Exploiting Bacterial Operons To Illuminate Human Iron–Sulfur Proteins
Abstract
Organisms from all kingdoms of life use iron-sulfur proteins (FeS-Ps) in a multitude of functional processes. We applied a bioinformatics approach to investigate the human portfolio of FeS-Ps. Sixty-one percent of human FeS-Ps bind Fe4S4 clusters, whereas 39% bind Fe2S2 clusters. However, this relative ratio varies significantly depending on the specific cellular compartment. We compared the portfolio of human FeS-Ps to 12 other eukaryotes and to about 700 prokaryotes. The comparative analysis of the organization of the prokaryotic homologues of human FeS-Ps within operons allowed us to reconstruct the human functional networks involving the conserved FeS-Ps common to prokaryotes and eukaryotes. These functional networks have been maintained during evolution and thus presumably represent fundamental cellular processes. The respiratory chain and the ISC machinery for FeS-P biogenesis are the two conserved processes that involve the majority of human FeS-Ps. Purine metabolism is another process including several FeS-Ps, in which BOLA proteins possibly have a regulatory role. The analysis of the co-occurrence of human FeS-Ps with other proteins highlighted numerous links between the iron-sulfur cluster machinery and the response mechanisms to cell damage, from repair to apoptosis. This relationship probably relates to the production of reactive oxygen species within the biogenesis and degradation of FeS-Ps.
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Eprenetapopt treatment up-regulated FDX1, DNAJA3, and ABCF2.
“Notably, our proteomics study revealed that cells treated with eprenetapopt up-regulated the levels of mitochondrial ferredoxin 1 (FDX1), a critical component of mitochondrial iron-sulfur cluster (ISC) biosynthesis (14), as well as two other proteins, DNAJA3 and ABCF2, which have reported roles in iron metabolism (Fig. 1I) (15, 16).”
From Eprenetapopt triggers ferroptosis, inhibits NFS1 cysteine desulfurase, and synergizes with serine and glycine dietary restriction (2022) · cites this paper as [16]
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1 retracted
Mitoneet mediates TNFα induced necroptosis promoted by fructose and ethanol exposure
Shulga, N., & Pastorino, J. G. (2013) · Journal of Cell Science · doi:10.1242/jcs.140764 · Cited by 20 · see citing works
RetractedGapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302 · see citing works
STRING v10: protein–protein interaction networks, integrated over the tree of life
Szklarczyk, D., Franceschini, A., Wyder, S., Forslund, K., Heller, D., Huerta-Cepas, J., Simonovic, M., Roth, A., Santos, A., Tsafou, K. P., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gku1003 · Cited by 10,436 · see citing works
Pfam: the protein families database
Finn, R. D., Bateman, A., Clements, J., Coggill, P., Eberhardt, R. Y., Eddy, S. R., Heger, A., Hetherington, K., Holm, L., Mistry, J., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1223 · Cited by 6,148 · see citing works
UniProt: a hub for protein information
The UniProt Consortium (2015) · Nucleic Acids Research · doi:10.1093/nar/gku989 · Cited by 5,106 · see citing works
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 · see citing works
Neuwald, A. F., Aravind, L., Spouge, J. L., & Koonin, E. V. (1999) · Genome Research · doi:10.1101/gr.9.1.27 · Cited by 1,811 · see citing works
Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage
Hoffman, B. M., Lukoyanov, D. A., Yang, Z., Dean, D. R., & Seefeldt, L. C. (2014) · Chemical Reviews · doi:10.1021/cr400641x · Cited by 1,776 · see citing works
Comparative Protein Structure Modeling Using MODELLER
Webb, B., & Šali, A. (2014) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0506s47 · Cited by 1,141 · see citing works
Conservation of gene order: a fingerprint of proteins that physically interact.
Dandekar, T., Snel, B., Huynen, M., & Bork, P. (1998) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/s0968-0004(98)01274-2 · Cited by 1,108 · see citing works
The BioGRID interaction database: 2015 update
Chatr‐aryamontri, A., Breitkreutz, B., Oughtred, R., Boucher, L., Heinicke, S., Chen, D., Stark, C., Breitkreutz, A., Kolas, N. K., O’Donnell, L., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1204 · Cited by 884 · see citing works
QMEAN server for protein model quality estimation
Benkert, P., Künzli, M., & Schwede, T. F. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp322 · Cited by 874 · see citing works
A Census of Human Soluble Protein Complexes
Havugimana, P. C., Hart, T., Nepusz, T., Yang, H., Turinsky, A. L., Li, Z., Wang, P. I., Boutz, D. R., Fong, V., Phanse, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.08.011 · Cited by 843 · see citing works
A Protein Complex Network of Drosophila melanogaster
Guruharsha, K. G., Rual, J.-F. M., Zhai, B., Mintseris, J., Vaidya, P., Vaidya, N., Beekman, C. N., Wong, C. S. F., Rhee, D. Y., Cenaj, O., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.047 · Cited by 654 · see citing works
Assembly of Iron-Sulfur Clusters
Zheng, L., Cash, V. L., Flint, D. H., & Dean, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13264 · Cited by 650 · see citing works
Zinc through the Three Domains of Life
Andreini, C., Banci, L., Bertini, I., & Rosato, A. (2006) · Journal of Proteome Research · doi:10.1021/pr0603699 · Cited by 648 · see citing works
Self-citationBattistuzzi, F. U., Feijao, A., & Hedges, S. B. (2004) · BMC Evolutionary Biology · doi:10.1186/1471-2148-4-44 · Cited by 581 · see citing works
Panorama of ancient metazoan macromolecular complexes
Wan, C., Borgeson, B., Phanse, S., Tu, F., Drew, K., Clark, G. W., Xiong, X., Kagan, O., Kwan, J., Bezginov, A., et al. (2015) · Nature · doi:10.1038/nature14877 · Cited by 521 · see citing works
The role of mitochondria in cellular iron–sulfur protein biogenesis and iron metabolism
Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., & Mühlenhoff, U. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.009 · Cited by 501 · see citing works
Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes
Netz, D. J. A., Stith, C. M. W., Stümpfig, M., Köpf, G., Vogel, D., Genau, H. M., Stodola, J. L., Lill, R., Burgers, P., & Pierik, A. J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.721 · Cited by 388 · see citing works
Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii
Jacobson, M. R., Brigle, K. E., Bennett, L. T., Setterquist, R. A., Wilson, M. S., Cash, V. L., Beynon, J., Newton, W. E., & Dean, D. R. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.2.1017-1027.1989 · Cited by 373 · see citing works
Metalloproteomes: A Bioinformatic Approach
Andreini, C., Bertini, I., & Rosato, A. (2009) · Accounts of Chemical Research · doi:10.1021/ar900015x · Cited by 370 · see citing works
Self-citationIron/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.2012.12.010 · Cited by 335 · see citing works
Reddy, T. B. K., Thomas, A. D., Stamatis, D., Bertsch, J., Isbandi, M., Jansson, J., Mallajosyula, J. K., Pagani, I., Lobos, E. A., & Kyrpides, N. C. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku950 · Cited by 334 · see citing works
Wiley, S. E., Murphy, A. N., Ross, S. A., van der Geer, P., & Dixon, J. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701078104 · Cited by 326 · see citing works
Iron–sulfur protein folds, iron–sulfur chemistry, and evolution
Meyer, J. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0318-7 · Cited by 266 · see citing works
Human Apurinic/Apyrimidinic Endonuclease 1
Li, M., & Wilson, D. M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5492 · Cited by 256 · see citing works
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
Sharma, S., Rios, P. D. L., Christen, P., Lustig, A., & Goloubinoff, P. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.455 · Cited by 227 · see citing works
Occurrence of Copper Proteins through the Three Domains of Life: A Bioinformatic Approach
Andreini, C., Banci, L., Bertini, I., & Rosato, A. (2007) · Journal of Proteome Research · doi:10.1021/pr070480u · Cited by 223 · see citing works
Self-citationEndonuclease III is an iron-sulfur protein
Cunningham, R. P., Asahara, H., Bank, J. F., Scholes, C. P., Salerno, J. C., Surerus, K. K., Münck, E., McCracken, J., Peisach, J., & Emptage, M. H. (1989) · Biochemistry · doi:10.1021/bi00436a049 · Cited by 221 · see citing works
Korbel, J., Jensen, L., von Mering, C., & Bork, P. (2004) · Nature Biotechnology · doi:10.1038/nbt988 · Cited by 210 · see citing works
Fe-S proteins in sensing and regulatory functions
Beinert, H., & Kiley, P. J. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80027-1 · Cited by 208 · see citing works
Crack, J. C., Green, J. D., THOMSON, A. J., & Brun, N. E. L. (2014) · Accounts of Chemical Research · doi:10.1021/ar5002507 · Cited by 204 · see citing works
Mammalian iron-sulphur proteins: novel insights into biogenesis and function
Rouault, T. A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3909 · Cited by 201 · see citing works
Organization of Iron-Sulfur Clusters in Respiratory Complex I
Hinchliffe, P., & Sazanov, L. A. (2005) · Science · doi:10.1126/science.1113988 · Cited by 197 · see citing works
Tamir, S., Paddock, M. L., Darash-Yahana-Baram, M., Holt, S. H., Sohn, Y. S., Agranat-Tamir, L., Michaeli, D., Stofleth, J. T., Lipper, C. H., Morcos, F., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.10.014 · Cited by 194 · see citing works
Lipoic Acid Metabolism in Microbial Pathogens
Spalding, M. D., & Prigge, S. T. (2010) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00008-10 · Cited by 193 · see citing works
Lill, R., Dutkiewicz, R., Freibert, S., Heidenreich, T., Mascarenhas, J., Netz, D. J. A., Paul, V. D., Pierik, A. J., Richter, N., Stümpfig, M., et al. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.002 · Cited by 188 · see citing works
Maturation of cytosolic and nuclear iron–sulfur proteins
Netz, D. J. A., Mascarenhas, J., Stehling, O., Pierik, A. J., & Lill, R. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.11.005 · Cited by 184 · see citing works
Webert, H., Freibert, S., Gallo, A., Heidenreich, T., Linne, U., Amlacher, S., Hurt, E., Mühlenhoff, U., Banci, L., & Lill, R. (2014) · Nature Communications · doi:10.1038/ncomms6013 · Cited by 177 · see citing works
Self-citationIron–sulfur cluster biosynthesis
Bandyopadhyay, S., Chandramouli, K., & Johnson, M. K. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361112 · Cited by 169 · see citing works
Cochaperone Binding to LYR Motifs Confers Specificity of Iron Sulfur Cluster Delivery
Maio, N., Singh, A., Uhrigshardt, H., Saxena, N., Tong, W.-H., & Rouault, T. A. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.015 · Cited by 167 · see citing works
ProOpDB: Prokaryotic Operon DataBase
Taboada, B., Ciria, R., Martínez-Guerrero, C. E., & Merino, E. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1020 · Cited by 163 · see citing works
The Conformational Dynamics of the Mitochondrial Hsp70 Chaperone
Mapa, K., Sikor, M., Kudryavtsev, V., Waegemann, K., Kalinin, S., Seidel, C. A. M., Neupert, W., Lamb, D. C., & Mokranjac, D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.03.010 · Cited by 160 · see citing works
Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis
Tong, W.-H., & Rouault, T. A. (2007) · BioMetals · doi:10.1007/s10534-006-9047-6 · Cited by 158 · see citing works
Syken, J., De-Medina, T., & Münger, K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8499 · Cited by 146 · see citing works
[2Fe-2S] cluster transfer in iron–sulfur protein biogenesis
Banci, L., Brancaccio, D., Ciofi‐Baffoni, S., Conte, R. D., Gadepalli, R., Mikołajczyk, M., Neri, S., Piccioli, M., & Winkelmann, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400102111 · Cited by 143 · see citing works
Self-citationEndogenous Production of Lipoic Acid Is Essential for Mouse Development
Yi, X., & Maeda, N. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.18.8387-8392.2005 · Cited by 137 · see citing works
Iron–sulphur clusters in nucleic acid processing enzymes
White, M. F., & Dillingham, M. S. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.11.004 · Cited by 136 · see citing works
Uzarska, M. A., Dutkiewicz, R., Freibert, S., Lill, R., & Mühlenhoff, U. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-09-0644 · Cited by 128 · see citing works
A hint to search for metalloproteins in gene banks
Andreini, C., Bertini, I., & Rosato, A. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth095 · Cited by 127 · see citing works
Self-citationFerecatu, I., Gonçalves, S., Golinelli‐Cohen, M., Clémancey, M., Martelli, A., Riquier, S., Guittet, É., Latour, J., Puccio, H. M., Drapier, J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.548438 · Cited by 125 · see citing works
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 118 · see citing works
Glutamate synthase: a complex iron-sulfur flavoprotein
Vanoni, M. A., & Curti, B. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050319 · Cited by 117 · see citing works
BolA Is a Transcriptional Switch That Turns Off Motility and Turns On Biofilm Development
Dressaire, C., Moreira, R. N., Barahona, S., Matos, A., & Arraiano, C. M. (2015) · mBio · doi:10.1128/mbio.02352-14 · Cited by 99 · see citing works
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 87 · see citing works
Recent advances in the Suf Fe–S cluster biogenesis pathway: Beyond the Proteobacteria
Outten, F. W. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.11.001 · Cited by 79 · see citing works
Non‐heme iron through the three domains of life
Andreini, C., Banci, L., Bertini, I., Elmi, S., & Rosato, A. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21324 · Cited by 79 · see citing works
Self-citationN-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin
Banci, L., Ciofi‐Baffoni, S., Gajda, K., Muzzioli, R., Peruzzini, R., & Winkelmann, J. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1892 · Cited by 76 · see citing works
Self-citationCheng, H., Cenciarelli, C., Shao, Z., Vidal, M., Parks, W. P., Pagano, M., & Cheng‐Mayer, C. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00540-1 · Cited by 76 · see citing works
Hernández, J. A., Curatti, L., Aznar, C. P., Perova, Z., Britt, R. D., & Rubio, L. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803576105 · Cited by 74 · see citing works
Role of IscX in Iron–Sulfur Cluster Biogenesis in Escherichia coli
Kim, J. H., Bothe, J. R., Frederick, R. O., Holder, J. C., & Markley, J. L. (2014) · Journal of the American Chemical Society · doi:10.1021/ja501260h · Cited by 73 · see citing works
Elucidating the Molecular Function of Human BOLA2 in GRX3-Dependent Anamorsin Maturation Pathway
Banci, L., Camponeschi, F., Ciofi‐Baffoni, S., & Muzzioli, R. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b10592 · Cited by 73 · see citing works
Self-citationTai-Nagara, I., Matsuoka, S., Ariga, H., & Suda, T. (2013) · Blood · doi:10.1182/blood-2013-06-508333 · Cited by 71 · see citing works
Schraders, M., Lee, K. D., Oostrik, J., Huygen, P. L. M., Ali, G., Hoefsloot, L. H., Veltman, J. A., Cremers, F. P. M., Basit, S., Ansar, M., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.12.017 · Cited by 70 · see citing works
Biosynthesis of complex iron–sulfur enzymes
Shepard, E. M., Boyd, E. S., Broderick, J. B., & Peters, J. W. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.02.012 · Cited by 69 · see citing works
Bioenergetic Evolution in Proteobacteria and Mitochondria
Esposti, M. D. (2014) · Genome Biology and Evolution · doi:10.1093/gbe/evu257 · Cited by 67 · see citing works
Vascotto, C., Bisetto, E., Li, M., Zeef, L. A. H., DˈAmbrosio, C., Domenis, R., Comelli, M., Delneri, D., Scaloni, A., Fabio Altieri, F., et al. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-05-0391 · Cited by 67 · see citing works
Molecular Cloning and Characterization of a Human AIF-like Gene with Ability to Induce Apoptosis
Xie, Q., Lin, T., Zhang, Y., Zheng, J., & Bonanno, J. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409517200 · Cited by 65 · see citing works
Iron-sulfur proteins hiding in plain sight
Rouault, T. A. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1843 · Cited by 64 · see citing works
A Grid-enabled web portal for NMR structure refinement with AMBER
Bertini, I., Case, D. A., Ferella, L., Giachetti, A., & Rosato, A. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr415 · Cited by 61 · see citing works
Self-citationDutkiewicz, R., Marszałek, J., Schilke, B. A., Craig, E. A., Lill, R., & Mühlenhoff, U. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513301200 · Cited by 61 · see citing works
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 · see citing works
Actin in hair cells and hearing loss
Drummond, M. C., Belyantseva, I. A., Friderici, K. H., & Friedman, T. B. (2011) · Hearing Research · doi:10.1016/j.heares.2011.12.003 · Cited by 58 · see citing works
DNA-Mediated Signaling by Proteins with 4Fe–4S Clusters Is Necessary for Genomic Integrity
Grodick, M. A., Segal, H. M., Zwang, T. J., & Barton, J. K. (2014) · Journal of the American Chemical Society · doi:10.1021/ja501973c · Cited by 58 · see citing works
Mutations in Grxcr1 Are The Basis for Inner Ear Dysfunction in the Pirouette Mouse
Odeh, H. M., Hunker, K. L., Belyantseva, I. A., Azaiez, H., Avenarius, M. R., Zheng, L., Peters, L. M., Gagnon, L. H., Hagiwara, N., Skynner, M. J., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.01.016 · Cited by 50 · see citing works
Iosefson, O., Sharon, S., Goloubinoff, P., & Azem, A. (2011) · Cell Stress and Chaperones · doi:10.1007/s12192-011-0285-3 · Cited by 49 · see citing works
Mechanism of glutaredoxin—ISU [2Fe–2S] cluster exchange
Qi, W., & Cowan, J. A. (2011) · Chemical Communications · doi:10.1039/c0cc05079b · Cited by 44 · see citing works
Brust, D., Hamann, A., & Osiewacz, H. D. (2010) · Current Genetics · doi:10.1007/s00294-010-0295-1 · Cited by 39 · see citing works
Qi, W., & Cowan, J. A. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.10.016 · Cited by 36 · see citing works
Goswami, A. V., Samaddar, M., Sinha, D., Purushotham, J., & D’Silva, P. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds162 · Cited by 35 · see citing works
Bentrop, D., Bertini, I., Iacoviello, R., Luchinat, C., Niikura, Y., Piccioli, M., Presenti, C., & Rosato, A. (1999) · Biochemistry · doi:10.1021/bi982647q · Cited by 31 · see citing works
Self-citationAndreini, C., Bertini, I., Cavallaro, G., Decaria, L., & Rosato, A. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci100392q · Cited by 28 · see citing works
Self-citationA 2‐D gel reference map of the basic human heart proteome
Polden, J., McManus, C. A., dos Remedios, C. G., & Dunn, M. J. (2011) · PROTEOMICS · doi:10.1002/pmic.201000182 · Cited by 16 · see citing works
Decisive role of apurinic/apyrimidinic endonuclease/Ref-1 in initiation of cell death
Cho, K., Kim, H. J., Park, S. C., Kim, H., & Kim, G. W. (2010) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.07.001 · Cited by 6 · see citing works
X-ray structure of a soluble Rieske-type ferredoxin fromMus musculus
Levin, E. J., Elsen, N. L., Seder, K. D., McCoy, J. G., Fox, B. G., & Phillips, G. N., Jr. (2008) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444908021653 · Cited by 5 · see citing works
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Lill, R., & Freibert, S.-A. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111540 · Cited by 453 · see citing works
Andreini, C., Putignano, V., Rosato, A., & Banci, L. (2018) · Metallomics · doi:10.1039/c8mt00146d · Cited by 179 · see citing works
Self-citationHypoxia Rescues Frataxin Loss by Restoring Iron Sulfur Cluster Biogenesis
Ast, T., Meisel, J. D., Patra, S., Wang, H., Grange, R. M. H., Kim, S. H., Calvo, S. E., Orefice, L. L., Nagashima, F., Ichinose, F., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.045 · Cited by 156 · see citing works
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Ciofi‐Baffoni, S., Nasta, V., & Banci, L. (2017) · Metallomics · doi:10.1039/c7mt00269f · Cited by 116 · see citing works
Self-citationFujihara, K. M., Zhang, B. Z., Jackson, T. D., Ogunkola, M. O., Nijagal, B., Milne, J. V., Sallman, D. A., Ang, C.-S., Nikolic, I., Kearney, C. J., et al. (2022) · Science Advances · doi:10.1126/sciadv.abm9427 · Cited by 103 · see citing works
“1I) ( 15 , 16 ).”
MetalPredator: a web server to predict iron–sulfur cluster binding proteomes
Valasatava, Y., Rosato, A., Banci, L., & Andreini, C. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw238 · Cited by 70 · see citing works
Self-citationAndreini, C., Rosato, A., & Banci, L. (2017) · PLoS ONE · doi:10.1371/journal.pone.0171279 · Cited by 69 · see citing works
Self-citationMETTL17 is an Fe-S cluster checkpoint for mitochondrial translation
Ast, T., Itoh, Y., Sadre, S., McCoy, J. G., Namkoong, G., Wengrod, J. C., Chicherin, I., Joshi, P. R., Kamenski, P., Suess, D. L. M., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.016 · Cited by 58 · see citing works
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 57 · see citing works
Self-citationNasta, V., Giachetti, A., Ciofi‐Baffoni, S., & Banci, L. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.05.005 · Cited by 54 · see citing works
Self-citationMetallomics: The Science of Biometals and Biometalloids
Maret, W. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-90143-5_1 · Cited by 53 · see citing works
Cai, K., Liu, G., Frederick, R. O., Xiao, R., Montelione, G. T., & Markley, J. L. (2016) · Structure · doi:10.1016/j.str.2016.08.020 · Cited by 50 · see citing works
Anamorsin/Ndor1 Complex Reduces [2Fe–2S]-MitoNEET via a Transient Protein–Protein Interaction
Camponeschi, F., Ciofi‐Baffoni, S., & Banci, L. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b05003 · Cited by 47 · see citing works
Self-citationThe NMR contribution to protein–protein networking in Fe–S protein maturation
Banci, L., Camponeschi, F., Ciofi‐Baffoni, S., & Piccioli, M. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1552-x · Cited by 45 · see citing works
Self-citationA pathway for assembling [4Fe‐4S]2+ clusters in mitochondrial iron–sulfur protein biogenesis
Nasta, V., Suraci, D., Gourdoupis, S., Ciofi‐Baffoni, S., & Banci, L. (2019) · FEBS Journal · doi:10.1111/febs.15140 · Cited by 43 · see citing works
Self-citationLipoylation is dependent on the ferredoxin FDX1 and dispensable under hypoxia in human cells
Joshi, P. R., Sadre, S., Guo, X. A., McCoy, J. G., & Mootha, V. K. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105075 · Cited by 40 · see citing works
Hypoxia and intra-complex genetic suppressors rescue complex I mutants by a shared mechanism
Meisel, J. D., Miranda, M., Skinner, O. S., Wiesenthal, P. P., Wellner, S. M., Jourdain, A. A., Ruvkun, G., & Mootha, V. K. (2024) · Cell · doi:10.1016/j.cell.2023.12.010 · Cited by 38 · see citing works
Mammalian Fe–S proteins: definition of a consensus motif recognized by the co-chaperone HSC20
Maio, N., & Rouault, T. A. (2016) · Metallomics · doi:10.1039/c6mt00167j · Cited by 34 · see citing works
Ferecatu, I., Canal, F., Fabbri, L., Mazure, N. M., Bouton, C., & Golinelli‐Cohen, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0194782 · Cited by 34 · see citing works
Cytosolic iron–sulfur protein assembly system identifies clients by a C-terminal tripeptide
Marquez, M. D., Greth, C., Buzuk, A., Liu, Y., Blinn, C. M., Beller, S., Leiskau, L., Hushka, A., Wu, K., Nur, K., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2311057120 · Cited by 26 · see citing works
Moore, M. J., Wofford, J. D., Dancis, A., & Lindahl, P. A. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b01034 · Cited by 26 · see citing works
Genome-Wide Search for Genes Required for Bifidobacterial Growth under Iron-Limitation
Lanigan, N., Bottacini, F., Casey, P. G., Motherway, M. O., & van Sinderen, D. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00964 · Cited by 25 · see citing works
Epigenetic Treatment of Persistent Viral Infections
Moos, W. H., Pinkert, C. A., Irwin, M. H., Faller, D. V., Kodukula, K., Glavas, I. P., & Steliou, K. (2016) · Drug Development Research · doi:10.1002/ddr.21366 · Cited by 25 · see citing works
Sen, S., Rao, B., Wachnowsky, C., & Cowan, J. A. (2018) · Metallomics · doi:10.1039/c8mt00128f · Cited by 24 · see citing works
Adaptation of the late ISC pathway in the anaerobic mitochondrial organelles of Giardia intestinalis
Motyčková, A., Voleman, L., Najdrová, V., Arbonová, L., Benda, M., Dohnálek, V., Janowicz, N. E., Malych, R., Šuťák, R., Ettema, T. J. G., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1010773 · Cited by 23 · see citing works
Metal cofactors trafficking and assembly in the cell: a molecular view
Camponeschi, F., & Banci, L. (2018) · Pure and Applied Chemistry · doi:10.1515/pac-2018-0720 · Cited by 21 · see citing works
Self-citationGenomics of Preaxostyla Flagellates Illuminates the Path Towards the Loss of Mitochondria
Novák, L., Treitli, S. C., Pyrih, J., Hałakuc, P., Pipaliya, S. V., Vacek, V., Brzoň, O., Soukal, P., Eme, L., Dacks, J. B., et al. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1011050 · Cited by 19 · see citing works
UvrC Coordinates an O 2 -Sensitive [4Fe4S] Cofactor
Silva, R. M. B., Grodick, M. A., & Barton, J. K. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c01671 · Cited by 16 · see citing works
ISCA1 Orchestrates ISCA2 and NFU1 in the Maturation of Human Mitochondrial [4Fe-4S] Proteins
Suraci, D., Saudino, G., Nasta, V., Ciofi‐Baffoni, S., & Banci, L. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166924 · Cited by 15 · see citing works
Self-citationTsai, C.-L., & Tainer, J. A. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.11.006 · Cited by 14 · see citing works
Cai, K., & Markley, J. L. (2018) · Molecules · doi:10.3390/molecules23092213 · Cited by 13 · see citing works
Ast, T., Wang, H., Marutani, E., Nagashima, F., Malhotra, R. K., Ichinose, F., & Mootha, V. K. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad091 · Cited by 12 · see citing works
A mathematical model of iron import and trafficking in wild-type and Mrs3/4ΔΔ yeast cells
Wofford, J. D., & Lindahl, P. A. (2019) · BMC Systems Biology · doi:10.1186/s12918-019-0702-2 · Cited by 11 · see citing works
Chasapis, C. T. (2018) · Archives of Microbiology · doi:10.1007/s00203-018-1571-6 · Cited by 10 · see citing works
NMN partially rescues cuproptosis by upregulating sirt2 to increase intracellular NADPH
Zhang, Y., Qiu, S., Shao, S., Cao, Y., Yu, H., Xu, X., Fang, X., Di, C., Yang, J. J., & Tan, X. (2024) · Scientific Reports · doi:10.1038/s41598-024-70245-5 · Cited by 7 · see citing works
Kropp, P. A., Wu, J., Reidy, M. J., Shrestha, S., Rhodehouse, K., Rogers, P. J., Sack, M. N., & Golden, A. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009771 · Cited by 7 · see citing works
Mutations in mitochondrial ferredoxin FDX2 suppress frataxin deficiency
Meisel, J. D., Joshi, P. R., Spelbring, A. N., Wang, H., Wellner, S. M., Wiesenthal, P. P., Miranda, M., McCoy, J. G., Barondeau, D. P., Ruvkun, G., et al. (2025) · Nature · doi:10.1038/s41586-025-09821-2 · Cited by 6 · see citing works
Shangguan, F., Zhou, H., Zhang, H., Thaiyuri, R., Bryan, M. P., Cui, R., Lin, J., Chen, Y., & Zheng, Y. (2025) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2025.111584 · Cited by 4 · see citing works
Shedding Light on the Electron Delocalization Pathway at the [Fe2S2]2+ Cluster of FDX2
Querci, L., Fiorucci, L., Grifagni, D., Costantini, P., Ravera, E., Ciofi‐Baffoni, S., & Piccioli, M. (2025) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5c00420 · Cited by 3 · see citing works
Fujihara, K. M., Zhang, B., Jackson, T. D., Nijiagel, B., Ang, C., Nikolić, I., Sutton, V. R., Trapani, J., Simpson, K. J., Stojanovski, D., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.29.398867 · Cited by 3 · see citing works
Twenty years in metalloprotein bioinformatics: A short history of a long journey
Andreini, C. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112854 · Cited by 2 · see citing works
Self-citationSun, J., Wang, J., & Chen, X. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c19257 · Cited by 2 · see citing works
Iron–Sulfur Protein Maturation in the Cytosol of Eukaryotes
Braymer, J. J., & Pierik, A. J. (2025) · Wiley eBooks · doi:10.1002/9783527843596.ch4 · Cited by 2 · see citing works
Lin, J., Zhou, H., Ma, N., Chen, Y., Chen, Q., Han, S., Yang, H., Zhang, X., & Shangguan, F. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104334 · Cited by 1 · see citing works
Fe-S cluster biosynthesis and maturation: Mass spectrometry-based methods advancing the field
Oney-Hawthorne, S. D., & Barondeau, D. P. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119784 · Cited by 1 · see citing works
Role of VDAC1 hypoxic form, VDAC1-∆C, in the expression of primary cilia and tumor progression
Fabbri, L. (2019) · theses.fr (ABES) · doi:10.70675/7a53239dzc652z4ea4z8b95z4a71961c83b4
- Authors
- Andreini, C., Banci, L., & Rosato, A.
- Affiliations
- University of Florence (IT)
- Corresponding author
- Banci, Lucia
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-03-02
- Volume
- 15
- Issue
- 4
- Pages
- 1308-1322
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2275585418
- Cited by
- 48
- References
- 86
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 4 · 2023: 6 · 2022: 2 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 9 · 2017: 7 · 2016: 4
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Proteome Research (publishedVersion)
- PubMed (publishedVersion)
- Florence Research (University of Florence) (submittedVersion)
- Funders
- Ente Cassa di Risparmio di Firenze (2013/7201)
- Ministero dell'Istruzione, dell'Università e della Ricerca (CTN01_00177_962865)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Keywords
- iron-sulfur proteins, bacterial operons, Fe4S4 cluster, [2Fe-2S] cluster, iron-sulfur cluster assembly, electron transport chain, purine metabolism, reactive oxygen species, apoptosis, comparative genomics
- MeSH terms
- Archaea, Bacteria, Bacterial Proteins, Cell Nucleus, Cytoplasm, Electron Transport, Biological Evolution, Humans, Iron-Sulfur Proteins, Mitochondria, Operon, Ribosomes, Saccharomyces cerevisiae, Species Specificity, User-Computer Interface, Gene Expression, Apoptosis, Arabidopsis, Reactive Oxygen Species, Protein Structure, Secondary, Computational Biology, Structural Homology, Protein
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