메뉴 건너뛰기




Volumn 1853, Issue 6, 2015, Pages 1513-1527

The roles of glutaredoxins ligating Fe-S clusters: Sensing, transfer or repair functions?

Author keywords

Glutaredoxins; Iron sensing; Iron sulfur center; Reductases

Indexed keywords

GLUTAREDOXIN; GLUTATHIONE; IRON SULFUR PROTEIN; PROTEIN BINDING;

EID: 84939938222     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.09.018     Document Type: Review
Times cited : (88)

References (154)
  • 1
    • 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. U. S. A. 1976, 73:2275-2279.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 2
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • Laurent T.C., Moore E.C., Reichard P. Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. J. Biol. Chem. 1964, 239:3436-3444.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 4
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • Johansson C., Lillig C.H., Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J. Biol. Chem. 2004, 279:7537-7543.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 5
    • 44049097906 scopus 로고    scopus 로고
    • Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin
    • Zaffagnini M., Michelet L., Massot V., Trost P., Lemaire S.D. Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin. J. Biol. Chem. 2008, 283:8868-8876.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8868-8876
    • Zaffagnini, M.1    Michelet, L.2    Massot, V.3    Trost, P.4    Lemaire, S.D.5
  • 6
    • 0346366724 scopus 로고    scopus 로고
    • Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction
    • Gelhaye E., Rouhier N., Jacquot J.P. Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction. FEBS Lett. 2003, 555:443-448.
    • (2003) FEBS Lett. , vol.555 , pp. 443-448
    • Gelhaye, E.1    Rouhier, N.2    Jacquot, J.P.3
  • 8
    • 84902294371 scopus 로고    scopus 로고
    • Glutaredoxin 2 reduces both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal
    • Zhang H., Du Y., Zhang X., Lu J., Holmgren A. Glutaredoxin 2 reduces both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal. Antioxid. Redox Signal. 2014, 21:669-681.
    • (2014) Antioxid. Redox Signal. , vol.21 , pp. 669-681
    • Zhang, H.1    Du, Y.2    Zhang, X.3    Lu, J.4    Holmgren, A.5
  • 12
    • 0040932016 scopus 로고    scopus 로고
    • Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae
    • Rodriguez-Manzaneque M.T., Ros J., Cabiscol E., Sorribas A., Herrero E. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol. Cell. Biol. 1999, 19:8180-8190.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8180-8190
    • Rodriguez-Manzaneque, M.T.1    Ros, J.2    Cabiscol, E.3    Sorribas, A.4    Herrero, E.5
  • 13
    • 67650999518 scopus 로고    scopus 로고
    • Evolution and diversity of glutaredoxins in photosynthetic organisms
    • Couturier J., Jacquot J.P., Rouhier N. Evolution and diversity of glutaredoxins in photosynthetic organisms. Cell. Mol. Life Sci. 2009, 66:2539-2557.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2539-2557
    • Couturier, J.1    Jacquot, J.P.2    Rouhier, N.3
  • 14
    • 65549160983 scopus 로고    scopus 로고
    • Evolution based on domain combinations: the case of glutaredoxins
    • Alves R., Vilaprinyo E., Sorribas A., Herrero E. Evolution based on domain combinations: the case of glutaredoxins. BMC Evol. Biol. 2009, 9:66.
    • (2009) BMC Evol. Biol. , vol.9 , pp. 66
    • Alves, R.1    Vilaprinyo, E.2    Sorribas, A.3    Herrero, E.4
  • 15
    • 42949085825 scopus 로고    scopus 로고
    • The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation
    • Rouhier N., Lemaire S.D., Jacquot J.P. The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation. Annu. Rev. Plant Biol. 2008, 59:143-166.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 143-166
    • Rouhier, N.1    Lemaire, S.D.2    Jacquot, J.P.3
  • 16
    • 34250731291 scopus 로고    scopus 로고
    • Monothiol glutaredoxins: a common domain for multiple functions
    • Herrero E., de la Torre-Ruiz M.A. Monothiol glutaredoxins: a common domain for multiple functions. Cell. Mol. Life Sci. 2007, 64:1518-1530.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1518-1530
    • Herrero, E.1    de la Torre-Ruiz, M.A.2
  • 17
    • 84901010141 scopus 로고    scopus 로고
    • Toward a refined classification of class I dithiol glutaredoxins from poplar: biochemical basis for the definition of two subclasses
    • Couturier J., Jacquot J.P., Rouhier N. Toward a refined classification of class I dithiol glutaredoxins from poplar: biochemical basis for the definition of two subclasses. Front. Plant Sci. 2013, 4:518.
    • (2013) Front. Plant Sci. , vol.4 , pp. 518
    • Couturier, J.1    Jacquot, J.P.2    Rouhier, N.3
  • 18
    • 84867730651 scopus 로고    scopus 로고
    • Protein-thiol oxidation and cell death: regulatory role of glutaredoxins
    • Allen E.M., Mieyal J.J. Protein-thiol oxidation and cell death: regulatory role of glutaredoxins. Antioxid. Redox Signal. 2012, 17:1748-1763.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1748-1763
    • Allen, E.M.1    Mieyal, J.J.2
  • 19
    • 84881422708 scopus 로고    scopus 로고
    • Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes
    • Comini M.A., Krauth-Siegel R.L., Bellanda M. Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes. Antioxid. Redox Signal. 2013, 19:708-722.
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 708-722
    • Comini, M.A.1    Krauth-Siegel, R.L.2    Bellanda, M.3
  • 20
    • 84876917760 scopus 로고    scopus 로고
    • Thioredoxins, glutaredoxins, and peroxiredoxins-molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling
    • Hanschmann E.M., Godoy J.R., Berndt C., Hudemann C., Lillig C.H. Thioredoxins, glutaredoxins, and peroxiredoxins-molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling. Antioxid. Redox Signal. 2013, 19:1539-1605.
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 1539-1605
    • Hanschmann, E.M.1    Godoy, J.R.2    Berndt, C.3    Hudemann, C.4    Lillig, C.H.5
  • 21
    • 84865411350 scopus 로고    scopus 로고
    • Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance
    • Meyer Y., Belin C., Delorme-Hinoux V., Reichheld J.P., Riondet C. Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance. Antioxid. Redox Signal. 2012, 17:1124-1160.
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1124-1160
    • Meyer, Y.1    Belin, C.2    Delorme-Hinoux, V.3    Reichheld, J.P.4    Riondet, C.5
  • 22
    • 77954722636 scopus 로고    scopus 로고
    • Plant glutaredoxins: pivotal players in redox biology and iron-sulphur centre assembly
    • Rouhier N. Plant glutaredoxins: pivotal players in redox biology and iron-sulphur centre assembly. New Phytol. 2010, 186:365-372.
    • (2010) New Phytol. , vol.186 , pp. 365-372
    • Rouhier, N.1
  • 24
    • 33745614344 scopus 로고    scopus 로고
    • Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site
    • Feng Y., Zhong N., Rouhier N., Hase T., Kusunoki M., Jacquot J.P., Jin C., Xia B. Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site. Biochemistry 2006, 45:7998-8008.
    • (2006) Biochemistry , vol.45 , 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
    • 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
    • Johansson C., Kavanagh K.L., Gileadi O., Oppermann U. Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria. J. Biol. Chem. 2007, 282:3077-3082.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3077-3082
    • Johansson, C.1    Kavanagh, K.L.2    Gileadi, O.3    Oppermann, U.4
  • 29
    • 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
    • Mesecke N., Mittler S., Eckers E., Herrmann J.M., Deponte M. Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron-sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins. Biochemistry 2008, 47:1452-1463.
    • (2008) Biochemistry , vol.47 , pp. 1452-1463
    • Mesecke, N.1    Mittler, S.2    Eckers, E.3    Herrmann, J.M.4    Deponte, M.5
  • 32
    • 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., Krauth-Siegel R.L. The dithiol glutaredoxins of African trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism. J. Biol. Chem. 2010, 285:35224-35237.
    • (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
  • 35
    • 84866153655 scopus 로고    scopus 로고
    • Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin
    • Wang L., Ouyang B., Li Y., Feng Y., Jacquot J.P., Rouhier N., Xia B. Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin. Protein Cell 2012, 3:714-721.
    • (2012) Protein Cell , vol.3 , pp. 714-721
    • Wang, L.1    Ouyang, B.2    Li, Y.3    Feng, Y.4    Jacquot, J.P.5    Rouhier, N.6    Xia, B.7
  • 37
    • 79954430645 scopus 로고    scopus 로고
    • Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange
    • Qi W., Cowan J.A. Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange. Chem. Commun. (Camb.) 2011, 47:4989-4991.
    • (2011) Chem. Commun. (Camb.) , vol.47 , pp. 4989-4991
    • Qi, W.1    Cowan, J.A.2
  • 38
    • 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 D.W., Kaur D., Chinta S.J., Rajagopalan S., Andersen J.K. 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. 2009, 11:2083-2094.
    • (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
  • 39
    • 55549131538 scopus 로고    scopus 로고
    • Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes
    • Comini M.A., Rettig J., Dirdjaja N., Hanschmann E.M., Berndt C., Krauth-Siegel R.L. Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes. J. Biol. Chem. 2008, 283:27785-27798.
    • (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
  • 40
  • 41
    • 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
    • Picciocchi A., Saguez C., Boussac A., Cassier-Chauvat C., 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 2007, 46:15018-15026.
    • (2007) Biochemistry , vol.46 , pp. 15018-15026
    • Picciocchi, A.1    Saguez, C.2    Boussac, A.3    Cassier-Chauvat, C.4    Chauvat, F.5
  • 45
    • 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 R.L., Bellanda M., Comini M.A. 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. 2013, 19:665-682.
    • (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
  • 46
    • 84885646670 scopus 로고    scopus 로고
    • Monothiol glutaredoxins can bind linear [Fe3S4]+and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications
    • Zhang B., Bandyopadhyay S., Shakamuri P., Naik S.G., Huynh B.H., Couturier J., Rouhier N., Johnson M.K. Monothiol glutaredoxins can bind linear [Fe3S4]+and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications. J. Am. Chem. Soc. 2013, 135:15153-15164.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 15153-15164
    • Zhang, B.1    Bandyopadhyay, S.2    Shakamuri, P.3    Naik, S.G.4    Huynh, B.H.5    Couturier, J.6    Rouhier, N.7    Johnson, M.K.8
  • 48
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque M.T., Tamarit J., Belli G., Ros J., Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 2002, 13:1109-1121.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 49
    • 0037053377 scopus 로고    scopus 로고
    • Regulation of protein S-thiolation by glutaredoxin 5 in the yeast Saccharomyces cerevisiae
    • Shenton D., Perrone G., Quinn K.A., Dawes I.W., Grant C.M. Regulation of protein S-thiolation by glutaredoxin 5 in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 2002, 277:16853-16859.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16853-16859
    • Shenton, D.1    Perrone, G.2    Quinn, K.A.3    Dawes, I.W.4    Grant, C.M.5
  • 50
    • 0038491193 scopus 로고    scopus 로고
    • Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin
    • Tamarit J., Belli G., Cabiscol E., Herrero E., Ros J. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J. Biol. Chem. 2003, 278:25745-25751.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25745-25751
    • Tamarit, J.1    Belli, G.2    Cabiscol, E.3    Herrero, E.4    Ros, J.5
  • 51
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Mühlenhoff U., Gerber J., Richhardt N., Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 2003, 22:4815-4825.
    • (2003) EMBO J. , vol.22 , pp. 4815-4825
    • Mühlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 58
    • 84878638881 scopus 로고    scopus 로고
    • [2Fe-2S]-ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin
    • Kim J.H., Frederick R.O., Reinen N.M., Troupis A.T., Markley J.L. [2Fe-2S]-ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin. J. Am. Chem. Soc. 2013, 135:8117-8120.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8117-8120
    • Kim, J.H.1    Frederick, R.O.2    Reinen, N.M.3    Troupis, A.T.4    Markley, J.L.5
  • 60
    • 80955125480 scopus 로고    scopus 로고
    • Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins
    • Mühlenhoff U., Richter N., Pines O., Pierik A.J., Lill R. Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins. J. Biol. Chem. 2011, 286:41205-41216.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41205-41216
    • Mühlenhoff, U.1    Richter, N.2    Pines, O.3    Pierik, A.J.4    Lill, R.5
  • 62
    • 84879562737 scopus 로고    scopus 로고
    • The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation
    • Uzarska M.A., Dutkiewicz R., Freibert S.A., Lill R., Muhlenhoff U. The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation. Mol. Biol. Cell 2013, 24:1830-1841.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1830-1841
    • Uzarska, M.A.1    Dutkiewicz, R.2    Freibert, S.A.3    Lill, R.4    Muhlenhoff, U.5
  • 63
    • 84866513533 scopus 로고    scopus 로고
    • Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins
    • Shakamuri P., Zhang B., Johnson M.K. Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins. J. Am. Chem. Soc. 2012, 134:15213-15216.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15213-15216
    • Shakamuri, P.1    Zhang, B.2    Johnson, M.K.3
  • 65
    • 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., 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. 2010, 392:467-472.
    • (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
  • 66
  • 68
    • 40749086415 scopus 로고    scopus 로고
    • Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes
    • Gelling C., Dawes I.W., Richhardt N., Lill R., Muhlenhoff U. Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes. Mol. Cell. Biol. 2008, 28:1851-1861.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1851-1861
    • Gelling, C.1    Dawes, I.W.2    Richhardt, N.3    Lill, R.4    Muhlenhoff, U.5
  • 69
    • 84897099325 scopus 로고    scopus 로고
    • Mammalian Fe-S cluster biogenesis and its implication in disease
    • Beilschmidt L.K., Puccio H.M. Mammalian Fe-S cluster biogenesis and its implication in disease. Biochimie 2014, 100:48-60.
    • (2014) Biochimie , vol.100 , pp. 48-60
    • Beilschmidt, L.K.1    Puccio, H.M.2
  • 70
    • 15444371876 scopus 로고    scopus 로고
    • Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis
    • Rutherford J.C., Ojeda L., Balk J., Muhlenhoff U., Lill R., Winge D.R. Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis. J. Biol. Chem. 2005, 280:10135-10140.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10135-10140
    • Rutherford, J.C.1    Ojeda, L.2    Balk, J.3    Muhlenhoff, U.4    Lill, R.5    Winge, D.R.6
  • 71
    • 84896803955 scopus 로고    scopus 로고
    • Structural basis for heavy metal detoxification by an Atm1-type ABC exporter
    • Lee J.Y., Yang J.G., Zhitnitsky D., Lewinson O., Rees D.C. Structural basis for heavy metal detoxification by an Atm1-type ABC exporter. Science 2014, 343:1133-1136.
    • (2014) Science , vol.343 , pp. 1133-1136
    • Lee, J.Y.1    Yang, J.G.2    Zhitnitsky, D.3    Lewinson, O.4    Rees, D.C.5
  • 72
    • 84896278245 scopus 로고    scopus 로고
    • A structural model for glutathione-complexed iron-sulfur cluster as a substrate for ABCB7-type transporters
    • Qi W., Li J., Cowan J.A. A structural model for glutathione-complexed iron-sulfur cluster as a substrate for ABCB7-type transporters. Chem. Commun. (Camb.) 2014, 50:3795-3798.
    • (2014) Chem. Commun. (Camb.) , vol.50 , pp. 3795-3798
    • Qi, W.1    Li, J.2    Cowan, J.A.3
  • 73
    • 84896800834 scopus 로고    scopus 로고
    • Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1
    • Srinivasan V., Pierik A.J., Lill R. Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1. Science 2014, 343:1137-1140.
    • (2014) Science , vol.343 , pp. 1137-1140
    • Srinivasan, V.1    Pierik, A.J.2    Lill, R.3
  • 74
    • 79954416607 scopus 로고    scopus 로고
    • Ancient and essential: the assembly of iron-sulfur clusters in plants
    • Balk J., Pilon M. Ancient and essential: the assembly of iron-sulfur clusters in plants. Trends Plant Sci. 2011, 16:218-226.
    • (2011) Trends Plant Sci. , vol.16 , pp. 218-226
    • Balk, J.1    Pilon, M.2
  • 76
    • 84891774934 scopus 로고    scopus 로고
    • The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions
    • Couturier J., Touraine B., Briat J.F., Gaymard F., Rouhier N. The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions. Front. Plant Sci. 2013, 4:259.
    • (2013) Front. Plant Sci. , vol.4 , pp. 259
    • Couturier, J.1    Touraine, B.2    Briat, J.F.3    Gaymard, F.4    Rouhier, N.5
  • 77
    • 33748747966 scopus 로고    scopus 로고
    • AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage
    • Cheng N.H., Liu J.Z., Brock A., Nelson R.S., Hirschi K.D. AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage. J. Biol. Chem. 2006, 281:26280-26288.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26280-26288
    • Cheng, N.H.1    Liu, J.Z.2    Brock, A.3    Nelson, R.S.4    Hirschi, K.D.5
  • 79
    • 84884852556 scopus 로고    scopus 로고
    • Arabidopsis thaliana Nfu2 accommodates [2Fe-2S] or [4Fe-4S] clusters and is competent for in vitro maturation of chloroplast [2Fe-2S] and [4Fe-4S] cluster-containing proteins
    • Gao H., Subramanian S., Couturier J., Naik S.G., Kim S.K., Leustek T., Knaff D.B., Wu H.C., Vignols F., Huynh B.H., Rouhier N., Johnson M.K. Arabidopsis thaliana Nfu2 accommodates [2Fe-2S] or [4Fe-4S] clusters and is competent for in vitro maturation of chloroplast [2Fe-2S] and [4Fe-4S] cluster-containing proteins. Biochemistry 2013, 52:6633-6645.
    • (2013) Biochemistry , vol.52 , pp. 6633-6645
    • Gao, H.1    Subramanian, S.2    Couturier, J.3    Naik, S.G.4    Kim, S.K.5    Leustek, T.6    Knaff, D.B.7    Wu, H.C.8    Vignols, F.9    Huynh, B.H.10    Rouhier, N.11    Johnson, M.K.12
  • 80
    • 80054720193 scopus 로고    scopus 로고
    • The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes
    • Yeung N., Gold B., Liu N.L., Prathapam R., Sterling H.J., Willams E.R., Butland G. The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes. Biochemistry 2011, 50:8957-8969.
    • (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
  • 82
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten F.W., Djaman O., Storz G. A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol. Microbiol. 2004, 52:861-872.
    • (2004) Mol. Microbiol. , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 83
    • 84877908405 scopus 로고    scopus 로고
    • Physical and functional interactions of a monothiol glutaredoxin and an iron sulfur cluster carrier protein with the sulfur-donating radical S-adenosyl-L-methionine enzyme MiaB
    • Boutigny S., Saini A., Baidoo E.E., Yeung N., Keasling J.D., Butland G. Physical and functional interactions of a monothiol glutaredoxin and an iron sulfur cluster carrier protein with the sulfur-donating radical S-adenosyl-L-methionine enzyme MiaB. J. Biol. Chem. 2013, 288:14200-14211.
    • (2013) J. Biol. Chem. , vol.288 , pp. 14200-14211
    • Boutigny, S.1    Saini, A.2    Baidoo, E.E.3    Yeung, N.4    Keasling, J.D.5    Butland, G.6
  • 84
    • 78649843329 scopus 로고    scopus 로고
    • An in vivo method for characterization of protein interactions within sulfur trafficking systems of E. coli
    • Bolstad H.M., Wood M.J. An in vivo method for characterization of protein interactions within sulfur trafficking systems of E. coli. J. Proteome Res. 2010, 9:6740-6751.
    • (2010) J. Proteome Res. , vol.9 , pp. 6740-6751
    • Bolstad, H.M.1    Wood, M.J.2
  • 85
    • 33644511398 scopus 로고    scopus 로고
    • AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis
    • Xu X.M., Moller S.G. AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis. EMBO J. 2006, 25:900-909.
    • (2006) EMBO J. , vol.25 , pp. 900-909
    • Xu, X.M.1    Moller, S.G.2
  • 86
    • 33646822978 scopus 로고    scopus 로고
    • CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation
    • Ye H., Abdel-Ghany S.E., Anderson T.D., Pilon-Smits E.A., Pilon M. CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation. J. Biol. Chem. 2006, 281:8958-8969.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8958-8969
    • Ye, H.1    Abdel-Ghany, S.E.2    Anderson, T.D.3    Pilon-Smits, E.A.4    Pilon, M.5
  • 88
    • 84866011930 scopus 로고    scopus 로고
    • Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes
    • Lanz N.D., Booker S.J. Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes. Biochim. Biophys. Acta 2012, 1824:1196-1212.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1196-1212
    • Lanz, N.D.1    Booker, S.J.2
  • 89
    • 0034326925 scopus 로고    scopus 로고
    • PICOT-HD: a highly conserved protein domain that is often associated with thioredoxin and glutaredoxin modules
    • Isakov N., Witte S., Altman A. PICOT-HD: a highly conserved protein domain that is often associated with thioredoxin and glutaredoxin modules. Trends Biochem. Sci. 2000, 25:537-539.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 537-539
    • Isakov, N.1    Witte, S.2    Altman, A.3
  • 90
    • 0035701961 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of PICOT and its translocation to the nucleus in response of human T cells to oxidative stress
    • Babichev Y., Isakov N. Tyrosine phosphorylation of PICOT and its translocation to the nucleus in response of human T cells to oxidative stress. Adv. Exp. Med. Biol. 2001, 495:41-45.
    • (2001) Adv. Exp. Med. Biol. , vol.495 , pp. 41-45
    • Babichev, Y.1    Isakov, N.2
  • 91
    • 79958013653 scopus 로고    scopus 로고
    • Arabidopsis monothiol glutaredoxin, AtGRXS17, is critical for temperature-dependent postembryonic growth and development via modulating auxin response
    • Cheng N.H., Liu J.Z., Liu X., Wu Q., Thompson S.M., Lin J., Chang J., Whitham S.A., Park S., Cohen J.D., Hirschi K.D. Arabidopsis monothiol glutaredoxin, AtGRXS17, is critical for temperature-dependent postembryonic growth and development via modulating auxin response. J. Biol. Chem. 2011, 286:20398-20406.
    • (2011) J. Biol. Chem. , vol.286 , pp. 20398-20406
    • Cheng, N.H.1    Liu, J.Z.2    Liu, X.3    Wu, Q.4    Thompson, S.M.5    Lin, J.6    Chang, J.7    Whitham, S.A.8    Park, S.9    Cohen, J.D.10    Hirschi, K.D.11
  • 92
    • 0942268722 scopus 로고    scopus 로고
    • Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin
    • Lopreiato R., Facchin S., Sartori G., Arrigoni G., Casonato S., Ruzzene M., Pinna L.A., Carignani G. Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin. Biochem. J. 2004, 377:395-405.
    • (2004) Biochem. J. , vol.377 , pp. 395-405
    • Lopreiato, R.1    Facchin, S.2    Sartori, G.3    Arrigoni, G.4    Casonato, S.5    Ruzzene, M.6    Pinna, L.A.7    Carignani, G.8
  • 93
    • 10644242480 scopus 로고    scopus 로고
    • Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins
    • Molina M.M., Belli G., de la Torre M.A., Rodriguez-Manzaneque M.T., Herrero E. Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins. J. Biol. Chem. 2004, 279:51923-51930.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51923-51930
    • Molina, M.M.1    Belli, G.2    de la Torre, M.A.3    Rodriguez-Manzaneque, M.T.4    Herrero, E.5
  • 95
    • 79956029734 scopus 로고    scopus 로고
    • Grx4 monothiol glutaredoxin is required for iron limitation-dependent inhibition of Fep1
    • Jbel M., Mercier A., Labbe S. Grx4 monothiol glutaredoxin is required for iron limitation-dependent inhibition of Fep1. Eukaryot. Cell 2011, 10:629-645.
    • (2011) Eukaryot. Cell , vol.10 , pp. 629-645
    • Jbel, M.1    Mercier, A.2    Labbe, S.3
  • 96
    • 84861714092 scopus 로고    scopus 로고
    • The monothiol glutaredoxin Grx4 exerts an iron-dependent inhibitory effect on Php4 function
    • Vachon P., Mercier A., Jbel M., Labbe S. The monothiol glutaredoxin Grx4 exerts an iron-dependent inhibitory effect on Php4 function. Eukaryot. Cell 2012, 11:806-819.
    • (2012) Eukaryot. Cell , vol.11 , pp. 806-819
    • Vachon, P.1    Mercier, A.2    Jbel, M.3    Labbe, S.4
  • 97
    • 78650320095 scopus 로고    scopus 로고
    • Glutaredoxins Grx4 and Grx3 of Saccharomyces cerevisiae play a role in actin dynamics through their Trx domains, which contributes to oxidative stress resistance
    • Pujol-Carrion N., de la Torre-Ruiz M.A. Glutaredoxins Grx4 and Grx3 of Saccharomyces cerevisiae play a role in actin dynamics through their Trx domains, which contributes to oxidative stress resistance. Appl. Environ. Microbiol. 2010, 76:7826-7835.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 7826-7835
    • Pujol-Carrion, N.1    de la Torre-Ruiz, M.A.2
  • 98
    • 0034695550 scopus 로고    scopus 로고
    • Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain
    • Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A. Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain. J. Biol. Chem. 2000, 275:1902-1909.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1902-1909
    • Witte, S.1    Villalba, M.2    Bi, K.3    Liu, Y.4    Isakov, N.5    Altman, A.6
  • 99
    • 34347209447 scopus 로고    scopus 로고
    • NGF-mediated transcriptional targets of p53 in PC12 neuronal differentiation
    • Brynczka C., Labhart P., Merrick B.A. NGF-mediated transcriptional targets of p53 in PC12 neuronal differentiation. BMC Genomics 2007, 8:139.
    • (2007) BMC Genomics , vol.8 , pp. 139
    • Brynczka, C.1    Labhart, P.2    Merrick, B.A.3
  • 102
    • 79959944018 scopus 로고    scopus 로고
    • A mammalian monothiol glutaredoxin, Grx3, is critical for cell cycle progression during embryogenesis
    • Cheng N.H., Zhang W., Chen W.Q., Jin J., Cui X., Butte N.F., Chan L., Hirschi K.D. A mammalian monothiol glutaredoxin, Grx3, is critical for cell cycle progression during embryogenesis. FEBS J. 2011, 278:2525-2539.
    • (2011) FEBS J. , vol.278 , pp. 2525-2539
    • Cheng, N.H.1    Zhang, W.2    Chen, W.Q.3    Jin, J.4    Cui, X.5    Butte, N.F.6    Chan, L.7    Hirschi, K.D.8
  • 105
    • 82355184470 scopus 로고    scopus 로고
    • Investigation of in vivo diferric tyrosyl radical formation in Saccharomyces cerevisiae Rnr2 protein: requirement of Rnr4 and contribution of Grx3/4 AND Dre2 proteins
    • Zhang Y., Liu L., Wu X., An X., Stubbe J., Huang M. Investigation of in vivo diferric tyrosyl radical formation in Saccharomyces cerevisiae Rnr2 protein: requirement of Rnr4 and contribution of Grx3/4 AND Dre2 proteins. J. Biol. Chem. 2011, 286:41499-41509.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41499-41509
    • Zhang, Y.1    Liu, L.2    Wu, X.3    An, X.4    Stubbe, J.5    Huang, M.6
  • 106
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • Lill R., Muhlenhoff U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 2008, 77:669-700.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 109
    • 84888133282 scopus 로고    scopus 로고
    • Iron sensing and regulation in Saccharomyces cerevisiae: Ironing out the mechanistic details
    • Outten C.E., Albetel A.N. Iron sensing and regulation in Saccharomyces cerevisiae: Ironing out the mechanistic details. Curr. Opin. Microbiol. 2013, 16:662-668.
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 662-668
    • Outten, C.E.1    Albetel, A.N.2
  • 110
    • 84861203729 scopus 로고    scopus 로고
    • The role of the Yap5 transcription factor in remodeling gene expression in response to Fe bioavailability
    • Pimentel C., Vicente C., Menezes R.A., Caetano S., Carreto L., Rodrigues-Pousada C. The role of the Yap5 transcription factor in remodeling gene expression in response to Fe bioavailability. PLoS One 2012, 7:e37434.
    • (2012) PLoS One , vol.7 , pp. e37434
    • Pimentel, C.1    Vicente, C.2    Menezes, R.A.3    Caetano, S.4    Carreto, L.5    Rodrigues-Pousada, C.6
  • 112
    • 33745872884 scopus 로고    scopus 로고
    • Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae
    • Ojeda L., Keller G., Muhlenhoff U., Rutherford J.C., Lill R., Winge D.R. Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae. J. Biol. Chem. 2006, 281:17661-17669.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17661-17669
    • Ojeda, L.1    Keller, G.2    Muhlenhoff, U.3    Rutherford, J.C.4    Lill, R.5    Winge, D.R.6
  • 113
    • 33751529756 scopus 로고    scopus 로고
    • Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae
    • Pujol-Carrion N., Belli G., Herrero E., Nogues A., de la Torre-Ruiz M.A. Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae. J. Cell Sci. 2006, 119:4554-4564.
    • (2006) J. Cell Sci. , vol.119 , pp. 4554-4564
    • Pujol-Carrion, N.1    Belli, G.2    Herrero, E.3    Nogues, A.4    de la Torre-Ruiz, M.A.5
  • 114
    • 84867415067 scopus 로고    scopus 로고
    • A role for iron-sulfur clusters in the regulation of transcription factor Yap5-dependent high iron transcriptional responses in yeast
    • Li L., Miao R., Bertram S., Jia X., Ward D.M., Kaplan J. A role for iron-sulfur clusters in the regulation of transcription factor Yap5-dependent high iron transcriptional responses in yeast. J. Biol. Chem. 2012, 287:35709-35721.
    • (2012) J. Biol. Chem. , vol.287 , pp. 35709-35721
    • Li, L.1    Miao, R.2    Bertram, S.3    Jia, X.4    Ward, D.M.5    Kaplan, J.6
  • 116
    • 0037126057 scopus 로고    scopus 로고
    • Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: evidence that Yfh1p affects Fe-S cluster synthesis
    • Chen O.S., Hemenway S., Kaplan J. Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: evidence that Yfh1p affects Fe-S cluster synthesis. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:12321-12326.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12321-12326
    • Chen, O.S.1    Hemenway, S.2    Kaplan, J.3
  • 117
    • 84871854500 scopus 로고    scopus 로고
    • Iron-induced dissociation of the Aft1p transcriptional regulator from target gene promoters is an initial event in iron-dependent gene suppression
    • Ueta R., Fujiwara N., Iwai K., Yamaguchi-Iwai Y. Iron-induced dissociation of the Aft1p transcriptional regulator from target gene promoters is an initial event in iron-dependent gene suppression. Mol. Cell. Biol. 2012, 32:4998-5008.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4998-5008
    • Ueta, R.1    Fujiwara, N.2    Iwai, K.3    Yamaguchi-Iwai, Y.4
  • 118
    • 34547763678 scopus 로고    scopus 로고
    • Mechanism underlying the iron-dependent nuclear export of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae
    • Ueta R., Fujiwara N., Iwai K., Yamaguchi-Iwai Y. Mechanism underlying the iron-dependent nuclear export of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae. Mol. Biol. Cell 2007, 18:2980-2990.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2980-2990
    • Ueta, R.1    Fujiwara, N.2    Iwai, K.3    Yamaguchi-Iwai, Y.4
  • 119
    • 0037166279 scopus 로고    scopus 로고
    • Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae
    • Yamaguchi-Iwai Y., Ueta R., Fukunaka A., Sasaki R. Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae. J. Biol. Chem. 2002, 277:18914-18918.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18914-18918
    • Yamaguchi-Iwai, Y.1    Ueta, R.2    Fukunaka, A.3    Sasaki, R.4
  • 120
    • 13744263291 scopus 로고    scopus 로고
    • Genome-wide screen for genes with effects on distinct iron uptake activities in Saccharomyces cerevisiae
    • Lesuisse E., Knight S.A., Courel M., Santos R., Camadro J.M., Dancis A. Genome-wide screen for genes with effects on distinct iron uptake activities in Saccharomyces cerevisiae. Genetics 2005, 169:107-122.
    • (2005) Genetics , vol.169 , pp. 107-122
    • Lesuisse, E.1    Knight, S.A.2    Courel, M.3    Santos, R.4    Camadro, J.M.5    Dancis, A.6
  • 121
    • 78650949287 scopus 로고    scopus 로고
    • Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast
    • Li H., Mapolelo D.T., Dingra N.N., Keller G., Riggs-Gelasco P.J., Winge D.R., Johnson M.K., Outten C.E. Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast. J. Biol. Chem. 2011, 286:867-876.
    • (2011) J. Biol. Chem. , vol.286 , pp. 867-876
    • Li, H.1    Mapolelo, D.T.2    Dingra, N.N.3    Keller, G.4    Riggs-Gelasco, P.J.5    Winge, D.R.6    Johnson, M.K.7    Outten, C.E.8
  • 124
    • 84888138587 scopus 로고    scopus 로고
    • Iron uptake and regulation in Schizosaccharomyces pombe
    • Labbe S., Khan M.G., Jacques J.F. Iron uptake and regulation in Schizosaccharomyces pombe. Curr. Opin. Microbiol. 2013, 16:669-676.
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 669-676
    • Labbe, S.1    Khan, M.G.2    Jacques, J.F.3
  • 125
    • 34248656479 scopus 로고    scopus 로고
    • Iron homeostasis in the fission yeast Schizosaccharomyces pombe
    • Labbe S., Pelletier B., Mercier A. Iron homeostasis in the fission yeast Schizosaccharomyces pombe. Biometals 2007, 20:523-537.
    • (2007) Biometals , vol.20 , pp. 523-537
    • Labbe, S.1    Pelletier, B.2    Mercier, A.3
  • 126
    • 33751174095 scopus 로고    scopus 로고
    • A transcription factor cascade involving Fep1 and the CCAAT-binding factor Php4 regulates gene expression in response to iron deficiency in the fission yeast Schizosaccharomyces pombe
    • Mercier A., Pelletier B., Labbe S. A transcription factor cascade involving Fep1 and the CCAAT-binding factor Php4 regulates gene expression in response to iron deficiency in the fission yeast Schizosaccharomyces pombe. Eukaryot. Cell 2006, 5:1866-1881.
    • (2006) Eukaryot. Cell , vol.5 , pp. 1866-1881
    • Mercier, A.1    Pelletier, B.2    Labbe, S.3
  • 127
    • 40949088915 scopus 로고    scopus 로고
    • Key function for the CCAAT-binding factor Php4 to regulate gene expression in response to iron deficiency in fission yeast
    • Mercier A., Watt S., Bahler J., Labbe S. Key function for the CCAAT-binding factor Php4 to regulate gene expression in response to iron deficiency in fission yeast. Eukaryot. Cell 2008, 7:493-508.
    • (2008) Eukaryot. Cell , vol.7 , pp. 493-508
    • Mercier, A.1    Watt, S.2    Bahler, J.3    Labbe, S.4
  • 128
    • 15744374257 scopus 로고    scopus 로고
    • Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe
    • Chung W.H., Kim K.D., Roe J.H. Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe. Biochem. Biophys. Res. Commun. 2005, 330:604-610.
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 604-610
    • Chung, W.H.1    Kim, K.D.2    Roe, J.H.3
  • 129
    • 79956202651 scopus 로고    scopus 로고
    • Multi-domain CGFS-type glutaredoxin Grx4 regulates iron homeostasis via direct interaction with a repressor Fep1 in fission yeast
    • Kim K.D., Kim H.J., Lee K.C., Roe J.H. Multi-domain CGFS-type glutaredoxin Grx4 regulates iron homeostasis via direct interaction with a repressor Fep1 in fission yeast. Biochem. Biophys. Res. Commun. 2011, 408:609-614.
    • (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
  • 130
    • 67749116417 scopus 로고    scopus 로고
    • Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1
    • Mercier A., Labbe S. Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1. J. Biol. Chem. 2009, 284:20249-20262.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20249-20262
    • Mercier, A.1    Labbe, S.2
  • 131
    • 84902477840 scopus 로고    scopus 로고
    • Fra2 is a co-regulator of fep1 inhibition in response to iron starvation
    • Jacques J.F., Mercier A., Brault A., Mourer T., Labbe S. Fra2 is a co-regulator of fep1 inhibition in response to iron starvation. PLoS One 2014, 9:e98959.
    • (2014) PLoS One , vol.9 , pp. e98959
    • Jacques, J.F.1    Mercier, A.2    Brault, A.3    Mourer, T.4    Labbe, S.5
  • 132
    • 12744251555 scopus 로고    scopus 로고
    • Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin
    • Huynen M.A., Spronk C.A., Gabaldon T., Snel B. Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin. FEBS Lett. 2005, 579:591-596.
    • (2005) FEBS Lett. , vol.579 , pp. 591-596
    • Huynen, M.A.1    Spronk, C.A.2    Gabaldon, T.3    Snel, B.4
  • 133
    • 84857780876 scopus 로고    scopus 로고
    • Evidence for network evolution in an Arabidopsis interactome map
    • Consortium A.I.M. Evidence for network evolution in an Arabidopsis interactome map. Science 2011, 333:601-607.
    • (2011) Science , vol.333 , pp. 601-607
    • Consortium, A.I.M.1
  • 137
    • 0033974688 scopus 로고    scopus 로고
    • Toward a protein-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins
    • Ito T., Tashiro K., Muta S., Ozawa R., Chiba T., Nishizawa M., Yamamoto K., Kuhara S., Sakaki Y. Toward a protein-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:1143-1147.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1143-1147
    • Ito, T.1    Tashiro, K.2    Muta, S.3    Ozawa, R.4    Chiba, T.5    Nishizawa, M.6    Yamamoto, K.7    Kuhara, S.8    Sakaki, Y.9
  • 139
  • 140
    • 84863229142 scopus 로고    scopus 로고
    • Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2
    • Li H., Mapolelo D.T., Randeniya S., Johnson M.K., Outten C.E. Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2. Biochemistry 2012, 51:1687-1696.
    • (2012) Biochemistry , vol.51 , pp. 1687-1696
    • Li, H.1    Mapolelo, D.T.2    Randeniya, S.3    Johnson, M.K.4    Outten, C.E.5
  • 141
    • 84861850380 scopus 로고    scopus 로고
    • Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis
    • Li H., Outten C.E. Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis. Biochemistry 2012, 51:4377-4389.
    • (2012) Biochemistry , vol.51 , pp. 4377-4389
    • Li, H.1    Outten, C.E.2
  • 143
    • 48949106599 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway
    • Izquierdo A., Casas C., Muhlenhoff U., Lillig C.H., Herrero E. Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway. Eukaryot. Cell 2008, 7:1415-1426.
    • (2008) Eukaryot. Cell , vol.7 , pp. 1415-1426
    • Izquierdo, A.1    Casas, C.2    Muhlenhoff, U.3    Lillig, C.H.4    Herrero, E.5
  • 144
    • 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., Herrmann J.M. A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance. Mol. Biol. Cell 2008, 19:2673-2680.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2673-2680
    • Mesecke, N.1    Spang, A.2    Deponte, M.3    Herrmann, J.M.4
  • 145
    • 84899794323 scopus 로고    scopus 로고
    • Zebrafish heart development is regulated via glutaredoxin 2 dependent migration and survival of neural crest cells
    • Berndt C., Poschmann G., Stuhler K., Holmgren A., Brautigam L. Zebrafish heart development is regulated via glutaredoxin 2 dependent migration and survival of neural crest cells. Redox Biol. 2014, 2:673-678.
    • (2014) Redox Biol. , vol.2 , pp. 673-678
    • Berndt, C.1    Poschmann, G.2    Stuhler, K.3    Holmgren, A.4    Brautigam, L.5
  • 148
    • 4444337091 scopus 로고    scopus 로고
    • Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide
    • Lillig C.H., Lonn M.E., Enoksson M., Fernandes A.P., Holmgren A. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:13227-13232.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13227-13232
    • Lillig, C.H.1    Lonn, M.E.2    Enoksson, M.3    Fernandes, A.P.4    Holmgren, A.5
  • 149
    • 80255140367 scopus 로고    scopus 로고
    • Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells
    • Wu H., Lin L., Giblin F., Ho Y.S., Lou M.F. Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells. Free Radic. Biol. Med. 2011, 51:2108-2117.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 2108-2117
    • Wu, H.1    Lin, L.2    Giblin, F.3    Ho, Y.S.4    Lou, M.F.5
  • 150
    • 84855350829 scopus 로고    scopus 로고
    • A dicotyledon-specific glutaredoxin GRXC1 family with dimer-dependent redox regulation is functionally redundant with GRXC2
    • Riondet C., Desouris J.P., Montoya J.G., Chartier Y., Meyer Y., Reichheld J.P. A dicotyledon-specific glutaredoxin GRXC1 family with dimer-dependent redox regulation is functionally redundant with GRXC2. Plant Cell Environ. 2012, 35:360-373.
    • (2012) Plant Cell Environ. , vol.35 , pp. 360-373
    • Riondet, C.1    Desouris, J.P.2    Montoya, J.G.3    Chartier, Y.4    Meyer, Y.5    Reichheld, J.P.6
  • 151
    • 63449137389 scopus 로고    scopus 로고
    • Glutaredoxin 5 regulates osteoblast apoptosis by protecting against oxidative stress
    • Linares G.R., Xing W., Govoni K.E., Chen S.T., Mohan S. Glutaredoxin 5 regulates osteoblast apoptosis by protecting against oxidative stress. Bone 2009, 44:795-804.
    • (2009) Bone , vol.44 , pp. 795-804
    • Linares, G.R.1    Xing, W.2    Govoni, K.E.3    Chen, S.T.4    Mohan, S.5
  • 152
    • 84900844646 scopus 로고    scopus 로고
    • Glutaredoxins are essential for stress adaptation in the cyanobacterium Synechocystis sp. PCC 6803
    • Sanchez-Riego A.M., Lopez-Maury L., Florencio F.J. Glutaredoxins are essential for stress adaptation in the cyanobacterium Synechocystis sp. PCC 6803. Front. Plant Sci. 2013, 4:428.
    • (2013) Front. Plant Sci. , vol.4 , pp. 428
    • Sanchez-Riego, A.M.1    Lopez-Maury, L.2    Florencio, F.J.3
  • 153
    • 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. 2008, 582:848-854.
    • (2008) FEBS Lett. , vol.582 , pp. 848-854
    • Cheng, N.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.