Cited by 464Redox biology and oxidative stressMetalloenzymes and iron-sulfur proteinsMitochondrial Function and Pathology

The DOI matches its Crossref record; 79 of the 79 references it cites were found in a registry or an index.

Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes

Open access

Rodrı́guez-Manzaneque, Marı́a Teresa, Tamarit, Jordi, Bellı́, Gemma, Ros, Joaquim, Herrero, Enrique·2002·Molecular Biology of the Cell

DOI 10.1091/mbc.01-10-0517PMC PMC102255

Open this paper in CoChat — free account Open PDF

Abstract

Yeast cells contain a family of three monothiol glutaredoxins: Grx3, 4, and 5. Absence of Grx5 leads to constitutive oxidative damage, exacerbating that caused by external oxidants. Phenotypic defects associated with the absence of Grx5 are suppressed by overexpression ofSSQ1 and ISA2, two genes involved in the synthesis and assembly of iron/sulfur clusters into proteins. Grx5 localizes at the mitochondrial matrix, like other proteins involved in the synthesis of these clusters, and the mature form lacks the first 29 amino acids of the translation product. Absence of Grx5 causes: 1) iron accumulation in the cell, which in turn could promote oxidative damage, and 2) inactivation of enzymes requiring iron/sulfur clusters for their activity. Reduction of iron levels in grx5 null mutants does not restore the activity of iron/sulfur enzymes, and cell growth defects are not suppressed in anaerobiosis or in the presence of disulfide reductants. Hence, Grx5 forms part of the mitochondrial machinery involved in the synthesis and assembly of iron/sulfur centers.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1091/mbc.01-10-0517

Cites

79 of 79 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Methods in yeast genetics
Sherman, F., Fink, G. R., & Hicks, J. B. (1979) · Cold Spring Harbor Laboratory eBooks · Cited by 7,430
New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
Gietz, R. D., & Sugino, A. (1988) · Gene · doi:10.1016/0378-1119(88)90185-0 · Cited by 2,851
Iron-sulfur clusters: nature's modular, multipurpose structures
Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944
Thioredoxin and Glutaredoxin Systems
Holmgren, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71625-6 · Cited by 1,804
BIOCHEMISTRY OF OXYGEN TOXICITY
Cadenas, E. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.000455 · Cited by 1,113
Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin
Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921
Superoxide accelerates DNA damage by elevating free-iron levels
Keyer, K., & Imlay, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13635 · Cited by 841
Roles of the Glutathione- and Thioredoxin-Dependent Reduction Systems in the Escherichia Coli and Saccharomyces Cerevisiae Responses to Oxidative Stress
Carmel‐Harel, O., & Storz, G. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.439 · Cited by 715
The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699
The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in the Escherichia coliCytoplasm
Prinz, W. A., Åslund, F., Holmgren, A., & Beckwith, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15661 · Cited by 662

Flagged first, then by citations

Show all 78 references

Research works printed but not linked: 2

Gietz R.D., 1988, Gene, 74, 3065
Pon L., 1991, The Molecular and Cellular Biology of the Yeast Saccharomyces, 1, 333

Sorted by citations

Items 101–200 of 463

The crystal structure of human GLRX5: iron–sulfur cluster co-ordination, tetrameric assembly and monomer activity
Johansson, C., Roos, A. K., Montaño, S., Sengupta, R., Filippakopoulos, P., Guo, K., von Delft, F., Holmgren, A., Oppermann, U. C. T., & Kavanagh, K. L. (2010) · Biochemical Journal · doi:10.1042/bj20101286 · Cited by 131
The roles of glutaredoxins ligating Fe–S clusters: Sensing, transfer or repair functions?
Couturier, J., Przybyla‐Toscano, J., Roret, T., Claude Didierjean, B., & Rouhier, N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.018 · Cited by 126
Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells
Philpott, C. C., Ryu, M., Frey, A. G., & Patel, S. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.791962 · Cited by 128
Molecular strategies of microbial iron assimilation: from high-affinity complexes to cofactor assembly systems
Miethke, M. (2012) · Metallomics · doi:10.1039/c2mt20193c · Cited by 126
Protein networks in the maturation of human iron–sulfur proteins
Ciofi‐Baffoni, S., Nasta, V., & Banci, L. (2017) · Metallomics · doi:10.1039/c7mt00269f · Cited by 119
Assembly of Fe/S proteins in bacterial systems
Blanc, B., Gerez, C., & de Choudens, S. O. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.009 · Cited by 123
The LYR Factors SDHAF1 and SDHAF3 Mediate Maturation of the Iron-Sulfur Subunit of Succinate Dehydrogenase
Na, U., Yu, W., Cox, J. E., Bricker, D. K., Brockmann, K., Rutter, J. P., Thummel, C. S., & Winge, D. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.05.014 · Cited by 114
The Yeast Scaffold Proteins Isu1p and Isu2p Are Required inside Mitochondria for Maturation of Cytosolic Fe/S Proteins
Gerber, J., Neumann, K., Prohl, C., Mühlenhoff, U., & Lill, R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.11.4848-4857.2004 · Cited by 120
Multi-tasking: nuclear transcription factors with novel roles in the mitochondria
Szczepanek, K., Lesnefsky, E. J., & Larner, A. C. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.05.001 · Cited by 114
Genome-wide expression analysis suggests glutaredoxin genes response to various stresses in cotton
Malik, W. A., Wang, X., Wang, X., Shu, N., Cui, R., Chen, X., Wang, D., Lu, X., Yin, Z., Wang, J., et al. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.021 · Cited by 111
Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins
Couturier, J., Ströher, E., Albetel, A., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., Tsan, P., Jacquot, J., Johnson, M. K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228726 · Cited by 112
Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation
Haunhorst, P., Hanschmann, E.-M., Bräutigam, L., Stehling, O., Hoffmann, B., Mühlenhoff, U., Lill, R., Berndt, C., & Lillig, C. H. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-09-0648 · Cited by 111
How Escherichia coli and Saccharomyces cerevisiae Build Fe/S Proteins
Barras, F., Loiseau, L., & Py, B. (2005) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(05)50002-x · Cited by 111
Nucleoredoxin, a Novel Thioredoxin Family Member Involved in Cell Growth and Differentiation
Funato, Y., & Miki, H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1550 · Cited by 117
A Proposed Role for the Azotobacter vinelandii NfuA Protein as an Intermediate Iron-Sulfur Cluster Carrier
Bandyopadhyay, S., Naik, S., O’Carroll, I. P., Huynh, B.-H., Dean, D. R., Johnson, M. K., & Santos, P. C. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709161200 · Cited by 111
Monothiol glutaredoxins and A-type proteins: partners in Fe–S cluster trafficking
Mapolelo, D. T., Zhang, B., Randeniya, S., Albetel, A., Li, H., Couturier, J., Outten, C. E., Rouhier, N., & Johnson, M. K. (2012) · Dalton Transactions · doi:10.1039/c2dt32263c · Cited by 110
Mitochondrial [4Fe-4S] protein assembly involves reductive [2Fe-2S] cluster fusion on ISCA1–ISCA2 by electron flow from ferredoxin FDX2
Weiler, B. D., Brück, M.-C., Kothe, I., Bill, E., Lill, R., & Mühlenhoff, U. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003982117 · Cited by 110
The mitochondrial monothiol glutaredoxin S15 is essential for iron-sulfur protein maturation in Arabidopsis thaliana
Moseler, A., Aller, I., Wagner, S., Nietzel, T., Przybyla‐Toscano, J., Mühlenhoff, U., Lill, R., Berndt, C., Rouhier, N., Schwarzländer, M., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510835112 · Cited by 108
The Thioredoxin-Thioredoxin Reductase System Can Function in Vivo as an Alternative System to Reduce Oxidized Glutathione in Saccharomyces cerevisiae
Tan, S., Greetham, D., Raeth, S., Grant, C. M., Dawes, I. W., & Perrone, G. G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.062844 · Cited by 106
Human Glutaredoxin 3 Forms [2Fe-2S]-Bridged Complexes with Human BolA2
Li, H., Mapolelo, D. T., Randeniya, S., Johnson, M. K., & Outten, C. E. (2012) · Biochemistry · doi:10.1021/bi2019089 · Cited by 106
Mitochondrial Mayhem: The Mitochondrion as a Modulator of Iron Metabolism and Its Role in Disease
Huang, M. L.-H., Lane, D. J. R., & Richardson, D. R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3921 · Cited by 103
Metal Ion availability in mitochondria
Pierrel, F., Cobine, P. A., & Winge, D. R. (2007) · BioMetals · doi:10.1007/s10534-006-9052-9 · Cited by 105
Iron–Sulfur Clusters: Biogenesis, Molecular Mechanisms, and Their Functional Significance
Xu, X. M., & Møller, S. G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3259 · Cited by 102
Bacterial Approaches for Assembling Iron-Sulfur Proteins
Esquilin-Lebron, K., Dubrac, S., Barras, F., & Boyd, J. M. (2021) · mBio · doi:10.1128/mbio.02425-21 · Cited by 106
How Does Iron–Sulfur Cluster Coordination Regulate the Activity of Human Glutaredoxin 2?
Berndt, C., Hudemann, C., Hanschmann, E.-M., Axelsson, R., Holmgren, A., & Lillig, C. H. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.9.151 · Cited by 101
Nuclear Monothiol Glutaredoxins of Saccharomyces cerevisiae Can Function as Mitochondrial Glutaredoxins
Molina‐Navarro, M. M., Bellı́, G., de la Torre-Ruiz, M. Á., Rodríguez‐Manzaneque, M. T., & Herrero, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410219200 · Cited by 100
Self-citation
Novel Antioxidant Role of Alcohol Dehydrogenase E from Escherichia coli
Echave, P., Tamarit, J., Cabiscol, E., & Ros, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304351200 · Cited by 98
Self-citation
Overlapping Roles of the Cytoplasmic and Mitochondrial Redox Regulatory Systems in the Yeast Saccharomyces cerevisiae
Trotter, E., & Grant, C. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.2.392-400.2005 · Cited by 100
Evolutionary conservation and in vitro reconstitution of microsporidian iron–sulfur cluster biosynthesis
Freibert, S., Goldberg, A. V., Hacker, C., Molik, S., Dean, P., Williams, T. A., Nakjang, S., Long, S., Sendra, K. M., Bill, E., et al. (2017) · Nature Communications · doi:10.1038/ncomms13932 · Cited by 98
Oxidative stress responses and lipid peroxidation damage are induced during dehydration in the production of dry active wine yeasts
Garré, E., Raginel, F., Palacios, A., Julien, A., & Matallana, E. (2009) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2009.10.018 · Cited by 97
Reactive oxygen species production induced by ethanol inSaccharomyces cerevisiaeincreases because of a dysfunctional mitochondrial iron-sulfur cluster assembly system
Pérez‐Gallardo, R. V., Sánchez‐Briones, L. A., Díaz-Pérez, A. L., Gutiérrez, S., Rodríguez‐Zavala, J. S., & Campos‐García, J. (2013) · FEMS Yeast Research · doi:10.1111/1567-1364.12090 · Cited by 97
Redox Pathways of the Mitochondrion
Koehler, C. M., Beverly, K. N., & Leverich, E. P. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.813 · Cited by 96
Monothiol Glutaredoxins Function in Storing and Transporting [Fe2S2] Clusters Assembled on IscU Scaffold Proteins
Shakamuri, P., Zhang, B., & Johnson, M. K. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306061x · Cited by 95
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. H., & Pilon, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512737200 · Cited by 93
Special delivery: distributing iron in the cytosol of mammalian cells
Philpott, C. C., & Ryu, M. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00173 · Cited by 96
Mechanism Underlying the Iron-dependent Nuclear Export of the Iron-responsive Transcription Factor Aft1p inSaccharomyces cerevisiae
Ueta, R., Fujiwara, N., Iwaï, K., & Yamaguchi‐Iwai, Y. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-11-1054 · Cited by 90
Arabidopsis Glutaredoxin S17 and Its Partner, the Nuclear Factor Y Subunit C11/Negative Cofactor 2α, Contribute to Maintenance of the Shoot Apical Meristem under Long-Day Photoperiod
Knuesting, J., Riondet, C., María, C., Kruse, I., Bécuwe, N., König, N., Berndt, C., Tourrette, S., Guilleminot, J., Herrero, E., et al. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.00049 · Cited by 88
Self-citation
Monothiol Glutaredoxin–BolA Interactions: Redox Control of Arabidopsis thaliana BolA2 and SufE1
Couturier, J., Wu, H.-C., Dhalleine, T., Pégeot, H., Sudre, D., Gualberto, J. M., Jacquot, J., Gaymard, F., Vignols, F., & Rouhier, N. (2013) · Molecular Plant · doi:10.1093/mp/sst156 · Cited by 95
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, M. M., Casas, C., Piedrafita, L., Bellı́, G., & Herrero, E. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.03.037 · Cited by 87
Self-citation
Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich's ataxia
Auchère, F., Santos, R., Planamente, S., Lesuisse, E., & Camadro, J. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn178 · Cited by 87
A Glutaredoxin·BolA Complex Serves as an Iron-Sulfur Cluster Chaperone for the Cytosolic Cluster Assembly Machinery
Frey, A. G., Palenchar, D. J., Wildemann, J. D., & Philpott, C. C. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744946 · Cited by 87
Thioredoxin Reductase System Mediates Iron Binding in IscA and Iron Delivery for the Iron-Sulfur Cluster Assembly in IscU*
Ding, H., Harrison, K., & Lü, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504638200 · Cited by 86
Structural Aspects of the Distinct Biochemical Properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae
Discola, K. F., de Oliveira, M. A., Cussiol, J. R. R., Monteiro, G., Bárcena, J. A., Porras, P., Padilla, C. A., Guimarães, B. G., & Netto, L. E. S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.055 · Cited by 87
Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins
Trnka, D., Engelke, A. D., Gellert, M., Moseler, A., Hossain, M. F., Lindenberg, T. T., Pedroletti, L., Odermatt, B., de Souza, J. V. B., Bronowska, A. K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17323-0 · Cited by 85
Linked thioredoxin-glutathione systems in platyhelminths
Salinas, G., Selkirk, M. E., Chalar, C., Maizels, R. M., & Fernández, C. (2004) · Trends in Parasitology · doi:10.1016/j.pt.2004.05.002 · Cited by 83
An Expanding Range of Functions for the Copper Chaperone/Antioxidant Protein Atox1
Hatori, Y., & Lutsenko, S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5086 · Cited by 82
Nuclear Redox Signaling
Lukosz, M., Jakob, S., Büchner, N., Zschauer, T.-C., Altschmied, J., & Haendeler, J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2609 · Cited by 83
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. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2489 · Cited by 81
Sugar metabolism, redox balance and oxidative stress response in the respiratory yeast Kluyveromyces lactis
González-Siso, M.-I., García-Leiro, A., Tarrío, N., & Cerdán, M. E. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-46 · Cited by 81
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. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00726-12 · Cited by 78
Transcriptional responses of male fathead minnows exposed to oil sands process-affected water
Wiseman, S. B., He, Y., El‐Din, M. G., Martin, J. W., Jones, P. D., Hecker, M., & Giesy, J. P. (2012) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2012.12.002 · Cited by 78
The Glutathione/Glutaredoxin System Is Essential for Arsenate Reduction in Synechocystis sp. Strain PCC 6803
López‐Maury, L., Sánchez-Riego, A. M., Reyes, J. C., & Florencio, F. J. (2009) · Journal of Bacteriology · doi:10.1128/jb.01798-08 · Cited by 77
Cloning and Characterization of CXIP1, a Novel PICOT Domain-containing Arabidopsis Protein That Associates with CAX1
Cheng, N., & Hirschi, K. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210883200 · Cited by 77
Reprint of: Iron/sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity
Roche, B., Aussel, L., Ezraty, B., Mandin, P., Py, B., & Barras, F. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.05.001 · Cited by 80
Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae
Wheeler, G. L., & Grant, C. M. (2004) · Physiologia Plantarum · doi:10.1111/j.0031-9317.2004.0193.x · Cited by 76
From the discovery to molecular understanding of cellular iron-sulfur protein biogenesis
Lill, R. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0117 · Cited by 73
Alternative mRNAs Arising from Trans-splicing Code for Mitochondrial and Cytosolic Variants of Echinococcus granulosus Thioredoxin Glutathione Reductase
Agorio, A., Chalar, C., Cardozo, S., & Salinas, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209266200 · Cited by 75
Glutaredoxins in plant development, abiotic stress response, and iron homeostasis: From model organisms to crops
Wu, Q., Yang, J., Cheng, N., Hirschi, K. D., White, F. F., & Park, S. (2017) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2017.04.007 · Cited by 74
Iron: Effect of Overload and Deficiency
Hider, R. C., & Kong, X. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_8 · Cited by 78
Structure-Function Analysis of Yeast Grx5 Monothiol Glutaredoxin Defines Essential Amino Acids for the Function of the Protein
Bellı́, G., Polaina, J., Tamarit, J., de la Torre-Ruiz, M. Á., Rodríguez‐Manzaneque, M. T., Ros, J., & Herrero, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201688200 · Cited by 74
Self-citation
Genes for iron metabolism influence circadian rhythms in Drosophila melanogaster
Mandilaras, K., & Missirlis, F. (2012) · Metallomics · doi:10.1039/c2mt20065a · Cited by 74
GintGRX1, the first characterized glomeromycotan glutaredoxin, is a multifunctional enzyme that responds to oxidative stress
Benabdellah, K., MERLOS, M., Azcón‐Aguilar, C., & Ferrol, N. (2008) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2008.09.013 · Cited by 78
The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC protein Rli1 for iron-sulfur cluster insertion
Paul, V. D., Mühlenhoff, U., Stümpfig, M., Seebacher, J., Kugler, K., Renicke, C. C., Taxis, C., Gavin, A., Pierik, A. J., & Lill, R. (2015) · eLife · doi:10.7554/elife.08231 · Cited by 74
A Novel Group of Glutaredoxins in thecis-Golgi Critical for Oxidative Stress Resistance
Mesecke, N., Spang, A., Deponte, M., & Herrmann, J. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0896 · Cited by 72
Origin and Diversification of Land Plant CC-Type Glutaredoxins
Ziemann, M., Bhave, M. R., & Zachgo, S. (2009) · Genome Biology and Evolution · doi:10.1093/gbe/evp025 · Cited by 72
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., Kim, H.-J., Lee, K.-C., & Roe, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.051 · Cited by 71
Glutaredoxin S15 Is Involved in Fe-S Cluster Transfer in Mitochondria Influencing Lipoic Acid-Dependent Enzymes, Plant Growth, and Arsenic Tolerance in Arabidopsis
Ströher, E., Grassl, J., Carrie, C., Fenske, R., Whelan, J., & Millar, A. H. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.01308 · Cited by 68
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. (2004) · Biochemical Journal · doi:10.1042/bj20030638 · Cited by 67
The Interaction of Mitochondrial Iron with Manganese Superoxide Dismutase
Naranuntarat, A., Jensen, L. T., Pazicni, S., Penner-Hahn, J. E., & Culotta, V. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026773 · Cited by 66
The Heme Synthesis Defect of Mutants Impaired in Mitochondrial Iron-Sulfur Protein Biogenesis Is Caused by Reversible Inhibition of Ferrochelatase
Lange, H., Mühlenhoff, U., Denzel, M. S., Kispál, G., & Lill, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403721200 · Cited by 66
Manganese Is the Link between Frataxin and Iron-Sulfur Deficiency in the Yeast Model of Friedreich Ataxia
Irazusta, V. P., Cabiscol, E., Reverter‐Branchat, G., Ros, J., & Tamarit, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511649200 · Cited by 63
Self-citation
Catalysis of Thiol/Disulfide Exchange
Xiao, R., Lundström-Ljung, J., Holmgren, A., & Gilbert, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411476200 · Cited by 65
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. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802010200 · Cited by 68
Saccharomyces cerevisiae Grx6 and Grx7 Are Monothiol Glutaredoxins Associated with the Early Secretory Pathway
Izquierdo, A., Casas, C., Mühlenhoff, U., Lillig, C. H., & Herrero, E. (2008) · Eukaryotic Cell · doi:10.1128/ec.00133-08 · Cited by 66
Self-citation
Global Transcriptional Profiles of the Copper Responses in the Cyanobacterium Synechocystis sp. PCC 6803
Giner‐Lamia, J., López‐Maury, L., & Florencio, F. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108912 · Cited by 63
Glutathionyl systems and metabolic dysfunction in obesity
Picklo, M. J., Long, E. K., & Vomhof‐DeKrey, E. E. (2015) · Nutrition Reviews · doi:10.1093/nutrit/nuv042 · Cited by 64
Nexus between mitochondrial function, iron, copper and glutathione in Parkinson's disease
Liddell, J. R., & White, A. R. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.05.016 · Cited by 64
Selenite-induced cell death in Saccharomyces cerevisiae: protective role of glutaredoxins
Izquierdo, A., Casas, C., & Herrero, E. (2010) · Microbiology · doi:10.1099/mic.0.039719-0 · Cited by 61
Self-citation
Saccharomyces cerevisiae Glutaredoxin 5-deficient Cells Subjected to Continuous Oxidizing Conditions Are Affected in the Expression of Specific Sets of Genes
Bellı́, G., Molina‐Navarro, M. M., García‐Martínez, J., Pérez-Ortín, J. E., & Herrero, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311879200 · Cited by 61
Self-citation
Cell volume as a factor limiting the replicative lifespan of the yeast Saccharomyces cerevisiae
Zadrąg‐Tęcza, R., Kwolek‐Mirek, M., Bartosz, G., & Biliński, T. (2008) · Biogerontology · doi:10.1007/s10522-008-9192-0 · Cited by 60
One Single In-frame AUG Codon Is Responsible for a Diversity of Subcellular Localizations of Glutaredoxin 2 in Saccharomyces cerevisiae
Porras, P., Padilla, C. A., Krayl, M., Voos, W., & Bárcena, J. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600790200 · Cited by 60
Molecular Mapping of Functionalities in the Solution Structure of Reduced Grx4, a Monothiol Glutaredoxin from Escherichia coli
Fladvad, M., Bellanda, M., Fernandes, A. P., Mammi, S., Vlamis‐Gardikas, A., Holmgren, A., & Sunnerhagen, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500679200 · Cited by 59
Glutaredoxin 1, glutaredoxin 2, thioredoxin 1, and thioredoxin peroxidase 3 play important roles in antioxidant defense in Apis cerana cerana
Yao, P., Chen, X., Yan, Y., Liu, F., Zhang, Y., Guo, X., & Xu, B. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.020 · Cited by 58
The thioredoxin superfamily in Chlamydomonas reinhardtii
Lemaire, S. D., & Myroslawa Miginiac-maslow, B. (2004) · Photosynthesis Research · doi:10.1007/s11120-004-1091-x · Cited by 59
A dicotyledon‐specific glutaredoxin GRXC1 family with dimer‐dependent redox regulation is functionally redundant with GRXC2
Riondet, C., de Souris, J. P., Guilleminot, J., Chartier, Y., Meyer, Y., & Reichheld, J. (2011) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2011.02355.x · Cited by 58
BOLA1 Is an Aerobic Protein That Prevents Mitochondrial Morphology Changes Induced by Glutathione Depletion
Willems, P. H. G. M., Wanschers, B. F. J., Esseling, J. J., Szklarczyk, R., Kudla, U., Duarte, I., Forkink, M., Nooteboom, M., Swarts, H. G. P., Gloerich, J., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4253 · Cited by 58
Biochemical Characterization of Dithiol Glutaredoxin 8 from Saccharomyces cerevisiae: The Catalytic Redox Mechanism Redux
Eckers, E., Bien, M., Stroobant, V., Herrmann, J. M., & Deponte, M. (2009) · Biochemistry · doi:10.1021/bi801859b · Cited by 59
Disorders associated with systemic or local iron overload: from pathophysiology to clinical practice
Sebastiani, G., & Pantopoulos, K. (2011) · Metallomics · doi:10.1039/c1mt00082a · Cited by 58
Grx4 Monothiol Glutaredoxin Is Required for Iron Limitation-Dependent Inhibition of Fep1
Jbel, M., Mercier, A., & Labbé, S. (2011) · Eukaryotic Cell · doi:10.1128/ec.00015-11 · Cited by 57
IBA57 Recruits ISCA2 to Form a [2Fe-2S] Cluster-Mediated Complex
Gourdoupis, S., Nasta, V., Calderone, V., Ciofi‐Baffoni, S., & Banci, L. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09061 · Cited by 60
The Cell's Cookbook For Iron–Sulfur Clusters: Recipes For Fool's Gold?
Balk, J., & Lill, R. (2004) · ChemBioChem · doi:10.1002/cbic.200400061 · Cited by 58
Redox properties and evolution of human glutaredoxins
Sagemark, J., Elgán, T. H., Bürglin, T. R., Johansson, C., Holmgren, A., & Berndt, K. D. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21416 · Cited by 58
Involvement of Arabidopsis glutaredoxin S14 in the maintenance of chlorophyll content
Rey, P., Bécuwe, N., Tourrette, S., & Rouhier, N. (2017) · Plant Cell & Environment · doi:10.1111/pce.13036 · Cited by 56
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., Huynh, B. H., Couturier, J., Rouhier, N., & Johnson, M. K. (2013) · Journal of the American Chemical Society · doi:10.1021/ja407059n · Cited by 56
Factors affecting yeast ethanol tolerance and fermentation efficiency
Vamvakas, S. M., & Kapolos, J. (2020) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-020-02881-8 · Cited by 66
Glutathione Reductase and a Mitochondrial Thioredoxin Play Overlapping Roles in Maintaining Iron-Sulfur Enzymes in Fission Yeast
Song, J.-Y., Cha, J., Lee, J., & Roe, J.-H. (2006) · Eukaryotic Cell · doi:10.1128/ec.00244-06 · Cited by 55
Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism
Marelja, Z., Leimkühler, S., & Missirlis, F. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00050 · Cited by 61
Thioredoxin and Glutaredoxin Systems as Potential Targets for the Development of New Treatments in Friedreich’s Ataxia
Seco-Cervera, M., González‐Cabo, P., Pallardó, F. V., Mateo, C. R., & García‐Giménez, J. L. (2020) · Antioxidants · doi:10.3390/antiox9121257 · Cited by 57
The Multidomain Thioredoxin-Monothiol Glutaredoxins Represent a Distinct Functional Group
Hoffmann, B., Uzarska, M. A., Berndt, C., Godoy, J. R., Haunhorst, P., Lillig, C. H., Lill, R., & Mühlenhoff, U. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3811 · Cited by 55
The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisited
Vlamis‐Gardikas, A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.03.013 · Cited by 54

Authors: Rodrı́guez-Manzaneque, M. T., Tamarit, J., Bellı́, G., Ros, J., & Herrero, E.
Affiliations: Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, 25198-Lleida, Spain
Universitat de Lleida (ES)
ORCID: Tamarit, Jordi
Bellı́, Gemma
Ros, Joaquim
Herrero, Enrique
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 2002-04
Volume: 13
Issue: 4
Pages: 1109-1121
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.01-10-0517
PMC: PMC102255
OpenAlex: W2090154662
Cited by: 464
References: 78
Citations by year: 2026: 6 · 2025: 10 · 2024: 11 · 2023: 14 · 2022: 13 · 2021: 14 · 2020: 21 · 2019: 11 · 2018: 21 · 2017: 26 · 2016: 18 · 2015: 14 · 2014: 20 · 2013: 20 · 2012: 25
FWCI: 6.37
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular Biology of the Cell (publishedVersion)
PubMed Central (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed (publishedVersion)
LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (publishedVersion, cc-by-nc-sa)
RECERCAT (Consorci de Serveis Universitaris de Catalunya) (publishedVersion, cc-by-nc-sa)
Repositori ObertUDL (University of Lleida) (publishedVersion, cc-by-nc-sa)
Funders: Generalitat de Catalunya
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords: glutaredoxin, iron-sulfur clusters, mitochondrial matrix, oxidative damage, iron accumulation, iron-sulfur cluster assembly, yeast, anaerobic conditions
MeSH terms: Amino Acid Sequence, Antifibrinolytic Agents, Iron, Iron-Sulfur Proteins, Mitochondria, Molecular Sequence Data, Mutation, Oxidation-Reduction, Oxidoreductases, Oxygen, Peptides, Plasmids, Protein Binding, Proteins, Saccharomyces cerevisiae, Time Factors, Blotting, Western, Mutagenesis, Site-Directed, Protein Structure, Tertiary, DNA, Complementary, Vitamin K 3, Glutaredoxins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks