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Volumn 19, Issue 7, 2013, Pages 665-682

Iron-sulfur cluster binding by mitochondrial monothiol glutaredoxin-1 of Trypanosoma brucei: Molecular basis of iron-sulfur cluster coordination and relevance for parasite infectivity

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DITHIOL DERIVATIVE; GLUTAREDOXIN; GLUTAREDOXIN 1; GLUTATHIONE; GLUTATHIONYLSPERMIDINE; IRON SULFUR PROTEIN; MUTANT PROTEIN; SPERMIDINE; TRYPANOTHIONE; UNCLASSIFIED DRUG;

EID: 84875755215     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4859     Document Type: Review
Times cited : (41)

References (78)
  • 2
    • 0035400398 scopus 로고    scopus 로고
    • Ovothiol and trypanothione as antioxidants in trypanosomatids
    • DOI 10.1016/S0166-6851(01)00285-7, PII S0166685101002857
    • Ariyanayagam MR and Fairlamb AH. Ovothiol and trypanothione as antioxidants in trypanosomatids. Mol Biochem Parasitol 115: 189-198, 2001. (Pubitemid 32566228)
    • (2001) Molecular and Biochemical Parasitology , vol.115 , Issue.2 , pp. 189-198
    • Ariyanayagam, M.R.1    Fairlamb, A.H.2
  • 3
    • 72749084211 scopus 로고    scopus 로고
    • An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations
    • Atkinson HJ 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.J.1    Babbitt, P.C.2
  • 5
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by 15n relaxation using inverse detected two-dimensional nmr spectroscopy: The central helix is flexible
    • Barbato G, Ikura M, Kay LE, Pastor RW, and Bax A. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 31: 5269-5278, 1992.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 6
    • 0037020228 scopus 로고    scopus 로고
    • Structure-function analysis of yeast grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein
    • Bellí G, Polaina J, Tamarit J, De La Torre MA, Rodríguez-Manzaneque MT, Ros J, and Herrero E. Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein. J Biol Chem 277: 37590-37596, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 37590-37596
    • Bellí, G.1    Polaina, J.2    Tamarit, J.3    De La Torre, M.A.4    Rodríguez-Manzaneque, M.T.5    Ros, J.6    Herrero, E.7
  • 7
    • 0035996729 scopus 로고    scopus 로고
    • 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR
    • DOI 10.1023/A:1016359412284
    • Bernadó P, de la Torre JG, and Pons M. Interpretation of 15N NMR relaxation data of globular protein using hydrodynamic calculations with HYDRONMR. J Biomol NMR 23: 139-150, 2002. (Pubitemid 34778166)
    • (2002) Journal of Biomolecular NMR , vol.23 , Issue.2 , pp. 139-150
    • Bernado, P.1    De La Torre, J.G.2    Pons, M.3
  • 9
  • 10
    • 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
  • 11
    • 0028181442 scopus 로고
    • The nuclear magnetic resonance s1lution 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 s1lution 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
  • 12
    • 78049356626 scopus 로고    scopus 로고
    • The dithiol gl1utaredoxins 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 gl1utaredoxins 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
    • 40349113000 scopus 로고    scopus 로고
    • Atgrx4, an arabidopsis chloroplastic monothiol glutaredoxin, is able to suppress yeast grx5 mutant phenotypes and respond to oxidative stress
    • Cheng N-H. AtGRX4, an Arabidopsis chloroplastic monothiol glutaredoxin, is able to suppress yeast grx5 mutant phenotypes and respond to oxidative stress. FEBS Lett 582: 848-854, 2008.
    • (2008) FEBS Lett , vol.582 , pp. 848-854
    • Cheng, N.-H.1
  • 14
    • 67649656107 scopus 로고    scopus 로고
    • Preparative enzymatic synthesis of trypanothione and trypanothione analogues
    • Comini MA, Dirdjaja N, Kaschel M, and Krauth-Siegel RL. Preparative enzymatic synthesis of trypanothione and trypanothione analogues. Int J Parasitol 39: 1059-1062, 2009.
    • (2009) Int J Parasitol , vol.39 , pp. 1059-1062
    • Comini, M.A.1    Dirdjaja, N.2    Kaschel, M.3    Krauth-Siegel, R.L.4
  • 15
    • 84881422708 scopus 로고    scopus 로고
    • Mono-and dithiol glutaredoxins in the trypanothione based redox metabolism of pathogenic trypanosomes
    • Comini MA, Krauth-Siegel RL, and Bellanda M. Mono-and dithiol glutaredoxins in the trypanothione based redox metabolism of pathogenic trypanosomes. Antioxid Redox Signal 19: 708-722, 2013.
    • (2013) Antioxid Redox Signal , vol.19 , pp. 708-722
    • Comini, M.A.1    Krauth-Siegel, R.L.2    Bellanda, M.3
  • 16
    • 33846963220 scopus 로고    scopus 로고
    • Depletion of the thioredoxin homologue trparedoxin impairs antioxidative defence in african trypanosomes
    • Comini MA, Krauth-Siegel RL, and Flohé L. Depletion of the thioredoxin homologue trparedoxin impairs antioxidative defence 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
  • 17
    • 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 E-M, 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
  • 21
    • 0023253710 scopus 로고
    • In vivo effects of difluoromethylornithine on trypanothione and polyamine levels in bloodstream forms of Trypanosoma brucei
    • Fairlamb AH, Henderson GB, Bacchi CJ, and Cerami A. In vivo effects of difluoromethylornithine on trypanothione and polyamine levels in bloodstream forms of Trypanosoma brucei. Mol Biochem Parasitol 24: 185-191, 1987. (Pubitemid 17120748)
    • (1987) Molecular and Biochemical Parasitology , vol.24 , Issue.2 , pp. 185-191
    • Fairlamb, A.H.1    Henderson, G.B.2    Bacchi, C.J.3    Cerami, A.4
  • 22
    • 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 J-P, 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
  • 24
    • 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
  • 25
    • 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
  • 26
    • 64549106959 scopus 로고    scopus 로고
    • Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation
    • Gallogly MM, Starke DW, and Mieyal JJ. Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation. Antioxid Redox Signal 11: 1059-1081, 2009.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1059-1081
    • Gallogly, M.M.1    Starke, D.W.2    Mieyal, J.J.3
  • 28
    • 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
  • 29
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • DOI 10.1006/jmbi.1997.1284
    • Guntert P, Mumenthaler C, and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273: 283-298, 1997. (Pubitemid 27460230)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 31
    • 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
  • 32
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • Herrmann T, Guntert P, and Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319: 209-227, 2002. (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 33
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • DOI 10.1023/A:1021614115432
    • Herrmann T, Guntert P, and Wuthrich K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 24: 171-189, 2002. (Pubitemid 36113646)
    • (2002) Journal of Biomolecular NMR , vol.24 , Issue.3 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 34
    • 83555173402 scopus 로고    scopus 로고
    • Glutathione: A key component of the cytoplasmic labile iron pool
    • Hider RC and Kong XL. Glutathione: a key component of the cytoplasmic labile iron pool. Biometals 24: 1179-1187, 2011.
    • (2011) Biometals , vol.24 , pp. 1179-1187
    • Hider, R.C.1    Kong, X.L.2
  • 37
    • 79952259946 scopus 로고    scopus 로고
    • Millisecond dynamics in glutaredoxin during catalytic turnover is dependent on substrate binding and absent in the resting states
    • Jensen KS, Winther JR, and Teilum K. Millisecond dynamics in glutaredoxin during catalytic turnover is dependent on substrate binding and absent in the resting states. J Am Chem Soc 133: 3034-3042, 2011.
    • (2011) J Am Chem Soc , vol.133 , pp. 3034-3042
    • Jensen, K.S.1    Winther, J.R.2    Teilum, K.3
  • 38
    • 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
  • 40
    • 0030993412 scopus 로고    scopus 로고
    • 15N NMR relaxation measurements
    • DOI 10.1021/bi962181g
    • Kelley JJ 3rd, Caputo TM, Eaton SF, Laue TM, and Bushweller JH. Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements. Biochemistry 36: 5029-5044, 1997. (Pubitemid 27180985)
    • (1997) Biochemistry , vol.36 , Issue.16 , pp. 5029-5044
    • Kelley III, J.J.1    Caputo, T.M.2    Eaton, S.F.3    Laue, T.M.4    Bushweller, J.H.5
  • 41
    • 76349122676 scopus 로고    scopus 로고
    • Monothiol glutaredoxin grx5 interacts with fe-s scaffold proteins isa1 and isa2 and supports fe-s assembly and dna integrity in mitochondria of fission yeast
    • Kim K-D, Chung W-H, Kim H-J, Lee K-C, and Roe J-H. Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast. Biochem Biophys Res Commun 392: 467-472, 2010.
    • (2010) Biochem Biophys Res Commun , vol.392 , pp. 467-472
    • Kim, K.-D.1    Chung, W.-H.2    Kim, H.-J.3    Lee, K.-C.4    Roe, J.-H.5
  • 42
    • 79956202651 scopus 로고    scopus 로고
    • Multi-domain cgfstype glutaredoxin grx4 regulates iron homeostasis via direct interaction with a repressor fep1 in fission yeast
    • Kim KD, Kim HJ, Lee KC, and Roe JH. Multi-domain CGFStype glutaredoxin Grx4 regulates iron homeostasis via direct interaction with a repressor Fep1 in fission yeast. Biochem Biophys Res Commun 408: 609-614, 2011.
    • (2011) Biochem Biophys Res Commun , vol.408 , pp. 609-614
    • Kim, K.D.1    Kim, H.J.2    Lee, K.C.3    Roe, J.H.4
  • 43
    • 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
  • 52
    • 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
  • 53
    • 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
  • 54
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • DOI 10.1093/emboj/cdg446
    • Muhlenhoff U, Gerber J, Richhardt N, and Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J 22: 4815-4825, 2003. (Pubitemid 37162917)
    • (2003) EMBO Journal , vol.22 , Issue.18 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 56
    • 83455235522 scopus 로고    scopus 로고
    • Contribution of innate immune responses towards resistance to african trypanosome infections
    • Namangala B. Contribution of innate immune responses towards resistance to African trypanosome infections. Scand J Immunol 75: 5-15, 2012.
    • (2012) Scand J Immunol , vol.75 , pp. 5-15
    • Namangala, B.1
  • 60
    • 0027061907 scopus 로고
    • Erythrocyte response to trypanosoma brucei in experimentally infected dogs
    • Omotainse SO and Anosa VO. Erythrocyte response to Trypanosoma brucei in experimentally infected dogs. Rev Elev Med Vet Pays Trop 45: 279-283, 1992.
    • (1992) Rev Elev Med Vet Pays Trop , vol.45 , pp. 279-283
    • Omotainse, S.O.1    Anosa, V.O.2
  • 61
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4: 2411-2423, 1995.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 62
    • 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 glutathioneligated [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
  • 63
    • 79954430645 scopus 로고    scopus 로고
    • Mechanism of glutaredoxin-isu [2fe-2s] cluster exchange
    • Qi W and Cowan JA. Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange. Chem Commun (Camb) 47: 4989-4991, 2011.
    • (2011) Chem Commun (Camb) , vol.47 , pp. 4989-4991
    • Qi, W.1    Cowan, J.A.2
  • 64
    • 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
  • 67
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of ironsulfur enzymes
    • 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: 1109-11721, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 1109-11721
    • Rodri'guez-Manzaneque, M.T.1    Tamarit, J.2    Bellí, G.3    Ros, J.4    Herrero, E.5
  • 68
    • 79960718370 scopus 로고    scopus 로고
    • Lipoamide dehydrogenase is essential for both bloodstream and procyclic trypanosoma brucei
    • Roldán A, Comini MA, Crispo M, and Krauth-Siegel RL. Lipoamide dehydrogenase is essential for both bloodstream and procyclic Trypanosoma brucei. Mol Microbiol 81: 623-639, 2011.
    • (2011) Mol Microbiol , vol.81 , pp. 623-639
    • Roldán, A.1    Comini, M.A.2    Crispo, M.3    Krauth-Siegel, R.L.4
  • 72
    • 84873331479 scopus 로고    scopus 로고
    • Determination of acidity and nucleophilicity in thiols by reaction with monobromobimane and fluorescence detection
    • 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 435:74-82, 2013.
    • (2013) Anal Biochem , vol.435 , pp. 74-82
    • Sardi, F.1    Manta, B.2    Portillo-Ledesma, S.3    Knoops, B.4    Comini, M.A.5    Ferrer-Sueta, G.6
  • 73
    • 77951666856 scopus 로고    scopus 로고
    • Prediction of xaa-pro peptide bond conformation from sequence and chemical shifts
    • Shen Y and Bax A. Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts. J Biomol NMR 46: 199-204, 2010.
    • (2010) J Biomol NMR , vol.46 , pp. 199-204
    • Shen, Y.1    Bax, A.2
  • 74
    • 77950859447 scopus 로고    scopus 로고
    • Scrutinizing the mechanisms underlying the induction of anemia of inflammation through gpimediated modulation of macrophage activation in a model of african trypanosomiasis
    • Stijlemans B, Vankrunkelsven A, Brys L, Raes G, Magez S, and De Baetselier P. Scrutinizing the mechanisms underlying the induction of anemia of inflammation through GPImediated modulation of macrophage activation in a model of African trypanosomiasis. Microbes Infect 12: 389-399, 2010.
    • (2010) Microbes Infect , vol.12 , pp. 389-399
    • Stijlemans, B.1    Vankrunkelsven, A.2    Brys, L.3    Raes, G.4    Magez, S.5    De Baetselier, P.6
  • 78
    • 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.