메뉴 건너뛰기




Volumn 80, Issue , 2007, Pages 93-133

Substrates of the Methionine Sulfoxide Reductase System and Their Physiological Relevance

Author keywords

[No Author keywords available]

Indexed keywords

DRUG DERIVATIVE; ENZYME; HORMONE; METHIONINE; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; OXIDOREDUCTASE; SCAVENGER; SERINE PROTEINASE INHIBITOR;

EID: 35348903730     PISSN: 00702153     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2153(07)80003-2     Document Type: Review
Times cited : (104)

References (166)
  • 1
    • 0019853331 scopus 로고
    • Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity
    • Abrams W.R., Weinbaum G., Weissbach L., Weissbach H., and Brot N. Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity. Proc. Natl. Acad. Sci. USA 78 (1981) 7483-7486
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 7483-7486
    • Abrams, W.R.1    Weinbaum, G.2    Weissbach, L.3    Weissbach, H.4    Brot, N.5
  • 2
    • 4444275438 scopus 로고    scopus 로고
    • Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen Helicobacter pylori
    • Alamuri P., and Maier R.J. Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen Helicobacter pylori. Mol. Microbiol. 53 (2004) 1397-1406
    • (2004) Mol. Microbiol. , vol.53 , pp. 1397-1406
    • Alamuri, P.1    Maier, R.J.2
  • 3
    • 33746577830 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase in Helicobacter pylori: Interaction with methionine-rich proteins and stress-induced expression
    • Alamuri P., and Maier R.J. Methionine sulfoxide reductase in Helicobacter pylori: Interaction with methionine-rich proteins and stress-induced expression. J. Bacteriol. 188 (2006) 5839-5850
    • (2006) J. Bacteriol. , vol.188 , pp. 5839-5850
    • Alamuri, P.1    Maier, R.J.2
  • 4
    • 0024443854 scopus 로고
    • Selective oxidation of methionine beta(55)D6 at the alpha 1 beta 1 interface in hemoglobin completely destabilizes the T-state
    • Amiconi G., Ascoli F., Barra D., Bertollini A., Matarese R.M., Verzili D., and Brunori M. Selective oxidation of methionine beta(55)D6 at the alpha 1 beta 1 interface in hemoglobin completely destabilizes the T-state. J. Biol. Chem. 264 (1989) 17745-17749
    • (1989) J. Biol. Chem. , vol.264 , pp. 17745-17749
    • Amiconi, G.1    Ascoli, F.2    Barra, D.3    Bertollini, A.4    Matarese, R.M.5    Verzili, D.6    Brunori, M.7
  • 5
    • 0029562244 scopus 로고    scopus 로고
    • Chromatographic methods for quantitation of apolipoprotein A-I
    • Anantharamaiah G.M., and Garber D.W. Chromatographic methods for quantitation of apolipoprotein A-I. Methods Enzymol. 263 (1996) 267-282
    • (1996) Methods Enzymol. , vol.263 , pp. 267-282
    • Anantharamaiah, G.M.1    Garber, D.W.2
  • 7
    • 0023677281 scopus 로고
    • Reversed phase high performance liquid chromatography of adrenocorticotropin 1-39 and its fragments in the native and oxidized forms
    • Antonini G., and Spoto G. Reversed phase high performance liquid chromatography of adrenocorticotropin 1-39 and its fragments in the native and oxidized forms. Biochem. Int. 16 (1988) 1009-1017
    • (1988) Biochem. Int. , vol.16 , pp. 1009-1017
    • Antonini, G.1    Spoto, G.2
  • 8
    • 0038182558 scopus 로고    scopus 로고
    • Calmodulin oxidation and methionine to glutamine substitutions reveal methionine residues critical for functional interaction with ryanodine receptor-1
    • Balog E.M., Norton L.E., Bloomquist R.A., Cornea R.L., Black D.J., Louis C.F., Thomas D.D., and Fruen B.R. Calmodulin oxidation and methionine to glutamine substitutions reveal methionine residues critical for functional interaction with ryanodine receptor-1. J. Biol. Chem. 278 (2003) 15615-15621
    • (2003) J. Biol. Chem. , vol.278 , pp. 15615-15621
    • Balog, E.M.1    Norton, L.E.2    Bloomquist, R.A.3    Cornea, R.L.4    Black, D.J.5    Louis, C.F.6    Thomas, D.D.7    Fruen, B.R.8
  • 9
    • 4644260271 scopus 로고    scopus 로고
    • Met-enkephalin modulates resistance to oxidative stress in mouse brain
    • Balog T., Sobocanec S., Sverko V., and Marotti T. Met-enkephalin modulates resistance to oxidative stress in mouse brain. Neuropeptides 38 (2004) 298-303
    • (2004) Neuropeptides , vol.38 , pp. 298-303
    • Balog, T.1    Sobocanec, S.2    Sverko, V.3    Marotti, T.4
  • 10
    • 0036033166 scopus 로고    scopus 로고
    • Mouse methionine sulfoxide reductase B: Effect of selenocysteine incorporation on its activity and expression of the seleno-containing enzyme in bacterial and mammalian cells
    • Bar-Noy S., and Moskovitz J. Mouse methionine sulfoxide reductase B: Effect of selenocysteine incorporation on its activity and expression of the seleno-containing enzyme in bacterial and mammalian cells. Biochem. Biophys. Res. Commun. 297 (2002) 956-961
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 956-961
    • Bar-Noy, S.1    Moskovitz, J.2
  • 11
    • 4444339761 scopus 로고    scopus 로고
    • Neuropeptide Y and epilepsy: Recent progress, prospects and controversies
    • Baraban S.C. Neuropeptide Y and epilepsy: Recent progress, prospects and controversies. Neuropeptides 38 (2004) 261-265
    • (2004) Neuropeptides , vol.38 , pp. 261-265
    • Baraban, S.C.1
  • 13
    • 0037465704 scopus 로고    scopus 로고
    • Oxidation of Met144 and Met145 in calmodulin blocks calmodulin dependent activation of the plasma membrane Ca-ATPase
    • Bartlett R.K., Bieber Urbauer R.J., Anbanandam A., Smallwood H.S., Urbauer J.L., and Squier T.C. Oxidation of Met144 and Met145 in calmodulin blocks calmodulin dependent activation of the plasma membrane Ca-ATPase. Biochemistry 42 (2003) 3231-3238
    • (2003) Biochemistry , vol.42 , pp. 3231-3238
    • Bartlett, R.K.1    Bieber Urbauer, R.J.2    Anbanandam, A.3    Smallwood, H.S.4    Urbauer, J.L.5    Squier, T.C.6
  • 15
    • 0031909323 scopus 로고    scopus 로고
    • Effects of dihydrolipoic acid on peptide methionine sulfoxide reductase. Implications for antioxidant drugs
    • Biewenga G.P., Veening-Griffioen D.H., Nicastia A.J., Haenen G.R., and Bast A. Effects of dihydrolipoic acid on peptide methionine sulfoxide reductase. Implications for antioxidant drugs. Arzneimittelforschung 48 (1998) 144-148
    • (1998) Arzneimittelforschung , vol.48 , pp. 144-148
    • Biewenga, G.P.1    Veening-Griffioen, D.H.2    Nicastia, A.J.3    Haenen, G.R.4    Bast, A.5
  • 16
    • 12844257477 scopus 로고    scopus 로고
    • Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins
    • Bigelow D.J., and Squier T.C. Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins. Biochim. Biophys. Acta 1703 (2005) 121-134
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 121-134
    • Bigelow, D.J.1    Squier, T.C.2
  • 17
    • 0028064657 scopus 로고
    • Oxidized mucus proteinase inhibitor: A fairly potent neutrophil elastase inhibitor
    • Boudier C., and Bieth J.G. Oxidized mucus proteinase inhibitor: A fairly potent neutrophil elastase inhibitor. Biochem. J. 303 Pt. 1 (1994) 61-68
    • (1994) Biochem. J. , vol.303 , Issue.PART 1 , pp. 61-68
    • Boudier, C.1    Bieth, J.G.2
  • 18
    • 28244486826 scopus 로고    scopus 로고
    • Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation
    • Breydo L., Bocharova O.V., Makarava N., Salnikov V.V., Anderson M., and Baskakov I.V. Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation. Biochemistry 44 (2005) 15534-15543
    • (2005) Biochemistry , vol.44 , pp. 15534-15543
    • Breydo, L.1    Bocharova, O.V.2    Makarava, N.3    Salnikov, V.V.4    Anderson, M.5    Baskakov, I.V.6
  • 19
    • 33845985580 scopus 로고    scopus 로고
    • Formation of methionine sulfoxide during glycoxidation and lipoxidation of ribonuclease A
    • Brock J.W., Ames J.M., Thorpe S.R., and Baynes J.W. Formation of methionine sulfoxide during glycoxidation and lipoxidation of ribonuclease A. Arch. Biochem. Biophys. 457 (2007) 170-176
    • (2007) Arch. Biochem. Biophys. , vol.457 , pp. 170-176
    • Brock, J.W.1    Ames, J.M.2    Thorpe, S.R.3    Baynes, J.W.4
  • 20
    • 0034467710 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase: Biochemistry and physiological role
    • Brot N., and Weissbach H. Peptide methionine sulfoxide reductase: Biochemistry and physiological role. Biopolymers 55 (2000) 288-296
    • (2000) Biopolymers , vol.55 , pp. 288-296
    • Brot, N.1    Weissbach, H.2
  • 23
    • 0037987893 scopus 로고    scopus 로고
    • The biological clock tunes the organs of the body: Timing by hormones and the autonomic nervous system
    • Buijs R.M., van Eden C.G., Goncharuk V.D., and Kalsbeek A. The biological clock tunes the organs of the body: Timing by hormones and the autonomic nervous system. J. Endocrinol. 177 (2003) 17-26
    • (2003) J. Endocrinol. , vol.177 , pp. 17-26
    • Buijs, R.M.1    van Eden, C.G.2    Goncharuk, V.D.3    Kalsbeek, A.4
  • 24
    • 33748177699 scopus 로고    scopus 로고
    • Inwardly rectifying potassium channels (Kir) in central nervous system glia: A special role for Kir4.1 in glial functions
    • Butt A.M., and Kalsi A. Inwardly rectifying potassium channels (Kir) in central nervous system glia: A special role for Kir4.1 in glial functions. J. Cell. Mol. Med. 10 (2006) 33-44
    • (2006) J. Cell. Mol. Med. , vol.10 , pp. 33-44
    • Butt, A.M.1    Kalsi, A.2
  • 25
    • 0042226507 scopus 로고
    • Oxidation of the methionine residues of Escherichia coli ribosomal protein L12 decreases the protein's biological activity
    • Caldwell P., Luk D.C., Weissbach H., and Brot N. Oxidation of the methionine residues of Escherichia coli ribosomal protein L12 decreases the protein's biological activity. Proc. Natl. Acad. Sci. USA 75 (1978) 5349-5352
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5349-5352
    • Caldwell, P.1    Luk, D.C.2    Weissbach, H.3    Brot, N.4
  • 26
    • 0017894884 scopus 로고
    • The oxidation of methionine and its effect of the properties of cardiotoxin VII1 from Naja melanoleuca venom
    • Carlsson F.H., and Louw A.I. The oxidation of methionine and its effect of the properties of cardiotoxin VII1 from Naja melanoleuca venom. Biochim. Biophys. Acta 534 (1978) 322-330
    • (1978) Biochim. Biophys. Acta , vol.534 , pp. 322-330
    • Carlsson, F.H.1    Louw, A.I.2
  • 27
    • 0019258204 scopus 로고
    • Inactivation of bronchial mucous proteinase inhibitor by cigarette smoke and phagocyte-derived oxidants
    • Carp H., and Janoff A. Inactivation of bronchial mucous proteinase inhibitor by cigarette smoke and phagocyte-derived oxidants. Exp. Lung Res. 1 (1980) 225-237
    • (1980) Exp. Lung Res. , vol.1 , pp. 225-237
    • Carp, H.1    Janoff, A.2
  • 28
    • 0030952676 scopus 로고    scopus 로고
    • Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems
    • Chao C.C., Ma Y.S., and Stadtman E.R. Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems. Proc. Natl. Acad. Sci. USA 94 (1997) 2969-2974
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2969-2974
    • Chao, C.C.1    Ma, Y.S.2    Stadtman, E.R.3
  • 29
    • 0034112773 scopus 로고    scopus 로고
    • Acceleration of P/C-type inactivation in voltage-gated K(+) channels by methionine oxidation
    • Chen J., Avdonin V., Ciorba M.A., Heinemann S.H., and Hoshi T. Acceleration of P/C-type inactivation in voltage-gated K(+) channels by methionine oxidation. Biophys. J. 78 (2000) 174-187
    • (2000) Biophys. J. , vol.78 , pp. 174-187
    • Chen, J.1    Avdonin, V.2    Ciorba, M.A.3    Heinemann, S.H.4    Hoshi, T.5
  • 30
    • 0037119359 scopus 로고    scopus 로고
    • Protein oxidation of cytochrome C by reactive halogen species enhances its peroxidase activity
    • Chen Y.R., Deterding L.J., Sturgeon B.E., Tomer K.B., and Mason R.P. Protein oxidation of cytochrome C by reactive halogen species enhances its peroxidase activity. J. Biol. Chem. 277 (2002) 29781-29791
    • (2002) J. Biol. Chem. , vol.277 , pp. 29781-29791
    • Chen, Y.R.1    Deterding, L.J.2    Sturgeon, B.E.3    Tomer, K.B.4    Mason, R.P.5
  • 32
    • 0027331010 scopus 로고
    • Met-8 of the beta 1-bungarotoxin phospholipase A2 subunit is essential for the phospholipase A2-independent neurotoxic effect
    • Chu S.T., Chu C.C., Tseng C.C., and Chen Y.H. Met-8 of the beta 1-bungarotoxin phospholipase A2 subunit is essential for the phospholipase A2-independent neurotoxic effect. Biochem. J. 295 Pt. 3 (1993) 713-718
    • (1993) Biochem. J. , vol.295 , Issue.PART 3 , pp. 713-718
    • Chu, S.T.1    Chu, C.C.2    Tseng, C.C.3    Chen, Y.H.4
  • 36
    • 0033592425 scopus 로고    scopus 로고
    • The tert-butyl hydroperoxide-induced oxidation of actin Cys-374 is coupled with structural changes in distant regions of the protein
    • DalleDonne I., Milzani A., and Colombo R. The tert-butyl hydroperoxide-induced oxidation of actin Cys-374 is coupled with structural changes in distant regions of the protein. Biochemistry 38 (1999) 12471-12480
    • (1999) Biochemistry , vol.38 , pp. 12471-12480
    • DalleDonne, I.1    Milzani, A.2    Colombo, R.3
  • 39
    • 0034163437 scopus 로고    scopus 로고
    • HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase
    • Davis D.A., Newcomb F.M., Moskovitz J., Wingfield P.T., Stahl S.J., Kaufman J., Fales H.M., Levine R.L., and Yarchoan R. HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase. Biochem. J. 346 Pt. 2 (2000) 305-311
    • (2000) Biochem. J. , vol.346 , Issue.PART 2 , pp. 305-311
    • Davis, D.A.1    Newcomb, F.M.2    Moskovitz, J.3    Wingfield, P.T.4    Stahl, S.J.5    Kaufman, J.6    Fales, H.M.7    Levine, R.L.8    Yarchoan, R.9
  • 41
    • 0019272521 scopus 로고
    • Oxidation of methionine residues in lutropin
    • De la Llosa P., El Abed A., and Roy M. Oxidation of methionine residues in lutropin. Can. J. Biochem. 58 (1980) 745-748
    • (1980) Can. J. Biochem. , vol.58 , pp. 745-748
    • De la Llosa, P.1    El Abed, A.2    Roy, M.3
  • 42
    • 0005449662 scopus 로고
    • Studies on pituitary adrenocorticotrophin. 3. Identification of the oxidation-reduction centre
    • Dedman M.L., Farmer T.H., and Morris C.J. Studies on pituitary adrenocorticotrophin. 3. Identification of the oxidation-reduction centre. Biochem. J. 78 (1961) 348-352
    • (1961) Biochem. J. , vol.78 , pp. 348-352
    • Dedman, M.L.1    Farmer, T.H.2    Morris, C.J.3
  • 43
    • 0030610119 scopus 로고    scopus 로고
    • Oxidation of a critical methionine modulates DNA binding of the Drosophila melanogaster high mobility group protein, HMG-D
    • Dow L.K., Changela A., Hefner H.E., and Churchill M.E. Oxidation of a critical methionine modulates DNA binding of the Drosophila melanogaster high mobility group protein, HMG-D. FEBS Lett. 414 (1997) 514-520
    • (1997) FEBS Lett. , vol.414 , pp. 514-520
    • Dow, L.K.1    Changela, A.2    Hefner, H.E.3    Churchill, M.E.4
  • 44
    • 0024430085 scopus 로고
    • Recognition of modified forms of ribonuclease A by the ubiquitin system
    • Dunten R.L., and Cohen R.E. Recognition of modified forms of ribonuclease A by the ubiquitin system. J. Biol. Chem. 264 (1989) 16739-16747
    • (1989) J. Biol. Chem. , vol.264 , pp. 16739-16747
    • Dunten, R.L.1    Cohen, R.E.2
  • 45
    • 26444507244 scopus 로고    scopus 로고
    • Physiology or medicine. Triumph of the ulcer-bug theory
    • Enserink M. Physiology or medicine. Triumph of the ulcer-bug theory. Science 310 (2005) 34-35
    • (2005) Science , vol.310 , pp. 34-35
    • Enserink, M.1
  • 46
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • Esmon C.T. The roles of protein C and thrombomodulin in the regulation of blood coagulation. J. Biol. Chem. 264 (1989) 4743-4746
    • (1989) J. Biol. Chem. , vol.264 , pp. 4743-4746
    • Esmon, C.T.1
  • 47
    • 2442506617 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli
    • Ezraty B., Grimaud R., El Hassouni M., Moinier D., and Barras F. Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli. EMBO J. 23 (2004) 1868-1877
    • (2004) EMBO J. , vol.23 , pp. 1868-1877
    • Ezraty, B.1    Grimaud, R.2    El Hassouni, M.3    Moinier, D.4    Barras, F.5
  • 48
    • 0028887870 scopus 로고
    • Molecular physiology of reverse cholesterol transport
    • Fielding C.J., and Fielding P.E. Molecular physiology of reverse cholesterol transport. J. Lipid Res. 36 (1995) 211-228
    • (1995) J. Lipid Res. , vol.36 , pp. 211-228
    • Fielding, C.J.1    Fielding, P.E.2
  • 49
    • 0021331956 scopus 로고
    • Oxidized forms of parathyroid hormone with biological activity. Separation and characterization of hormone forms oxidized at methionine 8 and methionine 18
    • Frelinger III A.L., and Zull J.E. Oxidized forms of parathyroid hormone with biological activity. Separation and characterization of hormone forms oxidized at methionine 8 and methionine 18. J. Biol. Chem. 259 (1984) 5507-5513
    • (1984) J. Biol. Chem. , vol.259 , pp. 5507-5513
    • Frelinger III, A.L.1    Zull, J.E.2
  • 51
    • 0032823578 scopus 로고    scopus 로고
    • Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain
    • Gabbita S.P., Aksenov M.Y., Lovell M.A., and Markesbery W.R. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J. Neurochem. 73 (1999) 1660-1666
    • (1999) J. Neurochem. , vol.73 , pp. 1660-1666
    • Gabbita, S.P.1    Aksenov, M.Y.2    Lovell, M.A.3    Markesbery, W.R.4
  • 52
    • 0029071683 scopus 로고
    • Identification of a specific methionine in mammalian 15-lipoxygenase which is oxygenated by the enzyme product 13-HPODE: Dissociation of sulfoxide formation from self-inactivation
    • Gan Q.F., Witkop G.L., Sloane D.L., Straub K.M., and Sigal E. Identification of a specific methionine in mammalian 15-lipoxygenase which is oxygenated by the enzyme product 13-HPODE: Dissociation of sulfoxide formation from self-inactivation. Biochemistry 34 (1995) 7069-7079
    • (1995) Biochemistry , vol.34 , pp. 7069-7079
    • Gan, Q.F.1    Witkop, G.L.2    Sloane, D.L.3    Straub, K.M.4    Sigal, E.5
  • 53
    • 0035066857 scopus 로고    scopus 로고
    • Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex
    • Gao J., Yao Y., and Squier T.C. Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex. Biophys. J. 80 (2001) 1791-1801
    • (2001) Biophys. J. , vol.80 , pp. 1791-1801
    • Gao, J.1    Yao, Y.2    Squier, T.C.3
  • 56
    • 0015971794 scopus 로고
    • Reaction of bovine growth hormone with hydrogen peroxide
    • Glaser C.B., and Li C.H. Reaction of bovine growth hormone with hydrogen peroxide. Biochemistry 13 (1974) 1044-1047
    • (1974) Biochemistry , vol.13 , pp. 1044-1047
    • Glaser, C.B.1    Li, C.H.2
  • 58
    • 0027103736 scopus 로고
    • Oxidation of a specific methionine in thrombomodulin by activated neutrophil products blocks cofactor activity. A potential rapid mechanism for modulation of coagulation
    • Glaser C.B., Morser J., Clarke J.H., Blasko E., McLean K., Kuhn I., Chang R.J., Lin J.H., Vilander L., Andrews W.H., and Light D.R. Oxidation of a specific methionine in thrombomodulin by activated neutrophil products blocks cofactor activity. A potential rapid mechanism for modulation of coagulation. J. Clin. Invest. 90 (1992) 2565-2573
    • (1992) J. Clin. Invest. , vol.90 , pp. 2565-2573
    • Glaser, C.B.1    Morser, J.2    Clarke, J.H.3    Blasko, E.4    McLean, K.5    Kuhn, I.6    Chang, R.J.7    Lin, J.H.8    Vilander, L.9    Andrews, W.H.10    Light, D.R.11
  • 59
    • 12844272205 scopus 로고    scopus 로고
    • Methionine oxidation, alpha-synuclein and Parkinson's disease
    • Glaser C.B., Yamin G., Uversky V.N., and Fink A.L. Methionine oxidation, alpha-synuclein and Parkinson's disease. Biochim. Biophys. Acta 1703 (2005) 157-169
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 157-169
    • Glaser, C.B.1    Yamin, G.2    Uversky, V.N.3    Fink, A.L.4
  • 60
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • Goedert M., and Spillantini M.G. A century of Alzheimer's disease. Science 314 (2006) 777-781
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 61
    • 24144479451 scopus 로고    scopus 로고
    • Redox regulation of the coagulation cascade
    • Gorlach A. Redox regulation of the coagulation cascade. Antioxid. Redox Signal. 7 (2005) 1398-1404
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1398-1404
    • Gorlach, A.1
  • 62
    • 33646483632 scopus 로고    scopus 로고
    • The role of the heme propionates in heme biochemistry
    • Guallar V., and Olsen B. The role of the heme propionates in heme biochemistry. J. Inorg. Biochem. 100 (2006) 755-760
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 755-760
    • Guallar, V.1    Olsen, B.2
  • 63
    • 0345009031 scopus 로고    scopus 로고
    • Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer
    • Gustavsson N., Harndahl U., Emanuelsson A., Roepstorff P., and Sundby C. Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer. Protein Sci. 8 (1999) 2506-2512
    • (1999) Protein Sci. , vol.8 , pp. 2506-2512
    • Gustavsson, N.1    Harndahl, U.2    Emanuelsson, A.3    Roepstorff, P.4    Sundby, C.5
  • 64
    • 0036006188 scopus 로고    scopus 로고
    • A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein
    • Gustavsson N., Kokke B.P., Harndahl U., Silow M., Bechtold U., Poghosyan Z., Murphy D., Boelens W.C., and Sundby C. A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein. Plant J. 29 (2002) 545-553
    • (2002) Plant J. , vol.29 , pp. 545-553
    • Gustavsson, N.1    Kokke, B.P.2    Harndahl, U.3    Silow, M.4    Bechtold, U.5    Poghosyan, Z.6    Murphy, D.7    Boelens, W.C.8    Sundby, C.9
  • 65
    • 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 (1956) 298-300
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 66
    • 0015870249 scopus 로고
    • Free radical theory of aging
    • Harman D. Free radical theory of aging. Triangle 12 (1973) 153-158
    • (1973) Triangle , vol.12 , pp. 153-158
    • Harman, D.1
  • 67
    • 0035830637 scopus 로고    scopus 로고
    • The chaperone-like activity of a small heat shock protein is lost after sulfoxidation of conserved methionines in a surface-exposed amphipathic alpha-helix
    • Harndahl U., Kokke B.P., Gustavsson N., Linse S., Berggren K., Tjerneld F., Boelens W.C., and Sundby C. The chaperone-like activity of a small heat shock protein is lost after sulfoxidation of conserved methionines in a surface-exposed amphipathic alpha-helix. Biochim. Biophys. Acta 1545 (2001) 227-237
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 227-237
    • Harndahl, U.1    Kokke, B.P.2    Gustavsson, N.3    Linse, S.4    Berggren, K.5    Tjerneld, F.6    Boelens, W.C.7    Sundby, C.8
  • 68
    • 0034749277 scopus 로고    scopus 로고
    • Vasoactive intestinal peptide: Cardiovascular effects
    • Henning R.J., and Sawmiller D.R. Vasoactive intestinal peptide: Cardiovascular effects. Cardiovasc. Res. 49 (2001) 27-37
    • (2001) Cardiovasc. Res. , vol.49 , pp. 27-37
    • Henning, R.J.1    Sawmiller, D.R.2
  • 70
    • 0037174835 scopus 로고    scopus 로고
    • Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease
    • Hou L., Kang I., Marchant R.E., and Zagorski M.G. Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease. J. Biol. Chem. 277 (2002) 40173-40176
    • (2002) J. Biol. Chem. , vol.277 , pp. 40173-40176
    • Hou, L.1    Kang, I.2    Marchant, R.E.3    Zagorski, M.G.4
  • 71
    • 0017162022 scopus 로고
    • Studies on pituitary prolactin. 39. Reaction of the ovine hormone with hydrogen peroxide
    • Houghten R.A., and Li C.H. Studies on pituitary prolactin. 39. Reaction of the ovine hormone with hydrogen peroxide. Biochim. Biophys. Acta 439 (1976) 240-249
    • (1976) Biochim. Biophys. Acta , vol.439 , pp. 240-249
    • Houghten, R.A.1    Li, C.H.2
  • 72
    • 0017369245 scopus 로고
    • Human somatotropin. Reaction with hydrogen peroxide
    • Houghten R.A., Glaser C.B., and Li C.H. Human somatotropin. Reaction with hydrogen peroxide. Arch. Biochem. Biophys. 178 (1977) 350-355
    • (1977) Arch. Biochem. Biophys. , vol.178 , pp. 350-355
    • Houghten, R.A.1    Glaser, C.B.2    Li, C.H.3
  • 73
    • 0029897141 scopus 로고    scopus 로고
    • In vitro methionine oxidation of Escherichia coli-derived human stem cell factor: Effects on the molecular structure, biological activity, and dimerization
    • Hsu Y.R., Narhi L.O., Spahr C., Langley K.E., and Lu H.S. In vitro methionine oxidation of Escherichia coli-derived human stem cell factor: Effects on the molecular structure, biological activity, and dimerization. Protein Sci. 5 (1996) 1165-1173
    • (1996) Protein Sci. , vol.5 , pp. 1165-1173
    • Hsu, Y.R.1    Narhi, L.O.2    Spahr, C.3    Langley, K.E.4    Lu, H.S.5
  • 76
    • 33750604604 scopus 로고    scopus 로고
    • Aspects of the biological redox chemistry of cysteine: From simple redox responses to sophisticated signalling pathways
    • Jacob C., Knight I., and Winyard P.G. Aspects of the biological redox chemistry of cysteine: From simple redox responses to sophisticated signalling pathways. Biol. Chem. 387 (2007) 1385-1397
    • (2007) Biol. Chem. , vol.387 , pp. 1385-1397
    • Jacob, C.1    Knight, I.2    Winyard, P.G.3
  • 77
    • 33947494971 scopus 로고    scopus 로고
    • Structural basis of peroxide mediated changes in human hemoglobin: A novel oxidative pathway
    • Jia Y., Buehler P., Boykins R.A., Venable R.M., and Alayash A.I. Structural basis of peroxide mediated changes in human hemoglobin: A novel oxidative pathway. J. Biol. Chem. 282 (2007) 4894-4907
    • (2007) J. Biol. Chem. , vol.282 , pp. 4894-4907
    • Jia, Y.1    Buehler, P.2    Boykins, R.A.3    Venable, R.M.4    Alayash, A.I.5
  • 78
    • 0014429904 scopus 로고
    • Selective and reversibe photo-oxidation of the methionyl residues in lysozyme
    • Jori G., Galiazzo G., Marzotto A., and Scoffone E. Selective and reversibe photo-oxidation of the methionyl residues in lysozyme. J. Biol. Chem. 243 (1968) 4272-4278
    • (1968) J. Biol. Chem. , vol.243 , pp. 4272-4278
    • Jori, G.1    Galiazzo, G.2    Marzotto, A.3    Scoffone, E.4
  • 79
    • 2342486214 scopus 로고    scopus 로고
    • Increased viability of PC12 cells exposed to amyloid-beta peptide by transduction with human TAT-methionine sulfoxide reductase
    • Jung B., Lee E.H., Chung W.S., Lee S.J., Shin S.H., Joo S.H., Kim S.K., and Lee J.H. Increased viability of PC12 cells exposed to amyloid-beta peptide by transduction with human TAT-methionine sulfoxide reductase. Neuroreport 14 (2003) 2349-2353
    • (2003) Neuroreport , vol.14 , pp. 2349-2353
    • Jung, B.1    Lee, E.H.2    Chung, W.S.3    Lee, S.J.4    Shin, S.H.5    Joo, S.H.6    Kim, S.K.7    Lee, J.H.8
  • 80
    • 0037024693 scopus 로고    scopus 로고
    • Oxidation of Ikappa Balpha at methionine 45 is one cause of taurine chloramine-induced inhibition of NF-kappa B activation
    • Kanayama A., Inoue J., Sugita-Konishi Y., Shimizu M., and Miyamoto Y. Oxidation of Ikappa Balpha at methionine 45 is one cause of taurine chloramine-induced inhibition of NF-kappa B activation. J. Biol. Chem. 277 (2002) 24049-24056
    • (2002) J. Biol. Chem. , vol.277 , pp. 24049-24056
    • Kanayama, A.1    Inoue, J.2    Sugita-Konishi, Y.3    Shimizu, M.4    Miyamoto, Y.5
  • 81
    • 14044249497 scopus 로고    scopus 로고
    • Stimulation of G-proteins in human control and Alzheimer's disease brain by FAD mutants of APP(714-723): Implication of oxidative mechanisms
    • Karelson E., Fernaeus S., Reis K., Bogdanovic N., and Land T. Stimulation of G-proteins in human control and Alzheimer's disease brain by FAD mutants of APP(714-723): Implication of oxidative mechanisms. J. Neurosci. Res. 79 (2005) 368-374
    • (2005) J. Neurosci. Res. , vol.79 , pp. 368-374
    • Karelson, E.1    Fernaeus, S.2    Reis, K.3    Bogdanovic, N.4    Land, T.5
  • 82
    • 0029875931 scopus 로고    scopus 로고
    • The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins
    • Keck R.G. The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins. Anal. Biochem. 236 (1996) 56-62
    • (1996) Anal. Biochem. , vol.236 , pp. 56-62
    • Keck, R.G.1
  • 83
    • 33644651183 scopus 로고    scopus 로고
    • [Role of Escherichia coli molecular chaperones in the protection of bacterial cells against irreversible aggregation induced by heat shock]
    • Kedzierska S. [Role of Escherichia coli molecular chaperones in the protection of bacterial cells against irreversible aggregation induced by heat shock]. Postepy Biochem. 51 (2005) 146-153
    • (2005) Postepy Biochem. , vol.51 , pp. 146-153
    • Kedzierska, S.1
  • 84
    • 2442456741 scopus 로고    scopus 로고
    • Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite (ONOO-)
    • Khor H.K., Fisher M.T., and Schoneich C. Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite (ONOO-). J. Biol. Chem. 279 (2004) 19486-19493
    • (2004) J. Biol. Chem. , vol.279 , pp. 19486-19493
    • Khor, H.K.1    Fisher, M.T.2    Schoneich, C.3
  • 85
    • 0016640844 scopus 로고
    • Oxidation of methionine residues of porcine and bovine pepsins
    • Kido K., and Kassell B. Oxidation of methionine residues of porcine and bovine pepsins. Biochemistry 14 (1975) 631-635
    • (1975) Biochemistry , vol.14 , pp. 631-635
    • Kido, K.1    Kassell, B.2
  • 86
    • 3142709434 scopus 로고    scopus 로고
    • Characterization of mouse endoplasmic reticulum methionine-R-sulfoxide reductase
    • Kim H.Y., and Gladyshev V.N. Characterization of mouse endoplasmic reticulum methionine-R-sulfoxide reductase. Biochem. Biophys. Res. Commun. 320 (2004) 1277-1283
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 1277-1283
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 87
    • 0024298709 scopus 로고
    • Methionine modification in cytochrome-c peroxidase
    • Kim K., and Erman J.E. Methionine modification in cytochrome-c peroxidase. Biochim. Biophys. Acta 954 (1988) 95-107
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 95-107
    • Kim, K.1    Erman, J.E.2
  • 88
    • 0033102631 scopus 로고    scopus 로고
    • Oxidation of methionine residues in coagulation factor VIIa
    • Kornfelt T., Persson E., and Palm L. Oxidation of methionine residues in coagulation factor VIIa. Arch. Biochem. Biophys. 363 (1999) 43-54
    • (1999) Arch. Biochem. Biophys. , vol.363 , pp. 43-54
    • Kornfelt, T.1    Persson, E.2    Palm, L.3
  • 91
    • 0022977024 scopus 로고
    • Inactivation of plasminogen activator inhibitor by oxidants
    • Lawrence D.A., and Loskutoff D.J. Inactivation of plasminogen activator inhibitor by oxidants. Biochemistry 25 (1986) 6351-6355
    • (1986) Biochemistry , vol.25 , pp. 6351-6355
    • Lawrence, D.A.1    Loskutoff, D.J.2
  • 92
    • 0033679959 scopus 로고    scopus 로고
    • Molecular and functional properties of two-pore-domain potassium channels
    • Lesage F., and Lazdunski M. Molecular and functional properties of two-pore-domain potassium channels. Am. J. Physiol. Renal Physiol. 279 (2000) F793-F801
    • (2000) Am. J. Physiol. Renal Physiol. , vol.279
    • Lesage, F.1    Lazdunski, M.2
  • 95
    • 0034456721 scopus 로고    scopus 로고
    • Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation
    • Levine R.L., Moskovitz J., and Stadtman E.R. Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation. IUBMB Life 50 (2000) 301-307
    • (2000) IUBMB Life , vol.50 , pp. 301-307
    • Levine, R.L.1    Moskovitz, J.2    Stadtman, E.R.3
  • 96
    • 0031970109 scopus 로고    scopus 로고
    • Biosynthesis and metabolism of native and oxidized neuropeptide Y in the hippocampal mossy fiber system
    • McCarthy J.B., Walker M., Pierce J., Camp P., and White J.D. Biosynthesis and metabolism of native and oxidized neuropeptide Y in the hippocampal mossy fiber system. J. Neurochem. 70 (1998) 1950-1963
    • (1998) J. Neurochem. , vol.70 , pp. 1950-1963
    • McCarthy, J.B.1    Walker, M.2    Pierce, J.3    Camp, P.4    White, J.D.5
  • 98
    • 33646761969 scopus 로고    scopus 로고
    • IkappaB is a sensitive target for oxidation by cell-permeable chloramines: Inhibition of NF-kappaB activity by glycine chloramine through methionine oxidation
    • Midwinter R.G., Cheah F.C., Moskovitz J., Vissers M.C., and Winterbourn C.C. IkappaB is a sensitive target for oxidation by cell-permeable chloramines: Inhibition of NF-kappaB activity by glycine chloramine through methionine oxidation. Biochem. J. 396 (2006) 71-78
    • (2006) Biochem. J. , vol.396 , pp. 71-78
    • Midwinter, R.G.1    Cheah, F.C.2    Moskovitz, J.3    Vissers, M.C.4    Winterbourn, C.C.5
  • 99
    • 0027265803 scopus 로고
    • Functional methionines in the collagen/gelatin binding domain of plasma fibronectin: Effects of chemical modification by chloramine T
    • Miles A.M., and Smith R.L. Functional methionines in the collagen/gelatin binding domain of plasma fibronectin: Effects of chemical modification by chloramine T. Biochemistry 32 (1993) 8168-8178
    • (1993) Biochemistry , vol.32 , pp. 8168-8178
    • Miles, A.M.1    Smith, R.L.2
  • 100
    • 0034678128 scopus 로고    scopus 로고
    • Activation of primary human monocytes by the oxidized form of alpha1-antitrypsin
    • Moraga F., and Janciauskiene S. Activation of primary human monocytes by the oxidized form of alpha1-antitrypsin. J. Biol. Chem. 275 (2000) 7693-7700
    • (2000) J. Biol. Chem. , vol.275 , pp. 7693-7700
    • Moraga, F.1    Janciauskiene, S.2
  • 101
    • 0034501374 scopus 로고    scopus 로고
    • Antiflammin peptides in the regulation of inflammatory response
    • Moreno J.J. Antiflammin peptides in the regulation of inflammatory response. Ann. N Y Acad. Sci. 923 (2000) 147-153
    • (2000) Ann. N Y Acad. Sci. , vol.923 , pp. 147-153
    • Moreno, J.J.1
  • 102
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • Moskovitz J. Methionine sulfoxide reductases: Ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim. Biophys. Acta 1703 (2005) 213-219
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 213-219
    • Moskovitz, J.1
  • 103
    • 17844372715 scopus 로고    scopus 로고
    • Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival
    • Moskovitz J. Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival. Curr. Pharm. Des. 11 (2005) 1451-1457
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 1451-1457
    • Moskovitz, J.1
  • 104
    • 35348906893 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase system: Possible roles in protection against neurodegenerative diseases
    • Luo Y., and Packer L. (Eds), CRC, New York, NY
    • Moskovitz J., and Bush A.I. Methionine sulfoxide reductase system: Possible roles in protection against neurodegenerative diseases. In: Luo Y., and Packer L. (Eds). "Oxidative Stress and Age-Related Neurodegeneration" (2005), CRC, New York, NY 197-210
    • (2005) "Oxidative Stress and Age-Related Neurodegeneration" , pp. 197-210
    • Moskovitz, J.1    Bush, A.I.2
  • 105
    • 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 N.A., Gilbert D.J., Copeland N.G., 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 (1996) 3205-3208
    • (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
  • 106
    • 0034640506 scopus 로고    scopus 로고
    • Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
    • Moskovitz J., Poston J.M., Berlett B.S., Nosworthy N.J., Szczepanowski R., and Stadtman E.R. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. J. Biol. Chem. 275 (2000) 14167-14172
    • (2000) J. Biol. Chem. , vol.275 , pp. 14167-14172
    • Moskovitz, J.1    Poston, J.M.2    Berlett, B.S.3    Nosworthy, N.J.4    Szczepanowski, R.5    Stadtman, E.R.6
  • 108
    • 0036297758 scopus 로고    scopus 로고
    • Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity
    • Moskovitz J., Singh V.K., Requena J., Wilkinson B.J., Jayaswal R.K., and Stadtman E.R. Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity. Biochem. Biophys. Res. Commun. 290 (2002) 62-65
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 62-65
    • Moskovitz, J.1    Singh, V.K.2    Requena, J.3    Wilkinson, B.J.4    Jayaswal, R.K.5    Stadtman, E.R.6
  • 109
    • 0019803793 scopus 로고
    • Additional observations on cholecystokinin and the vasoactive intestinal polypeptide
    • Mutt V. Additional observations on cholecystokinin and the vasoactive intestinal polypeptide. Peptides 2 Suppl. 2 (1981) 209-214
    • (1981) Peptides , vol.2 , Issue.SUPPL. 2 , pp. 209-214
    • Mutt, V.1
  • 110
    • 0029620489 scopus 로고
    • Oxidation of recombinant human parathyroid hormone: Effect of oxidized position on the biological activity
    • Nabuchi Y., Fujiwara E., Ueno K., Kuboniwa H., Asoh Y., and Ushio H. Oxidation of recombinant human parathyroid hormone: Effect of oxidized position on the biological activity. Pharm. Res. 12 (1995) 2049-2052
    • (1995) Pharm. Res. , vol.12 , pp. 2049-2052
    • Nabuchi, Y.1    Fujiwara, E.2    Ueno, K.3    Kuboniwa, H.4    Asoh, Y.5    Ushio, H.6
  • 111
    • 7244234330 scopus 로고    scopus 로고
    • Folding analysis of hormonal polypeptide calcitonins and the oxidized calcitonins using electrospray ionization mass spectrometry combined with H/D exchange
    • Nabuchi Y., Asoh Y., and Takayama M. Folding analysis of hormonal polypeptide calcitonins and the oxidized calcitonins using electrospray ionization mass spectrometry combined with H/D exchange. J. Am. Soc. Mass Spectrom. 15 (2004) 1556-1564
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1556-1564
    • Nabuchi, Y.1    Asoh, Y.2    Takayama, M.3
  • 113
    • 0023784538 scopus 로고
    • Chemical modification of tryptophanase by chloramine T: A possible involvement of the methionine residue in enzyme activity
    • Oda T., and Tokushige M. Chemical modification of tryptophanase by chloramine T: A possible involvement of the methionine residue in enzyme activity. J. Biochem. (Tokyo) 104 (1988) 178-183
    • (1988) J. Biochem. (Tokyo) , vol.104 , pp. 178-183
    • Oda, T.1    Tokushige, M.2
  • 114
    • 12844266113 scopus 로고    scopus 로고
    • Formation of methionine sulfoxide-containing specific forms of oxidized high-density lipoproteins
    • Panzenbock U., and Stocker R. Formation of methionine sulfoxide-containing specific forms of oxidized high-density lipoproteins. Biochim. Biophys. Acta 1703 (2005) 171-181
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 171-181
    • Panzenbock, U.1    Stocker, R.2
  • 115
  • 116
    • 33749043006 scopus 로고    scopus 로고
    • Regulation of cholesterol homeostasis in macrophages and consequences for atherosclerotic lesion development
    • Pennings M., Meurs I., Ye D., Out R., Hoekstra M., Van Berkel T.J., and Van Eck M. Regulation of cholesterol homeostasis in macrophages and consequences for atherosclerotic lesion development. FEBS Lett. 580 (2006) 5588-5596
    • (2006) FEBS Lett. , vol.580 , pp. 5588-5596
    • Pennings, M.1    Meurs, I.2    Ye, D.3    Out, R.4    Hoekstra, M.5    Van Berkel, T.J.6    Van Eck, M.7
  • 117
    • 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 (2001) 819-825
    • (2001) Biochem. J. , vol.355 , pp. 819-825
    • Petropoulos, I.1    Mary, J.2    Perichon, M.3    Friguet, B.4
  • 118
    • 0037980148 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid peptide as a source of neurotoxic free radicals: The role of structural effects
    • Pogocki D. Alzheimer's beta-amyloid peptide as a source of neurotoxic free radicals: The role of structural effects. Acta Neurobiol. Exp. (Wars.) 63 (2003) 131-145
    • (2003) Acta Neurobiol. Exp. (Wars.) , vol.63 , pp. 131-145
    • Pogocki, D.1
  • 119
    • 0037715143 scopus 로고    scopus 로고
    • Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
    • Rachidi W., Vilette D., Guiraud P., Arlotto M., Riondel J., Laude H., Lehmann S., and Favier A. Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J. Biol. Chem. 278 (2003) 9064-9072
    • (2003) J. Biol. Chem. , vol.278 , pp. 9064-9072
    • Rachidi, W.1    Vilette, D.2    Guiraud, P.3    Arlotto, M.4    Riondel, J.5    Laude, H.6    Lehmann, S.7    Favier, A.8
  • 120
    • 0021345915 scopus 로고
    • Methionine sulfoxide formation: The cause of self-inactivation of reticulocyte lipoxygenase
    • Rapoport S., Hartel B., and Hausdorf G. Methionine sulfoxide formation: The cause of self-inactivation of reticulocyte lipoxygenase. Eur. J. Biochem. 139 (1984) 573-576
    • (1984) Eur. J. Biochem. , vol.139 , pp. 573-576
    • Rapoport, S.1    Hartel, B.2    Hausdorf, G.3
  • 121
    • 0000195695 scopus 로고
    • Evidence for involvement of a methionine residue in the enzymatic action of phosphoglucomutase and chymotrypsin
    • Ray Jr. W.J., Latham Jr. H.G., Katsoulis M., and Koshland Jr. D.E. Evidence for involvement of a methionine residue in the enzymatic action of phosphoglucomutase and chymotrypsin. J. Am. Chem. Soc. 82 (1960) 4743-4744
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 4743-4744
    • Ray Jr., W.J.1    Latham Jr., H.G.2    Katsoulis, M.3    Koshland Jr., D.E.4
  • 123
    • 33845207273 scopus 로고    scopus 로고
    • Critical role of methionine-722 in the stimulation of human brain G-proteins and neurotoxicity induced by London familial Alzheimer's disease (FAD) mutated V717G-APP(714-723)
    • Reis K., Zharkovsky A., Bogdanovic N., Karelson E., and Land T. Critical role of methionine-722 in the stimulation of human brain G-proteins and neurotoxicity induced by London familial Alzheimer's disease (FAD) mutated V717G-APP(714-723). Neuroscience 144 (2007) 571-578
    • (2007) Neuroscience , vol.144 , pp. 571-578
    • Reis, K.1    Zharkovsky, A.2    Bogdanovic, N.3    Karelson, E.4    Land, T.5
  • 124
    • 0026041548 scopus 로고
    • Oxidation-resistant variants of recombinant antileucoprotease are better inhibitors of human-neutrophil-elastase-induced emphysema in hamsters than natural recombinant antileucoprotease
    • Rudolphus A., Heinzel-Wieland R., Vincent V.A., Saunders D., Steffens G.J., Dijkman J.H., and Kramps J.A. Oxidation-resistant variants of recombinant antileucoprotease are better inhibitors of human-neutrophil-elastase-induced emphysema in hamsters than natural recombinant antileucoprotease. Clin. Sci. (Lond.) 81 (1991) 777-784
    • (1991) Clin. Sci. (Lond.) , vol.81 , pp. 777-784
    • Rudolphus, A.1    Heinzel-Wieland, R.2    Vincent, V.A.3    Saunders, D.4    Steffens, G.J.5    Dijkman, J.H.6    Kramps, J.A.7
  • 125
    • 33846019656 scopus 로고    scopus 로고
    • Selenocompounds can serve as oxidoreductants with the methionine sulfoxide reductase enzymes
    • Sagher D., Brunell D., Brot N., Vallee B.L., and Weissbach H. Selenocompounds can serve as oxidoreductants with the methionine sulfoxide reductase enzymes. J. Biol. Chem. 281 (2006) 31184-31187
    • (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
  • 128
    • 0028287639 scopus 로고
    • Reduction of HDL- and LDL-associated cholesterylester and phospholipid hydroperoxides by phospholipid hydroperoxide glutathione peroxidase and Ebselen (PZ 51)
    • Sattler W., Maiorino M., and Stocker R. Reduction of HDL- and LDL-associated cholesterylester and phospholipid hydroperoxides by phospholipid hydroperoxide glutathione peroxidase and Ebselen (PZ 51). Arch. Biochem. Biophys. 309 (1994) 214-221
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 214-221
    • Sattler, W.1    Maiorino, M.2    Stocker, R.3
  • 129
    • 0017733498 scopus 로고
    • Interconversion of methionine and methionine sulfoxide
    • Savige W.E., and Fontana A. Interconversion of methionine and methionine sulfoxide. Methods Enzymol. 47 (1977) 453-459
    • (1977) Methods Enzymol. , vol.47 , pp. 453-459
    • Savige, W.E.1    Fontana, A.2
  • 130
    • 33646941974 scopus 로고    scopus 로고
    • Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I
    • Shao B., Oda M.N., Bergt C., Fu X., Green P.S., Brot N., Oram J.F., and Heinecke J.W. Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I. J. Biol. Chem. 281 (2006) 9001-9004
    • (2006) J. Biol. Chem. , vol.281 , pp. 9001-9004
    • Shao, B.1    Oda, M.N.2    Bergt, C.3    Fu, X.4    Green, P.S.5    Brot, N.6    Oram, J.F.7    Heinecke, J.W.8
  • 131
    • 0017599173 scopus 로고
    • Effect of oxidation of methionine residues in chicken ovoinhibitor on its inhibitory activities against trypsin, chymotrypsin, and elastase
    • Shechter Y., Burnstein Y., and Gertler A. Effect of oxidation of methionine residues in chicken ovoinhibitor on its inhibitory activities against trypsin, chymotrypsin, and elastase. Biochemistry 16 (1977) 992-997
    • (1977) Biochemistry , vol.16 , pp. 992-997
    • Shechter, Y.1    Burnstein, Y.2    Gertler, A.3
  • 132
    • 0032555370 scopus 로고    scopus 로고
    • Enzymatic repair of oxidative damage to human apolipoprotein A-I
    • Sigalov A.B., and Stern L.J. Enzymatic repair of oxidative damage to human apolipoprotein A-I. FEBS Lett. 433 (1998) 196-200
    • (1998) FEBS Lett. , vol.433 , pp. 196-200
    • Sigalov, A.B.1    Stern, L.J.2
  • 133
    • 0023094302 scopus 로고
    • Ozone effects on inhibitors of human neutrophil proteinases
    • Smith C.E., Stack M.S., and Johnson D.A. Ozone effects on inhibitors of human neutrophil proteinases. Arch. Biochem. Biophys. 253 (1987) 146-155
    • (1987) Arch. Biochem. Biophys. , vol.253 , pp. 146-155
    • Smith, C.E.1    Stack, M.S.2    Johnson, D.A.3
  • 134
    • 0020332694 scopus 로고
    • The effect of oxidation of the Met27 residue of [125I]monoiodoglucagon on receptor-binding affinity
    • Sonne O., Larsen U.D., and Markussen J. The effect of oxidation of the Met27 residue of [125I]monoiodoglucagon on receptor-binding affinity. Hoppe Seylers Z. Physiol. Chem. 363 (1982) 95-101
    • (1982) Hoppe Seylers Z. Physiol. Chem. , vol.363 , pp. 95-101
    • Sonne, O.1    Larsen, U.D.2    Markussen, J.3
  • 135
    • 4244218956 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism
    • Stadtman E.R., Moskovitz J., Berlett B.S., and Levine R.L. Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol. Cell. Biochem. 234-235 (2002) 3-9
    • (2002) Mol. Cell. Biochem. , vol.234-235 , pp. 3-9
    • Stadtman, E.R.1    Moskovitz, J.2    Berlett, B.S.3    Levine, R.L.4
  • 136
    • 0014670698 scopus 로고
    • The effect on subtilisin activity of oxidizing a methionine residue
    • Stauffer C.E., and Etson D. The effect on subtilisin activity of oxidizing a methionine residue. J. Biol. Chem. 244 (1969) 5333-5338
    • (1969) J. Biol. Chem. , vol.244 , pp. 5333-5338
    • Stauffer, C.E.1    Etson, D.2
  • 137
    • 0030221106 scopus 로고    scopus 로고
    • Chemical modification of methionines in a cobra venom cytotoxin differentiates between lytic and binding domains
    • Stevens-Truss R., and Hinman C.L. Chemical modification of methionines in a cobra venom cytotoxin differentiates between lytic and binding domains. Toxicol. Appl. Pharmacol. 139 (1996) 234-242
    • (1996) Toxicol. Appl. Pharmacol. , vol.139 , pp. 234-242
    • Stevens-Truss, R.1    Hinman, C.L.2
  • 138
    • 0033961244 scopus 로고    scopus 로고
    • The antithrombotic factor singlet oxygen/light (1O2/h nu)
    • Stief T.W., and Fareed J. The antithrombotic factor singlet oxygen/light (1O2/h nu). Clin. Appl. Thromb. Hemost. 6 (2000) 22-30
    • (2000) Clin. Appl. Thromb. Hemost. , vol.6 , pp. 22-30
    • Stief, T.W.1    Fareed, J.2
  • 139
    • 0023940734 scopus 로고
    • Oxidative inactivation of purified human alpha-2-antiplasmin, antithrombin III, and C1-inhibitor
    • Stief T.W., Aab A., and Heimburger N. Oxidative inactivation of purified human alpha-2-antiplasmin, antithrombin III, and C1-inhibitor. Thromb. Res. 49 (1988) 581-589
    • (1988) Thromb. Res. , vol.49 , pp. 581-589
    • Stief, T.W.1    Aab, A.2    Heimburger, N.3
  • 140
    • 0025875223 scopus 로고
    • Effect of oxidants on proteases of the fibrinolytic system: Possible role for methionine residues in the interaction between tissue type plasminogen activator and fibrin
    • Stief T.W., Martin E., Jimenez J., Digon J., and Rodriguez J.M. Effect of oxidants on proteases of the fibrinolytic system: Possible role for methionine residues in the interaction between tissue type plasminogen activator and fibrin. Thromb. Res. 61 (1991) 191-200
    • (1991) Thromb. Res. , vol.61 , pp. 191-200
    • Stief, T.W.1    Martin, E.2    Jimenez, J.3    Digon, J.4    Rodriguez, J.M.5
  • 141
    • 0033524399 scopus 로고    scopus 로고
    • Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase
    • Sun H., Gao J., Ferrington D.A., Biesiada H., Williams T.D., and Squier T.C. Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase. Biochemistry 38 (1999) 105-112
    • (1999) Biochemistry , vol.38 , pp. 105-112
    • Sun, H.1    Gao, J.2    Ferrington, D.A.3    Biesiada, H.4    Williams, T.D.5    Squier, T.C.6
  • 143
    • 0023897673 scopus 로고
    • Methionine sulfoxide and the oxidative regulation of plasma proteinase inhibitors
    • Swaim M.W., and Pizzo S.V. Methionine sulfoxide and the oxidative regulation of plasma proteinase inhibitors. J. Leukoc. Biol. 43 (1988) 365-379
    • (1988) J. Leukoc. Biol. , vol.43 , pp. 365-379
    • Swaim, M.W.1    Pizzo, S.V.2
  • 144
    • 0034282683 scopus 로고    scopus 로고
    • Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity
    • Taggart C., Cervantes-Laurean D., Kim G., McElvaney N.G., Wehr N., Moss J., and Levine R.L. Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity. J. Biol. Chem. 275 (2000) 27258-27265
    • (2000) J. Biol. Chem. , vol.275 , pp. 27258-27265
    • Taggart, C.1    Cervantes-Laurean, D.2    Kim, G.3    McElvaney, N.G.4    Wehr, N.5    Moss, J.6    Levine, R.L.7
  • 146
    • 0023250901 scopus 로고
    • Methionine oxidation in human growth hormone and human chorionic somatomammotropin. Effects on receptor binding and biological activities
    • Teh L.C., Murphy L.J., Huq N.L., Surus A.S., Friesen H.G., Lazarus L., and Chapman G.E. Methionine oxidation in human growth hormone and human chorionic somatomammotropin. Effects on receptor binding and biological activities. J. Biol. Chem. 262 (1987) 6472-6477
    • (1987) J. Biol. Chem. , vol.262 , pp. 6472-6477
    • Teh, L.C.1    Murphy, L.J.2    Huq, N.L.3    Surus, A.S.4    Friesen, H.G.5    Lazarus, L.6    Chapman, G.E.7
  • 148
    • 4043135996 scopus 로고    scopus 로고
    • Metabolic modulation of potassium channels
    • Trauner D., and Kramer R.H. Metabolic modulation of potassium channels. Sci. STKE 2004 (2004) pe22
    • (2004) Sci. STKE , vol.2004
    • Trauner, D.1    Kramer, R.H.2
  • 149
    • 0020046391 scopus 로고
    • Degradation and oxidation of methionine enkephalin by human neutrophils
    • Turkall R.M., Denison R.C., and Tsan M.F. Degradation and oxidation of methionine enkephalin by human neutrophils. J. Lab. Clin. Med. 99 (1982) 418-427
    • (1982) J. Lab. Clin. Med. , vol.99 , pp. 418-427
    • Turkall, R.M.1    Denison, R.C.2    Tsan, M.F.3
  • 150
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions?. Proteins 41 (2000) 415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 151
    • 0037165646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro
    • Uversky V.N., Yamin G., Souillac P.O., Goers J., Glaser C.B., and Fink A.L. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS Lett. 517 (2002) 239-244
    • (2002) FEBS Lett. , vol.517 , pp. 239-244
    • Uversky, V.N.1    Yamin, G.2    Souillac, P.O.3    Goers, J.4    Glaser, C.B.5    Fink, A.L.6
  • 153
    • 0024159190 scopus 로고
    • Biological activity of oxidized and reduced iodinated bombesins
    • Vigna S.R., Giraud A.S., Reeve Jr. J.R., and Walsh J.H. Biological activity of oxidized and reduced iodinated bombesins. Peptides 9 (1988) 923-926
    • (1988) Peptides , vol.9 , pp. 923-926
    • Vigna, S.R.1    Giraud, A.S.2    Reeve Jr., J.R.3    Walsh, J.H.4
  • 154
    • 0028598408 scopus 로고
    • Oxidants generated by the myeloperoxidase-halide system activate the fifth component of human complement, C5
    • Vogt W., and Hesse D. Oxidants generated by the myeloperoxidase-halide system activate the fifth component of human complement, C5. Immunobiology 192 (1994) 1-9
    • (1994) Immunobiology , vol.192 , pp. 1-9
    • Vogt, W.1    Hesse, D.2
  • 155
    • 0026584152 scopus 로고
    • Activation of the fifth component of human complement, C5, without cleavage, by methionine oxidizing agents
    • Vogt W., Zimmermann B., Hesse D., and Nolte R. Activation of the fifth component of human complement, C5, without cleavage, by methionine oxidizing agents. Mol. Immunol. 29 (1992) 251-256
    • (1992) Mol. Immunol. , vol.29 , pp. 251-256
    • Vogt, W.1    Zimmermann, B.2    Hesse, D.3    Nolte, R.4
  • 156
    • 0029586382 scopus 로고
    • Large-scale expression, purification and characterization of small fragments of thrombomodulin: The roles of the sixth domain and of methionine 388
    • White C.E., Hunter M.J., Meininger D.P., White L.R., and Komives E.A. Large-scale expression, purification and characterization of small fragments of thrombomodulin: The roles of the sixth domain and of methionine 388. Protein Eng. 8 (1995) 1177-1187
    • (1995) Protein Eng. , vol.8 , pp. 1177-1187
    • White, C.E.1    Hunter, M.J.2    Meininger, D.P.3    White, L.R.4    Komives, E.A.5
  • 157
    • 1942502252 scopus 로고    scopus 로고
    • Ageing and exposure to oxidative stress in vivo differentially affect cellular levels of PrP in mouse cerebral microvessels and brain parenchyma
    • Williams W.M., Stadtman E.R., and Moskovitz J. Ageing and exposure to oxidative stress in vivo differentially affect cellular levels of PrP in mouse cerebral microvessels and brain parenchyma. Neuropathol. Appl. Neurobiol. 30 (2004) 161-168
    • (2004) Neuropathol. Appl. Neurobiol. , vol.30 , pp. 161-168
    • Williams, W.M.1    Stadtman, E.R.2    Moskovitz, J.3
  • 160
    • 33750370804 scopus 로고    scopus 로고
    • Understanding the molecular causes of Parkinson's disease
    • Wood-Kaczmar A., Gandhi S., and Wood N.W. Understanding the molecular causes of Parkinson's disease. Trends Mol. Med. 12 (2006) 521-528
    • (2006) Trends Mol. Med. , vol.12 , pp. 521-528
    • Wood-Kaczmar, A.1    Gandhi, S.2    Wood, N.W.3
  • 162
    • 12844253127 scopus 로고    scopus 로고
    • Structural and functional consequences of methionine oxidation in thrombomodulin
    • Wood M.J., Helena Prieto J., and Komives E.A. Structural and functional consequences of methionine oxidation in thrombomodulin. Biochim. Biophys. Acta 1703 (2005) 141-147
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 141-147
    • Wood, M.J.1    Helena Prieto, J.2    Komives, E.A.3
  • 163
    • 0041845349 scopus 로고    scopus 로고
    • Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein
    • Yamin G., Glaser C.B., Uversky V.N., and Fink A.L. Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein. J. Biol. Chem. 278 (2003) 27630-27635
    • (2003) J. Biol. Chem. , vol.278 , pp. 27630-27635
    • Yamin, G.1    Glaser, C.B.2    Uversky, V.N.3    Fink, A.L.4
  • 164
    • 0030044406 scopus 로고    scopus 로고
    • Oxidative degradation of antiflammin 2
    • Ye J.M., and Wolfe J.L. Oxidative degradation of antiflammin 2. Pharm. Res. 13 (1996) 250-255
    • (1996) Pharm. Res. , vol.13 , pp. 250-255
    • Ye, J.M.1    Wolfe, J.L.2
  • 166
    • 33748349405 scopus 로고    scopus 로고
    • [The role of macroglobulin family proteins in the regulation of inflammation]
    • Zorin N.A., Zorina V.N., and Zorina R.M. [The role of macroglobulin family proteins in the regulation of inflammation]. Biomed. Khim. 52 (2006) 229-238
    • (2006) Biomed. Khim. , vol.52 , pp. 229-238
    • Zorin, N.A.1    Zorina, V.N.2    Zorina, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.