메뉴 건너뛰기




Volumn 2, Issue 11, 2004, Pages

Protein thiol modifications visualized in vivo

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CYSTEINE; DIHYDROLIPOAMIDE DEHYDROGENASE; DIHYDROLIPOYL TRANSACETYLASE; DISULFIDE; ENZYME; GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE I; HYDROGEN PEROXIDE; METHIONINE SYNTHASE; THIOL; THIOREDOXIN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; METE PROTEIN, E COLI; METHYLTRANSFERASE; OXYGEN; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); THIOL DERIVATIVE;

EID: 14044257165     PISSN: 15449173     EISSN: None     Source Type: Journal    
DOI: 10.1371/journal.pbio.0020333     Document Type: Article
Times cited : (200)

References (61)
  • 1
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status
    • Aslund F, Zheng M, Beckwith J, Storz G (1999) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci U S A 96: 6161-6165.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6161-6165
    • Aslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 2
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization
    • Baker LM, Raudonikiene A, Hoffman PS, Poole LB (2001) Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: Genetic and kinetic characterization. J Bacteriol 183: 1961-1973.
    • (2001) J Bacteriol , vol.183 , pp. 1961-1973
    • Baker, L.M.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 3
    • 0037422610 scopus 로고    scopus 로고
    • Proteomics gives insight into the regulatory function of chloroplast thioredoxins
    • Balmer Y, Koller A, del Val G, Manieri W, Schurmann P, et al. (2003) Proteomics gives insight into the regulatory function of chloroplast thioredoxins. Proc Natl Acad Sci U S A 100: 370-375.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 370-375
    • Balmer, Y.1    Koller, A.2    Del Val, G.3    Manieri, W.4    Schurmann, P.5
  • 4
    • 0028028387 scopus 로고
    • Building bridges: Disulphide bond formation in the cell
    • Bardwell JC (1994) Building bridges: Disulphide bond formation in the cell. Mol Microbiol 14: 199-205.
    • (1994) Mol Microbiol , vol.14 , pp. 199-205
    • Bardwell, J.C.1
  • 5
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell JC, McGovern K, Beckwith J (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67: 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 6
    • 0033580609 scopus 로고    scopus 로고
    • Regulation of PTP1B via glutathionylation of the active site cysteine 215
    • Barrett WC, DeGnore JP, Konig S, Fales HM, Keng YF, et al. (1999) Regulation of PTP1B via glutathionylation of the active site cysteine 215. Biochemistry 38: 6699-6705.
    • (1999) Biochemistry , vol.38 , pp. 6699-6705
    • Barrett, W.C.1    DeGnore, J.P.2    Konig, S.3    Fales, H.M.4    Keng, Y.F.5
  • 8
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • Carmel-Harel O, Storz G (2000) Roles of the glutathione- and thioredox-independent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu Rev Microbiol 54: 439-461.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 9
    • 1542272169 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: Insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins
    • Choi J, Choi S, Cha MK, Kim IH, Shin W (2003) Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: Insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins. J Biol Chem 278: 49478-49486.
    • (2003) J Biol Chem , vol.278 , pp. 49478-49486
    • Choi, J.1    Choi, S.2    Cha, M.K.3    Kim, I.H.4    Shin, W.5
  • 10
    • 0035212036 scopus 로고    scopus 로고
    • Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli
    • Costa Seaver L, Imlay JA (2001) Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J Bacteriol 183: 7182-7189.
    • (2001) J Bacteriol , vol.183 , pp. 7182-7189
    • Costa Seaver, L.1    Imlay, J.A.2
  • 11
    • 0036369545 scopus 로고    scopus 로고
    • S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: Role of thiol oxidation and catalysis by glutaredoxin
    • Cotgreave IA, Gerdes R, Schuppe-Koistinen I, Lind C (2002) S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: Role of thiol oxidation and catalysis by glutaredoxin. Methods Enzymol 348: 175-182.
    • (2002) Methods Enzymol , vol.348 , pp. 175-182
    • Cotgreave, I.A.1    Gerdes, R.2    Schuppe-Koistinen, I.3    Lind, C.4
  • 12
    • 0035059355 scopus 로고    scopus 로고
    • Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity
    • Cronk JD, Endrizzi JA, Cronk MR, O'Neill J W, Zhang KY (2001) Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity. Protein Sci 10: 911-922.
    • (2001) Protein Sci , vol.10 , pp. 911-922
    • Cronk, J.D.1    Endrizzi, J.A.2    Cronk, M.R.3    O'Neill, J.W.4    Zhang, K.Y.5
  • 13
    • 2542469551 scopus 로고    scopus 로고
    • Protein disulfide bond formation in the cytoplasm during oxidative stress
    • Cumming RC, Andon NL, Haynes PA, Park M, Fischer WH, et al. (2004) Protein disulfide bond formation in the cytoplasm during oxidative stress. J Biol Chem 279: 21749-21758.
    • (2004) J Biol Chem , vol.279 , pp. 21749-21758
    • Cumming, R.C.1    Andon, N.L.2    Haynes, P.A.3    Park, M.4    Fischer, W.H.5
  • 14
    • 0021764402 scopus 로고
    • Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli
    • Darlison MG, Guest JR (1984) Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli. Biochem J 223: 507-517.
    • (1984) Biochem J , vol.223 , pp. 507-517
    • Darlison, M.G.1    Guest, J.R.2
  • 15
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman AI, Prinz WA, Belin D, Beckwith J (1993) Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262: 1744-1747.
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 16
    • 0025787778 scopus 로고
    • The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR
    • Donald LJ, Crane BR, Anderson DH, Duckworth HW (1991) The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR. J Biol Chem 266: 20709-20713.
    • (1991) J Biol Chem , vol.266 , pp. 20709-20713
    • Donald, L.J.1    Crane, B.R.2    Anderson, D.H.3    Duckworth, H.W.4
  • 17
    • 0038058016 scopus 로고    scopus 로고
    • Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: Implication for NAD binding and cooperativity
    • Duee E, Olivier-Deyris L, Fanchon E, Corbier C, Branlant G, et al. (1996) Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: Implication for NAD binding and cooperativity. J Mol Biol 257: 814-838.
    • (1996) J Mol Biol , vol.257 , pp. 814-838
    • Duee, E.1    Olivier-Deyris, L.2    Fanchon, E.3    Corbier, C.4    Branlant, G.5
  • 18
    • 0028786979 scopus 로고
    • Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis
    • Dunten P, Mowbray SL (1995) Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis. Protein Sci 4: 2327-2334.
    • (1995) Protein Sci , vol.4 , pp. 2327-2334
    • Dunten, P.1    Mowbray, S.L.2
  • 19
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium
    • Ellis HR, Poole LB (1997) Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry 36: 13349-13356.
    • (1997) Biochemistry , vol.36 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 20
    • 0033614003 scopus 로고    scopus 로고
    • A detailed structural description of Escherichia coli succinyl-CoA synthetase
    • Fraser ME, James MN, Bridger WA, Wolodko WT (1999) A detailed structural description of Escherichia coli succinyl-CoA synthetase. J Mol Biol 285: 1633-1653.
    • (1999) J Mol Biol , vol.285 , pp. 1633-1653
    • Fraser, M.E.1    James, M.N.2    Bridger, W.A.3    Wolodko, W.T.4
  • 21
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli M, Demol H, Puype M, Casagrande S, Eberini I, et al. (2002) Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc Natl Acad Sci U S A 99: 3505-3510.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Eberini, I.5
  • 22
    • 0042622254 scopus 로고    scopus 로고
    • PSORT-B: Improving protein subcellular localization prediction for Gram-negative bacteria
    • Gardy JL, Spencer C, Wang K, Ester M, Tusnady GE, et al. (2003) PSORT-B: Improving protein subcellular localization prediction for Gram-negative bacteria. Nucleic Acids Res 31: 3613-3617.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3613-3617
    • Gardy, J.L.1    Spencer, C.2    Wang, K.3    Ester, M.4    Tusnady, G.E.5
  • 23
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna R, Jaken S (2000) Protein kinase C signaling and oxidative stress. Free Radic Biol Med 28: 1349-1361.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 24
    • 0024991511 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Characterization of the sulfhydryl groups and sitespecific labeling of enzyme I
    • Han MK, Roseman S, Brand L (1990) Sugar transport by the bacterial phosphotransferase system. Characterization of the sulfhydryl groups and sitespecific labeling of enzyme I. J Biol Chem 265: 1985-1995.
    • (1990) J Biol Chem , vol.265 , pp. 1985-1995
    • Han, M.K.1    Roseman, S.2    Brand, L.3
  • 25
    • 0027525666 scopus 로고
    • Aldehyde dehydrogenases: Widespread structural and functional diversity within a shared framework
    • Hempel J, Nicholas H, Lindahl R (1993) Aldehyde dehydrogenases: Widespread structural and functional diversity within a shared framework. Protein Sci 2: 1890-1900.
    • (1993) Protein Sci , vol.2 , pp. 1890-1900
    • Hempel, J.1    Nicholas, H.2    Lindahl, R.3
  • 26
    • 1842477219 scopus 로고    scopus 로고
    • In vivo substrate specificity of periplasmic disulfide oxidoreductases
    • Hiniker A, Bardwell JC (2004) In vivo substrate specificity of periplasmic disulfide oxidoreductases. J Biol Chem 279: 12967-12973.
    • (2004) J Biol Chem , vol.279 , pp. 12967-12973
    • Hiniker, A.1    Bardwell, J.C.2
  • 27
    • 14044271464 scopus 로고    scopus 로고
    • Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli
    • Hondorp ER, Matthews RG (2004) Oxidative stress inactivates cobalaminindependent methionine synthase (MetE) in Escherichia coli. PLoS Biol 2: e336.
    • (2004) PLoS Biol , vol.2
    • Hondorp, E.R.1    Matthews, R.G.2
  • 28
    • 0037189575 scopus 로고    scopus 로고
    • Activation of c-Raf kinase by ultraviolet light. Regulation by retinoids
    • Hoyos B, Imam A, Korichneva I, Levi E, Chua R, et al. (2002) Activation of c-Raf kinase by ultraviolet light. Regulation by retinoids. J Biol Chem 277: 23949-23957.
    • (2002) J Biol Chem , vol.277 , pp. 23949-23957
    • Hoyos, B.1    Imam, A.2    Korichneva, I.3    Levi, E.4    Chua, R.5
  • 29
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob U, Muse W, Eser M, Bardwell JC (1999) Chaperone activity with a redox switch. Cell 96: 341-352.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 30
    • 1642556877 scopus 로고    scopus 로고
    • Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding
    • Kadokura H, Tian H, Zander T, Bardwell JC, Beckwith J (2004) Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding. Science 303: 534-537.
    • (2004) Science , vol.303 , pp. 534-537
    • Kadokura, H.1    Tian, H.2    Zander, T.3    Bardwell, J.C.4    Beckwith, J.5
  • 31
    • 0033517138 scopus 로고    scopus 로고
    • RsrA, an anti-sigma factor regulated by redox change
    • Kang JG, Paget MS, Seok YJ, Hahn MY, Bae JB, et al. (1999) RsrA, an anti-sigma factor regulated by redox change. EMBO J 18: 4292-4298.
    • (1999) EMBO J , vol.18 , pp. 4292-4298
    • Kang, J.G.1    Paget, M.S.2    Seok, Y.J.3    Hahn, M.Y.4    Bae, J.B.5
  • 32
    • 0026770508 scopus 로고
    • Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli
    • Karsten WE, Viola RE (1992) Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Biochim Biophys Acta 1121: 234-238.
    • (1992) Biochim Biophys Acta , vol.1121 , pp. 234-238
    • Karsten, W.E.1    Viola, R.E.2
  • 33
    • 0037013155 scopus 로고    scopus 로고
    • OxyR: A molecular code for redox-related signaling
    • Kim SO, Merchant K, Nudelman R, Beyer WFJ, Keng T, et al. (2002) OxyR: A molecular code for redox-related signaling. Cell 109: 383-396.
    • (2002) Cell , vol.109 , pp. 383-396
    • Kim, S.O.1    Merchant, K.2    Nudelman, R.3    Beyer, W.F.J.4    Keng, T.5
  • 34
    • 0028948780 scopus 로고
    • Redox states of DsbA in the periplasm of Escherichia coli
    • Kishigami S, Akiyama Y, Ito K (1995) Redox states of DsbA in the periplasm of Escherichia coli. FEBS Lett 364: 55-58.
    • (1995) FEBS Lett , vol.364 , pp. 55-58
    • Kishigami, S.1    Akiyama, Y.2    Ito, K.3
  • 35
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin
    • Krause G, Lundstrom J, Barea JL, Pueyo de la Cuesta C, Holmgren A (1991) Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin. J Biol Chem 266: 9494-9500.
    • (1991) J Biol Chem , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundstrom, J.2    Barea, J.L.3    Pueyo De La Cuesta, C.4    Holmgren, A.5
  • 36
    • 0035726624 scopus 로고    scopus 로고
    • Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation
    • Kuge S, Arita M, Murayama A, Maeta K, Izawa S, et al. (2001) Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation. Mol Cell Biol 21: 6139-6150.
    • (2001) Mol Cell Biol , vol.21 , pp. 6139-6150
    • Kuge, S.1    Arita, M.2    Murayama, A.3    Maeta, K.4    Izawa, S.5
  • 37
    • 1642363933 scopus 로고    scopus 로고
    • Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli
    • Kumar JK, Tabor S, Richardson CC (2004) Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. Proc Natl Acad Sci U S A 101: 3759-3764.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 3759-3764
    • Kumar, J.K.1    Tabor, S.2    Richardson, C.C.3
  • 38
    • 0142137134 scopus 로고    scopus 로고
    • Redox regulation of PI 3-kinase signalling via inactivation of PTEN
    • Leslie NR, Bennett D, Lindsay YE, Stewart H, Gray A, et al. (2003) Redox regulation of PI 3-kinase signalling via inactivation of PTEN. EMBO J 22: 5501-5510.
    • (2003) EMBO J , vol.22 , pp. 5501-5510
    • Leslie, N.R.1    Bennett, D.2    Lindsay, Y.E.3    Stewart, H.4    Gray, A.5
  • 39
    • 0001007592 scopus 로고    scopus 로고
    • X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution
    • Li C, Kappock TJ, Stubbe J, Weaver TM, Ealick SE (1999) X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution. Structure Fold Des 7: 1155-1166.
    • (1999) Structure Fold Des , vol.7 , pp. 1155-1166
    • Li, C.1    Kappock, T.J.2    Stubbe, J.3    Weaver, T.M.4    Ealick, S.E.5
  • 40
    • 0042763566 scopus 로고    scopus 로고
    • Not every disulfide lasts forever: Disulfide bond formation as a redox switch
    • Linke K, Jakob U (2003) Not every disulfide lasts forever: Disulfide bond formation as a redox switch. Antioxid Redox Signal 5: 425-434.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 425-434
    • Linke, K.1    Jakob, U.2
  • 41
    • 0026335998 scopus 로고
    • Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain
    • Maeda-Yorita K, Russell GC, Guest JR, Massey V, Williams CH (1991) Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain. Biochemistry 30: 11788-11795.
    • (1991) Biochemistry , vol.30 , pp. 11788-11795
    • Maeda-Yorita, K.1    Russell, G.C.2    Guest, J.R.3    Massey, V.4    Williams, C.H.5
  • 42
    • 0013352438 scopus 로고
    • On the reaction mechanism of lipoyl dehydrogenase
    • Massey V, Veeger C (1960) On the reaction mechanism of lipoyl dehydrogenase. Biochim Biophys Acta 40: 184-185.
    • (1960) Biochim Biophys Acta , vol.40 , pp. 184-185
    • Massey, V.1    Veeger, C.2
  • 46
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with coomassie blue dyes in polyacrylamide gels - A systematic analysis
    • Neuhoff V, Stamm R, Eibl H (1985) Clear background and highly sensitive protein staining with coomassie blue dyes in polyacrylamide gels - a systematic analysis. Electrophoresis 6: 427-448.
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 47
    • 9144274340 scopus 로고    scopus 로고
    • Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution
    • Page R, Nelson MS, von Delft F, Elsliger MA, Canaves JM, et al. (2004) Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution. Proteins 54: 157-161.
    • (2004) Proteins , vol.54 , pp. 157-161
    • Page, R.1    Nelson, M.S.2    Von Delft, F.3    Elsliger, M.A.4    Canaves, J.M.5
  • 48
    • 0348047627 scopus 로고    scopus 로고
    • Proteomic signatures: Amino acid and oligopeptide compositions differentiate among phyla
    • Pe'er I, Felder CE, Man O, Silman I, Sussman JL, et al. (2004) Proteomic signatures: Amino acid and oligopeptide compositions differentiate among phyla. Proteins 54: 20-40.
    • (2004) Proteins , vol.54 , pp. 20-40
    • Pe'er, I.1    Felder, C.E.2    Man, O.3    Silman, I.4    Sussman, J.L.5
  • 49
    • 0037166354 scopus 로고    scopus 로고
    • Protein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase, and function
    • Potamitou A, Holmgren A, Vlamis-Gardikas A (2002) Protein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase, and function. J Biol Chem 277: 18561-18567.
    • (2002) J Biol Chem , vol.277 , pp. 18561-18567
    • Potamitou, A.1    Holmgren, A.2    Vlamis-Gardikas, A.3
  • 50
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz WA, Aslund F, Holmgren A, Beckwith J (1997) The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J Biol Chem 272: 15661-15667.
    • (1997) J Biol Chem , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 52
    • 0037436338 scopus 로고    scopus 로고
    • Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I
    • Rebelo J, Auerbach G, Bader G, Bracher A, Nar H, et al. (2003) Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I. J Mol Biol 326: 503-516.
    • (2003) J Mol Biol , vol.326 , pp. 503-516
    • Rebelo, J.1    Auerbach, G.2    Bader, G.3    Bracher, A.4    Nar, H.5
  • 53
    • 0021881054 scopus 로고
    • Serine hydroxymethyltransferase from Escherichia coli Purification and properties
    • Schirch V, Hopkins S, Villar E, Angelaccio S (1985) Serine hydroxymethyltransferase from Escherichia coli Purification and properties. J Bacteriol 163: 1-7.
    • (1985) J Bacteriol , vol.163 , pp. 1-7
    • Schirch, V.1    Hopkins, S.2    Villar, E.3    Angelaccio, S.4
  • 54
    • 0029646113 scopus 로고
    • The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands
    • Tame JR, Dodson EJ, Murshudov G, Higgins CF, Wilkinson AJ (1995) The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands. Structure 3: 1395-1406.
    • (1995) Structure , vol.3 , pp. 1395-1406
    • Tame, J.R.1    Dodson, E.J.2    Murshudov, G.3    Higgins, C.F.4    Wilkinson, A.J.5
  • 55
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • Varghese S, Tang Y, Imlay JA (2003) Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J Bacteriol 185: 221-230.
    • (2003) J Bacteriol , vol.185 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 56
    • 0034636974 scopus 로고    scopus 로고
    • Structure of 3-deoxyd-arabino-heptulosonate-7-phosphate synthase from Escherichia coli Comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis
    • Wagner T, Shumilin IA, Bauerle R, Kretsinger RH (2000) Structure of 3-deoxyd-arabino-heptulosonate-7-phosphate synthase from Escherichia coli Comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2- phosphoenolpyruvate complexes and implications for catalysis. J Mol Biol 301: 389-399.
    • (2000) J Mol Biol , vol.301 , pp. 389-399
    • Wagner, T.1    Shumilin, I.A.2    Bauerle, R.3    Kretsinger, R.H.4
  • 57
    • 0038393058 scopus 로고    scopus 로고
    • Oxidation of nuclear thioredoxin during oxidative stress
    • Watson WH, Jones DP (2003) Oxidation of nuclear thioredoxin during oxidative stress. FEBS Lett 543: 144-147.
    • (2003) FEBS Lett , vol.543 , pp. 144-147
    • Watson, W.H.1    Jones, D.P.2
  • 60
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M, Aslund F, Storz G (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 61
    • 0033619734 scopus 로고    scopus 로고
    • Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli
    • Zhou ZS, Peariso K, Penner-Hahn JE, Matthews RG (1999) Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli. Biochemistry 38: 15915-15926.
    • (1999) Biochemistry , vol.38 , pp. 15915-15926
    • Zhou, Z.S.1    Peariso, K.2    Penner-Hahn, J.E.3    Matthews, R.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.