CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA

Molecular Cloning: A Laboratory Manual

Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589 · see citing works

Measurement of protein using bicinchoninic acid

Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482 · see citing works

The complete genome sequence of the gram-positive bacterium Bacillus subtilis.

Kunst, F., Ogasawara, N., Moszer, I., Albertini, A. M., Alloni, G., Azevedo, V., Bertero, M. G., Bessières, P., Bolotin, A., Borchert, S., et al. (1997) · Nature · doi:10.1038/36786 · Cited by 3,679 · see citing works

Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide Dismutase

Rae, T., Schmidt, P. J., Pufahl, R. A., Culotta, V., & O’Halloran, T. V. (1999) · Science · doi:10.1126/science.284.5415.805 · Cited by 1,628 · see citing works

The biological chemistry of the elements: the inorganic chemistry of life

(1992) · Choice Reviews Online · doi:10.5860/choice.30-0286 · Cited by 1,326 · see citing works

BACTERIAL HEAVY METAL RESISTANCE: New Surprises

Silver, S. D., & Phung, L. T. (1996) · Annual Review of Microbiology · doi:10.1146/annurev.micro.50.1.753 · Cited by 1,289 · see citing works

The Biological Chemistry of the Elements: The Inorganic Chemistry of Life

Fraústo da Silva, J. J. R., & Williams, R. J. P. (2001) · doi:10.1093/oso/9780198508472.001.0001 · Cited by 1,005 · see citing works

Metallochaperones, an Intracellular Shuttle Service for Metal Ions

O'Halloran, T. V., & Culotta, V. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.r000006200 · Cited by 806 · see citing works

Molecular mechanisms of copper uptake and distribution

Puig, S., & Thiele, D. J. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00298-3 · Cited by 720 · see citing works

A vector for systematic gene inactivation in Bacillus subtilis

Vagner, V., Dervyn, E., & Ehrlich, S. D. (1998) · Microbiology · doi:10.1099/00221287-144-11-3097 · Cited by 640 · see citing works

Antibiotic-resistance cassettes for Bacillus subtilis

Guérout, A.-M., Shazand, K., Frandsen, N., & Stragier, P. (1995) · Gene · doi:10.1016/0378-1119(95)00652-4 · Cited by 595 · see citing works

CopA: An Escherichia coli Cu(I)-translocating P-type ATPase

Rensing, C., Fan, B., Sharma, R., Mitra, B., & Rosen, B. P. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.652 · Cited by 517 · see citing works

CPx-type ATPases: a class of P-type ATPases that pump heavy metals

Solioz, M., & Vulpe, C. D. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)20016-7 · Cited by 478 · see citing works

Molecular basis for resistance to silver cations in Salmonella

Gupta, A. K., Matsui, K., Lo, J., & Silver, S. D. (1999) · Nature Medicine · doi:10.1038/5545 · Cited by 474 · see citing works

The <i>zntA</i> gene of <i>Escherichia coli</i> encodes a Zn(II)-translocating P-type ATPase

Rensing, C., Mitra, B., & Rosen, B. P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14326 · Cited by 419 · see citing works

A Novel Family of Ubiquitous Heavy Metal Ion Transport Proteins

Paulsen, I. T., & Saier, M. H. (1997) · The Journal of Membrane Biology · doi:10.1007/s002329900192 · Cited by 393 · see citing works

Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae

Odermatt, A., Suter, H., Krapf, R., & Solioz, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31455-8 · Cited by 377 · see citing works

Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadmium-efflux ATPase.

Nucifora, G., Chu, L., Misra, T. K., & Silver, S. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3544 · Cited by 359 · see citing works

SCO1 and SCO2 Act as High Copy Suppressors of a Mitochondrial Copper Recruitment Defect in Saccharomyces cerevisiae

Glerum, D. M., Shtanko, A., & Tzagoloff, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20531 · Cited by 323 · see citing works

Intracellular copper routing: the role of copper chaperones

Harrison, M. D., JONES, C., Solioz, M., & Dameron, C. T. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01492-9 · Cited by 260 · see citing works

Crystal structure of the Atx1 metallochaperone protein at 1.02 Å resolution

Rosenzweig, A. C., Huffman, D. L., Hou, M. Y., Wernimont, A. K., Pufahl, R. A., & O’Halloran, T. V. (1999) · Structure · doi:10.1016/s0969-2126(99)80082-3 · Cited by 236 · see citing works

Analysis of Sporulation Mutants II. Mutants Blocked in the Citric Acid Cycle

Fortnagel, P., & Freese, E. (1968) · Journal of Bacteriology · doi:10.1128/jb.95.4.1431-1438.1968 · Cited by 207 · see citing works

Two trans-Acting Metalloregulatory Proteins Controlling Expression of the Copper-ATPases of Enterococcus hirae*

Odermatt, A., & Solioz, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4349 · Cited by 190 · see citing works

Yeast Sco1, a Protein Essential for Cytochrome cOxidase Function Is a Cu(I)-binding Protein

Nittis, T., George, G. N., & Winge, D. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107077200 · Cited by 183 · see citing works

Zinc(II) tolerance in Escherichia coli K‐12: evidence that the zntA gene (o732) encodes a cation transport ATPase

Beard, S. J., Hashim, R., Membrillo‐Hernández, J., Hughes, M., & Poole, R. K. (1997) · Molecular Microbiology · doi:10.1111/j.1365-2958.1997.mmi518.x · Cited by 181 · see citing works

Solution Structure of the Cu(I) and Apo Forms of the Yeast Metallochaperone, Atx1,

Arnesano, F., Banci, L., Bertini, I., Huffman, D. L., & O’Halloran, T. V. (2001) · Biochemistry · doi:10.1021/bi0014711 · Cited by 179 · see citing works

An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter

Thelwell, C., Robinson, N. J., & Turner-Cavet, J. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10728 · Cited by 179 · see citing works

SmtB is a metal-dependent repressor of the cyanobacterial metallothionein genesmtA: identification of a Zn inhibited DNA-protein complex

Morby, A. P., Turner, J. S., Huckle, J. W., & Robinson, N. J. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.4.921 · Cited by 173 · see citing works

The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor

Cobine, P. A., Wickramasinghe, W. A., Harrison, M. D., Weber, T., Solioz, M., & Dameron, C. T. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00091-5 · Cited by 169 · see citing works

Characterization of the Binding Interface between the Copper Chaperone Atx1 and the First Cytosolic Domain of Ccc2 ATPase

Arnesano, F., Banci, L., Bertini, I., Cantini, F., Ciofi‐Baffoni, S., Huffman, D. L., & O’Halloran, T. V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104807200 · Cited by 153 · see citing works

Two Menkes-type ATPases Supply Copper for Photosynthesis inSynechocystis PCC 6803

Tottey, S., Rich, P. R., Rondet, S., & Robinson, N. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011243200 · Cited by 152 · see citing works

Solution Structure of the Yeast Copper Transporter Domain Ccc2a in the Apo and Cu(I)-loaded States

Banci, L., Bertini, I., Ciofi‐Baffoni, S., Huffman, D. L., & O’Halloran, T. V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008389200 · Cited by 137 · see citing works

Cobalt-dependent Transcriptional Switching by a Dual-effector MerR-like Protein Regulates a Cobalt-exporting Variant CPx-type ATPase

Rutherford, J. C., Cavet, J. S., & Robinson, N. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25827 · Cited by 130 · see citing works

NMR Structure and Metal Interactions of the CopZ Copper Chaperone

Wimmer, R., Herrmann, T., Solioz, M., & Kurt Wüthrich, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22597 · Cited by 129 · see citing works

Construction and properties of Tn917-lac, a transposon derivative that mediates transcriptional gene fusions in Bacillus subtilis.

Perkins, J. B., & Youngman, P. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.1.140 · Cited by 114 · see citing works

Copper Trafficking: the Solution Structure of Bacillus subtilis CopZ

Banci, L., Bertini, I., Conte, R. D., Markey, J., & Ruiz-Dueñas, F. J. (2001) · Biochemistry · doi:10.1021/bi0112715 · Cited by 112 · see citing works

Characterization of YpmQ, an Accessory Protein Required for the Expression of Cytochrome c Oxidase in Bacillus subtilis

Mattatall, N. R., Jazairi, J., & Hill, B. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002741200 · Cited by 102 · see citing works

Genes required for cytochrome c synthesis inBacillus subtilis

Brun, N. E. L., Bengtsson, J., & Hederstedt, L. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01883.x · Cited by 102 · see citing works

A Copper Metallochaperone for Photosynthesis and Respiration Reveals Metal-specific Targets, Interaction with an Importer, and Alternative Sites for Copper Acquisition

Tottey, S., Rondet, S., Borrelly, G. P. M., Robinson, P. J., Rich, P. R., & Robinson, N. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m105857200 · Cited by 99 · see citing works

Escherichia coli Soft Metal Ion-translocating ATPases

Gatti, D. L., Mitra, B., & Rosen, B. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.r000012200 · Cited by 84 · see citing works

[38] Molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex

Hederstedt, L. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(86)26040-1 · Cited by 82 · see citing works

Bacillus subtilis CPx-type ATPases: Characterization of Cd, Zn, Co and Cu efflux systems

Gaballa, A., & Helmann, J. D. (2003) · BioMetals · doi:10.1023/a:1023425321617 · Cited by 79 · see citing works

Mutations in the Thiol-Disulfide Oxidoreductases BdbC and BdbD Can Suppress CytochromecDeficiency of CcdA-DefectiveBacillus subtilisCells

Erlendsson, L. S., & Hederstedt, L. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.5.1423-1429.2002 · Cited by 76 · see citing works

Interaction of the CopZ Copper Chaperone with the CopA Copper ATPase of Enterococcus hirae Assessed by Surface Plasmon Resonance

Multhaup, G., Strausak, D., Bissig, K.-D., & Solioz, M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5757 · Cited by 75 · see citing works

Bacillus subtilis chytochrome oxidase mutants: biochemical analysis and genetic evidence for two aa3‐type oxidases

John van der, O. O. S. T., von Wachenfeld, C., Hederstedt, L., & Saraste, M. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb00829.x · Cited by 69 · see citing works

Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states

Banci, L., Bertini, I., Ciofi‐Baffoni, S., D’Onofrio, M., Gonnelli, L., Marhuenda-Egea, F. C., & Ruiz-Dueñas, F. J. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2002.5430 · Cited by 69 · see citing works

Copper-mediated dimerization of CopZ, a predicted copper chaperone from Bacillus subtilis

Kihlken, M. A., Leech, A., & Brun, N. E. L. (2002) · Biochemical Journal · doi:10.1042/bj20021036 · Cited by 58 · see citing works

CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN

Rosenzweig, A. C., Huffman, D. L., Pufahl, M. Y. R. A., Hou, T. V. O., & Wernimont, A. K. (1999) · Worldwide Protein Data Bank · doi:10.2210/pdb1cc7/pdb · Cited by 44 · see citing works

Investigation of the yvgW Bacillus subtilis chromosomal gene involved in Cd 2+ ion resistance

Solovieva, I. M., & Entian, K. (2002) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2002.tb11068.x · Cited by 31 · see citing works

How do bacterial cells ensure that metalloproteins get the correct metal?

Waldron, K. J., & Robinson, N. J. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro2057 · Cited by 835 · see citing works

Copper Metallochaperones

Robinson, N. J., & Winge, D. R. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143539 · Cited by 708 · see citing works

Structural Biology of Copper Trafficking

Boal, A. K., & Rosenzweig, A. C. (2009) · Chemical Reviews · doi:10.1021/cr900104z · Cited by 418 · see citing works

Molecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypes

de Bie, P., Muller, P. A. J., Wijmenga, C., & Klomp, L. W. J. (2007) · Journal of Medical Genetics · doi:10.1136/jmg.2007.052746 · Cited by 391 · see citing works

Coordination chemistry of copper proteins: How nature handles a toxic cargo for essential function

Rubino, J. T., & Franz, K. J. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.11.024 · Cited by 369 · see citing works

Response of Gram-positive bacteria to copper stress

Solioz, M., Abicht, H. K., Mermod, M., & Mancini, S. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0588-3 · Cited by 221 · see citing works

Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake.

Achila, D., Banci, L., Bertini, I., Bunce, J., Ciofi-Baffoni, S., & Huffman, D. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504472103 · Cited by 169 · see citing works

Copper Homeostasis in Bacteria

Osman, D., & Cavet, J. S. (2008) · Advances in applied microbiology · doi:10.1016/s0065-2164(08)00608-4 · Cited by 166 · see citing works

Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity

Cassat, J. E., & Skaar, E. P. (2012) · Seminars in Immunopathology · doi:10.1007/s00281-011-0294-4 · Cited by 155 · see citing works

Copper Transport and Trafficking at the Host–Bacterial Pathogen Interface

Fu, Y., Chang, F.-M. J., & Giedroc, D. P. (2014) · Accounts of Chemical Research · doi:10.1021/ar500300n · Cited by 146 · see citing works

Toxicity effects on metal sequestration by microbially-induced carbonate precipitation

Mugwar, A., & Harbottle, M. (2016) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2016.04.039 · Cited by 147 · see citing works

CsoR regulates the copper efflux operon copZA in Bacillus subtilis

Smaldone, G. T., & Helmann, J. D. (2007) · Microbiology · doi:10.1099/mic.0.2007/011742-0 · Cited by 132 · see citing works

The copper supply pathway to a S almonella C u, Z n‐superoxide dismutase ( SodCII ) involves P 1 B ‐type ATPase copper efflux and periplasmic CueP

Osman, D., Patterson, C. J., Bailey, K. L., Fisher, K., Robinson, N. J., Rigby, S. E. J., & Cavet, J. S. (2012) · Molecular Microbiology · doi:10.1111/mmi.12107 · Cited by 108 · see citing works

Cyanobacterial metallochaperone inhibits deleterious side reactions of copper

Tottey, S., Patterson, C. J., Banci, L., Bertini, I., Felli, I. C., Pavelkova, A., Dainty, S. J., Pernil, R., Waldron, K. J., Foster, A. W., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117515109 · Cited by 97 · see citing works

The combined actions of the copper‐responsive repressor CsoR and copper‐metallochaperone CopZ modulate CopA‐mediated copper efflux in the intracellular pathogen Listeria monocytogenes

Corbett, D., Schuler, S., Glenn, S. M., Andrew, P. W., Cavet, J. S., & Roberts, I. S. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07705.x · Cited by 89 · see citing works

Perspectives in Inorganic Structural Genomics: A Trafficking Route for Copper

Arnesano, F., Banci, L., Bertini, I., & Ciofi‐Baffoni, S. (2004) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.200300841 · Cited by 80 · see citing works

Molecular characterization of the copper transport system in Staphylococcus aureus

Sitthisak, S., Knutsson, L., Webb, J. W., & Jayaswal, R. K. (2007) · Microbiology · doi:10.1099/mic.0.2007/009860-0 · Cited by 74 · see citing works

Regulation of copper homeostasis in Pseudomonas fluorescens SBW25

Zhang, X., & Rainey, P. B. (2008) · Environmental Microbiology · doi:10.1111/j.1462-2920.2008.01720.x · Cited by 64 · see citing works

Microbial copper resistance: importance in biohydrometallurgy

Martínez‐Bussenius, C., Navarro, C. A., & Jerez, C. A. (2016) · Microbial Biotechnology · doi:10.1111/1751-7915.12450 · Cited by 64 · see citing works

Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity

Vita, N., Landolfi, G., Baslé, A., Platsaki, S., Lee, J., Waldron, K. J., & Dennison, C. (2016) · Scientific Reports · doi:10.1038/srep39065 · Cited by 62 · see citing works

High Cu(I) and low proton affinities of the CXXC motif of Bacillus subtilis CopZ

Zhou, L., Singleton, C., & Brun, N. E. L. (2008) · Biochemical Journal · doi:10.1042/bj20080467 · Cited by 61 · see citing works

Trace Metal Acquisition by Marine Heterotrophic Bacterioplankton with Contrasting Trophic Strategies

Hogle, S., Thrash, J. C., Dupont, C. L., & Barbeau, K. A. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.03128-15 · Cited by 60 · see citing works

Comparative transcriptome analysis of the biocontrol strain Bacillus amyloliquefaciens FZB42 as response to biofilm formation analyzed by RNA sequencing

Kröber, M., Verwaaijen, B., Wibberg, D., Winkler, A., Pühler, A., & Schlüter, A. (2016) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2016.06.013 · Cited by 60 · see citing works

The delivery of copper for thylakoid import observed by NMR

Banci, L., Bertini, I., Ciofi‐Baffoni, S., Kandias, N. G., Robinson, N. J., Spyroulias, G. A., Su, X., Tottey, S., & Vanarotti, M. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600142103 · Cited by 60 · see citing works

Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer

Singleton, C., & Brun, N. E. L. (2007) · BioMetals · doi:10.1007/s10534-006-9068-1 · Cited by 58 · see citing works

Structural Basis for the Function of the N-terminal Domain of the ATPase CopA from Bacillus subtilis

Banci, L., Bertini, I., Ciofi‐Baffoni, S., Gonnelli, L., & Su, X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307389200 · Cited by 54 · see citing works

Solution Structures of a Cyanobacterial Metallochaperone

Banci, L., Bertini, I., Ciofi‐Baffoni, S., Su, X., Borrelly, G. P. M., & Robinson, N. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402005200 · Cited by 54 · see citing works

The copBL operon protects Staphylococcus aureus from copper toxicity: CopL is an extracellular membrane–associated copper-binding protein

Rosario‐Cruz, Z., Eletsky, A., Daigham, N. S., Al‐Tameemi, H., Swapna, G. V. T., Kahn, P. C., Szyperski, T., Montelione, G. T., & Boyd, J. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004723 · Cited by 52 · see citing works

New insights into the mechanisms of acetic acid resistance in Acetobacter pasteurianus using iTRAQ-dependent quantitative proteomic analysis

Xia, K., Zang, N., Zhang, J., Zhang, H., Li, Y., Liu, Y., Feng, W., & Liang, X. (2016) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2016.09.016 · Cited by 48 · see citing works

Predicting metals sensed by ArsR‐SmtB repressors: allosteric interference by a non‐effector metal

Harvie, D. R., Andreini, C., Cavallaro, G., Meng, W., Connolly, B. A., Yoshida, K., Fujita, Y., Harwood, C. R., Radford, D. S., Tottey, S., et al. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05029.x · Cited by 46 · see citing works

The interplay of the metallosensor CueR with two distinct CopZ chaperones defines copper homeostasis in Pseudomonas aeruginosa

Novoa‐Aponte, L., Ramírez, D., & ARGÜELLO, J. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006316 · Cited by 46 · see citing works

Characterization of a Multicopper Oxidase Gene from Staphylococcus aureus

Sitthisak, S., Howieson, K., Amezola, C., & Jayaswal, R. K. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.9.5650-5653.2005 · Cited by 45 · see citing works

Metal Sensing in Salmonella

Osman, D., & Cavet, J. S. (2011) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/b978-0-12-381043-4.00005-2 · Cited by 41 · see citing works

Proteomic responses to gold( iii )-toxicity in the bacterium Cupriavidus metallidurans CH34

Zammit, C. M., Weiland, F., Brugger, J., Wade, B. P., Winderbaum, L., Nies, D. H., Southam, G., Hoffmann, P., & Reith, F. (2016) · Metallomics · doi:10.1039/c6mt00142d · Cited by 37 · see citing works

Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon

Gaballa, A., Cao, M., & Helmann, J. D. (2003) · Microbiology · doi:10.1099/mic.0.26225-0 · Cited by 36 · see citing works

Structure and Cu(I)-binding properties of the N-terminal soluble domains of Bacillus subtilis CopA

Singleton, C., Banci, L., Ciofi‐Baffoni, S., Tenori, L., Kihlken, M. A., Boetzel, R., & Brun, N. E. L. (2008) · Biochemical Journal · doi:10.1042/bj20071620 · Cited by 36 · see citing works

Distinct functions of serial metal‐binding domains in the E scherichia coli P 1 B ‐ ATP ase CopA

Drees, S. L., Beyer, D. F., Lenders‐Lomscher, C., & Lübben, M. (2015) · Molecular Microbiology · doi:10.1111/mmi.13038 · Cited by 35 · see citing works

Transcriptome and Volatilome Analysis During Growth of Brochothrix thermosphacta in Food: Role of Food Substrate and Strain Specificity for the Expression of Spoilage Functions

Illikoud, N., Gohier, R., Werner, D., Barrachina, C., Roche, D., Jaffrès, E., & Zagorec, M. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02527 · Cited by 34 · see citing works

The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity

Okkeri, J., & Haltia, T. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.06.008 · Cited by 34 · see citing works

Copper tolerance in Frankia sp. strain EuI1c involves surface binding and copper transport

Rehan, M., Furnholm, T., Finethy, R., Feixia Chu, C., El-Fadly, G., & Tisa, L. S. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5849-6 · Cited by 31 · see citing works

Metabolic Rearrangements Causing Elevated Proline and Polyhydroxybutyrate Accumulation During the Osmotic Adaptation Response of Bacillus megaterium

Godard, T., Zühlke, D., Richter, G., Wall, M., Rohde, M., Riedel, K., Poblete‐Castro, I., Krull, R., & Biedendieck, R. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00047 · Cited by 30 · see citing works

Copper Resistance Promotes Fitness of Methicillin-Resistant Staphylococcus aureus during Urinary Tract Infection

Saenkham, P., Hyre, A. N., Hanson, B. S., Donati, G. L., Adams, L. G., Ryan, C., Londoño, A., Moustafa, A. M., Planet, P. J., & Subashchandrabose, S. (2021) · mBio · doi:10.1128/mbio.02038-21 · Cited by 30 · see citing works

Cytoplasmic CopZ-Like Protein and Periplasmic Rusticyanin and AcoP Proteins as Possible Copper Resistance Determinants in Acidithiobacillus ferrooxidans ATCC 23270

Navarro, C. A., von Bernath, D., Martínez‐Bussenius, C., Castillo, R. A. M., & Jerez, C. A. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.02810-15 · Cited by 30 · see citing works

Mass spectrometry of B. subtilis CopZ: Cu( i )-binding and interactions with bacillithiol

Kay, K. L., Hamilton, C. J., & Brun, N. E. L. (2016) · Metallomics · doi:10.1039/c6mt00036c · Cited by 29 · see citing works

Testing the Capacity of Staphylococcus equorum for Calcium and Copper Removal through MICP Process

Sepúlveda, S., Duarte-Nass, C., Rivas, M., Azócar, L., Ramirez-Madrid, A., Toledo-Alarcón, J., Gutiérrez, L., Jeison, D., & Torres-Aravena, Á. (2021) · Minerals · doi:10.3390/min11080905 · Cited by 29 · see citing works

Responses of Lactic Acid Bacteria to Heavy Metal Stress

Solioz, M., Mermod, M., Abicht, H. K., & Mancini, S. (2011) · Springer eBooks · doi:10.1007/978-0-387-92771-8_9 · Cited by 29 · see citing works

Mechanistic insights into Cu(I) cluster transfer between the chaperone CopZ and its cognate Cu(I)-transporting P-type ATPase, CopA

Singleton, C., Hearnshaw, S. J., Zhou, L., Brun, N. E. L., & Hemmings, A. M. (2009) · Biochemical Journal · doi:10.1042/bj20091079 · Cited by 28 · see citing works

ARMC Subfamily: Structures, Functions, Evolutions, Interactions, and Diseases

Huang, Y., Jiang, Z., Gao, X., Luo, P., & Jiang, X. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.791597 · Cited by 28 · see citing works

A novel copper site in a cyanobacterial metallochaperone

Borrelly, G. P. M., Blindauer, C. A., Schmid, R., Butler, C. S., Cooper, C. E., Harvey, I., Sadler, P. J., & Robinson, N. J. (2004) · Biochemical Journal · doi:10.1042/bj20031669 · Cited by 28 · see citing works

The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbb3 oxidase assembly

Utz, M., Andrei, A., Milanov, M., Trasnea, P., Marckmann, D., Daldal, F., & Koch, H. (2018) · Molecular Microbiology · doi:10.1111/mmi.14190 · Cited by 27 · see citing works

Transcriptome analysis reveals manganese tolerance mechanisms in a novel native bacterium of Bacillus altitudinis strain HM-12

Huo, Y., Mo, J., He, Y., Twagirayezu, G., & Xue, L. (2022) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2022.157394 · Cited by 26 · see citing works

Metal Ion Homeostasis in Listeria monocytogenes and Importance in Host–Pathogen Interactions

Jesse, H. E., Roberts, I. S., & Cavet, J. S. (2014) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2014.08.003 · Cited by 24 · see citing works

The YcnI protein from Bacillus subtilis contains a copper-binding domain

Damle, M. S., Singh, A. N., Peters, S. C., Szalai, V. A., & Fisher, O. S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101078 · Cited by 21 · see citing works

Sequence-Based Functional Metagenomics Reveals Novel Natural Diversity of Functional CopA in Environmental Microbiomes

Li, W.-J., Wang, L., Li, X., Zheng, X. S., Cohen, M. F., & Liu, Y. (2022) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2022.08.006 · Cited by 19 · see citing works

Distinct characteristics of Ag+ and Cd2+ binding to CopZ from Bacillus subtilis

Kihlken, M. A., Singleton, C., & Brun, N. E. L. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0388-1 · Cited by 19 · see citing works

Hospital sink traps as a potential source of the emerging multidrug-resistant pathogen Cupriavidus pauculus: characterization and draft genome sequence of strain MF1

Butler, J. A., Kelly, S. D., Muddiman, K. J., Besinis, A., & Upton, M. (2022) · Journal of Medical Microbiology · doi:10.1099/jmm.0.001501 · Cited by 19 · see citing works

Understanding How Cells Allocate Metals

Tottey, S., Harvie, D. R., & Robinson, N. J. (2007) · Springer eBooks · doi:10.1007/7171_2006_072 · Cited by 19 · see citing works

The N-terminal soluble domains of Bacillus subtilis CopA exhibit a high affinity and capacity for Cu( i ) ions

Singleton, C., & Brun, N. E. L. (2008) · Dalton Transactions · doi:10.1039/b810412c · Cited by 19 · see citing works

A copper-responsive gene cluster is required for copper homeostasis and contributes to oxidative resistance in Deinococcus radiodurans R1

Zhao, Z., Zhou, Z., Li, L., Xian, X., Ke, X., Chen, M., & Zhang, Y. (2014) · Molecular BioSystems · doi:10.1039/c4mb00320a · Cited by 18 · see citing works

Functional Diversity of Bacterial Strategies to Cope With Metal Toxicity

Gillet, S., Lawarée, E., & Matroule, J. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-814849-5.00023-x · Cited by 18 · see citing works

An Italian contribution to structural genomics: Understanding metalloproteins

Arnesano, F., Banci, L., Bertini, I., Capozzi, F., Ciofi‐Baffoni, S., Ciurli, S., Luchinat, C., Mangani, S., Rosato, A., Turano, P., et al. (2006) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2006.01.008 · Cited by 18 · see citing works

Membrane Transporters Involved in the Antimicrobial Activities of Pyrithione in Escherichia coli

Salcedo-Sora, J. E., Robison, A. T. R., Zaengle-Barone, J. M., Franz, K. J., & Kell, D. B. (2021) · Molecules · doi:10.3390/molecules26195826 · Cited by 17 · see citing works

Copper Tolerance Mechanism of the Novel Marine Multi-Stress Tolerant Yeast Meyerozyma guilliermondii GXDK6 as Revealed by Integrated Omics Analysis

Bu, R., Yan, B., Sun, H., Zhou, M., Bai, H., Cai, X., Mo, X., Su, G., & Jiang, C. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.771878 · Cited by 17 · see citing works

Streamlined copper defenses make Bordetella pertussis reliant on custom-made operon

Rivera-Millot, A., Slupek, S., Chatagnon, J., Roy, G., Saliou, J., Gabriel Billon, A., Alaimo, V., Hot, D., Salomé‐Desnoulez, S., Locht, C., et al. (2021) · Communications Biology · doi:10.1038/s42003-020-01580-2 · Cited by 17 · see citing works

Determinants of Copper Resistance in Acidithiobacillus Ferrivorans ACH Isolated from the Chilean Altiplano

Barahona, S., Castro‐Severyn, J., Dorador, C., Saavedra, C. P., & Remonsellez, F. (2020) · Genes · doi:10.3390/genes11080844 · Cited by 16 · see citing works

Copper trafficking in biology: An NMR approach

Banci, L., Bertini, I., & Ciofi‐Baffoni, S. (2009) · HFSP journal · doi:10.2976/1.3078306 · Cited by 16 · see citing works

Kinetic analysis of copper transfer from a chaperone to its target protein mediated by complex formation

Kay, K. L., Zhou, L., Tenori, L., Bradley, J. M., Singleton, C., Kihlken, M. A., Ciofi‐Baffoni, S., & Brun, N. E. L. (2017) · Chemical Communications · doi:10.1039/c6cc08966f · Cited by 15 · see citing works

Tuning of Copper-Loop Flexibility in Bacillus subtilis CopZ Copper Chaperone: Role of Conserved Residues

Rodriguez-Granillo, A., & Wittung-Stafshede, P. E. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp807594q · Cited by 15 · see citing works

Metalloregulation inBacillus subtilis: thecopZchromosomal gene is involved in cadmium resistance

Solovieva, I. M., & Entian, K. (2004) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2004.tb09636.x · Cited by 14 · see citing works

Functional characterization of a cadmium resistance operon in Staphylococcus aureus ATCC12600: CadC does not function as a repressor

Hoogewerf, A. J., Dyk, L. A. V., Buit, T. S., Roukema, D., Resseguie, E. A., Rosenberger, C. L., Le, N., Heeringa, L. P., & Griend, D. A. V. (2014) · Journal of Basic Microbiology · doi:10.1002/jobm.201400498 · Cited by 12 · see citing works

Cd2+‐ or Hg2+‐binding proteins can replace the Cu+‐chaperone Atx1 in delivering Cu+ to the secretory pathway in yeast

Morin, I., Cuillel, M., Lowe, J., Crouzy, S., Guillain, F., & Mintz, E. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.008 · Cited by 13 · see citing works

Metalloregulation in Bacillus subtilis: the copZ chromosomal gene is involved in cadmium resistance

Solovieva, I. M. (2004) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2004.05.031 · Cited by 13 · see citing works

YtkA (CtaK) and YozB (CtaM) function in the biogenesis of cytochrome c oxidase in Bacillus subtilis

von Wachenfeldt, C., Hällgren, J., & Hederstedt, L. (2021) · Molecular Microbiology · doi:10.1111/mmi.14701 · Cited by 12 · see citing works

Mass spectrometric studies of Cu(I)-binding to the N-terminal domains of B. subtilis CopA and influence of bacillithiol

Kay, K. L., Hamilton, C. J., & Brun, N. E. L. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.10.004 · Cited by 12 · see citing works

Genomic Insights Into Cadmium Resistance of a Newly Isolated, Plasmid-Free Cellulomonas sp. Strain Y8

Chen, J., Wang, L., Li, W., Zheng, X. S., & Li, X. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.784575 · Cited by 10 · see citing works

Copper delivery to an endospore coat protein of Bacillus subtilis

Lee, J., Dalton, R. A., & Dennison, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.916114 · Cited by 11 · see citing works

Cu(I)‐ and proton‐binding properties of the first N‐terminal soluble domain of Bacillus subtilis CopA

Zhou, L., Singleton, C., Hecht, O., Moore, G. R., & Brun, N. E. L. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08422.x · Cited by 11 · see citing works

Copper homeostasis-related genes in three separate transcriptional units regulated by CsoR in Corynebacterium glutamicum

Teramoto, H., Yukawa, H., & Inui, M. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-015-6373-z · Cited by 11 · see citing works

Copper Disposition in Bacteria

Solioz, M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-810532-0.00011-2 · Cited by 11 · see citing works

Mechanism of resistance focusing on copper, mercury and arsenic in extremophilic organisms, how acidophiles and thermophiles cope with these metals

Norambuena, J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818322-9.00003-4 · Cited by 10 · see citing works

CopAb, the second N-terminal soluble domain of Bacillus subtilis CopA, dominates the Cu(i)-binding properties of CopAab

Zhou, L., Singleton, C., & Brun, N. E. L. (2012) · Dalton Transactions · doi:10.1039/c2dt30126a · Cited by 10 · see citing works

Structural insight into the distinct properties of copper transport by the Helicobacter pylori CopP protein

Park, S. J., Jung, Y., Kim, J., Seo, M., & Lee, B. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21957 · Cited by 8 · see citing works

Copper Efflux System Required in Murine Lung Infection by Haemophilus influenzae Composed of a Canonical ATPase Gene and Tandem Chaperone Gene Copies

Wong, S. M. S., Gawronski, J. D., & Akerley, B. J. (2023) · Infection and Immunity · doi:10.1128/iai.00091-23 · Cited by 7 · see citing works

Stenotrophomonas pavanii MY01 induces phosphate precipitation of Cu(II) and Zn(II) by degrading glyphosate: performance, pathway and possible genes involved

Zhao, S., Xu, Z., & Wang, J. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1479902 · Cited by 3 · see citing works

Copper in Prokaryotes

Brun, N. E. L. (2014) · Royal Society of Chemistry eBooks · doi:10.1039/9781849739979-00461 · Cited by 2 · see citing works

Eco-friendly decolorization of synthetic dyes using radiation-induced whole cell biocatalyst with enhanced copper resistance

Jeon, M. S., Jeong, S., Yang, S.-K., Jung, K., Gong, G., Ahn, J. H., Seo, M., Lim, S., & Jung, J. (2025) · Environmental Research · doi:10.1016/j.envres.2025.120891 · Cited by 1 · see citing works

Pathways of copper import and utilization that support respiration in Bacillus subtilis

Barnes, G. J., Hederstedt, L., Fisher, O. S., von Wachenfeldt, C., & Helmann, J. D. (2026) · mBio · doi:10.1128/mbio.01069-26 · Cited by 1 · see citing works

Functional Diversity of Bacterial Systems for Metal Homeostasis

Cherry, P., Gillet, S., & Matroule, J. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-13320-6.00040-8 · Cited by 1 · see citing works

Heavy Metal ATPases from Archaeabacteria to Plants

Orofino, M. J. (2006) · Digital WPI

Intracellular copper storage and delivery in a bacteriumPreprint

Lee, J., & Dennison, C. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.05.475036

Copper resistance and genetic determinants in C hilean strains of Clavibacter michiganensis the causal agent of bacterial canker of tomato

Valenzuela, M. P., Vásconez, I. N., Méndez, V., Fuentes, B., Altimira, F., Valdés, F., Montenegro, I., Besoain, X. A., & Seeger, M. (2026) · Pest Management Science · doi:10.1002/ps.70665

Caractérisation des mécanismes d'altération des produits camés et de la mer par Brochothrix thermosphacta

Illikoud, N. (2018) · doi:10.70675/87aeee1dz5b2fz4f91za77bz49f4ab9da97b

Étude d'une nouvelle classe de métallochaperons impliqués dans la résistance à l'intoxication par les métaux chez Mycobacterium tuberculosis

Boudehen, Y. (2020) · doi:10.70675/4aae412fz4269z4058zb0e9zbf70d71e9d7a

Mécanismes de l’homéostasie du cuivre chez un pathogène strictement humain, Bordetella pertussis

Rivera-Millot, A. (2020) · doi:10.70675/2af44bf7ze41ez41ecz9697z81ed156fc7d6

Caractérisation de l'activité antimicrobienne du laiton AB+®

Dauvergne, E. (2021) · theses.fr (ABES) · doi:10.70675/48d2c12cz0ae1z4d0az82caz0becb61c014f

Pan-genomic analysis reveals ecological adaptation and biocontrol of Bacillus pumilus

Adjei, M. O., Guan, C., Dilshad, A., & Fan, B. (2026) · Journal of Plant Physiology · doi:10.1016/j.jplph.2026.154834

Genome-based identification of heavy metal resistance-associated genes in Bacillus enclensis ABF750 isolated from the polluted sediment of Versova Creek

Fulke, A. B., Sharma, N., Sonker, S., & Nadekar, J. S. (2026) · BioMetals · doi:10.1007/s10534-026-00845-3

Regulation of the Staphylococcus aureus stress response pathway by copper ions

Xiong, Y., Lǚ, K., Lu, Y., Wang, J., Huang, X., Zhao, H., Wang, J., He, M., Lin, W., Mao, Z., et al. (2026) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2026.113441

The molecular basis of the interactions of copper metallochaperones

Aggarwal, S. (2011)

CopZ Cu-metallochaperone from Bacillus subtilis interacts in vivo with Cu-induced Cu-exporter CopA, but enhances Cu atoms per cell

Radford, D., Kihlken, M., Borrelly, G. P. M., Harwood, C. R., Le, B. N., Robinson, N., & Cavet, J. (2003) · Newcastle University ePrints (Newcastle Univesity) · doi:10.25405/ncl.34136304

Understanding Copper Trafficking in Bacteria:  Interaction between the Copper Transport Protein CopZ and the N-Terminal Domain of the Copper ATPase CopA from <i>Bacillus subtilis</i>

Banci, L., Bertini, I., Ciofi-Baffoni, S., Del Conte, R., & Gonnelli, L. (2003) · Biochemistry · doi:10.1021/bi027096p · Cited by 85 · see citing works

Metalloregulation inBacillus subtilis: thecopZchromosomal gene is involved in cadmium resistance

Solovieva, I. M., & Entian, K. (2004) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2004.tb09636.x · Cited by 14 · see citing works

Copper Transfer from the Cu(I) Chaperone, CopZ, to the Repressor, Zn(II)CopY: Metal Coordination Environments and Protein Interactions

Cobine, P. A., George, G. N., Jones, C. E., Wickramasinghe, W. A., Solioz, M., & Dameron, C. T. (2002) · Biochemistry · doi:10.1021/bi025515c · Cited by 137 · see citing works

High Cu(I) and low proton affinities of the CXXC motif of Bacillus subtilis CopZ

Zhou, L., Singleton, C., & Brun, N. E. L. (2008) · Biochemical Journal · doi:10.1042/bj20080467 · Cited by 61 · see citing works