Every reference with a DOI in the deposited reference list resolved to a known
work in Crossref or DataCite at the dated check, and none carried a retraction,
withdrawal, or removal notice.
The 180 checked references that resolve
resolves10.2307/2412962The Evolution of Iron-Sulfur Protein Containing Organisms
resolves10.1073/pnas.0812808106The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
resolves10.1128/AEM.07368-11Silver(I), Mercury(II), Cadmium(II), and Zinc(II) Target Exposed Enzymic Iron-Sulfur Clusters when They Toxify Escherichia coli
resolves10.1039/c1mt00107hCopper toxicity and the origin of bacterial resistance—new insights and applications
resolves10.1007/s10534-010-9404-3The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function
resolves10.1128/mBio.00293-11Novel Transporter Required for Biogenesis of
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<sup>+</sup>
chaperones directly transfer Cu
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resolves10.1073/pnas.0900666106A P-type ATPase importer that discriminates between essential and toxic transition metals
resolves10.1016/j.biortech.2011.09.050Influence of sludge retention time on tolerance of copper toxicity for polyphosphate accumulating organisms linked to polyhydroxyalkanoates metabolism and phosphate removal
resolves10.1007/s10534-011-9510-xThe copper-inducible ComR (YcfQ) repressor regulates expression of ComC (YcfR), which affects copper permeability of the outer membrane of Escherichia coli
resolves10.1046/j.1365-2958.1999.01626.xIdentification and characterization of a <i>Streptococcus pyogenes</i> ABC transporter with multiple specificity for metal cations
resolves10.1021/ic070107oConserved Mechanism of Copper Binding and Transfer. A Comparison of the Copper-Resistance Proteins PcoC from <i>Escherichia coli</i> and CopC from <i>Pseudomonas syringae</i>
resolves10.1021/ja034112cA Strategy for the NMR Characterization of Type II Copper(II) Proteins: the Case of the Copper Trafficking Protein CopC from<i>Pseudomonas</i><i>S</i><i>yringae</i>
resolves10.1073/pnas.0636904100A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites
resolves10.1128/JB.01616-08Copper Acquisition Is Mediated by YcnJ and Regulated by YcnK and CsoR in
<i>Bacillus subtilis</i>
resolves10.1128/aem.59.5.1671-1674.1993Copper Hypersensitivity and Uptake in
<i>Pseudomonas syringae</i>
Containing Cloned Components of the Copper Resistance Operon
resolves10.1093/nar/25.17.3389Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
resolves10.1007/s12275-008-0278-9Molecular analysis of the copper-responsive CopRSCD of a pathogenic Pseudomonas fluorescens strain
resolves10.1016/j.bbamem.2010.07.008The interplay between siderophore secretion and coupled iron and copper transport in the heterocyst-forming cyanobacterium Anabaena sp. PCC 7120
resolves10.1006/bbrc.2001.5474CueO Is a Multi-copper Oxidase That Confers Copper Tolerance in Escherichia coli
resolves10.1371/journal.pone.0001378Comparative Genomic Analyses of Copper Transporters and Cuproproteomes Reveal Evolutionary Dynamics of Copper Utilization and Its Link to Oxygen
resolves10.1021/pr049862fOrtholog Search of Proteins Involved in Copper Delivery to Cytochrome<i>c</i>Oxidase and Functional Analysis of Paralogs and Gene Neighbors by Genomic Context
resolves10.1021/ja910759vAnatomy of a Red Copper Center: Spectroscopic Identification and Reactivity of the Copper Centers of <i>Bacillus subtilis</i> Sco and Its Cys-to-Ala Variants
resolves10.1007/s00775-010-0725-zThe essential role of the Cu(II) state of Sco in the maturation of the CuA center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis Sco
resolves10.1021/bi901480gH135A Controls the Redox Activity of the Sco Copper Center. Kinetic and Spectroscopic Studies of the His135Ala Variant of <i>Bacillus subtilis</i> Sco
resolves10.1007/s00775-009-0590-9Multicopper oxidases: a workshop on copper coordination chemistry, electron transfer, and metallophysiology
resolves10.1002/tcr.20125Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
resolves10.1128/AEM.01757-09LccA, an Archaeal Laccase Secreted as a Highly Stable Glycoprotein into the Extracellular Medium by
<i>Haloferax volcanii</i>
resolves10.1073/pnas.052710499Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in
<i>Escherichia coli</i>
resolves10.1021/ja9091903Reaction Mechanisms of the Multicopper Oxidase CueO from <i>Escherichia coli</i> Support Its Functional Role as a Cuprous Oxidase
resolves10.1128/IAI.01208-09The Multi-Copper-Ion Oxidase CueO of
<i>Salmonella enterica</i>
Serovar Typhimurium Is Required for Systemic Virulence
resolves10.1110/ps.9.8.1439Blue copper proteins: A comparative analysis of their molecular interaction properties
resolves10.1021/bi971797iCrystal Structures of the Copper-Containing Amine Oxidase from <i>Arthrobacter globiformis</i> in the Holo and Apo Forms: Implications for the Biogenesis of Topaquinone<sup>,</sup>
resolves10.1046/j.1365-2958.1997.4801846.xCopper‐dependent reciprocal transcriptional regulation of methane monooxygenase genes in <i>Methylococcus capsulatus</i> and <i>Methylosinus trichosporium</i>
resolves10.1073/pnas.0702879104Methane monooxygenase gene expression mediated by methanobactin in the presence of mineral copper sources
resolves10.1038/nature03311Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
resolves10.1021/bi800598hThe Metal Centers of Particulate Methane Monooxygenase from <i>Methylosinus trichosporium</i> OB3b
resolves10.1021/bi200801zCrystal Structure and Characterization of Particulate Methane Monooxygenase from <i>Methylocystis</i> species Strain M
resolves10.1515/BC.2009.085A soluble form of ammonia monooxygenase in <i>Nitrosomonas europaea</i>
resolves10.1007/s10534-010-9308-2Electron paramagnetic studies of the copper and iron containing soluble ammonia monooxygenase from Nitrosomonas europaea
resolves10.1038/ismej.2012.40Diversity, abundance and expression of nitrite reductase (
<i>nirK</i>
)-like genes in marine thaumarchaea
resolves10.1021/cr0006627Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NO<i><sub>x</sub></i> Redox Chemistry
resolves10.1021/bi001811iThe Catalytic Center in Nitrous Oxide Reductase, Cu<sub>Z</sub>, Is a Copper−Sulfide Cluster
resolves10.1042/BJ20020782Crystal structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 A resolution
resolves10.1128/JB.185.3.887-896.2003Requirements for Cu
<sub>A</sub>
and Cu-S Center Assembly of Nitrous Oxide Reductase Deduced from Complete Periplasmic Enzyme Maturation in the Nondenitrifier
<i>Pseudomonas putida</i>
resolves10.1038/nature10332N2O binding at a [4Cu:2S] copper–sulphur cluster in nitrous oxide reductase
resolves10.1099/mic.0.28724-0Molecular characterization of a conserved archaeal copper resistance (cop) gene cluster and its copper-responsive regulator in Sulfolobus solfataricus P2
resolves10.1021/bi201418kBacterial Transition Metal P<sub>1B</sub>-ATPases: Transport Mechanism and Roles in Virulence
resolves10.1111/j.1472-765X.2010.02832.xNovel polymerase chain reaction primers for the specific detection of bacterial copper P-type ATPases gene sequences in environmental isolates and metagenomic DNA
resolves10.1006/bbrc.1994.1891Induction of the Putative Copper ATPases, CopA and Copb, of Enterococcus hirae by Ag+ and Cu2+, and Ag+ Extrusion by CopB
resolves10.1021/bi027096pUnderstanding 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>
resolves10.1038/5545Molecular basis for resistance to silver cations in Salmonella
resolves10.1099/00221287-147-4-965The product of the ybdE gene of the Escherichia coli chromosome is involved in detoxification of silver ions
resolves10.1021/bi050827bA Novel Copper-Binding Fold for the Periplasmic Copper Resistance Protein CusF<sup>,</sup>
resolves10.1021/bi0612622Periplasmic Metal-Resistance Protein CusF Exhibits High Affinity and Specificity for Both Cu<sup>I</sup> and Ag<sup>I</sup>
resolves10.1110/ps.073021307Unusual Cu(I)/Ag(I) coordination of <i>Escherichia coli</i> CusF as revealed by atomic resolution crystallography and X‐ray absorption spectroscopy
resolves10.1007/s00775-009-0503-yTryptophan Cu(I)–π interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF
resolves10.1021/bi102012jInteractions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
resolves10.1021/bi801638mDirect Metal Transfer between Periplasmic Proteins Identifies a Bacterial Copper Chaperone
resolves10.1038/35016007Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
resolves10.1038/nature09395Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport
resolves10.1038/nature09743Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli
resolves10.1128/JB.01323-10Switch or Funnel: How RND-Type Transport Systems Control Periplasmic Metal Homeostasis
resolves10.1107/S1744309111010645Crystallization and preliminary X-ray crystallographic analysis of<i>Salmonella</i>Typhimurium CueP
resolves10.1128/JB.00159-11PtrA Is a Periplasmic Protein Involved in Cu Tolerance in Pseudomonas aeruginosa
resolves10.1099/mic.0.28593-0Transcriptomic and proteomic analyses of the pMOL30-encoded copper resistance in Cupriavidus metallidurans strain CH34
resolves10.1021/bi060328qCopH from <i>Cupriavidus metallidurans </i>CH34. A Novel Periplasmic Copper-Binding Protein
resolves10.1007/s00203-004-0670-8Identification of a regulatory pathway that controls the heavy-metal resistance system Czc via promoter czcNp in Ralstonia metallidurans
resolves10.1021/bi100001zEvidence for Conformational Changes upon Copper Binding to <i>Cupriavidus metallidurans</i> CzcE
resolves10.1073/pnas.88.20.8915Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins.
resolves10.1016/S0378-1119(00)00509-6Control of copper homeostasis in Escherichia coli by a P-type ATPase, CopA, and a MerR-like transcriptional activator, CopR
resolves10.1099/00221287-148-9-2857Molecular characterization of an operon, cueAR, encoding a putative P1-type ATPase and a MerR-type regulatory protein involved in copper homeostasis in Pseudomonas putida The GenBank accession number for the sequence reported in this paper is AF390440.
resolves10.1099/mic.0.051607-0The RSP_2889 gene product of Rhodobacter sphaeroides is a CueR homologue controlling copper-responsive genes
resolves10.1007/s10295-005-0040-9Disruption of the copper efflux pump (CopA) of Serratia marcescens ATCC 274 pleiotropically affects copper sensitivity and production of the tripyrrole secondary metabolite, prodigiosin
resolves10.1046/j.1365-2958.2002.02791.xActP controls copper homeostasis in <i>Rhizobium leguminosarum</i> bv. <i>viciae</i> and <i>Sinorhizobium meliloti</i> preventing low pH‐induced copper toxicity
resolves10.1099/mic.0.051862-0CopR of Sulfolobus solfataricus represents a novel class of archaeal-specific copper-responsive activators of transcription
resolves10.1007/s10534-005-3715-9Copper Chaperone Cycling and Degradation in the Regulation of theCop Operon of Enterococcus Hirae
resolves10.1021/bi025515cCopper Transfer from the Cu(I) Chaperone, CopZ, to the Repressor, Zn(II)CopY: Metal Coordination Environments and Protein Interactions
resolves10.1006/bbrc.1999.0807Effects of Promoter Mutations on the in Vivo Regulation of the cop Operon of Enterococcus hirae by Copper(I) and Copper(II)
resolves10.1006/bbrc.2001.5757Interaction of the CopZ Copper Chaperone with the CopA Copper ATPase of Enterococcus hirae Assessed by Surface Plasmon Resonance
resolves10.1007/s00775-004-0536-1Interaction kinetics of the copper-responsive CopY repressor with the cop promoter of Enterococcus hirae
resolves10.1042/BJ20081713The copper-responsive repressor CopR of <i>Lactococcus lactis</i> is a ‘winged helix’ protein
resolves10.1111/j.1365-2958.2011.07758.xThe <i>cop</i> operon is required for copper homeostasis and contributes to virulence in <i>Streptococcus pneumoniae</i>
resolves10.1021/bi801313yA Cu<sup>I</sup>-Sensing ArsR Family Metal Sensor Protein with a Relaxed Metal Selectivity Profile
resolves10.1038/nchembio844CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator
resolves10.1111/j.1365-2958.2011.07705.xThe combined actions of the copper‐responsive repressor CsoR and copper‐metallochaperone CopZ modulate CopA‐mediated copper efflux in the intracellular pathogen <i>Listeria monocytogenes</i>
resolves10.1099/mic.0.037382-0Structural and functional characterization of the transcriptional repressor CsoR from Thermus thermophilus HB8
resolves10.1021/bi900115wMolecular Insights into the Metal Selectivity of the Copper(I)-Sensing Repressor CsoR from
<i>Bacillus subtilis</i>
resolves10.1128/jb.175.6.1656-1664.1993A two-component regulatory system required for copper-inducible expression of the copper resistance operon of Pseudomonas syringae
resolves10.1099/00221287-143-4-1191Copper-inducible transcriptional regulation at two promoters in the Escherichia coli copper resistance determinant pco
resolves10.1016/S0378-1119(02)00918-6Genetic and transcriptional analysis of a novel plasmid-encoded copper resistance operon from Lactococcus lactis
resolves10.1073/pnas.1100410108Iron enzyme ribulose-5-phosphate 3-epimerase in
<i>Escherichia coli</i>
is rapidly damaged by hydrogen peroxide but can be protected by manganese
resolves10.1016/j.aquatox.2010.05.018Effects of copper sulfate, hydrogen peroxide and N-phenyl-2-naphthylamine on oxidative stress and the expression of genes involved photosynthesis and microcystin disposition in Microcystis aeruginosa
resolves10.1099/mic.0.27650-0The expression profile of Escherichia coli K-12 in response to minimal, optimal and excess copper concentrations
resolves10.1128/JB.01847-07The Global Responses of
<i>Mycobacterium tuberculosis</i>
to Physiological Levels of Copper
resolves10.1128/JB.00837-06Survival and Growth in the Presence of Elevated Copper: Transcriptional Profiling of Copper-Stressed
<i>Pseudomonas aeruginosa</i>
resolves10.1021/bi200841fMolecular Basis of the Cooperative Binding of Cu(I) and Cu(II) to the CopK Protein from <i>Cupriavidus metallidurans</i> CH34
resolves10.1021/ja9083896CopK from Cupriavidus metallidurans CH34 Binds Cu(I) in a Tetrathioether Site: Characterization by X-ray Absorption and NMR Spectroscopy
resolves10.1021/bi201031qSpectroscopic Characterization of the Metal-Binding Sites in the Periplasmic Metal-Sensor Domain of CnrX from <i>Cupriavidus metallidurans</i> CH34
resolves10.1039/c1mt00073jBacterial ATP-driven transporters of transition metals: physiological roles, mechanisms of action, and roles in bacterial virulence
resolves10.1016/j.ecoenv.2011.03.003Ecofriendly degradation, decolorization and detoxification of textile effluent by a developed bacterial consortium
resolves10.1186/1471-2091-12-30Engineering Klebsiella sp. 601 multicopper oxidase enhances the catalytic efficiency towards phenolic substrates
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