메뉴 건너뛰기




Volumn 19, Issue 9, 2013, Pages 958-969

The methionine sulfoxide reduction system: Selenium utilization and methionine sulfoxide reductase enzymes and their functions

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; MSRB1 PROTEIN; PHOSPHOSERYL TRNA KINASE; SELENIUM; SELENOPHOSPHATE SYNTHASE; SELENOPHOSPHATE SYNTHETASE 2; SELENOPROTEIN; SERINE TRANSFER RNA LIGASE; UNCLASSIFIED DRUG;

EID: 84883345286     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.5081     Document Type: Review
Times cited : (89)

References (122)
  • 1
    • 80054001981 scopus 로고    scopus 로고
    • Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2
    • Aachmann FL, Kwak GH, Del Conte R, Kim HY, Gladyshev VN, and Dikiy A. Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2. Proteins 79: 3123-3131, 2011.
    • (2011) Proteins , vol.79 , pp. 3123-3131
    • Aachmann, F.L.1    Kwak, G.H.2    Del Conte, R.3    Kim, H.Y.4    Gladyshev, V.N.5    Dikiy, A.6
  • 2
    • 77958471283 scopus 로고    scopus 로고
    • Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis
    • Aachmann FL, Sal LS, Kim HY, Marino SM, Gladyshev VN, and Dikiy A. Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis. J Biol Chem 285: 33315-33323, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 33315-33323
    • Aachmann, F.L.1    Sal, L.S.2    Kim, H.Y.3    Marino, S.M.4    Gladyshev, V.N.5    Dikiy, A.6
  • 3
    • 79959525303 scopus 로고    scopus 로고
    • Hydrogen sulfide: Redox metabolism and signaling
    • Banerjee R. Hydrogen sulfide: redox metabolism and signaling. Antioxid Redox Signal 15: 339-341, 2011.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 339-341
    • Banerjee, R.1
  • 4
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman KB and Ames BN. The free radical theory of aging matures. Physiol Rev 78: 547-581, 1998.
    • (1998) Physiol Rev , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 5
    • 0025743489 scopus 로고
    • Recognition of UGA as a selenocysteine codon in type i deiodinase requires sequences in the 3¢ untranslated region
    • Berry MJ, Banu L, Chen YY, Mandel SJ, Kieffer JD, Harney JW, and Larsen PR. Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3¢ untranslated region. Nature 353: 273-276, 1991.
    • (1991) Nature , vol.353 , pp. 273-276
    • Berry, M.J.1    Banu, L.2    Chen, Y.Y.3    Mandel, S.J.4    Kieffer, J.D.5    Harney, J.W.6    Larsen, P.R.7
  • 7
    • 0034680847 scopus 로고    scopus 로고
    • A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli
    • Boschi-Muller S, Azza S, Sanglier-Cianferani S, Talfournier F, Van Dorsselear A, and Branlant G. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J Biol Chem 275: 35908-35913, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 35908-35913
    • Boschi-Muller, S.1    Azza, S.2    Sanglier-Cianferani, S.3    Talfournier, F.4    Van Dorsselear, A.5    Branlant, G.6
  • 8
    • 44549088533 scopus 로고    scopus 로고
    • The methionine sulfoxide reductases: Catalysis and substrate specificities
    • Boschi-Muller S, Gand A, and Branlant G. The methionine sulfoxide reductases: catalysis and substrate specificities. Arch Biochem Biophys 474: 266-273, 2008.
    • (2008) Arch Biochem Biophys , vol.474 , pp. 266-273
    • Boschi-Muller, S.1    Gand, A.2    Branlant, G.3
  • 10
    • 47749151115 scopus 로고    scopus 로고
    • Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxida-tive stress-induced cell death and protein damage
    • Cabreiro F, Picot CR, Perichon M, Castel J, Friguet B, and Petropoulos I. Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxida-tive stress-induced cell death and protein damage. J Biol Chem 283: 16673-16681, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 16673-16681
    • Cabreiro, F.1    Picot, C.R.2    Perichon, M.3    Castel, J.4    Friguet, B.5    Petropoulos, I.6
  • 13
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione peroxidase gene: The selenocysteine in the active site is encoded by the 'termination' codon, TGA
    • Chambers I, Frampton J, Goldfarb P, Affara N, McBain W, and Harrison PR. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA. EMBO J 5: 1221-1227, 1986.
    • (1986) EMBO J , vol.5 , pp. 1221-1227
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    McBain, W.5    Harrison, P.R.6
  • 14
    • 20444480652 scopus 로고    scopus 로고
    • Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes
    • Chavatte L, Brown BA, and Driscoll DM. Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes. Nat Struct Mol Biol 12: 408-416, 2005.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 408-416
    • Chavatte, L.1    Brown, B.A.2    Driscoll, D.M.3
  • 15
    • 83055180487 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A regulates cell growth through the p53-p21 pathway
    • Choi SH and Kim HY. Methionine sulfoxide reductase A regulates cell growth through the p53-p21 pathway. Biochem Biophys Res Commun 416: 70-75, 2011.
    • (2011) Biochem Biophys Res Commun , vol.416 , pp. 70-75
    • Choi, S.H.1    Kim, H.Y.2
  • 16
    • 77955659347 scopus 로고    scopus 로고
    • The Drosophila homolog of methionine sulfoxide reductase A extends lifespan and increases nuclear localization of FOXO
    • Chung H, Kim AK, Jung SA, Kim SW, Yu K, and Lee JH. The Drosophila homolog of methionine sulfoxide reductase A extends lifespan and increases nuclear localization of FOXO. FEBS Lett 584: 3609-3614, 2010.
    • (2010) FEBS Lett , vol.584 , pp. 3609-3614
    • Chung, H.1    Kim, A.K.2    Jung, S.A.3    Kim, S.W.4    Yu, K.5    Lee, J.H.6
  • 17
    • 0033520478 scopus 로고    scopus 로고
    • Purification, redox sensitivity, and RNA binding properties of SECIS-binding protein 2, a protein involved in selenoprotein biosynthesis
    • Copeland PR and Driscoll DM. Purification, redox sensitivity, and RNA binding properties of SECIS-binding protein 2, a protein involved in selenoprotein biosynthesis. J Biol Chem 274: 25447-25454, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 25447-25454
    • Copeland, P.R.1    Driscoll, D.M.2
  • 18
    • 0035131148 scopus 로고    scopus 로고
    • Insight into mammalian selenocysteine insertion: Domain structure and ribosome binding properties of Sec insertion sequence binding protein 2
    • Copeland PR, Stepanik VA, and Driscoll DM. Insight into mammalian selenocysteine insertion: domain structure and ribosome binding properties of Sec insertion sequence binding protein 2. Mol Cell Biol 21: 1491-1498, 2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 1491-1498
    • Copeland, P.R.1    Stepanik, V.A.2    Driscoll, D.M.3
  • 19
    • 34250218580 scopus 로고    scopus 로고
    • Important roles of multiple Sp1 binding sites and epigenetic modifications in the regulation of the methionine sulphoxide reductase B1 (MsrB1) promoter
    • De Luca A, Sacchetta P, NiedduM, Di Ilio C, and Favaloro B. Important roles of multiple Sp1 binding sites and epigenetic modifications in the regulation of the methionine sulphoxide reductase B1 (MsrB1) promoter. BMC Mol Biol 8: 39, 2007.
    • (2007) BMC Mol Biol , vol.8 , pp. 39
    • De Luca, A.1    Sacchetta, P.2    Nieddum Di Ilio, C.3    Favaloro, B.4
  • 20
    • 33845904920 scopus 로고    scopus 로고
    • Molecular evolution of peptide methionine sulfoxide reductases (MsrA and MsrB): On the early development of a mechanism that protects against oxidative damage
    • Delaye L, Becerra A, Orgel L, and Lazcano A. Molecular evolution of peptide methionine sulfoxide reductases (MsrA and MsrB): on the early development of a mechanism that protects against oxidative damage. J Mol Evol 64: 15-32, 2007.
    • (2007) J Mol Evol , vol.64 , pp. 15-32
    • Delaye, L.1    Becerra, A.2    Orgel, L.3    Lazcano, A.4
  • 22
    • 0032786120 scopus 로고    scopus 로고
    • Identification of a protein component of a mammalian tRNA(Sec) complex implicated in the decoding of UGA as selenocysteine
    • Ding F and Grabowski PJ. Identification of a protein component of a mammalian tRNA(Sec) complex implicated in the decoding of UGA as selenocysteine. RNA 5: 1561-1569, 1999.
    • (1999) RNA , vol.5 , pp. 1561-1569
    • Ding, F.1    Grabowski, P.J.2
  • 24
    • 0037427533 scopus 로고    scopus 로고
    • A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide
    • Etienne F, Spector D, Brot N, and Weissbach H. A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide. Biochem Biophys Res Commun 300: 378-382, 2003.
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 378-382
    • Etienne, F.1    Spector, D.2    Brot, N.3    Weissbach, H.4
  • 25
    • 0034282536 scopus 로고    scopus 로고
    • Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation
    • Fagegaltier D, Hubert N, Yamada K, Mizutani T, Carbon P, and Krol A. Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation. EMBO J 19: 4796-4805, 2000.
    • (2000) EMBO J , vol.19 , pp. 4796-4805
    • Fagegaltier, D.1    Hubert, N.2    Yamada, K.3    Mizutani, T.4    Carbon, P.5    Krol, A.6
  • 27
    • 0025736565 scopus 로고
    • Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence
    • Forchhammer K and Bock A. Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence. J Biol Chem 266: 6324-6328, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 6324-6328
    • Forchhammer, K.1    Bock, A.2
  • 28
    • 0029973142 scopus 로고    scopus 로고
    • Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene
    • Gladyshev VN, Jeang KT, and Stadtman TC. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc Natl Acad Sci USA 93: 6146-6151, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6146-6151
    • Gladyshev, V.N.1    Jeang, K.T.2    Stadtman, T.C.3
  • 32
    • 1642464647 scopus 로고    scopus 로고
    • A second human methionine sulfoxide reductase (hMSRB2) reducing methionine-R-sulfoxide displays a tissue expression pattern distinct from hMSRB1
    • Hansel A, Jung S, Hoshi T, and Heinemann SH. A second human methionine sulfoxide reductase (hMSRB2) reducing methionine-R-sulfoxide displays a tissue expression pattern distinct from hMSRB1. Redox Rep 8: 384-388, 2003.
    • (2003) Redox Rep , vol.8 , pp. 384-388
    • Hansel, A.1    Jung, S.2    Hoshi, T.3    Heinemann, S.H.4
  • 33
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D. Aging: a theory based on free radical and radiation chemistry. J Gerontol 11: 298-300, 1956.
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 34
    • 0001239924 scopus 로고
    • Opal suppressor serine tRNAs from bovine liver form phosphoseryl-tRNA
    • Hatfield D, Diamond A, and Dudock B. Opal suppressor serine tRNAs from bovine liver form phosphoseryl-tRNA. Proc Natl Acad Sci USA 79: 6215-6219, 1982.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6215-6219
    • Hatfield, D.1    Diamond, A.2    Dudock, B.3
  • 35
    • 0036094506 scopus 로고    scopus 로고
    • How selenium has altered our understanding of the genetic code
    • Hatfield DL and Gladyshev VN. How selenium has altered our understanding of the genetic code. Mol Cell Biol 22: 3565-3576, 2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 3565-3576
    • Hatfield, D.L.1    Gladyshev, V.N.2
  • 36
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor
    • Ho YS, Burden LM, and Hurley JH. Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor. EMBO J 19: 5288-5299, 2000.
    • (2000) EMBO J , vol.19 , pp. 5288-5299
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 37
    • 0032783980 scopus 로고    scopus 로고
    • Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases
    • Huang W, Escribano J, Sarfarazi M, and Coca-Prados M. Identification, expression and chromosome localization of a human gene encoding a novel protein with similarity to the pilB family of transcriptional factors (pilin) and to bacterial peptide methionine sulfoxide reductases. Gene 233: 233-240, 1999.
    • (1999) Gene , vol.233 , pp. 233-240
    • Huang, W.1    Escribano, J.2    Sarfarazi, M.3    Coca-Prados, M.4
  • 38
    • 0042314356 scopus 로고    scopus 로고
    • Sulfur and selenium: The role of oxidation state in protein structure and function
    • Jacob C, Giles GI, Giles NM, and Sies H. Sulfur and selenium: the role of oxidation state in protein structure and function. Angew Chem Int Ed Engl 42: 4742-4758, 2003.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 4742-4758
    • Jacob, C.1    Giles, G.I.2    Giles, N.M.3    Sies, H.4
  • 39
    • 0037063326 scopus 로고    scopus 로고
    • Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: HCBS1
    • Jung S, Hansel A, Kasperczyk H, Hoshi T, and Heinemann SH. Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1. FEBS Lett 527: 91-94, 2002.
    • (2002) FEBS Lett , vol.527 , pp. 91-94
    • Jung, S.1    Hansel, A.2    Kasperczyk, H.3    Hoshi, T.4    Heinemann, S.H.5
  • 41
    • 12844273604 scopus 로고    scopus 로고
    • The three-dimensional structures of peptide methionine sulfoxide reductases: Current knowledge and open questions
    • Kauffmann B, Aubry A, and Favier F. The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions. Biochim Biophys Acta 1703: 249-260, 2005.
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 249-260
    • Kauffmann, B.1    Aubry, A.2    Favier, F.3
  • 42
    • 77952893296 scopus 로고    scopus 로고
    • Dual sites of protein initiation control the localization and myristoylation of methionine sulfoxide reductase A
    • Kim G, Cole NB, Lim JC, Zhao H, and Levine RL. Dual sites of protein initiation control the localization and myristoylation of methionine sulfoxide reductase A. J Biol Chem 285: 18085-18094, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 18085-18094
    • Kim, G.1    Cole, N.B.2    Lim, J.C.3    Zhao, H.4    Levine, R.L.5
  • 43
    • 84863430482 scopus 로고    scopus 로고
    • Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine
    • Kim HY. Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine. Acta Biochim Biophys Sin (Shanghai) 44: 623-627, 2012.
    • (2012) Acta Biochim Biophys Sin (Shanghai) , vol.44 , pp. 623-627
    • Kim, H.Y.1
  • 44
    • 33751220854 scopus 로고    scopus 로고
    • Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases
    • Kim HY, Fomenko DE, Yoon YE, and Gladyshev VN. Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases. Biochemistry 45: 13697-13704, 2006.
    • (2006) Biochemistry , vol.45 , pp. 13697-13704
    • Kim, H.Y.1    Fomenko, D.E.2    Yoon, Y.E.3    Gladyshev, V.N.4
  • 45
    • 3142709434 scopus 로고    scopus 로고
    • Characterization of mouse endoplasmic reticulum methionine-R-sulfoxide reductase
    • Kim HY and Gladyshev VN. Characterization of mouse endoplasmic reticulum methionine-R-sulfoxide reductase. Biochem Biophys Res Commun 320: 1277-1283, 2004.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 1277-1283
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 46
    • 1542313980 scopus 로고    scopus 로고
    • Methionine sulfoxide reduction in mammals: Characterization of methionine-R-sulfoxide reductases
    • Kim HY and Gladyshev VN. Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases. Mol Biol Cell 15: 1055-1064, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 1055-1064
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 47
    • 29144494461 scopus 로고    scopus 로고
    • Different catalytic mechanisms in mammalian selenocysteine-and cysteinecontaining methionine-R-sulfoxide reductases
    • Kim HY and Gladyshev VN. Different catalytic mechanisms in mammalian selenocysteine-and cysteinecontaining methionine-R-sulfoxide reductases. PLoS Biol 3: e375, 2005.
    • (2005) PLoS Biol , vol.3
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 48
    • 20144375447 scopus 로고    scopus 로고
    • Role of structural and functional elements of mouse methionine-S- sulfoxide reductase in its subcellular distribution
    • KimHY and Gladyshev VN. Role of structural and functional elements of mouse methionine-S-sulfoxide reductase in its subcellular distribution. Biochemistry 44: 8059-8067, 2005.
    • (2005) Biochemistry , vol.44 , pp. 8059-8067
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 49
    • 33645651622 scopus 로고    scopus 로고
    • Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases
    • Kim HY and Gladyshev VN. Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases. BMC Mol Biol 7: 11, 2006.
    • (2006) BMC Mol Biol , vol.7 , pp. 11
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 50
    • 35748932403 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Selenoprotein forms and roles in antioxidant protein repair in mammals
    • Kim HY and Gladyshev VN. Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem J 407: 321-329, 2007.
    • (2007) Biochem J , vol.407 , pp. 321-329
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 51
    • 43549109795 scopus 로고    scopus 로고
    • Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine
    • Kim HY and Kim JR. Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine. Biochem Biophys Res Commun 371: 490-494, 2008.
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 490-494
    • Kim, H.Y.1    Kim, J.R.2
  • 52
    • 61449267536 scopus 로고    scopus 로고
    • The selenoproteome of Clostridium sp. OhILAs: Characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A
    • Kim HY, Zhang Y, Lee BC, Kim JR, and Gladyshev VN. The selenoproteome of Clostridium sp. OhILAs: characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase A. Proteins 74: 1008-1017, 2009.
    • (2009) Proteins , vol.74 , pp. 1008-1017
    • Kim, H.Y.1    Zhang, Y.2    Lee, B.C.3    Kim, J.R.4    Gladyshev, V.N.5
  • 53
    • 84876929380 scopus 로고    scopus 로고
    • Protective role of methionine sulfoxide reductase A against ischemia/reperfusion injury in mouse kidney and its involvement in the regulation of trans-sulfuration pathway
    • Kim JI, Choi SH, Jung KJ, Lee E, Kim HY, and Park KM. Protective role of methionine sulfoxide reductase A against ischemia/reperfusion injury in mouse kidney and its involvement in the regulation of trans-sulfuration pathway. Antioxid Redox Signal 18:2241-2250, 2012.
    • (2012) Antioxid Redox Signal , vol.18 , pp. 2241-2250
    • Kim, J.I.1    Choi, S.H.2    Jung, K.J.3    Lee, E.4    Kim, H.Y.5    Park, K.M.6
  • 54
    • 79951808111 scopus 로고    scopus 로고
    • Tandem use of selenocysteine: Adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase
    • Kim MJ, Lee BC, Jeong J, Lee KJ, Hwang KY, Gladyshev VN, and Kim HY. Tandem use of selenocysteine: adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase. Mol Microbiol 79: 1194-1203, 2011.
    • (2011) Mol Microbiol , vol.79 , pp. 1194-1203
    • Kim, M.J.1    Lee, B.C.2    Jeong, J.3    Lee, K.J.4    Hwang, K.Y.5    Gladyshev, V.N.6    Kim, H.Y.7
  • 55
    • 65349106531 scopus 로고    scopus 로고
    • Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae
    • Kim YK, Shin YJ, Lee WH, Kim HY, and Hwang KY. Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae. Mol Microbiol 72: 699-709, 2009.
    • (2009) Mol Microbiol , vol.72 , pp. 699-709
    • Kim, Y.K.1    Shin, Y.J.2    Lee, W.H.3    Kim, H.Y.4    Hwang, K.Y.5
  • 56
    • 2542612966 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and-independent components of aging
    • Koc A, Gasch AP, Rutherford JC, Kim HY, and Gladyshev VN. Methionine sulfoxide reductase regulation of yeast lifespan reveals reactive oxygen species-dependent and-independent components of aging. Proc Natl Acad Sci USA 101: 7999-8004, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7999-8004
    • Koc, A.1    Gasch, A.P.2    Rutherford, J.C.3    Kim, H.Y.4    Gladyshev, V.N.5
  • 58
    • 0033607529 scopus 로고    scopus 로고
    • New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements
    • Kryukov GV, Kryukov VM, and Gladyshev VN. New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements. J Biol Chem 274: 33888-33897, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 33888-33897
    • Kryukov, G.V.1    Kryukov, V.M.2    Gladyshev, V.N.3
  • 59
    • 0037007089 scopus 로고    scopus 로고
    • Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase
    • Kryukov GV, Kumar RA, Koc A, Sun Z, and Gladyshev VN. Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase. Proc Natl Acad Sci USA 99: 4245-4250, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4245-4250
    • Kryukov, G.V.1    Kumar, R.A.2    Koc, A.3    Sun, Z.4    Gladyshev, V.N.5
  • 60
    • 0037020249 scopus 로고    scopus 로고
    • Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase
    • Kumar RA, Koc A, Cerny RL, and Gladyshev VN. Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase. J Biol Chem 277: 37527-37535, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 37527-37535
    • Kumar, R.A.1    Koc, A.2    Cerny, R.L.3    Gladyshev, V.N.4
  • 61
    • 0032770232 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA)
    • Kuschel L, Hansel A, Schonherr R, Weissbach H, Brot N, Hoshi T, and Heinemann SH. Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). FEBS Lett 456: 17-21, 1999.
    • (1999) FEBS Lett , vol.456 , pp. 17-21
    • Kuschel, L.1    Hansel, A.2    Schonherr, R.3    Weissbach, H.4    Brot, N.5    Hoshi, T.6    Heinemann, S.H.7
  • 62
    • 84865419117 scopus 로고    scopus 로고
    • Analyses of methionine sulfoxide reductase activities towards free and peptidyl methionine sulfoxides
    • Kwak GH, Hwang KY, and Kim HY. Analyses of methionine sulfoxide reductase activities towards free and peptidyl methionine sulfoxides. Arch Biochem Biophys 527: 1-5, 2012.
    • (2012) Arch Biochem Biophys , vol.527 , pp. 1-5
    • Kwak, G.H.1    Hwang, K.Y.2    Kim, H.Y.3
  • 63
    • 63049119870 scopus 로고    scopus 로고
    • Expression, subcellular localization, and antioxidant role of mammalian methionine sulfoxide reductases in Saccharomyces cerevisiae
    • Kwak GH, Kim JR, and Kim HY. Expression, subcellular localization, and antioxidant role of mammalian methionine sulfoxide reductases in Saccharomyces cerevisiae. BMB Rep 42: 113-118, 2009.
    • (2009) BMB Rep , vol.42 , pp. 113-118
    • Kwak, G.H.1    Kim, J.R.2    Kim, H.Y.3
  • 64
    • 84862815806 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase B3 protects from endoplasmic reticulum stress in Drosophila and in mammalian cells
    • Kwak GH, Lim DH, Han JY, Lee YS, and Kim HY. Methionine sulfoxide reductase B3 protects from endoplasmic reticulum stress in Drosophila and in mammalian cells. Biochem Biophys Res Commun 420: 130-135, 2012.
    • (2012) Biochem Biophys Res Commun , vol.420 , pp. 130-135
    • Kwak, G.H.1    Lim, D.H.2    Han, J.Y.3    Lee, Y.S.4    Kim, H.Y.5
  • 66
    • 72649087731 scopus 로고    scopus 로고
    • Functions and evolution of selenoprotein methionine sulfoxide reductases
    • Lee BC, Dikiy A, Kim HY, and Gladyshev VN. Functions and evolution of selenoprotein methionine sulfoxide reductases. Biochim Biophys Acta 1790: 1471-1477, 2009.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1471-1477
    • Lee, B.C.1    Dikiy, A.2    Kim, H.Y.3    Gladyshev, V.N.4
  • 67
    • 80055017121 scopus 로고    scopus 로고
    • Selective reduction of methylsulfinyl-containing compounds by mammalian MsrA suggests a strategy for improved drug efficacy
    • Lee BC, Fomenko DE, and Gladyshev VN. Selective reduction of methylsulfinyl-containing compounds by mammalian MsrA suggests a strategy for improved drug efficacy. ACS Chem Biol 6: 1029-1035, 2011.
    • (2011) ACS Chem Biol , vol.6 , pp. 1029-1035
    • Lee, B.C.1    Fomenko, D.E.2    Gladyshev, V.N.3
  • 68
    • 79956318386 scopus 로고    scopus 로고
    • A 4-selenocysteine, 2-selenocysteine insertion sequence (SECIS) element methionine sulfoxide reductase from Metridium senile reveals a non-catalytic function of selenocysteines
    • Lee BC, Lobanov AV, Marino SM, Kaya A, Seravalli J, Hatfield DL, and Gladyshev VN. A 4-selenocysteine, 2-selenocysteine insertion sequence (SECIS) element methionine sulfoxide reductase from Metridium senile reveals a non-catalytic function of selenocysteines. J Biol Chem 286: 18747-18755, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 18747-18755
    • Lee, B.C.1    Lobanov, A.V.2    Marino, S.M.3    Kaya, A.4    Seravalli, J.5    Hatfield, D.L.6    Gladyshev, V.N.7
  • 69
    • 0034646457 scopus 로고    scopus 로고
    • Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity
    • Lee SR, Bar-Noy S, Kwon J, Levine RL, Stadtman TC, and Rhee SG. Mammalian thioredoxin reductase: oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity. Proc Natl Acad Sci USA 97: 2521-2526, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2521-2526
    • Lee, S.R.1    Bar-Noy, S.2    Kwon, J.3    Levine, R.L.4    Stadtman, T.C.5    Rhee, S.G.6
  • 70
    • 52049084778 scopus 로고    scopus 로고
    • An anaerobic bacterial MsrB model reveals catalyticmechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide
    • Lee TH and Kim HY. An anaerobic bacterial MsrB model reveals catalyticmechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide. Arch BiochemBiophys 478: 175-180, 2008.
    • (2008) Arch BiochemBiophys , vol.478 , pp. 175-180
    • Lee, T.H.1    Kim, H.Y.2
  • 71
    • 0024353278 scopus 로고
    • Occurrence in vivo of selenocysteyl-tRNA(SERUCA) in Escherichia coli. Effect of sel mutations
    • Leinfelder W, Stadtman TC, and Bock A. Occurrence in vivo of selenocysteyl-tRNA(SERUCA) in Escherichia coli. Effect of sel mutations. J Biol Chem 264: 9720-9723, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 9720-9723
    • Leinfelder, W.1    Stadtman, T.C.2    Bock, A.3
  • 72
    • 0033621335 scopus 로고    scopus 로고
    • Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif
    • Lescure A, Gautheret D, Carbon P, and Krol A. Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem 274: 38147-38154, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 38147-38154
    • Lescure, A.1    Gautheret, D.2    Carbon, P.3    Krol, A.4
  • 73
    • 77955374397 scopus 로고    scopus 로고
    • Diversity of protein and mRNA forms of mammalian methionine sulfoxide reductase B1 due to intronization and protein processing
    • Liang X, Fomenko DE, Hua D, Kaya A, and Gladyshev VN. Diversity of protein and mRNA forms of mammalian methionine sulfoxide reductase B1 due to intronization and protein processing. PLoS One 5: e11497, 2010.
    • (2010) PLoS One , vol.5
    • Liang, X.1    Fomenko, D.E.2    Hua, D.3    Kaya, A.4    Gladyshev, V.N.5
  • 75
    • 33845428642 scopus 로고    scopus 로고
    • Thioredoxin and related molecules-from biology to health and disease
    • Lillig CH and Holmgren A. Thioredoxin and related molecules-from biology to health and disease. Antioxid Redox Signal 9: 25-47, 2007.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 25-47
    • Lillig, C.H.1    Holmgren, A.2
  • 76
    • 84862832312 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase B in the endoplasmic reticulum is critical for stress resistance and aging in Drosophila
    • Lim DH, Han JY, Kim JR, Lee YS, and Kim HY. Methionine sulfoxide reductase B in the endoplasmic reticulum is critical for stress resistance and aging in Drosophila. Biochem Biophys Res Commun 419: 20-6, 2012.
    • (2012) Biochem Biophys Res Commun , vol.419 , pp. 20-26
    • Lim, D.H.1    Han, J.Y.2    Kim, J.R.3    Lee, Y.S.4    Kim, H.Y.5
  • 77
    • 34447308960 scopus 로고    scopus 로고
    • Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function
    • Lin Z, Johnson LC, Weissbach H, Brot N, Lively MO, and Lowther WT. Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function. Proc Natl Acad Sci USA 104: 9597-9602, 2007.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 9597-9602
    • Lin, Z.1    Johnson, L.C.2    Weissbach, H.3    Brot, N.4    Lively, M.O.5    Lowther, W.T.6
  • 78
    • 0034612330 scopus 로고    scopus 로고
    • Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase
    • Lowther WT, Brot N, Weissbach H, Honek JF, and Matthews BW. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proc Natl Acad Sci USA 97: 6463-6468, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6463-6468
    • Lowther, W.T.1    Brot, N.2    Weissbach, H.3    Honek, J.F.4    Matthews, B.W.5
  • 79
    • 0034619554 scopus 로고    scopus 로고
    • Structure and mechanism of peptide methionine sulfoxide reductase an anti-oxidation enzyme
    • Lowther WT, Brot N, Weissbach H, and Matthews BW. Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme. Biochemistry 39: 13307-13312, 2000.
    • (2000) Biochemistry , vol.39 , pp. 13307-13312
    • Lowther, W.T.1    Brot, N.2    Weissbach, H.3    Matthews, B.W.4
  • 81
    • 59649127414 scopus 로고    scopus 로고
    • Methionine in proteins defends against oxidative stress
    • Luo S and Levine RL. Methionine in proteins defends against oxidative stress. FASEB J 23: 464-472, 2009.
    • (2009) FASEB J , vol.23 , pp. 464-472
    • Luo, S.1    Levine, R.L.2
  • 82
    • 33748680912 scopus 로고    scopus 로고
    • Silencing of the methionine sulfoxide reductase A gene results in loss of mitochondrial membrane potential and increased ROS production in human lens cells
    • Marchetti MA, Lee W, Cowell TL, Wells TM, Weissbach H, and Kantorow M. Silencing of the methionine sulfoxide reductase A gene results in loss of mitochondrial membrane potential and increased ROS production in human lens cells. Exp Eye Res 83: 1281-1286, 2006.
    • (2006) Exp Eye Res , vol.83 , pp. 1281-1286
    • Marchetti, M.A.1    Lee, W.2    Cowell, T.L.3    Wells, T.M.4    Weissbach, H.5    Kantorow, M.6
  • 85
    • 0032564345 scopus 로고    scopus 로고
    • Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress
    • Moskovitz J, Flescher E, Berlett BS, Azare J, Poston JM, and Stadtman ER. Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci USA 95: 14071-14075, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14071-14075
    • Moskovitz, J.1    Flescher, E.2    Berlett, B.S.3    Azare, J.4    Poston, J.M.5    Stadtman, E.R.6
  • 86
    • 0029912239 scopus 로고    scopus 로고
    • Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues
    • Moskovitz J, Jenkins NA, Gilbert DJ, Copeland NG, Jursky F, Weissbach H, and Brot N. Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues. Proc Natl Acad Sci USA 93: 3205-3208, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3205-3208
    • Moskovitz, J.1    Jenkins, N.A.2    Gilbert, D.J.3    Copeland, N.G.4    Jursky, F.5    Weissbach, H.6    Brot, N.7
  • 87
    • 0029935647 scopus 로고    scopus 로고
    • Cloning and expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins
    • Moskovitz J, Weissbach H, and Brot N. Cloning and expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc Natl Acad Sci USA 93: 2095-2099, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2095-2099
    • Moskovitz, J.1    Weissbach, H.2    Brot, N.3
  • 90
    • 35348903730 scopus 로고    scopus 로고
    • Substrates of the methionine sulfoxide reductase system and their physiological relevance
    • Oien DB and Moskovitz J. Substrates of the methionine sulfoxide reductase system and their physiological relevance. Curr Top Dev Biol 80: 93-133, 2008.
    • (2008) Curr Top Dev Biol , vol.80 , pp. 93-133
    • Oien, D.B.1    Moskovitz, J.2
  • 91
    • 27644551030 scopus 로고    scopus 로고
    • Insights into the role of the metal binding site in methionine-R- sulfoxide reductases B
    • Olry A, Boschi-Muller S, Yu H, Burnel D, and Branlant G. Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B. Protein Sci 14: 2828-2837, 2005.
    • (2005) Protein Sci , vol.14 , pp. 2828-2837
    • Olry, A.1    Boschi-Muller, S.2    Yu, H.3    Burnel, D.4    Branlant, G.5
  • 92
    • 34250318625 scopus 로고    scopus 로고
    • From selenium to selenoproteins: Synthesis identity, and their role in human health
    • Papp LV, Lu J, Holmgren A, and Khanna KK. From selenium to selenoproteins: synthesis, identity, and their role in human health. Antioxid Redox Signal 9: 775-806, 2007.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 775-806
    • Papp, L.V.1    Lu, J.2    Holmgren, A.3    Khanna, K.K.4
  • 93
    • 0035339675 scopus 로고    scopus 로고
    • Rat peptide methionine sulphoxide reductase: Cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging
    • Petropoulos I, Mary J, Perichon M, and Friguet B. Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem J 355: 819-825, 2001.
    • (2001) Biochem J , vol.355 , pp. 819-825
    • Petropoulos, I.1    Mary, J.2    Perichon, M.3    Friguet, B.4
  • 94
    • 0842346324 scopus 로고    scopus 로고
    • The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts
    • Picot CR, Perichon M, Cintrat JC, Friguet B, and Petropoulos I. The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts. FEBS Lett 558: 74-78, 2004.
    • (2004) FEBS Lett , vol.558 , pp. 74-78
    • Picot, C.R.1    Perichon, M.2    Cintrat, J.C.3    Friguet, B.4    Petropoulos, I.5
  • 95
    • 33646231787 scopus 로고    scopus 로고
    • S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity
    • Prudova A, Bauman Z, Braun A, Vitvitsky V, Lu SC, and Banerjee R. S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity. Proc Natl Acad Sci USA 103: 6489-6494, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6489-6494
    • Prudova, A.1    Bauman, Z.2    Braun, A.3    Vitvitsky, V.4    Lu, S.C.5    Banerjee, R.6
  • 97
    • 77955511394 scopus 로고    scopus 로고
    • Dynamic change of hydrogen sulfide during global cerebral ischemia-reperfusion and its effect in rats
    • Ren C, Du A, Li D, Sui J, Mayhan WG, and Zhao H. Dynamic change of hydrogen sulfide during global cerebral ischemia-reperfusion and its effect in rats. Brain Res 1345: 197-205, 2010.
    • (2010) Brain Res , vol.1345 , pp. 197-205
    • Ren, C.1    Du, A.2    Li, D.3    Sui, J.4    Mayhan, W.G.5    Zhao, H.6
  • 100
    • 33846019656 scopus 로고    scopus 로고
    • Selenocompounds can serve as oxidoreductants with the methionine sulfoxide reductase enzymes
    • Sagher D, Brunell D, Brot N, Vallee BL, and Weissbach H. Selenocompounds can serve as oxidoreductants with the methionine sulfoxide reductase enzymes. J Biol Chem 281: 31184-31187, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 31184-31187
    • Sagher, D.1    Brunell, D.2    Brot, N.3    Vallee, B.L.4    Weissbach, H.5
  • 102
    • 70349693474 scopus 로고    scopus 로고
    • Lack of methionine sulfoxide reductase A in mice increases sensitivity to oxidative stress but does not diminish life span
    • Salmon AB, Perez VI, Bokov A, Jernigan A, Kim G, Zhao H, Levine RL, and Richardson A. Lack of methionine sulfoxide reductase A in mice increases sensitivity to oxidative stress but does not diminish life span. FASEB J 23: 3601-3608, 2009.
    • (2009) FASEB J , vol.23 , pp. 3601-3608
    • Salmon, A.B.1    Perez, V.I.2    Bokov, A.3    Jernigan, A.4    Kim, G.5    Zhao, H.6    Levine, R.L.7    Richardson, A.8
  • 104
    • 0032815727 scopus 로고    scopus 로고
    • Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase
    • Sharov VS, Ferrington DA, Squier TC, and Schoneich C. Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase. FEBS Lett 455: 247-250, 1999.
    • (1999) FEBS Lett , vol.455 , pp. 247-250
    • Sharov, V.S.1    Ferrington, D.A.2    Squier, T.C.3    Schoneich, C.4
  • 105
    • 80051925711 scopus 로고    scopus 로고
    • Analyses of fruit flies that do not express selenoproteins or express the mouse selenoprotein, methionine sulfoxide reductase B1, reveal a role of selenoproteins in stress resistance
    • Shchedrina VA, Kabil H, Vorbruggen G, Lee BC, Turanov AA, Hirosawa-Takamori M, Kim HY, Harshman LG, Hatfield DL, and Gladyshev VN. Analyses of fruit flies that do not express selenoproteins or express the mouse selenoprotein, methionine sulfoxide reductase B1, reveal a role of selenoproteins in stress resistance. J Biol Chem 286: 29449-29461, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 29449-29461
    • Shchedrina, V.A.1    Kabil, H.2    Vorbruggen, G.3    Lee, B.C.4    Turanov, A.A.5    Hirosawa-Takamori, M.6    Kim, H.Y.7    Harshman, L.G.8    Hatfield, D.L.9    Gladyshev, V.N.10
  • 109
    • 9244265496 scopus 로고    scopus 로고
    • Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation
    • Tamura T, Yamamoto S, Takahata M, Sakaguchi H, Tanaka H, Stadtman TC, and Inagaki K. Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation. Proc Natl Acad Sci USA 101: 16162-16167, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16162-16167
    • Tamura, T.1    Yamamoto, S.2    Takahata, M.3    Sakaguchi, H.4    Tanaka, H.5    Stadtman, T.C.6    Inagaki, K.7
  • 110
    • 84863797987 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding
    • Tarrago L,KayaA,Weerapana E,MarinoSM, and Gladyshev VN. Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding. J Biol Chem 287: 24448-24459, 2012.
    • (2012) J Biol Chem , vol.287 , pp. 24448-24459
    • Tarrago, L.1    Kaya, A.2    Weerapana, E.3    Marino, S.M.4    Gladyshev, V.N.5
  • 111
    • 65249142849 scopus 로고    scopus 로고
    • Protein-repairing methionine sulfoxide reductases in photosynthetic organisms: Gene organization, reduction mechanisms, and physiological roles
    • Tarrago L, Laugier E, and Rey P. Protein-repairing methionine sulfoxide reductases in photosynthetic organisms: gene organization, reduction mechanisms, and physiological roles. Mol Plant 2: 202-217, 2009.
    • (2009) Mol Plant , vol.2 , pp. 202-217
    • Tarrago, L.1    Laugier, E.2    Rey, P.3
  • 112
    • 67650511700 scopus 로고    scopus 로고
    • Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins
    • Tarrago L, Laugier E, Zaffagnini M, Marchand C, Le Marechal P, Rouhier N, and Lemaire SD, Rey P. Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins. J Biol Chem 284: 18963-18971, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 18963-18971
    • Tarrago, L.1    Laugier, E.2    Zaffagnini, M.3    Marchand, C.4    Le Marechal, P.5    Rouhier, N.6    Lemaire, S.D.7    Rey, P.8
  • 113
    • 0038154089 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine
    • Taylor AB, Benglis DM, Jr., Dhandayuthapani S, and Hart PJ. Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine. J Bacteriol 185: 4119-4126, 2003.
    • (2003) J Bacteriol , vol.185 , pp. 4119-4126
    • Taylor, A.B.1    Benglis Jr., D.M.2    Dhandayuthapani, S.3    Hart, P.J.4
  • 114
    • 0034435463 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9A resolution
    • Tete-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G, and Aubry A. Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9A resolution. Structure 8: 1167-1178, 2000.
    • (2000) Structure , vol.8 , pp. 1167-1178
    • Tete-Favier, F.1    Cobessi, D.2    Boschi-Muller, S.3    Azza, S.4    Branlant, G.5    Aubry, A.6
  • 115
    • 34548503203 scopus 로고    scopus 로고
    • Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B
    • Vieira Dos Santos C, Laugier E, Tarrago L, Massot V, Issakidis-Bourguet E, Rouhier N, and Rey P. Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B. FEBS Lett 581: 4371-4376, 2007.
    • (2007) FEBS Lett , vol.581 , pp. 4371-4376
    • Vieira Dos Santos, C.1    Laugier, E.2    Tarrago, L.3    Massot, V.4    Issakidis-Bourguet, E.5    Rouhier, N.6    Rey, P.7
  • 116
    • 0041845204 scopus 로고    scopus 로고
    • Subcellular localization of methionine sulphoxide reductase A (MsrA): Evidence for mitochondrial and cytosolic isoforms in rat liver cells
    • Vougier S, Mary J, and Friguet B. Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells. Biochem J 373: 531-537, 2003.
    • (2003) Biochem J , vol.373 , pp. 531-537
    • Vougier, S.1    Mary, J.2    Friguet, B.3
  • 117
    • 16844365759 scopus 로고    scopus 로고
    • The Nterminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases
    • Wu J, Neiers F, Boschi-Muller S, and Branlant G. The Nterminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases. J Biol Chem 280: 12344-12350, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 12344-12350
    • Wu, J.1    Neiers, F.2    Boschi-Muller, S.3    Branlant, G.4
  • 119
    • 64049088497 scopus 로고    scopus 로고
    • Hydrogen sulfide triggers late-phase preconditioning in postischemic small intestine by an NO-and p38 MAPKdependent mechanism
    • Yusof M, Kamada K, Kalogeris T, Gaskin FS, and Korthuis RJ. Hydrogen sulfide triggers late-phase preconditioning in postischemic small intestine by an NO-and p38 MAPKdependent mechanism. Am J Physiol Heart Circ Physiol 296: H868-H876, 2009.
    • (2009) Am J Physiol Heart Circ Physiol , vol.296
    • Yusof, M.1    Kamada, K.2    Kalogeris, T.3    Gaskin, F.S.4    Korthuis, R.J.5
  • 121
    • 84861372172 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase contributes to meeting dietary methionine requirements
    • Zhao H, Kim G, and Levine RL. Methionine sulfoxide reductase contributes to meeting dietary methionine requirements. Arch Biochem Biophys 522: 37-43, 2012.
    • (2012) Arch Biochem Biophys , vol.522 , pp. 37-43
    • Zhao, H.1    Kim, G.2    Levine, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.