메뉴 건너뛰기




Volumn 19, Issue 7, 2013, Pages 708-722

Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACID; DISULFIDE; DITHIOL DERIVATIVE; GLUTAREDOXIN; GLUTATHIONE DISULFIDE; GLYCINE; IRON; OXIDOREDUCTASE; SULFUR; THIOL DERIVATIVE; TRYPANOTHIONE; TRYPAREDOXIN; UNCLASSIFIED DRUG;

EID: 84881422708     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4932     Document Type: Review
Times cited : (37)

References (91)
  • 1
    • 0037830694 scopus 로고    scopus 로고
    • Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei. Photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function
    • DOI 10.1074/jbc.M301526200
    • Alphey MS, Gabrielsen M, Micossi E, Leonard GA, McSweeney SM, Ravelli RB, Tetaud E, Fairlamb AH, Bond CS, and Hunter WN. Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function. J Biol Chem 278: 25919-25925, 2003. (Pubitemid 36835354)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25919-25925
    • Alphey, M.S.1    Gabrielsen, M.2    Micossi, E.3    Leonard, G.A.4    McSweeney, S.M.5    Ravelli, R.B.G.6    Tetaud, E.7    Fairlamb, A.H.8    Bond, C.S.9    Hunter, W.N.10
  • 3
    • 0015947802 scopus 로고
    • Mechanism of action of enzymes catalyzing thiol-disulfide interchange. Thioltransferases rather than transhydrogenases
    • Askelof P, Axelsson K, Eriksson S, and Mannervik B. Mechanism of action of enzymes catalyzing thiol-disulfide interchange. Thioltransferases rather than transhydrogenases. FEBS Lett 38: 263-267, 1974.
    • (1974) FEBS Lett , vol.38 , pp. 263-267
    • Askelof, P.1    Axelsson, K.2    Eriksson, S.3    Mannervik, B.4
  • 4
    • 72749084211 scopus 로고    scopus 로고
    • An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations
    • Atkinson H, and Babbitt PC. An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLoS Comput. Biol 5: -e1000541, 2009.
    • (2009) PLoS Comput. Biol , vol.5
    • Atkinson, H.1    Babbitt, P.C.2
  • 5
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense
    • DOI 10.1074/jbc.M408011200
    • Beer SM, Taylor ER, Brown SE, Dahm CC, Costa NJ, Runswick MJ, and Murphy MP. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense. J Biol Chem 279: 47939-47951, 2004. (Pubitemid 39540945)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 7
    • 77951625744 scopus 로고    scopus 로고
    • Trypanothione efficiently intercepts nitric oxide as a harmless iron complex in trypanosomatid parasites
    • Bocedi A, Dawood KF, Fabrini R, Federici G, Gradoni L, Pedersen JZ, and Ricci G. Trypanothione efficiently intercepts nitric oxide as a harmless iron complex in trypanosomatid parasites. FASEB J 24: 1035-1042, 2010.
    • (2010) FASEB J , vol.24 , pp. 1035-1042
    • Bocedi, A.1    Dawood, K.F.2    Fabrini, R.3    Federici, G.4    Gradoni, L.5    Pedersen, J.Z.6    Ricci, G.7
  • 8
    • 0037959650 scopus 로고    scopus 로고
    • Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of trypanosoma brucei brucei
    • DOI 10.1515/BC.2003.069
    • Budde H, Flohé L, Hecht HJ, Hofmann B, Stehr M, Wissing J, and Lunsdorf H. Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei. Biol Chem 384: 619-633, 2003 (Pubitemid 36609177)
    • (2003) Biological Chemistry , vol.384 , Issue.4 , pp. 619-633
    • Budde, H.1    Flohe, L.2    Hecht, H.-J.3    Hofmann, B.4    Stehr, M.5    Wissing, J.6    Lunsdorf, H.7
  • 9
    • 0026799490 scopus 로고
    • Structural and functional characterization of the mutant escherichia coli glutaredoxin c14/s and its mixed disulfide with glutathione
    • Bushweller JH, Aslund F, Wuthrich K, and Holmgren A. Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14/S) and its mixed disulfide with glutathione. Biochemistry 31: 9288-9293, 1992.
    • (1992) Biochemistry , vol.31 , pp. 9288-9293
    • Bushweller, J.H.1    Aslund, F.2    Wuthrich, K.3    Holmgren, A.4
  • 10
    • 0028181442 scopus 로고
    • The nuclear magnetic resonance solution structure of the mixed disulfide between escherichia coli glutaredoxin (c14s) and glutathione
    • Bushweller JH, Billeter M, Holmgren A, and Wuthrich K. The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin (C14S) and glutathione. J Mol Biol 235: 1585-1597, 1994.
    • (1994) J Mol Biol , vol.235 , pp. 1585-1597
    • Bushweller, J.H.1    Billeter, M.2    Holmgren, A.3    Wuthrich, K.4
  • 11
    • 34548013116 scopus 로고    scopus 로고
    • The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload
    • DOI 10.1182/blood-2007-02-072520
    • Camaschella C, Campanella A, De Falco L, Boschetto L, Merlini R, Silvestri L, Levi S, and Iolascon A. The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload. Blood 110: 1353-1358, 2007. (Pubitemid 47281436)
    • (2007) Blood , vol.110 , Issue.4 , pp. 1353-1358
    • Camaschella, C.1    Campanella, A.2    De Falco, L.3    Boschetto, L.4    Merlini, R.5    Silvestri, L.6    Levi, S.7    Iolascon, A.8
  • 12
    • 78049356626 scopus 로고    scopus 로고
    • The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism
    • Ceylan S, Seidel V, Ziebart N, Berndt C, Dirdjaja N, and Krauth-Siegel RL. The dithiol glutaredoxins of African trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism. J Biol Chem 285: 35224-35237, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 35224-35237
    • Ceylan, S.1    Seidel, V.2    Ziebart, N.3    Berndt, C.4    Dirdjaja, N.5    Krauth-Siegel, R.L.6
  • 13
    • 33748747966 scopus 로고    scopus 로고
    • AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage
    • DOI 10.1074/jbc.M601354200
    • Cheng NH, Liu JZ, Brock A, Nelson RS, and Hirschi KD. AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage. J Biol Chem 281: 26280-26288, 2006. (Pubitemid 44401836)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26280-26288
    • Cheng, N.-H.1    Liu, J.-Z.2    Brock, A.3    Nelson, R.S.4    Hirschi, K.D.5
  • 14
    • 35349012982 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression in trypanosomes and leishmanias
    • DOI 10.1016/j.molbiopara.2007.07.007, PII S0166685107002101
    • Clayton C and Shapira M. Post-transcriptional regulation of gene expression in trypanosomes and leishmanias. Mol Biochem Parasitol 156: 93-101, 2007. (Pubitemid 47600362)
    • (2007) Molecular and Biochemical Parasitology , vol.156 , Issue.2 , pp. 93-101
    • Clayton, C.1    Shapira, M.2
  • 15
    • 33846963220 scopus 로고    scopus 로고
    • Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defense in african trypanosomes
    • Comini MA, Krauth-Siegel RL, and Flohé L. Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defense in African trypanosomes. Biochem J 402: 43-49, 2007.
    • (2007) Biochem J , vol.402 , pp. 43-49
    • Comini, M.A.1    Krauth-Siegel, R.L.2    Flohé, L.3
  • 16
    • 55549131538 scopus 로고    scopus 로고
    • Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of african trypanosomes
    • Comini MA, Rettig J, Dirdjaja N, Hanschmann EM, Berndt C, and Krauth-Siegel RL. Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes. J Biol Chem 283: 27785-27798, 2008
    • (2008) J Biol Chem , vol.283 , pp. 27785-27798
    • Comini, M.A.1    Rettig, J.2    Dirdjaja, N.3    Hanschmann, E.M.4    Berndt, C.5    Krauth-Siegel, R.L.6
  • 18
    • 14944367451 scopus 로고    scopus 로고
    • Plasmodium falciparum glutaredoxin-like proteins
    • DOI 10.1515/BC.2005.005
    • Deponte M, Becker K, and Rahlfs S. Plasmodium falciparum glutaredoxin-like proteins. Biol Chem 386: 33-40, 2005 (Pubitemid 40361449)
    • (2005) Biological Chemistry , vol.386 , Issue.1 , pp. 33-40
    • Deponte, M.1    Becker, K.2    Rahlfs, S.3
  • 20
    • 0035815655 scopus 로고    scopus 로고
    • Trypanothione-dependent Synthesis of Deoxyribonucleotides by Trypanosoma brucei Ribonucleotide Reductase
    • DOI 10.1074/jbc.M010352200
    • Dormeyer M, Reckenfelderbaumer N, Ludemann H, and Krauth-Siegel RL. Trypanothione-dependent synthesis of deoxyribonucleotides by Trypanosoma brucei ribonucleotide reductase. J Biol Chem 276: 10602-10606, 2001. (Pubitemid 38094248)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10602-10606
    • Dormeyer, M.1    Reckenfelderbaumer, N.2    Ludemann, H.3    Krauth-Siegel, R.L.4
  • 21
    • 30344443401 scopus 로고    scopus 로고
    • The presence of four iron-containing superoxide dismutase isozymes in Trypanosomatidae: Characterization, subcellular localization, and phylogenetic origin in Trypanosoma brucei
    • DOI 10.1016/j.freeradbiomed.2005.06.021, PII S0891584905003837
    • Dufernez F, Yernaux C, Gerbod D, Noel C, Chauvenet M, Wintjens R, Edgcomb VP, Capron M, Opperdoes FR, and Viscogliosi E. The presence of four iron-containing superoxide dismutase isozymes in trypanosomatidae: characterization, subcellular localization, and phylogenetic origin in Trypanosoma brucei. Free Radic Biol Med 40: 210-225, 2006. (Pubitemid 43069347)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.2 , pp. 210-225
    • Dufernez, F.1    Yernaux, C.2    Gerbod, D.3    Noel, C.4    Chauvenet, M.5    Wintjens, R.6    Edgcomb, V.P.7    Capron, M.8    Opperdoes, F.R.9    Viscogliosi, E.10
  • 22
    • 64349107040 scopus 로고    scopus 로고
    • Biochemical characterization of dithiol glutaredoxin 8 from saccharomyces cerevisiae: The catalytic redox mechanism redux
    • Eckers E, Bien M, Stroobant V, Herrmann JM, and Deponte M. Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: The catalytic redox mechanism redux. Biochemistry 48: 1410-1423, 2009.
    • (2009) Biochemistry , vol.48 , pp. 1410-1423
    • Eckers, E.1    Bien, M.2    Stroobant, V.3    Herrmann, J.M.4    Deponte, M.5
  • 23
    • 57749093461 scopus 로고    scopus 로고
    • Quantifying escherichia coli glutaredoxin-3 substrate specificity using ligand-induced stability
    • Elgán TH and Berndt KD. Quantifying Escherichia coli glutaredoxin-3 substrate specificity using ligand-induced stability. J Biol Chem 283: 32839-32847, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 32839-32847
    • Elgán, T.H.1    Berndt, K.D.2
  • 24
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the kinetoplastida
    • Fairlamb AH and Cerami A. Metabolism and functions of trypanothione in the Kinetoplastida. Annu Rev Microbiol 46: 695-729, 1992.
    • (1992) Annu Rev Microbiol , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 25
    • 33745614344 scopus 로고    scopus 로고
    • Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site
    • DOI 10.1021/bi060444t
    • Feng Y, Zhong N, Rouhier N, Hase T, Kusunoki M, Jacquot JP, Jin C, and Xia B. Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site. Biochemistry 45: 7998-8008, 2006. (Pubitemid 43993221)
    • (2006) Biochemistry , vol.45 , Issue.26 , pp. 7998-8008
    • Feng, Y.1    Zhong, N.2    Rouhier, N.3    Hase, T.4    Kusunoki, M.5    Jacquot, J.-P.6    Jin, C.7    Xia, B.8
  • 27
    • 37349126094 scopus 로고    scopus 로고
    • Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1
    • DOI 10.1515/BC.2007.147
    • Filser M, Comini MA, Molina-Navarro MM, Dirdjaja N, Herrero E, and Krauth-Siegel RL. Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1. Biol Chem 389: 21-32, 2008. (Pubitemid 350308201)
    • (2008) Biological Chemistry , vol.389 , Issue.1 , pp. 21-32
    • Filser, M.1    Comini, M.A.2    Molina-Navarro, M.M.3    Dirdjaja, N.4    Herrero, E.5    Krauth-Siegel, R.L.6
  • 28
    • 21644481715 scopus 로고    scopus 로고
    • Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli
    • DOI 10.1074/jbc.M500679200
    • Fladvad M, Bellanda M, Fernandes AP, Mammi S, Vlamis-Gardikas A, Holmgren A, and Sunnerhagen M. Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli. J Biol Chem 280: 24553-24561, 2005. (Pubitemid 40934542)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24553-24561
    • Fladvad, M.1    Bellanda, M.2    Fernandes, A.P.3    Mammi, S.4    Vlamis-Gardikas, A.5    Holmgren, A.6    Sunnerhagen, M.7
  • 30
    • 51349142890 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: Implications for intracellular roles
    • Gallogly MM, Starke DW, Leonberg AK, Ospina SM, and Mieyal JJ. Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: Implications for intracellular roles. Biochemistry 47: 11144-11157, 2008.
    • (2008) Biochemistry , vol.47 , pp. 11144-11157
    • Gallogly, M.M.1    Starke, D.W.2    Leonberg, A.K.3    Ospina, S.M.4    Mieyal, J.J.5
  • 32
    • 84855878395 scopus 로고    scopus 로고
    • Comprehensive automation for nmr structure determination of proteins
    • Guerry P and Herrmann T. Comprehensive automation for NMR structure determination of proteins. Methods Mol Biol 831: 429-451, 2012.
    • (2012) Methods Mol Biol , vol.831 , pp. 429-451
    • Guerry, P.1    Herrmann, T.2
  • 33
    • 34250731291 scopus 로고    scopus 로고
    • Monothiol glutaredoxins: A common domain for multiple functions
    • DOI 10.1007/s00018-007-6554-8
    • Herrero E and de la Torre-Ruiz MA. Monothiol glutaredoxins: A common domain for multiple functions. Cell Mol Life Sci 64: 1518-1530, 2007. (Pubitemid 46954154)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.12 , pp. 1518-1530
    • Herrero, E.1    De La Torre-Ruiz, M.A.2
  • 34
    • 0037470229 scopus 로고    scopus 로고
    • A second class of peroxidases linked to the trypanothione metabolism
    • DOI 10.1074/jbc.M210392200
    • Hillebrand H, Schmidt A, and Krauth-Siegel RL. A second class of peroxidases linked to the trypanothione metabolism. J Biol Chem 278: 6809-6815, 2003. (Pubitemid 36800670)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 6809-6815
    • Hillebrand, H.1    Schmidt, A.2    Krauth-Siegel, R.L.3
  • 36
    • 2042476756 scopus 로고
    • Hydrogen donor system for escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione
    • Holmgren A. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc Natl Acad Sci USA 73: 2275-2279, 1976.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 37
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254: 9627-9632, 1979. (Pubitemid 10248727)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.19 , pp. 9627-9632
    • Holmgren, A.1
  • 38
    • 78649803037 scopus 로고    scopus 로고
    • Conformational analysis and design of crossstrand disulfides in antiparallel b-sheets
    • Indu S, Kochat V, Thakurela S, Ramakrishnan C, and Varadarajan R. Conformational analysis and design of crossstrand disulfides in antiparallel b-sheets. Proteins 79: 244-260, 2011.
    • (2011) Proteins , vol.79 , pp. 244-260
    • Indu, S.1    Kochat, V.2    Thakurela, S.3    Ramakrishnan, C.4    Varadarajan, R.5
  • 39
    • 54949087530 scopus 로고    scopus 로고
    • Insights into the redox biology of trypanosoma cruzi: Trypanothione metabolism and oxidant detoxification
    • Irigoín F, Cibils L, Comini MA, Wilkinson SR, Flohé L, and Radi R. Insights into the redox biology of Trypanosoma cruzi: Trypanothione metabolism and oxidant detoxification. Free Radic Biol Med 45: 733-742, 2008.
    • (2008) Free Radic Biol Med , vol.45 , pp. 733-742
    • Irigoín, F.1    Cibils, L.2    Comini, M.A.3    Wilkinson, S.R.4    Flohé, L.5    Radi, R.6
  • 40
  • 41
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • DOI 10.1074/jbc.M312719200
    • Johansson C, Lillig CH, and Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J Biol Chem 279: 7537-7543, 2004. (Pubitemid 38294632)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 42
    • 34047250626 scopus 로고    scopus 로고
    • Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria
    • DOI 10.1074/jbc.M608179200
    • Johansson C, Kavanagh KL, Gileadi O, and Oppermann U. Reversible sequestration of active site cysteines in a 2Fe-2Sbridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria. J Biol Chem 282: 3077-3082, 2007. (Pubitemid 47084316)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.5 , pp. 3077-3082
    • Johansson, C.1    Kavanagh, K.L.2    Gileadi, O.3    Oppermann, U.4
  • 44
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism
    • Krauth-Siegel RL and Comini MA. Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism. Biochim Biophys Acta 1780: 1236-1248, 2008.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 46
    • 68949203453 scopus 로고    scopus 로고
    • A disruption in iron sulfur center biogenesis via inhibition of mitochondrial dithiol glutaredoxin 2 may contribute to mitochondrial and cellular iron dysregulation in mammalian glutathione-depleted dopaminergic cells: Implications for parkinson's disease
    • Lee DW, Kaur D, Chinta SJ, Rajagopalan S, and Andersen JK. A disruption in iron sulfur center biogenesis via inhibition of mitochondrial dithiol glutaredoxin 2 may contribute to mitochondrial and cellular iron dysregulation in mammalian glutathione-depleted dopaminergic cells: Implications for Parkinson's disease. Antioxid Redox Signal 11: 2083-2094, 2009.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2083-2094
    • Lee, D.W.1    Kaur, D.2    Chinta, S.J.3    Rajagopalan, S.4    Andersen, J.K.5
  • 48
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill R and Muhlenhoff U. Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases. Annu Rev Biochem 77: 669-700, 2008.
    • (2008) Annu Rev Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 51
    • 38349028576 scopus 로고    scopus 로고
    • Expression pattern of human glutaredoxin 2 isoforms: Identification and characterization of two testis/cancer cell-specific isoforms
    • Lonn ME, Hudemann C, Berndt C, Cherkasov V, Capani F, Holmgren A, and Lillig CH. Expression pattern of human glutaredoxin 2 isoforms: Identification and characterization of two testis/cancer cell-specific isoforms. Antioxid Redox Signal 10: 547-557, 2008.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 547-557
    • Lonn, M.E.1    Hudemann, C.2    Berndt, C.3    Cherkasov, V.4    Capani, F.5    Holmgren, A.6    Lillig, C.H.7
  • 52
    • 0038790585 scopus 로고    scopus 로고
    • Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes
    • DOI 10.1016/S0014-5793(98)00793-5, PII S0014579398007935
    • Ludemann H, Dormeyer M, Sticherling C, Stallmann D, Follmann H, and Krauth-Siegel RL. Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes. FEBS Lett 431: 381-385, 1998. (Pubitemid 28352394)
    • (1998) FEBS Letters , vol.431 , Issue.3 , pp. 381-385
    • Ludemann, H.1    Dormeyer, M.2    Sticherling, C.3    Stallmann, D.4    Follmann, H.5    Krauth-Siegel, R.L.6
  • 55
    • 84881410181 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic trypanosomes
    • In: Iron Metabolism, Arora S. Rajica, ed
    • Manta B, Fleitas L, and Comini MA. Iron metabolism in pathogenic trypanosomes. In: Iron Metabolism, Arora S. Rajica, ed. Croatia: INTECH, 2012, pp. 1-40.
    • (2012) Croatia: INTECH , pp. 1-40
    • Manta, B.1    Fleitas, L.2    Comini, M.A.3
  • 56
    • 84875755215 scopus 로고    scopus 로고
    • Iron-sulfur cluster binding by mitochondrial monothiol glutaredoxin-1 of trypanosoma brucei: Molecular basis of iron-sulfur cluster coordination and relevance for parasite infectivity
    • Manta B, Pavan C, Sturlese M, Medeiros A, Crispo M, Berndt C, Krauth-Siegel RL, Bellanda M and Comini MA. Iron-sulfur cluster binding by mitochondrial monothiol glutaredoxin-1 of Trypanosoma brucei: Molecular basis of iron-sulfur cluster coordination and relevance for parasite infectivity. Antioxid Redox Signal 19: 665-682, 2013.
    • (2013) Antioxid Redox Signal , vol.19 , pp. 665-682
    • Manta, B.1    Pavan, C.2    Sturlese, M.3    Medeiros, A.4    Crispo, M.5    Berndt, C.6    Krauth-Siegel, R.L.7    Bellanda, M.8    Comini, M.A.9
  • 58
    • 0029165589 scopus 로고
    • Thioredoxin: A fold for all reasons
    • Martin JL. Thioredoxin: A fold for all reasons. Structure 3: 245-250, 1995.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 60
    • 38849206923 scopus 로고    scopus 로고
    • Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron-sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins
    • DOI 10.1021/bi7017865
    • Mesecke N, Mittler S, Eckers E, Herrmann JM, and Deponte M. Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron-sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins. Biochemistry 47: 1452-1463, 2008. (Pubitemid 351198720)
    • (2008) Biochemistry , vol.47 , Issue.5 , pp. 1452-1463
    • Mesecke, N.1    Mittler, S.2    Eckers, E.3    Herrmann, J.M.4    Deponte, M.5
  • 61
    • 48749085761 scopus 로고    scopus 로고
    • A novel group of glutaredoxins in the cis-golgi critical for oxidative stress resistance
    • Mesecke N, Spang A, Deponte M, and Herrmann JM. A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance. Mol Biol Cell 19: 2673-2680, 2008.
    • (2008) Mol Biol Cell , vol.19 , pp. 2673-2680
    • Mesecke, N.1    Spang, A.2    Deponte, M.3    Herrmann, J.M.4
  • 62
    • 33645990964 scopus 로고    scopus 로고
    • Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of grx5 in the biogenesis of fe/s clusters in yeast mitochondria
    • Molina-Navarro MM, Casas C, Piedrafita L, Bellí G, and Herrero E. Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria. FEBS Lett 580: 2273-2280, 2006.
    • (2006) FEBS Lett , vol.580 , pp. 2273-2280
    • Molina-Navarro, M.M.1    Casas, C.2    Piedrafita, L.3    Bellí, G.4    Herrero, E.5
  • 64
    • 0030861413 scopus 로고    scopus 로고
    • A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata
    • Nogoceke E, Gommel DU, Kiess M, Kalisz HM, and Flohé L. A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol Chem 378: 827-836, 1997. (Pubitemid 27388943)
    • (1997) Biological Chemistry , vol.378 , Issue.8 , pp. 827-836
    • Nogoceke, E.1    Gommel, D.U.2    Kiess, M.3    Kalisz, H.M.4    Flohe, L.5
  • 65
    • 0026709542 scopus 로고
    • The mitochondrion in bloodstream forms of trypanosoma brucei is energized by the electrogenic pumping of protons catalysed by the f1f0-atpase
    • Nolan DP and Voorheis HP. The mitochondrion in bloodstream forms of Trypanosoma brucei is energized by the electrogenic pumping of protons catalysed by the F1F0-ATPase. Eur J Biochem 209: 207-216, 1992.
    • (1992) Eur J Biochem , vol.209 , pp. 207-216
    • Nolan, D.P.1    Voorheis, H.P.2
  • 66
    • 35448993279 scopus 로고    scopus 로고
    • What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?
    • DOI 10.1089/ars.2007.1642
    • Pai HV, Starke DW, Lesnefsky EJ, Hoppel CL, and Mieyal JJ. What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria Antioxid Redox Signal 9: 2027-2033, 2007. (Pubitemid 47622345)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.11 , pp. 2027-2033
    • Pai, H.V.1    Starke, D.W.2    Lesnefsky, E.J.3    Hoppel, C.L.4    Mieyal, J.J.5
  • 67
    • 30644463938 scopus 로고    scopus 로고
    • On the occurrence of thioredoxin in Trypanosoma cruzi
    • DOI 10.1016/j.actatropica.2005.10.005, PII S0001706X0500327X
    • Piattoni CV, Blancato VS, Miglietta H, Iglesias AA, and Guerrero SA. On the occurrence of thioredoxin in Trypanosoma cruzi. Acta Trop 97: 151-160, 2006. (Pubitemid 43087748)
    • (2006) Acta Tropica , vol.97 , Issue.2 , pp. 151-160
    • Piattoni, C.V.1    Blancato, V.S.2    Miglietta, H.3    Iglesias, A.A.4    Guerrero, S.A.5
  • 68
    • 37349036175 scopus 로고    scopus 로고
    • CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster
    • DOI 10.1021/bi7013272
    • Picciocchi A, Saguez C, Boussac A, Cassier-Chauvat C, and Chauvat F. CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster. Biochemistry 46: 15018-15026, 2007. (Pubitemid 350308893)
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 15018-15026
    • Picciocchi, A.1    Saguez, C.2    Boussac, A.3    Cassier-Chauvat, C.4    Chauvat, F.5
  • 69
    • 11344272919 scopus 로고    scopus 로고
    • Structural classification of thioredoxin-like fold proteins
    • DOI 10.1002/prot.20329
    • Qi Y and Grishin NV. Structural classification of thioredoxin-like fold proteins. Proteins 58: 376-388, 2005. (Pubitemid 40076051)
    • (2005) Proteins: Structure, Function and Genetics , vol.58 , Issue.2 , pp. 376-388
    • Qi, Y.1    Grishin, N.V.2
  • 70
    • 0035813229 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a picot homology domain
    • Rahlfs S, Fischer M, and Becker K. Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain. J Biol Chem 276: 37133-37140, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 37133-37140
    • Rahlfs, S.1    Fischer, M.2    Becker, K.3
  • 73
    • 0040932016 scopus 로고    scopus 로고
    • Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae
    • Rodríguez-Manzaneque MT, Ros J, Cabiscol E, Sorribas A, and Herrero E. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19: 8180-8190, 1999. (Pubitemid 30414012)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.12 , pp. 8180-8190
    • Rodriguez-Manzaneque, M.T.1    Ros, J.2    Cabiscol, E.3    Sorribas, A.4    Herrero, E.5
  • 74
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • DOI 10.1091/mbc.01-10-0517
    • Rodri'guez-Manzaneque MT, Tamarit J, Bellí G, Ros J, and Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell 13: 1109-1121, 2002. (Pubitemid 34309609)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.4 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 77
    • 0342275186 scopus 로고    scopus 로고
    • Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A
    • DOI 10.1021/bi970851s
    • Ruoppolo M, Lundstrom-Ljung J, Talamo F, Pucci P, and Marino G. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A. Biochemistry 36: 12259-12267, 1997. (Pubitemid 27440964)
    • (1997) Biochemistry , vol.36 , Issue.40 , pp. 12259-12267
    • Ruoppolo, M.1    Lundstrom-Ljung, J.2    Talamo, F.3    Pucci, P.4    Marino, G.5
  • 78
    • 84873331479 scopus 로고    scopus 로고
    • Determination of acidity and nucleophilicity in thiols by reaction with monobromobimane and fluorescence detection
    • DOI: 10.1016/j.ab.2012.12.017 [In Press].
    • Sardi F, Manta B, Portillo-Ledesma S, Knoops B, Comini MA, and Ferrer-Sueta G. Determination of acidity and nucleophilicity in thiols by reaction with monobromobimane and fluorescence detection. Anal Biochem 2013. DOI: 10.1016/j.ab.2012.12.017 [In Press].
    • (2013) Anal Biochem
    • Sardi, F.1    Manta, B.2    Portillo-Ledesma, S.3    Knoops, B.4    Comini, M.A.5    Ferrer-Sueta, G.6
  • 79
    • 17644393919 scopus 로고    scopus 로고
    • Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei
    • DOI 10.1074/jbc.M413338200
    • Schlecker T, Schmidt A, Dirdjaja N, Voncken F, Clayton C, and Krauth-Siegel RL. Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei. J Biol Chem 280: 14385-14394, 2005. (Pubitemid 40562777)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14385-14394
    • Schlecker, T.1    Schmidt, A.2    Dirdjaja, N.3    Voncken, F.4    Clayton, C.5    Krauth-Siegel, R.L.6
  • 80
    • 0344875617 scopus 로고    scopus 로고
    • Functional and Physicochemical Characterization of the Thioredoxin System in Trypanosoma brucei
    • DOI 10.1074/jbc.M305338200
    • Schmidt H and Krauth-Siegel RL. Functional and physicochemical characterization of the thioredoxin system in Trypanosoma brucei. J Biol Chem 278: 46329-46336, 2003. (Pubitemid 37452203)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46329-46336
    • Schmidt, H.1    Krauth-Siegel, R.L.2
  • 82
    • 33749415299 scopus 로고    scopus 로고
    • Knock-downs of iron-sulfur cluster assembly proteins IscS and IscU down-regulate the active mitochondrion of procyclic Trypanosoma brucei
    • DOI 10.1074/jbc.M513781200
    • Smíd O, Horáková E, Vilímová V, Hrdy I, Cammack R, Horváth A, Lukes J, and Tachezy J. Knock-downs of ironsulfur cluster assembly proteins IscS and IscU downregulate the active mitochondrion of procyclic Trypanosoma brucei. J Biol Chem 281: 28679-28686, 2006. (Pubitemid 44507010)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28679-28686
    • Smid, O.1    Horakova, E.2    Vilimova, V.3    Hrdy, I.4    Cammack, R.5    Horvath, A.6    Lukes, J.7    Tachezy, J.8
  • 83
    • 0031000775 scopus 로고    scopus 로고
    • PH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • DOI 10.1021/bi962017t
    • Srinivasan U, Mieyal PA, and Mieyal JJ. pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry 36: 3199-3206, 1997. (Pubitemid 27142392)
    • (1997) Biochemistry , vol.36 , Issue.11 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 84
    • 0038491193 scopus 로고    scopus 로고
    • Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin
    • DOI 10.1074/jbc.M303477200
    • Tamarit J, Belli G, Cabiscol E, Herrero E, and Ros J. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J Biol Chem 278: 25745-25751, 2003. (Pubitemid 36835331)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25745-25751
    • Tamarit, J.1    Belli, G.2    Cabiscol, E.3    Herrero, E.4    Ros, J.5
  • 85
    • 77953618426 scopus 로고    scopus 로고
    • Iron metabolism in trypanosomatids, and its crucial role in infection
    • Taylor MC and Kelly JM. Iron metabolism in trypanosomatids, and its crucial role in infection. Parasitology 137: 899-917, 2010.
    • (2010) Parasitology , vol.137 , pp. 899-917
    • Taylor, M.C.1    Kelly, J.M.2
  • 86
    • 0034889645 scopus 로고    scopus 로고
    • Molecular characterisation of mitochondrial and cytosolic trypanothione-dependent tryparedoxin peroxidases in Trypanosoma brucei
    • DOI 10.1016/S0166-6851(01)00320-6, PII S0166685101003206
    • Tetaud E, Giroud C, Prescott AR, Parkin DW, Baltz D, Biteau N, Baltz T, and Fairlamb AH. Molecular characterisation of mitochondrial and cytosolic trypanothionedependent tryparedoxin peroxidases in Trypanosoma brucei. Mol Biochem Parasitol 116: 171-183, 2001. (Pubitemid 32777826)
    • (2001) Molecular and Biochemical Parasitology , vol.116 , Issue.2 , pp. 171-183
    • Tetaud, E.1    Giroud, C.2    Prescott, A.R.3    Parkin, D.W.4    Baltz, D.5    Biteau, N.6    Baltz, T.7    Fairlamb, A.H.8
  • 87
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, and Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680, 1994. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 91
    • 80054720193 scopus 로고    scopus 로고
    • The e. Coli monothiol glutaredoxin grxd forms homodimeric and heterodimeric fes cluster containing complexes
    • Yeung N, Gold B, Liu NL, Prathapam R, Sterling HJ, Willams ER, and Butland G. The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes. Biochemistry 50: 8957-8969, 2011.
    • (2011) Biochemistry , vol.50 , pp. 8957-8969
    • Yeung, N.1    Gold, B.2    Liu, N.L.3    Prathapam, R.4    Sterling, H.J.5    Willams, E.R.6    Butland, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.