinetic characterization of rat thyroid iodotyrosine dehalogenase and iodothyronine deiodinase type 1. J. Endocrinol. 2004, 181:385-392.
    • (2004) J. Endocrinol. , vol.181 , pp. 385-392
    • Solis-S, J.C.1    Villalobos, P.2    Valverde-R, C.3
  • 26
    • 0042944051 scopus 로고
    • The occurrence of mono- and diiodotyrosine in the blood of a patient with congential goiter
    • Stanbury J.B., Kassenaar A.A.H., Meijer J.W.A., Terpstra J. The occurrence of mono- and diiodotyrosine in the blood of a patient with congential goiter. J. Clin. Endocrinol. Metab. 1955, 15:1216-1227.
    • (1955) J. Clin. Endocrinol. Metab. , vol.15 , pp. 1216-1227
    • Stanbury, J.B.1    Kassenaar, A.A.H.2    Meijer, J.W.A.3    Terpstra, J.4
  • 27
    • 33744866883 scopus 로고
    • The metabolism of iodotyrosines. I. The fate of mono- and diiodotyrosine in normal subjects and in patients with various diseases
    • Stanbury J.B., Kassenaar A.A.H., Meijer J.W.A. The metabolism of iodotyrosines. I. The fate of mono- and diiodotyrosine in normal subjects and in patients with various diseases. J. Clin. Endocrinol. Metab. 1956, 16:735-746.
    • (1956) J. Clin. Endocrinol. Metab. , vol.16 , pp. 735-746
    • Stanbury, J.B.1    Kassenaar, A.A.H.2    Meijer, J.W.A.3
  • 29
    • 3042719148 scopus 로고
    • The requirement of monoiodotyrosine deiodinase for triphosphopyridine nucleotide
    • Stanbury J.B. The requirement of monoiodotyrosine deiodinase for triphosphopyridine nucleotide. J. Biol. Chem. 1957, 228:801-811.
    • (1957) J. Biol. Chem. , vol.228 , pp. 801-811
    • Stanbury, J.B.1
  • 30
    • 0345055859 scopus 로고
    • Deiodination of diiodotyrosine by cell-free systems
    • Stanbury J.B., Morris M.L. Deiodination of diiodotyrosine by cell-free systems. J. Biol. Chem. 1958, 233:106-108.
    • (1958) J. Biol. Chem. , vol.233 , pp. 106-108
    • Stanbury, J.B.1    Morris, M.L.2
  • 31
    • 0014187720 scopus 로고
    • Deiodination of iodinated amino acids by pig thyroid microsomes
    • Matsuzaki S., Suzuki M. Deiodination of iodinated amino acids by pig thyroid microsomes. J. Biochem. (Tokyo) 1967, 62:746-755.
    • (1967) J. Biochem. (Tokyo) , vol.62 , pp. 746-755
    • Matsuzaki, S.1    Suzuki, M.2
  • 32
    • 0014315340 scopus 로고
    • Inhibition of thyroidal iodotyrosine deiodination by tyrosine analogues
    • Green W.L. Inhibition of thyroidal iodotyrosine deiodination by tyrosine analogues. Endocrinology 1968, 83:336-346.
    • (1968) Endocrinology , vol.83 , pp. 336-346
    • Green, W.L.1
  • 33
    • 0014336439 scopus 로고
    • Changes in thyroid secretion produced by inhibition of iodotyrosine deiodinase
    • Green M.A., Grimm Y. Changes in thyroid secretion produced by inhibition of iodotyrosine deiodinase. Endocrinology 1968, 83:405-410.
    • (1968) Endocrinology , vol.83 , pp. 405-410
    • Green, M.A.1    Grimm, Y.2
  • 34
    • 0018801620 scopus 로고
    • Purification and characterization of a flavoprotein from bovine thyroid with iodotyrosine deiodinase activity
    • Rosenberg I.N., Goswami A. Purification and characterization of a flavoprotein from bovine thyroid with iodotyrosine deiodinase activity. J. Biol. Chem. 1979, 254:12318-12325.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12318-12325
    • Rosenberg, I.N.1    Goswami, A.2
  • 35
    • 67749120727 scopus 로고    scopus 로고
    • Crystal structure of iodotyrosine deiodinase, a novel flavoprotein responsible for iodide salvage in thyroid glands
    • Thomas S., McTamney P.M., Adler J.M., LaRonde-LeBlanc N., Rokita S.E. Crystal structure of iodotyrosine deiodinase, a novel flavoprotein responsible for iodide salvage in thyroid glands. J. Biol. Chem. 2009, 284:19659-19667.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19659-19667
    • Thomas, S.1    McTamney, P.M.2    Adler, J.M.3    LaRonde-LeBlanc, N.4    Rokita, S.E.5
  • 36
    • 0018801621 scopus 로고
    • Characterization of a flavoprotein iodotyrosine deiodinase from bovine thyroid
    • Goswami A., Rosenberg I.N. Characterization of a flavoprotein iodotyrosine deiodinase from bovine thyroid. J. Biol. Chem. 1979, 254:12326-12330.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12326-12330
    • Goswami, A.1    Rosenberg, I.N.2
  • 37
    • 0019515671 scopus 로고
    • Ferredoxin and ferredoxin reductase activities in bovine thyroid. Possible relationship to iodotyrosine deiodinase
    • Goswami A., Rosenberg I.N. Ferredoxin and ferredoxin reductase activities in bovine thyroid. Possible relationship to iodotyrosine deiodinase. J. Biol. Chem. 1981, 256:893-899.
    • (1981) J. Biol. Chem. , vol.256 , pp. 893-899
    • Goswami, A.1    Rosenberg, I.N.2
  • 38
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • Massey V. The chemical and biological versatility of riboflavin. Biochem. Soc. Trans. 2000, 28:283-296.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 283-296
    • Massey, V.1
  • 39
  • 41
    • 34447500880 scopus 로고    scopus 로고
    • The diverse roles of flavin coenzymes - nature's most versatile thespians
    • Mansoorabadi S.O., Thibodeaux C.J., Liu H.-w. The diverse roles of flavin coenzymes - nature's most versatile thespians. J. Org. Chem. 2007, 72:6329-6342.
    • (2007) J. Org. Chem. , vol.72 , pp. 6329-6342
    • Mansoorabadi, S.O.1    Thibodeaux, C.J.2    Liu, H.-W.3
  • 42
    • 0038240633 scopus 로고    scopus 로고
    • Bacterial mercury resistance from atoms to ecosystems
    • Barkay T., Miller S.M., Summers A.O. Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol. Rev. 2003, 27:355-384.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 355-384
    • Barkay, T.1    Miller, S.M.2    Summers, A.O.3
  • 43
    • 33646816419 scopus 로고    scopus 로고
    • Flavin-dependent halogenases involved in secondary metabolism in bacteria
    • van Pée K.-H., Patallo E.P. Flavin-dependent halogenases involved in secondary metabolism in bacteria. Appl. Microbiol. Biotechnol. 2006, 70:631-641.
    • (2006) Appl. Microbiol. Biotechnol. , vol.70 , pp. 631-641
    • van Pée, K.-H.1    Patallo, E.P.2
  • 44
    • 0014802828 scopus 로고
    • Dechlorination of DDT by membranes isolated from Escherichia coli
    • French A.L., Hoopingarner R.A. Dechlorination of DDT by membranes isolated from Escherichia coli. J. Econ. Entomol. 1970, 63:756-759.
    • (1970) J. Econ. Entomol. , vol.63 , pp. 756-759
    • French, A.L.1    Hoopingarner, R.A.2
  • 45
    • 1642393044 scopus 로고    scopus 로고
    • Generation of optically active glycerol derivatives by microbial resolution or development of useful synthetic units for pharmaceuticals
    • Suzuki T., Kasia N. Generation of optically active glycerol derivatives by microbial resolution or development of useful synthetic units for pharmaceuticals. Trends Glycosci. Glycotechnol. 2003, 15:329-349.
    • (2003) Trends Glycosci. Glycotechnol. , vol.15 , pp. 329-349
    • Suzuki, T.1    Kasia, N.2
  • 47
    • 0033583737 scopus 로고    scopus 로고
    • Transition-state stabilization by a mammalian reductive dehalogenase
    • Kunishima M., Friedman J.E., Rokita S.E. Transition-state stabilization by a mammalian reductive dehalogenase. J. Am. Chem. Soc. 1999, 121:4722-4723.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4722-4723
    • Kunishima, M.1    Friedman, J.E.2    Rokita, S.E.3
  • 48
    • 1642490149 scopus 로고    scopus 로고
    • Aromatic dehalogenases: insights into structures, mechanisms, and evolutionary origins
    • Kluwer Academic Publishers, Boston, M.M. Häggblom, I.D. Bossert (Eds.)
    • Copley S.D. Aromatic dehalogenases: insights into structures, mechanisms, and evolutionary origins. Dehalogenation: Microbial Processes and Environmental Applications 2003, 227-259. Kluwer Academic Publishers, Boston. M.M. Häggblom, I.D. Bossert (Eds.).
    • (2003) Dehalogenation: Microbial Processes and Environmental Applications , pp. 227-259
    • Copley, S.D.1
  • 49
    • 36048998185 scopus 로고    scopus 로고
    • Pre-steady-state kinetic studies of the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase
    • Warner J.R., Copley S.D. Pre-steady-state kinetic studies of the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase. Biochemistry 2007, 46:13211-13222.
    • (2007) Biochemistry , vol.46 , pp. 13211-13222
    • Warner, J.R.1    Copley, S.D.2
  • 50
    • 0014868461 scopus 로고
    • Purification of iodotyrosine from bovine thyroid
    • Rosenberg I.N. Purification of iodotyrosine from bovine thyroid. Metabolism 1970, 19:785-798.
    • (1970) Metabolism , vol.19 , pp. 785-798
    • Rosenberg, I.N.1
  • 51
    • 0017642382 scopus 로고
    • Studies on a soluble thyroid iodotyrosine deiodinase: activation by NADPH and electron carriers
    • Goswami A., Rosenberg I.N. Studies on a soluble thyroid iodotyrosine deiodinase: activation by NADPH and electron carriers. Endocrinology 1977, 101:331-341.
    • (1977) Endocrinology , vol.101 , pp. 331-341
    • Goswami, A.1    Rosenberg, I.N.2
  • 52
    • 0024339293 scopus 로고
    • The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid
    • Poole L.B., Claiborne A. The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid. J. Biol. Chem. 1989, 264:12330-12338.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12330-12338
    • Poole, L.B.1    Claiborne, A.2
  • 53
    • 40949144098 scopus 로고    scopus 로고
    • Flavoprotein iodotyrosine deiodinase functions without cysteine residues
    • Watson J.A., McTamney P.M., Adler J.M., Rokita S.E. Flavoprotein iodotyrosine deiodinase functions without cysteine residues. ChemBioChem 2008, 9:504-506.
    • (2008) ChemBioChem , vol.9 , pp. 504-506
    • Watson, J.A.1    McTamney, P.M.2    Adler, J.M.3    Rokita, S.E.4
  • 55
    • 0034969238 scopus 로고    scopus 로고
    • Cloning of tissue-specific genes using serial analysis of gene expression and a novel computation subtraction approach
    • Moreno J.C., Pauws E., van Kampen A.H.C., Jedlicková M., de Vijlder J.J.M., Ris-Stalpers C. Cloning of tissue-specific genes using serial analysis of gene expression and a novel computation subtraction approach. Genomics 2001, 75:70-76.
    • (2001) Genomics , vol.75 , pp. 70-76
    • Moreno, J.C.1    Pauws, E.2    van Kampen, A.H.C.3    Jedlicková, M.4    de Vijlder, J.J.M.5    Ris-Stalpers, C.6
  • 56
    • 0042151174 scopus 로고    scopus 로고
    • Cloning and characterization of a novel thyroidal gene encoding proteins with a conserved nitroreductase domain
    • Moreno J.C., Keijser R., Aarraas S., de Vijlder J.J.M., Ris-Stalpers C. Cloning and characterization of a novel thyroidal gene encoding proteins with a conserved nitroreductase domain. J. Endocrinol. Invest. 2002, 25(Suppl. 7):23.
    • (2002) J. Endocrinol. Invest. , vol.25 , Issue.SUPPL. 7 , pp. 23
    • Moreno, J.C.1    Keijser, R.2    Aarraas, S.3    de Vijlder, J.J.M.4    Ris-Stalpers, C.5
  • 57
    • 0029960505 scopus 로고    scopus 로고
    • Flavin reductase P: structure of a dimeric enzyme that reduces flavin
    • Tanner J.J., Lei B., Tu S.C., Krause K.L. Flavin reductase P: structure of a dimeric enzyme that reduces flavin. Biochemistry 1996, 35:13531-13539.
    • (1996) Biochemistry , vol.35 , pp. 13531-13539
    • Tanner, J.J.1    Lei, B.2    Tu, S.C.3    Krause, K.L.4
  • 58
    • 0034609776 scopus 로고    scopus 로고
    • Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme
    • Parkinson G.N., Skelly J.V., Neidle S. Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme. J. Med. Chem. 2000, 43:3624-3631.
    • (2000) J. Med. Chem. , vol.43 , pp. 3624-3631
    • Parkinson, G.N.1    Skelly, J.V.2    Neidle, S.3
  • 60
    • 33751052250 scopus 로고    scopus 로고
    • Cloning and characterization of a novel isoform of iodotyrosine dehalogenase 1 (DEHAL1) DEHAL1C from human thyroid: comparisons with DEHAL1 and DEHAL1B
    • Gnidehou S., Lacriox L.S., Sezan A., Ohayon R., Noël-Hudson M.-S., Morand S., Francon J., Courtin F., Virion A., Dupuy C. Cloning and characterization of a novel isoform of iodotyrosine dehalogenase 1 (DEHAL1) DEHAL1C from human thyroid: comparisons with DEHAL1 and DEHAL1B. Thyroid 2006, 16:715-724.
    • (2006) Thyroid , vol.16 , pp. 715-724
    • Gnidehou, S.1    Lacriox, L.S.2    Sezan, A.3    Ohayon, R.4    Noël-Hudson, M.-S.5    Morand, S.6    Francon, J.7    Courtin, F.8    Virion, A.9    Dupuy, C.10
  • 61
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: diverse catalysts with recurrent features
    • Fraaije M.W., Mattevi A. Flavoenzymes: diverse catalysts with recurrent features. Trends Biochem. Sci. 2000, 25:126-132.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 62
    • 33646457379 scopus 로고    scopus 로고
    • Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment
    • Lyubimov A.Y., Lario P.I., Moustafa I., Vrielink A. Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment. Nat. Chem. Biol. 2006, 2:259-264.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 259-264
    • Lyubimov, A.Y.1    Lario, P.I.2    Moustafa, I.3    Vrielink, A.4
  • 63
    • 0346364993 scopus 로고    scopus 로고
    • Model systems for flavoenzyme activity: relationships between cofactor structure, binding and redox properties
    • Legrand Y.-M., Gray M., Cooke G., Rotello V.M. Model systems for flavoenzyme activity: relationships between cofactor structure, binding and redox properties. J. Am. Chem. Soc. 2003, 125:15789-15795.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 15789-15795
    • Legrand, Y.-M.1    Gray, M.2    Cooke, G.3    Rotello, V.M.4
  • 64
    • 70350029207 scopus 로고    scopus 로고
    • A mammalian reductive deiodinase has broad power to dehalogenate chlorinated and brominated substrates
    • McTamney P.M., Rokita S.E. A mammalian reductive deiodinase has broad power to dehalogenate chlorinated and brominated substrates. J. Am. Chem. Soc. 2009, 131:14212-14213.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14212-14213
    • McTamney, P.M.1    Rokita, S.E.2
  • 65
    • 0018800960 scopus 로고
    • Oxygen-sensitive and -insensitive nitroreduction by Escherichia coli and rat hepatic microsomes
    • Peterson F.J., Mason R.P., Hovsepian J., Holtzman J.L. Oxygen-sensitive and -insensitive nitroreduction by Escherichia coli and rat hepatic microsomes. J. Biol. Chem. 1979, 254:4009-4014.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4009-4014
    • Peterson, F.J.1    Mason, R.P.2    Hovsepian, J.3    Holtzman, J.L.4
  • 67
    • 0346119143 scopus 로고    scopus 로고
    • Identification of novel genes involved in congenital hypothyroidism using serial analysis of gene expression
    • Moreno J.C. Identification of novel genes involved in congenital hypothyroidism using serial analysis of gene expression. Horm. Res. 2003, 3:96-102.
    • (2003) Horm. Res. , vol.3 , pp. 96-102
    • Moreno, J.C.1
  • 68
    • 0033596905 scopus 로고    scopus 로고
    • 3-Bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: potential markers for eosinophil-dependent tissue injury in vivo
    • Wu W., Chen Y., d'Avignon A., Hazen S.L. 3-Bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: potential markers for eosinophil-dependent tissue injury in vivo. Biochemistry 1999, 38:3538-3548.
    • (1999) Biochemistry , vol.38 , pp. 3538-3548
    • Wu, W.1    Chen, Y.2    d'Avignon, A.3    Hazen, S.L.4
  • 69
    • 0037372157 scopus 로고    scopus 로고
    • 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: association with adverse respiratory outcome
    • Buss I.H., Senthilmohan R., Darlow B.A., Mogridge N., Kettle A.J., Winterbourn C.C. 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: association with adverse respiratory outcome. Pediatr. Res. 2003, 53:455-462.
    • (2003) Pediatr. Res. , vol.53 , pp. 455-462
    • Buss, I.H.1    Senthilmohan, R.2    Darlow, B.A.3    Mogridge, N.4    Kettle, A.J.5    Winterbourn, C.C.6
  • 70
    • 67649986506 scopus 로고    scopus 로고
    • What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach
    • Pattison D.I., Hawkins C.L., Davies M.J. What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach. Chem. Res. Toxicol. 2009, 22:807-817.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 807-817
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.