메뉴 건너뛰기




Volumn 5, Issue 4, 2010, Pages

Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CYSTEINE; LACTOYLGLUTATHIONE LYASE; DISULFIDE; GLUTATHIONE; METHIONINE;

EID: 77956446949     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0010399     Document Type: Article
Times cited : (82)

References (58)
  • 1
    • 0027454552 scopus 로고
    • The Glyoxalase System in Health and Disease
    • Thornalley PJ (1993) The Glyoxalase System in Health and Disease. Mol Aspects Med 14(4): 287-371.
    • (1993) Mol Aspects Med , vol.14 , Issue.4 , pp. 287-371
    • Thornalley, P.J.1
  • 2
    • 4244040278 scopus 로고    scopus 로고
    • Glutathione-dependent detoxification of alpha-oxoalde-hydes by the glyoxalase system: Involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors
    • Thornalley PJ (1998) Glutathione-dependent detoxification of alpha-oxoalde-hydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors. Chem Biol Interact 111-112: 137-151.
    • (1998) Chem Biol Interact , vol.111 , pp. 137-151
    • Thornalley, P.J.1
  • 3
    • 0030041937 scopus 로고    scopus 로고
    • Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: Aldose reductase, glyoxalase I, and glyoxalase II-a clinical research center study
    • Ratliff DM, Van der Jagt DJ, Eaton RP, Van der Jagt DL (1996) Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II-a clinical research center study. J Clin Endocrinol Metab 81(2): 488-492.
    • (1996) J Clin Endocrinol Metab , vol.81 , Issue.2 , pp. 488-492
    • Ratliff, D.M.1    van der Jagt, D.J.2    Eaton, R.P.3    van der Jagt, D.L.4
  • 4
    • 33751330181 scopus 로고    scopus 로고
    • Age- and stage-dependent glyoxalase I expression and its activity in normal and Alzheimer's disease brains
    • Kuhla B, Boeck K, Schmidt A, Ogunlade V, Arendt T, et al. (2007) Age- and stage-dependent glyoxalase I expression and its activity in normal and Alzheimer's disease brains. Neurobiol Aging 28(1): 29-41.
    • (2007) Neurobiol Aging , vol.28 , Issue.1 , pp. 29-41
    • Kuhla, B.1    Boeck, K.2    Schmidt, A.3    Ogunlade, V.4    Arendt, T.5
  • 5
    • 0027512818 scopus 로고
    • Glyoxalase activities in human tumour cell lines in vitro
    • Ayoub F, Zaman M, Thornalley P, Masters J (1993) Glyoxalase activities in human tumour cell lines in vitro. Anticancer Res 13(1): 151-155.
    • (1993) Anticancer Res , vol.13 , Issue.1 , pp. 151-155
    • Ayoub, F.1    Zaman, M.2    Thornalley, P.3    Masters, J.4
  • 6
    • 33748293101 scopus 로고    scopus 로고
    • Upregulation of glyoxalase I fails to normalize methylglyoxal levels: A possible mechanism for biochemical changes in diabetic mouse lenses
    • Staniszewska MM, Nagaraj RH (2006) Upregulation of glyoxalase I fails to normalize methylglyoxal levels: a possible mechanism for biochemical changes in diabetic mouse lenses. Mol Cell Biochem 288(1-2): 29-36.
    • (2006) Mol Cell Biochem , vol.288 , Issue.1-2 , pp. 29-36
    • Staniszewska, M.M.1    Nagaraj, R.H.2
  • 7
    • 69849099059 scopus 로고    scopus 로고
    • Glyoxalase I gene deletion mutants of Leishmania donovani exhibit reduced methylglyoxal detoxification
    • Chauhan SC, Madhubala R (2009) Glyoxalase I gene deletion mutants of Leishmania donovani exhibit reduced methylglyoxal detoxification. PLOS One 4(8): e6805.
    • (2009) PLOS One , vol.4 , Issue.8
    • Chauhan, S.C.1    Madhubala, R.2
  • 8
    • 0030792637 scopus 로고    scopus 로고
    • Multiple roles of glutathione in the central nervous system
    • Cooper AJ, Kristal BS (1997) Multiple roles of glutathione in the central nervous system. Biol Chem 378(8): 793-802.
    • (1997) Biol Chem , vol.378 , Issue.8 , pp. 793-802
    • Cooper, A.J.1    Kristal, B.S.2
  • 9
    • 0030927104 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping
    • Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA (1997) Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping. Embo J 16(12): 3386-3395.
    • (1997) Embo J , vol.16 , Issue.12 , pp. 3386-3395
    • Cameron, A.D.1    Olin, B.2    Ridderstrom, M.3    Mannervik, B.4    Jones, T.A.5
  • 10
    • 0029866943 scopus 로고    scopus 로고
    • Optimized heterologous expression of the human zinc enzyme glyoxalase I
    • Ridderstrom M, Mannervik B (1996) Optimized heterologous expression of the human zinc enzyme glyoxalase I. Biochem J 314(Pt 2): 463-467.
    • (1996) Biochem J , vol.314 , Issue.PART 2 , pp. 463-467
    • Ridderstrom, M.1    Mannervik, B.2
  • 11
    • 0347419281 scopus 로고    scopus 로고
    • Glyoxalase I - structure, function and a critical role in the enzymatic defence against glycation
    • Thornalley PJ (2003) Glyoxalase I - structure, function and a critical role in the enzymatic defence against glycation. Biochem Soc Trans 31(Pt 6): 1343-1348.
    • (2003) Biochem Soc Trans , vol.31 , Issue.6 , pp. 1343-1348
    • Thornalley, P.J.1
  • 12
    • 35148868745 scopus 로고    scopus 로고
    • Tumour necrosis factor induces phosphorylation primarily of the nitric-oxide-responsive form of glyoxalase I
    • de Hemptinne V, Rondas D, Vandekerckhove J, Vancompernolle K (2007) Tumour necrosis factor induces phosphorylation primarily of the nitric-oxide-responsive form of glyoxalase I. Biochem J 407(1): 121-128.
    • (2007) Biochem J , vol.407 , Issue.1 , pp. 121-128
    • de Hemptinne, V.1    Rondas, D.2    Vandekerckhove, J.3    Vancompernolle, K.4
  • 13
    • 0037154172 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced modulation of glyoxalase I activities through phosphorylation by PKA results in cell death and is accompanied by the formation of a specific methylglyoxal-derived AGE
    • Van Herreweghe F, Mao J, Chaplen FW, Grooten J, Gevaert K, et al. (2002) Tumor necrosis factor-induced modulation of glyoxalase I activities through phosphorylation by PKA results in cell death and is accompanied by the formation of a specific methylglyoxal-derived AGE. Proc Natl Acad Sci USA 99(2): 949-954.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.2 , pp. 949-954
    • van Herreweghe, F.1    Mao, J.2    Chaplen, F.W.3    Grooten, J.4    Gevaert, K.5
  • 14
    • 64249161093 scopus 로고    scopus 로고
    • Phosphory-lation on Thr-106 and NO-modification of glyoxalase I suppress the TNF-induced transcriptional activity of NF-kB
    • Hemptinne F, Rondas D, Toepoel M, Vancompernolle K (2009) Phosphory-lation on Thr-106 and NO-modification of glyoxalase I suppress the TNF-induced transcriptional activity of NF-kB. Mol Cell Biochem 325: 169-178.
    • (2009) Mol Cell Biochem , vol.325 , pp. 169-178
    • Hemptinne, F.1    Rondas, D.2    Toepoel, M.3    Vancompernolle, K.4
  • 15
    • 0033772831 scopus 로고    scopus 로고
    • Nitric Oxide Inactivates Glyoxalase I in Cooperation with Glutathione
    • Mitsumoto A, Kim KR, Oshima G, Kunimoto M, Okawa K, et al. (2000) Nitric Oxide Inactivates Glyoxalase I in Cooperation with Glutathione. J Biochem 128(4): 647-654.
    • (2000) J Biochem , vol.128 , Issue.4 , pp. 647-654
    • Mitsumoto, A.1    Kim, K.R.2    Oshima, G.3    Kunimoto, M.4    Okawa, K.5
  • 16
    • 0033572849 scopus 로고    scopus 로고
    • Glyoxalase I is a novel nitric-oxide-responsive protein
    • Mitsumoto A, Kim KR, Oshima G, Kunimoto M, Okawa K, et al. (1999) Glyoxalase I is a novel nitric-oxide-responsive protein. Biochem J 344(Pt 3): 837-844.
    • (1999) Biochem J , vol.344 , Issue.PART 3 , pp. 837-844
    • Mitsumoto, A.1    Kim, K.R.2    Oshima, G.3    Kunimoto, M.4    Okawa, K.5
  • 17
    • 0032537553 scopus 로고    scopus 로고
    • Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: Evidence for optimal activation by nickel ions
    • Clugston SL, Barnard JF, Kinach R, Miedema D, Ruman R, et al. (1998) Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: evidence for optimal activation by nickel ions. Biochemistry 37(24): 8754-8763.
    • (1998) Biochemistry , vol.37 , Issue.24 , pp. 8754-8763
    • Clugston, S.L.1    Barnard, J.F.2    Kinach, R.3    Miedema, D.4    Ruman, R.5
  • 18
    • 52849138817 scopus 로고    scopus 로고
    • Characterization of Glyoxalase I (E. coli)-Inhibitor Interactions by Electrospray Time-of-Flight Mass Spectrometry and Enzyme Kinetic Analysis
    • Stokvis E, Clugston SL, Honek JF, Heck AJ (2000) Characterization of Glyoxalase I (E. coli)-Inhibitor Interactions by Electrospray Time-of-Flight Mass Spectrometry and Enzyme Kinetic Analysis. J Protein Chem 19(5): 389-397.
    • (2000) J Protein Chem , vol.19 , Issue.5 , pp. 389-397
    • Stokvis, E.1    Clugston, S.L.2    Honek, J.F.3    Heck, A.J.4
  • 19
    • 0027417473 scopus 로고
    • Cloning and Characterization of Human Colon Glyoxalase 1
    • Ranganathan S, Walsh ES, Godwin AK, Tew KD (1993) Cloning and Characterization of Human Colon Glyoxalase 1, J Biol Chem 268(8): 5661-5667.
    • (1993) J Biol Chem , vol.268 , Issue.8 , pp. 5661-5667
    • Ranganathan, S.1    Walsh, E.S.2    Godwin, A.K.3    Tew, K.D.4
  • 20
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell, S J (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20(18): 3551-3567.
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, S.J.4
  • 21
    • 0034711184 scopus 로고    scopus 로고
    • N-a-terminal Acetylation of Eukaryotic Proteins
    • Polevoda B, Sherman F (2000) N-a-terminal Acetylation of Eukaryotic Proteins. J Biol Chem 275(47): 36479-36482.
    • (2000) J Biol Chem , vol.275 , Issue.47 , pp. 36479-36482
    • Polevoda, B.1    Sherman, F.2
  • 22
    • 0033863181 scopus 로고    scopus 로고
    • Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/ electrospray ionization tandem mass spectrometry
    • Yen TY, Joshi RK, Yan H, Seto NO, Palcic MM, et al. (2000) Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/ electrospray ionization tandem mass spectrometry. J Mass Spectrom 35(8): 990-1002.
    • (2000) J Mass Spectrom , vol.35 , Issue.8 , pp. 990-1002
    • Yen, T.Y.1    Joshi, R.K.2    Yan, H.3    Seto, N.O.4    Palcic, M.M.5
  • 23
    • 0036161645 scopus 로고    scopus 로고
    • Characterizing closely spaced, complex disulfide bond patterns in peptides and proteins by liquid chromatography/ electrospray ionization tandem mass spectrometry
    • Yen TY, Yan H, Macher BA (2002) Characterizing closely spaced, complex disulfide bond patterns in peptides and proteins by liquid chromatography/ electrospray ionization tandem mass spectrometry. J Mass Spectrom 37(1): 15-30.
    • (2002) J Mass Spectrom , vol.37 , Issue.1 , pp. 15-30
    • Yen, T.Y.1    Yan, H.2    Macher, B.A.3
  • 24
    • 0033550054 scopus 로고    scopus 로고
    • Reaction Mechanism of Glyoxalase I Explored by an X-ray Crystallo-graphic Analysis of the Human Enzyme in Complex with a Transition State Analogue
    • Cameron AD, Ridderström M, Olin B, Kavarana MJ, Creighton DJ, et al. (1999) Reaction Mechanism of Glyoxalase I Explored by an X-ray Crystallo-graphic Analysis of the Human Enzyme in Complex with a Transition State Analogue. Biochemistry 38(41): 13480-13490.
    • (1999) Biochemistry , vol.38 , Issue.41 , pp. 13480-13490
    • Cameron, A.D.1    Ridderström, M.2    Olin, B.3    Kavarana, M.J.4    Creighton, D.J.5
  • 25
    • 0002835970 scopus 로고
    • An Experimental Investigation of the 'Ring Hypothesis' of Arsenical Toxicity
    • Whittaker VP (1947) An Experimental Investigation of the 'Ring Hypothesis' of Arsenical Toxicity. Biochem J 41(1): 56-62.
    • (1947) Biochem J , vol.41 , Issue.1 , pp. 56-62
    • Whittaker, V.P.1
  • 26
    • 51049091712 scopus 로고    scopus 로고
    • Regulation by Reversible S-Glutathionylation: Molecular Targets Implicated in Inflammatory Diseases
    • Shelton M, Mieyal J (2008) Regulation by Reversible S-Glutathionylation: Molecular Targets Implicated in Inflammatory Diseases. Mol Cells 25(3): 332-346.
    • (2008) Mol Cells , vol.25 , Issue.3 , pp. 332-346
    • Shelton, M.1    Mieyal, J.2
  • 27
    • 0042164949 scopus 로고    scopus 로고
    • Redox proteomics: Identification of oxidatively modified proteins
    • Ghezzi P, Bonetto V (2003) Redox proteomics: Identification of oxidatively modified proteins. Proteomics 3(7): 1145-1153.
    • (2003) Proteomics , vol.3 , Issue.7 , pp. 1145-1153
    • Ghezzi, P.1    Bonetto, V.2
  • 28
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionyla-tion in redox signaling and oxidative stress
    • Gallogly MM, Mieyal JJ (2007) Mechanisms of reversible protein glutathionyla-tion in redox signaling and oxidative stress. Curr Opin Pharmacol 7(4): 381-391.
    • (2007) Curr Opin Pharmacol , vol.7 , Issue.4 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 29
    • 0021950214 scopus 로고
    • Protein mixed-disulfides in cardiac cells. S-litiolation of soluble proteins in response to diamide
    • Grimm LM, Collison MW, Fisher RA, Thomas JA (1985) Protein mixed-disulfides in cardiac cells. S-litiolation of soluble proteins in response to diamide. Biochim Biophys Acta 844(1): 50-54.
    • (1985) Biochim Biophys Acta , vol.844 , Issue.1 , pp. 50-54
    • Grimm, L.M.1    Collison, M.W.2    Fisher, R.A.3    Thomas, J.A.4
  • 30
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr S, Hallak H, de Boitte A, Lapetina EG, Brune B (1999) Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 274(14): 9427-9430.
    • (1999) J Biol Chem , vol.274 , Issue.14 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    de Boitte, A.3    Lapetina, E.G.4    Brune, B.5
  • 31
    • 34347329257 scopus 로고    scopus 로고
    • Oxidative stress inhibits human p53 by glutathionylation of cysteines in the proximal DNA-binding domain and disruption of dimerization
    • Velu CS, Niture SK, Doneanu CE, Pattabiraman N, Srivenugopal KS (2007) Oxidative stress inhibits human p53 by glutathionylation of cysteines in the proximal DNA-binding domain and disruption of dimerization. Biochemistry 46(26): 7765-7780.
    • (2007) Biochemistry , vol.46 , Issue.26 , pp. 7765-7780
    • Velu, C.S.1    Niture, S.K.2    Doneanu, C.E.3    Pattabiraman, N.4    Srivenugopal, K.S.5
  • 32
    • 34547128886 scopus 로고    scopus 로고
    • Glutathione Supplementation Potentiates Hypoxic Apoptosis by S-Glutathionylation of p65-NFkB
    • Qanungo S, Starke DW, Pai HV, Mieyal JJ, Nieminen AL (2007) Glutathione Supplementation Potentiates Hypoxic Apoptosis by S-Glutathionylation of p65-NFkB. J Biol Chem 282(25): 18427-18436.
    • (2007) J Biol Chem , vol.282 , Issue.25 , pp. 18427-18436
    • Qanungo, S.1    Starke, D.W.2    Pai, H.V.3    Mieyal, J.J.4    Nieminen, A.L.5
  • 33
    • 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 USA 99: 3505-3510.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Eberini, I.5
  • 34
    • 34249874824 scopus 로고    scopus 로고
    • Thioredoxins, glutaredoxins, and glutathionylation: New crosstalks to explore
    • Michelet L, Zaffagnini M, Massot V, Keryer E, Vanacker H, et al. (2006) Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore. Photosynth Res 89(2-3): 225-245.
    • (2006) Photosynth Res , vol.89 , Issue.2-3 , pp. 225-245
    • Michelet, L.1    Zaffagnini, M.2    Massot, V.3    Keryer, E.4    Vanacker, H.5
  • 35
    • 0042665896 scopus 로고    scopus 로고
    • Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells
    • Fratelli M, Demol H, Puype M, Casagrande S, Villa P, et al. (2003) Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells. Proteomics 3(7): 1154-1161.
    • (2003) Proteomics , vol.3 , Issue.7 , pp. 1154-1161
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Villa, P.5
  • 36
  • 37
    • 0001371953 scopus 로고
    • The Mechanism of the Glyoxalase I Reaction, and the Effect of Ophthalmic Acid as an Inhibitor
    • Cliffe EE, Waley SG (1961) The Mechanism of the Glyoxalase I Reaction, and the Effect of Ophthalmic Acid as an Inhibitor. Biochem J 79: 475-482.
    • (1961) Biochem J , vol.79 , pp. 475-482
    • Cliffe, E.E.1    Waley, S.G.2
  • 38
    • 0035969865 scopus 로고    scopus 로고
    • Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: Roles for glutathione in both enzymes and implications for diabetic complications
    • Vander Jagt DL, Hassebrook RK, Hunsaker LA, Brown WM, Royer RE (2001) Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications. Chem-Biol Interactions. pp 130-132, 549-562.
    • (2001) Chem-Biol Interactions , vol.549-562 , pp. 130-132
    • van der Jagt, D.L.1    Hassebrook, R.K.2    Hunsaker, L.A.3    Brown, W.M.4    Royer, R.E.5
  • 39
    • 49349099815 scopus 로고    scopus 로고
    • Ethyl pyruvate and ethyl lactate down-regulate the production of pro-inflammatory cytokines and modulate expression of immune receptors
    • Hollenbach M, Hintersdorf A, Huse K, Sack U, Bigl M, et al. (2008) Ethyl pyruvate and ethyl lactate down-regulate the production of pro-inflammatory cytokines and modulate expression of immune receptors. Biochem Pharmacol 76: 631-644.
    • (2008) Biochem Pharmacol , vol.76 , pp. 631-644
    • Hollenbach, M.1    Hintersdorf, A.2    Huse, K.3    Sack, U.4    Bigl, M.5
  • 40
    • 0036371627 scopus 로고    scopus 로고
    • C-Jun regulation by S-glutathionylation
    • Klatt P, Lamas S (2002) C-Jun regulation by S-glutathionylation. Methods Enzymol 348: 157-174.
    • (2002) Methods Enzymol , vol.348 , pp. 157-174
    • Klatt, P.1    Lamas, S.2
  • 41
    • 0029053976 scopus 로고
    • Evidence for a (triosephophate Isomerase-like) ''Catalytic Loop'' near the active Site of Glyoxalase I
    • Lan Y (1995) Evidence for a (triosephophate Isomerase-like) ''Catalytic Loop'' near the active Site of Glyoxalase I. J Biol Chem 270(22): 12957-12960.
    • (1995) J Biol Chem , vol.270 , Issue.22 , pp. 12957-12960
    • Lan, Y.1
  • 42
    • 0020460509 scopus 로고
    • Fluorescence and Nuclear Relaxation Enhancement Studies of the Binding of Glutathione Derivatives to Manganese-Reconstituted Glyoxalase I from Human Erythrocytes. A Model for the Catalytic Mechanism of the Enzyme Involving a Hydrated Metal Ion
    • Sellin S, Eriksson LEG, Mannervik B (1982) Fluorescence and Nuclear Relaxation Enhancement Studies of the Binding of Glutathione Derivatives to Manganese-Reconstituted Glyoxalase I from Human Erythrocytes. A Model for the Catalytic Mechanism of the Enzyme Involving a Hydrated Metal Ion. Biochemistry 21: 4850-4875.
    • (1982) Biochemistry , vol.21 , pp. 4850-4875
    • Sellin, S.1    Eriksson, L.E.G.2    Mannervik, B.3
  • 44
    • 0035823539 scopus 로고    scopus 로고
    • Two Vicinal Cysteines Confer a Peculiar Redox Regulation to Low Molecular Weight Protein Tyrosine Phosphatase in Response to Platelet-derived Growth Factor Receptor Stimulation
    • Chiarugi P, Fiaschi T, Taddei ML, Talini D, Giannoni E, et al. (2001) Two Vicinal Cysteines Confer a Peculiar Redox Regulation to Low Molecular Weight Protein Tyrosine Phosphatase in Response to Platelet-derived Growth Factor Receptor Stimulation. J Biol Chem 276(36): 33478-33487.
    • (2001) J Biol Chem , vol.276 , Issue.36 , pp. 33478-33487
    • Chiarugi, P.1    Fiaschi, T.2    Taddei, M.L.3    Talini, D.4    Giannoni, E.5
  • 46
    • 36248939782 scopus 로고    scopus 로고
    • ''Forbidden'' Disulfides: Their Role as Redox Switches
    • Wouters MA, George RA, Haworth NL (2007) ''Forbidden'' Disulfides: Their Role as Redox Switches. Curr Protein Pept Sci 8(5): 484-495.
    • (2007) Curr Protein Pept Sci , vol.8 , Issue.5 , pp. 484-495
    • Wouters, M.A.1    George, R.A.2    Haworth, N.L.3
  • 47
    • 0027510941 scopus 로고
    • Inactivation of a redox-sensitive protein phosphatase during the early events of tumor necrosis factor/interleukin-1 signal transduction
    • Guy GR, Cairns J, Ng SB, Tan YH (1993) Inactivation of a redox-sensitive protein phosphatase during the early events of tumor necrosis factor/interleukin-1 signal transduction. J Biol Chem 268(3): 2141-2148.
    • (1993) J Biol Chem , vol.268 , Issue.3 , pp. 2141-2148
    • Guy, G.R.1    Cairns, J.2    Ng, S.B.3    Tan, Y.H.4
  • 48
    • 0035095366 scopus 로고    scopus 로고
    • Inhibition of human squalene monooxygenase by tellurium compounds: Evidence of interaction with vicinal sulfhydryls
    • Laden BP, Porter TD (2001) Inhibition of human squalene monooxygenase by tellurium compounds: evidence of interaction with vicinal sulfhydryls. J Lipid Res 42(2): 235-240.
    • (2001) J Lipid Res , vol.42 , Issue.2 , pp. 235-240
    • Laden, B.P.1    Porter, T.D.2
  • 49
    • 43849087330 scopus 로고    scopus 로고
    • Arsenic-Based Antineoplastic Drugs and Their Mechanisms of Action
    • Ralph SJ (2008) Arsenic-Based Antineoplastic Drugs and Their Mechanisms of Action. Met Based Drugs 2008(260146): 1-13.
    • (2008) Met Based Drugs , vol.2008 , pp. 1-13
    • Ralph, S.J.1
  • 50
    • 33644993314 scopus 로고    scopus 로고
    • Effect of PAO (phenylarsine oxide) on the Inhibitory Effect of Insulin and IGF-1 on Insulin Release from INS-1 Cells
    • Verspohl E (2006) Effect of PAO (phenylarsine oxide) on the Inhibitory Effect of Insulin and IGF-1 on Insulin Release from INS-1 Cells. Endocr J 53(1): 21-26.
    • (2006) Endocr J , vol.53 , Issue.1 , pp. 21-26
    • Verspohl, E.1
  • 51
    • 58149193255 scopus 로고    scopus 로고
    • The Effect of Oxidant and the Non-Oxidant Alteration of Cellular Thiol Concentration on the Formation of Protein Mixed-Disulfides in HEK 293 Cells
    • Gilge JL, Fisher M, Chai Y-C (2008) The Effect of Oxidant and the Non-Oxidant Alteration of Cellular Thiol Concentration on the Formation of Protein Mixed-Disulfides in HEK 293 Cells. PLoS One 3(12): e4015.
    • (2008) PLoS One , vol.3 , Issue.12
    • Gilge, J.L.1    Fisher, M.2    Chai, Y.-C.3
  • 52
    • 0024836625 scopus 로고
    • Erythrocyte glyoxalase activity in genetically obese (ob/ob) and streptozotocin diabetic mice
    • Atkins TW, Thornally PJ (1989) Erythrocyte glyoxalase activity in genetically obese (ob/ob) and streptozotocin diabetic mice. Diabetes Res 11(3): 125-9.
    • (1989) Diabetes Res , vol.11 , Issue.3 , pp. 125-129
    • Atkins, T.W.1    Thornally, P.J.2
  • 53
    • 0013879131 scopus 로고
    • Congenital nonspherocytic hemolytic anemia, associated with glutathione deficiency of the erythrocytes
    • Prins HK, Oort M, Loos JA, Zuercher C, Beckers T (1966) Congenital nonspherocytic hemolytic anemia, associated with glutathione deficiency of the erythrocytes. Blood 27(2): 145-66.
    • (1966) Blood , vol.27 , Issue.2 , pp. 145-166
    • Prins, H.K.1    Oort, M.2    Loos, J.A.3    Zuercher, C.4    Beckers, T.5
  • 54
    • 55649097940 scopus 로고    scopus 로고
    • Cucurmin Inhibits Glyoxalase 1- a Possible Link to Its Anti-Inflammatory and Anti-Tumor Activity
    • Santel T, Pflug G, Hemdan NYA, Schaefer A, Hollenbach M, et al. (2008) Cucurmin Inhibits Glyoxalase 1- A Possible Link to its Anti-Inflammatory and Anti-Tumor Activity. PLoS ONE 3(10): e3508.
    • (2008) PLoS ONE , vol.3 , Issue.10
    • Santel, T.1    Pflug, G.2    Hemdan, N.Y.A.3    Schaefer, A.4    Hollenbach, M.5
  • 55
    • 34247359088 scopus 로고    scopus 로고
    • Methylglyoxal impairs glucose metabolism and leads to energy depletion in neuronal cells - protection by carbonyl scavengers
    • de Arriba SG, Stuchbury G, Yarin J, Burnell J, Loske C, et al. (2007) Methylglyoxal impairs glucose metabolism and leads to energy depletion in neuronal cells - protection by carbonyl scavengers. Neurobiol Aging 28(7): 1044-1050.
    • (2007) Neurobiol Aging , vol.28 , Issue.7 , pp. 1044-1050
    • de Arriba, S.G.1    Stuchbury, G.2    Yarin, J.3    Burnell, J.4    Loske, C.5
  • 57
    • 34447252547 scopus 로고    scopus 로고
    • Methylglyoxal suppresses TNF-a-induced NF-kB activation by inhibiting NF-kB DNA-binding
    • Laga M, Cottyn A, Van Herreweghe F, Vanden Berghe W, Haegeman G, et al. (2007) Methylglyoxal suppresses TNF-a-induced NF-kB activation by inhibiting NF-kB DNA-binding. Biochem Pharmacol 74(4): 579-589.
    • (2007) Biochem Pharmacol , vol.74 , Issue.4 , pp. 579-589
    • Laga, M.1    Cottyn, A.2    van Herreweghe, F.3    van den Berghe, W.4    Haegeman, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.