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NTIS 바로가기Antioxidants & redox signaling, v.17 no.9, 2012년, pp.1264 - 1276
Spiro, Stephen (Department of Molecular and Cell Biology, University of Texas at Dallas, Richardson, Texas.) , D'Autréaux, Benoît (Institut de Chimie des Substances Naturelles, UPR2301, Centre de Recherche de Gif, Centre National de la Recherche Scientifique (CNRS), Gif-Sur-Yvette Cedex, France.)
In bacteria, transcriptional responses to reactive oxygen and nitrogen species (ROS and RNS, respectively) are typically coordinated by regulatory proteins that employ metal centers or reactive thiols to detect the presence of those species. This review is focused on the structure, function and mech...
Adrait, A., Jacquamet, L., Le Pape, L., Gonzalez de Peredo, A., Aberdam, D., Hazemann, J.-L., Latour, J.-M., Michaud-Soret, I.. Spectroscopic and Saturation Magnetization Properties of the Manganese- and Cobalt-Substituted Fur (Ferric Uptake Regulation) Protein from Escherichia coli. Biochemistry, vol.38, no.19, 6248-6260.
Ahmad, Rafi, Brandsdal, Bjørn Olav, Michaud-Soret, Isabelle, Willassen, Nils-Peder. Ferric uptake regulator protein: Binding free energy calculations and per-residue free energy decomposition. Proteins, vol.75, no.2, 373-386.
Althaus, E. W., Outten, C. E., Olson, K. E., Cao, H., O'Halloran, T. V.. The Ferric Uptake Regulation (Fur) Repressor Is a Zinc Metalloprotein. Biochemistry, vol.38, no.20, 6559-6569.
Andrews, Simon C, Robinson, Andrea K, Rodrı́guez-Quiñones, Francisco. Bacterial iron homeostasis. FEMS microbiology reviews, vol.27, no.2, 215-237.
Arai, Hiroyuki, Hayashi, Michiko, Kuroi, Azusa, Ishii, Masaharu, Igarashi, Yasuo. Transcriptional Regulation of the Flavohemoglobin Gene for Aerobic Nitric Oxide Detoxification by the Second Nitric Oxide-Responsive Regulator of Pseudomonas aeruginosa. Journal of bacteriology, vol.187, no.12, 3960-3968.
Aravind, L.. The GAF domain: an evolutionary link between diverse phototransducing proteins. Trends in biochemical sciences, vol.22, no.12, 458-459.
Baichoo, Noel, Wang, Tao, Ye, Rick, Helmann, John D.. Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. Molecular microbiology, vol.45, no.6, 1613-1629.
Bang, Iel-Soo, Liu, Limin, Vazquez-Torres, Andrés, Crouch, Marie-Laure, Stamler, Jonathan S., Fang, Ferric C.. Maintenance of Nitric Oxide and Redox Homeostasis by the Salmonella Flavohemoglobin Hmp. The Journal of biological chemistry, vol.281, no.38, 28039-28047.
Brenot, Audrey, King, Katherine Y., Caparon, Michael G.. The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes. Molecular microbiology, vol.55, no.1, 221-234.
Bsat, N, Chen, L, Helmann, J D. Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes. Journal of bacteriology, vol.178, no.22, 6579-6586.
Bsat, Nada, Herbig, Andrew, Casillas‐Martinez, Lilliam, Setlow, Peter, Helmann, John D.. Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Molecular microbiology, vol.29, no.1, 189-198.
Büsch, Andrea, Pohlmann, Anne, Friedrich, Bärbel, Cramm, Rainer. A DNA Region Recognized by the Nitric Oxide-Responsive Transcriptional Activator NorR Is Conserved in β- and γ-Proteobacteria. Journal of bacteriology, vol.186, no.23, 7980-7987.
Bush, Matthew, Ghosh, Tamaswati, Tucker, Nicholas, Zhang, Xiaodong, Dixon, Ray. Nitric oxide-responsive interdomain regulation targets the σ 54 -interaction surface in the enhancer binding protein NorR. Molecular microbiology, vol.77, no.5, 1278-1288.
Carpenter, Beth M., Whitmire, Jeannette M., Merrell, D. Scott. This Is Not Your Mother's Repressor: the Complex Role of Fur in Pathogenesis. Infection and immunity, vol.77, no.7, 2590-2601.
Casillas-Martinez, Lilliam, Driks, Adam, Setlow, Barbara, Setlow, Peter. Lack of a significant role for the PerR regulator in Bacillus subtilis spore resistance. FEMS microbiology letters, vol.188, no.2, 203-208.
Chen, L, Keramati, L, Helmann, J D. Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions.. Proceedings of the National Academy of Sciences of the United States of America, vol.92, no.18, 8190-8194.
Cornelis, Pierre, Wei, Qing, Andrews, Simon C., Vinckx, Tiffany. Iron homeostasis and management of oxidative stress response in bacteria. Metallomics : integrated biometal science, vol.3, no.6, 540-549.
Cramm, Rainer, Pohlmann, Anne, Friedrich, Bärbel. Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16. FEBS letters, vol.460, no.1, 6-10.
D'Aquino, J. Alejandro, Tetenbaum-Novatt, Jaclyn, White, Andre, Berkovitch, Fred, Ringe, Dagmar. Mechanism of metal ion activation of the diphtheria toxin repressor DtxR. Proceedings of the National Academy of Sciences of the United States of America, vol.102, no.51, 18408-18413.
D'Autreaux, B., Horner, O., Oddou, J.-L., Jeandey, C., Gambarelli, S., Berthomieu, C., Latour, J.-M., Michaud-Soret, I.. Spectroscopic Description of the Two Nitrosyl−Iron Complexes Responsible for Fur Inhibition by Nitric Oxide. Journal of the American Chemical Society, vol.126, no.19, 6005-6016.
D'Autreaux, B., Pecqueur, L., Gonzalez de Peredo, A., Diederix, R. E. M., Caux-Thang, C., Tabet, L., Bersch, B., Forest, E., Michaud-Soret, I.. Reversible Redox- and Zinc-Dependent Dimerization of the Escherichia coli Fur Protein. Biochemistry, vol.46, no.5, 1329-1342.
D'Autréaux, Benoît, Touati, Danièle, Bersch, Beate, Latour, Jean-Marc, Michaud-Soret, Isabelle. Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron. Proceedings of the National Academy of Sciences of the United States of America, vol.99, no.26, 16619-16624.
D'Autréaux, Benoît, Tucker, Nicholas P., Dixon, Ray, Spiro, Stephen. A non-haem iron centre in the transcription factor NorR senses nitric oxide. Nature, vol.437, no.7059, 769-772.
Delany, Isabel, Grifantini, Renata, Bartolini, Erika, Rappuoli, Rino, Scarlato, Vincenzo. Effect of Neisseria meningitidis Fur Mutations on Global Control of Gene Transcription. Journal of bacteriology, vol.188, no.7, 2483-2492.
Delany, Isabel, Rappuoli, Rino, Scarlato, Vincenzo. Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis. Molecular microbiology, vol.52, no.4, 1081-1090.
Dian, Cyril, Vitale, Sylvia, Leonard, Gordon A., Bahlawane, Christelle, Fauquant, Caroline, Leduc, Damien, Muller, Cécile, de Reuse, Hilde, Michaud‐Soret, Isabelle, Terradot, Laurent. The structure of the Helicobacter pylori ferric uptake regulator Fur reveals three functional metal binding sites. Molecular microbiology, vol.79, no.5, 1260-1275.
Dowds, B.C.A.. The oxidative stress response in Bacillus subtilis. FEMS microbiology letters, vol.124, no.3, 255-263.
Dussurget, Olivier, Rodriguez, Marcela, Smith, Issar. An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative‐stress response. Molecular microbiology, vol.22, no.3, 535-544.
Ernst, Florian D., Bereswill, Stefan, Waidner, Barbara, Stoof, Jeroen, Mäder, Ulrike, Kusters, Johannes G., Kuipers, Ernst J., Kist, Manfred, van Vliet, Arnoud H. M., Homuth, Georg. Transcriptional profiling of Helicobacter pylori Fur- and iron-regulated gene expression. Microbiology, vol.151, no.2, 533-546.
Fang, Ferric C.. Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nature reviews. Microbiology, vol.2, no.10, 820-832.
Faulkner, Melinda J., Helmann, John D.. Peroxide Stress Elicits Adaptive Changes in Bacterial Metal Ion Homeostasis. Antioxidants & redox signaling, vol.15, no.1, 175-189.
Faulkner, M. J., Ma, Z., Fuangthong, M., Helmann, J. D.. Derepression of the Bacillus subtilis PerR Peroxide Stress Response Leads to Iron Deficiency. Journal of bacteriology, vol.194, no.5, 1226-1235.
Flatley, Janet, Barrett, Jason, Pullan, Steven T., Hughes, Martin N., Green, Jeffrey, Poole, Robert K.. Transcriptional Responses of Escherichia coli to S-Nitrosoglutathione under Defined Chemostat Conditions Reveal Major Changes in Methionine Biosynthesis. The Journal of biological chemistry, vol.280, no.11, 10065-10072.
Fleischhacker, Angela S, Kiley, Patricia J. Iron-containing transcription factors and their roles as sensors. Current opinion in chemical biology, vol.15, no.2, 335-341.
Fuangthong, Mayuree, Herbig, Andrew F., Bsat, Nada, Helmann, John D.. Regulation of theBacillus subtilis furandperRGenes by PerR: Not All Members of the PerR Regulon Are Peroxide Inducible. Journal of bacteriology, vol.184, no.12, 3276-3286.
Gaballa, Ahmed, Helmann, John D.. A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis. Molecular microbiology, vol.45, no.4, 997-1005.
Gardner, Anne M., Gessner, Christopher R., Gardner, Paul R.. Regulation of the Nitric Oxide Reduction Operon (norRVW) in Escherichia coli. The Journal of biological chemistry, vol.278, no.12, 10081-10086.
Gardner, Anne M., Helmick, Ryan A., Gardner, Paul R.. Flavorubredoxin, an Inducible Catalyst for Nitric Oxide Reduction and Detoxification in Escherichia coli. The Journal of biological chemistry, vol.277, no.10, 8172-8177.
Gomes, Cláudio M., Giuffrè, Alessandro, Forte, Elena, Vicente, João B., Saraiva, Lı́gia M., Brunori, Maurizio, Teixeira, Miguel. A Novel Type of Nitric-oxide Reductase. The Journal of biological chemistry, vol.277, no.28, 25273-25276.
Gonzalez de Peredo, A., Saint-Pierre, C., Adrait, A., Jacquamet, L., Latour, J.-M., Michaud-Soret, I., Forest, E.. Identification of the Two Zinc-Bound Cysteines in the Ferric Uptake Regulation Protein from Escherichia coli: Chemical Modification and Mass Spectrometry Analysis. Biochemistry, vol.38, no.26, 8582-8589.
Gryllos, Ioannis, Grifantini, Renata, Colaprico, Annalisa, Cary, Max E., Hakansson, Anders, Carey, David W., Suarez-Chavez, Maria, Kalish, Leslie A., Mitchell, Paul D., White, Gary L., Wessels, Michael R.. PerR Confers Phagocytic Killing Resistance and Allows Pharyngeal Colonization by Group A Streptococcus. PLoS pathogens, vol.4, no.9, e1000145-.
Free Radicals in Biology and Medicine Gutteridge J 2007
Herbig, Andrew F., Helmann, John D.. Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA. Molecular microbiology, vol.41, no.4, 849-859.
Hochgräfe, Falko, Wolf, Carmen, Fuchs, Stephan, Liebeke, Manuel, Lalk, Michael, Engelmann, Susanne, Hecker, Michael. Nitric Oxide Stress Induces Different Responses but Mediates Comparable Protein Thiol Protection in Bacillus subtilis and Staphylococcus aureus. Journal of bacteriology, vol.190, no.14, 4997-5008.
Hutchings, Matthew I., Mandhana, Neeraj, Spiro, Stephen. The NorR Protein of Escherichia coli Activates Expression of the Flavorubredoxin Gene norV in Response to Reactive Nitrogen Species. Journal of bacteriology, vol.184, no.16, 4640-4643.
Hyduke, Daniel R., Jarboe, Laura R., Tran, Linh M., Chou, Katherine J. Y., Liao, James C.. Integrated network analysis identifies nitric oxide response networks and dihydroxyacid dehydratase as a crucial target in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, vol.104, no.20, 8484-8489.
Imlay, James A.. PATHWAYS OF OXIDATIVE DAMAGE. Annual review of microbiology, vol.57, 395-418.
Imlay, James A.. Cellular Defenses against Superoxide and Hydrogen Peroxide. Annual review of biochemistry, vol.77, 755-776.
Jacquamet, L., Aberdam, D., Adrait, A., Hazemann, J.-L., Latour, J.-M., Michaud-Soret, I.. X-ray Absorption Spectroscopy of a New Zinc Site in the Fur Protein fromEscherichia coli. Biochemistry, vol.37, no.8, 2564-2571.
Jacquamet, L., Traoré, D. A. K., Ferrer, J.-L., Proux, O., Testemale, D., Hazemann, J.-L., Nazarenko, E., El Ghazouani, A., Caux-Thang, C., Duarte, V., Latour, J.-M.. Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding. Molecular microbiology, vol.73, no.1, 20-31.
Jacquamet, L., Dole, F., Jeandey, C., Oddou, J.-L., Perret, E., Le Pape, L., Aberdam, D., Hazemann, J.-L., Michaud-Soret, I., Latour, J.-M.. First Spectroscopic Characterization of FeII-Fur, the Physiological Active Form of the Fur Protein. Journal of the American Chemical Society, vol.122, no.2, 394-395.
Justino, Marta C., Almeida, Cláudia C., Teixeira, Miguel, Saraiva, Lígia M.. Escherichia coli Di-iron YtfE Protein Is Necessary for the Repair of Stress-damaged Iron-Sulfur Clusters. The Journal of biological chemistry, vol.282, no.14, 10352-10359.
Justino, Marta C., Vicente, João B., Teixeira, Miguel, Saraiva, Lígia M.. New Genes Implicated in the Protection of Anaerobically Grown Escherichia coli against Nitric Oxide. The Journal of biological chemistry, vol.280, no.4, 2636-2643.
Keyer, Kay, Imlay, James A.. Superoxide accelerates DNA damage by elevating free-iron levels. Proceedings of the National Academy of Sciences of the United States of America, vol.93, no.24, 13635-13640.
King, Katherine Y., Horenstein, Joshua A., Caparon, Michael G.. Aerotolerance and Peroxide Resistance in Peroxidase and PerR Mutants of Streptococcus pyogenes. Journal of bacteriology, vol.182, no.19, 5290-5299.
Klink, Andrea, Elsner, Bettina, Strube, Katja, Cramm, Rainer. Characterization of the Signaling Domain of the NO-Responsive Regulator NorR from Ralstonia eutropha H16 by Site-Directed Mutagenesis. Journal of bacteriology, vol.189, no.7, 2743-2749.
Koskenkorva-Frank, Taija S., Kallio, Pauli T.. Induction ofPseudomonas aeruginosafhpandfhpRby reactive oxygen species. Canadian journal of microbiology, vol.55, no.6, 657-663.
Lee, Cheolju, Lee, Soon Mi, Mukhopadhyay, Partha, Kim, Seung Jun, Lee, Sang Chul, Ahn, Woo-Sung, Yu, Myeong-Hee, Storz, Gisela, Ryu, Seong Eon. Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path. Nature structural & molecular biology, vol.11, no.12, 1179-1185.
Lee, Jin-Won, Helmann, John D.. Biochemical Characterization of the Structural Zn2+ Site in the Bacillus subtilis Peroxide Sensor PerR. The Journal of biological chemistry, vol.281, no.33, 23567-23578.
Lee, Jin-Won, Helmann, John D.. The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation. Nature, vol.440, no.7082, 363-367.
Lee, Jin-Won, Helmann, John D.. Functional specialization within the Fur family of metalloregulators. Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, vol.20, no.3, 485-499.
Lewin, Allison C., Doughty, Phillip A., Flegg, Lynda, Moore, Geoffrey R., Spiro, Stephen. The ferric uptake regulator of Pseudomonas aeruginosa has no essential cysteine residues and does not contain a structural zinc ion. Microbiology, vol.148, no.8, 2449-2456.
Ma, Zhen, Lee, Jin-Won, Helmann, John D.. Identification of altered function alleles that affect Bacillus subtilis PerR metal ion selectivity. Nucleic acids research, vol.39, no.12, 5036-5044.
Marletta, Michael A., Spiering, Michelle M.. Trace Elements and Nitric Oxide function. The Journal of nutrition, vol.133, no.5, 1431S-1433S.
Massé, Eric, Gottesman, Susan. A small RNA regulates the expression of genes involved in iron metabolism in Escherichiacoli. Proceedings of the National Academy of Sciences of the United States of America, vol.99, no.7, 4620-4625.
Masse, E., Salvail, H., Desnoyers, G., Arguin, M.. Small RNAs controlling iron metabolism. Current opinion in microbiology, vol.10, no.2, 140-145.
McLean, S., Bowman, L.A.H., Poole, R.K.. KatG from Salmonella Typhimurium is a peroxynitritase. FEBS letters, vol.584, no.8, 1628-1632.
Moore, Charles M., Nakano, Michiko M., Wang, Tao, Ye, Rick W., Helmann, John D.. Response ofBacillus subtilisto Nitric Oxide and the Nitrosating Agent Sodium Nitroprusside. Journal of bacteriology, vol.186, no.14, 4655-4664.
Mukhopadhyay, Partha, Zheng, Ming, Bedzyk, Laura A., LaRossa, Robert A., Storz, Gisela. Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species. Proceedings of the National Academy of Sciences of the United States of America, vol.101, no.3, 745-750.
Nandal, Anjali, Huggins, Cerys C. O., Woodhall, Mark R., McHugh, Jonathan, Rodríguez‐Quiñones, Francisco, Quail, Michael A., Guest, John R., Andrews, Simon C.. Induction of the ferritin gene (ftnA) of Escherichia coli by Fe2+–Fur is mediated by reversal of H‐NS silencing and is RyhB independent. Molecular microbiology, vol.75, no.3, 637-657.
Olsen, Katja N., Larsen, Marianne H., Gahan, Cormac G. M., Kallipolitis, Birgitte, Wolf, Xenia A., Rea, Rosemary, Hill, Colin, Ingmer, Hanne. The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells. Microbiology, vol.151, no.3, 925-933.
Outten, F. Wayne, Djaman, Ouliana, Storz, Gisela. A suf operon requirement for Fe–S cluster assembly during iron starvation in Escherichia coli. Molecular microbiology, vol.52, no.3, 861-872.
Overton, Tim W., Whitehead, Rebekah, Li, Ying, Snyder, Lori A.S., Saunders, Nigel J., Smith, Harry, Cole, Jeff A.. Coordinated Regulation of the Neisseria gonorrhoeae-truncated Denitrification Pathway by the Nitric Oxide-sensitive Repressor, NsrR, and Nitrite-insensitive NarQ-NarP. The Journal of biological chemistry, vol.281, no.44, 33115-33126.
Palyada, Kiran, Sun, Yi-Qian, Flint, Annika, Butcher, James, Naikare, Hemant, Stintzi, Alain. Characterization of the oxidative stress stimulon and PerR regulon of Campylobacter jejuni. BMC genomics, vol.10, 481-481.
Park, Sunny, You, Xiaojun, Imlay, James A.. Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx - mutants of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, vol.102, no.26, 9317-9322.
Pecqueur, Ludovic, D'Autréaux, Benoît, Dupuy, Jérome, Nicolet, Yvain, Jacquamet, Lilian, Brutscher, Bernhard, Michaud-Soret, Isabelle, Bersch, Beate. Structural Changes of Escherichia coli Ferric Uptake Regulator during Metal-dependent Dimerization and Activation Explored by NMR and X-ray Crystallography. The Journal of biological chemistry, vol.281, no.30, 21286-21295.
Pohl, Ehmke, Haller, Jon C., Mijovilovich, Ana, Meyer-Klaucke, Wolfram, Garman, Elspeth, Vasil, Michael L.. Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator. Molecular microbiology, vol.47, no.4, 903-915.
Pohlmann, Anne, Cramm, Rainer, Schmelz, Karin, Friedrich, Bärbel. A novel NO-responding regulator controls the reduction of nitric oxide in Ralstonia eutropha. Molecular microbiology, vol.38, no.3, 626-638.
Pomposiello, Pablo J., Bennik, Marjon H. J., Demple, Bruce. Genome-Wide Transcriptional Profiling of the Escherichia coli Responses to Superoxide Stress and Sodium Salicylate. Journal of bacteriology, vol.183, no.13, 3890-3902.
Prajsnar, Tomasz K., Cunliffe, Vincent T., Foster, Simon J., Renshaw, Stephen A.. A novel vertebrate model of Staphylococcus aureus infection reveals phagocyte-dependent resistance of zebrafish to non-host specialized pathogens. Cellular microbiology, vol.10, no.11, 2312-2325.
Pullan, Steven T., Gidley, Mark D., Jones, Richard A., Barrett, Jason, Stevanin, Tania M., Read, Robert C., Green, Jeffrey, Poole, Robert K.. Nitric Oxide in Chemostat-Cultured Escherichia coli Is Sensed by Fnr and Other Global Regulators: Unaltered Methionine Biosynthesis Indicates Lack of S Nitrosation. Journal of bacteriology, vol.189, no.5, 1845-1855.
Pulliainen, Arto Tapio, Hytönen, Jukka, Haataja, Sauli, Finne, Jukka. Deficiency of the Rgg Regulator Promotes H 2 O 2 Resistance, AhpCF-Mediated H 2 O 2 Decomposition, and Virulence in Streptococcus pyogenes. Journal of bacteriology, vol.190, no.9, 3225-3235.
Rappas, Mathieu, Bose, Daniel, Zhang, Xiaodong. Bacterial enhancer-binding proteins: unlocking σ54-dependent gene transcription. Current opinion in structural biology, vol.17, no.1, 110-116.
Rea, Rosemarie B., Gahan, Cormac G. M., Hill, Colin. Disruption of Putative Regulatory Loci in Listeria monocytogenes Demonstrates a Significant Role for Fur and PerR in Virulence. Infection and immunity, vol.72, no.2, 717-727.
Rea, Rosemarie, Hill, Colin, Gahan, Cormac G. M.. Listeria monocytogenes PerR Mutants Display a Small-Colony Phenotype, Increased Sensitivity to Hydrogen Peroxide, and Significantly Reduced Murine Virulence. Applied and environmental microbiology, vol.71, no.12, 8314-8322.
Mol Microbiol Ren B 953 70 2008 10.1111/j.1365-2958.2008.06464.x
Ricci, Susanna, Janulczyk, Robert, Björck, Lars. The Regulator PerR Is Involved in Oxidative Stress Response and Iron Homeostasis and Is Necessary for Full Virulence of Streptococcus pyogenes. Infection and immunity, vol.70, no.9, 4968-4976.
Richardson, Anthony R., Dunman, Paul M., Fang, Ferric C.. The nitrosative stress response of Staphylococcus aureus is required for resistance to innate immunity. Molecular microbiology, vol.61, no.4, 927-939.
Rodionov, Dmitry A, Dubchak, Inna L, Arkin, Adam P, Alm, Eric J, Gelfand, Mikhail S. Dissimilatory Metabolism of Nitrogen Oxides in Bacteria: Comparative Reconstruction of Transcriptional Networks. PLoS computational biology, vol.1, no.5, e55-.
Schapiro, Jeffrey M., Libby, Stephen J., Fang, Ferric C.. Inhibition of bacterial DNA replication by zinc mobilization during nitrosative stress. Proceedings of the National Academy of Sciences of the United States of America, vol.100, no.14, 8496-8501.
Sheikh, Md. Arif, Taylor, Garry L.. Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co-ordination. Molecular microbiology, vol.72, no.5, 1208-1220.
Spiro, Stephen. Regulators of bacterial responses to nitric oxide. FEMS microbiology reviews, vol.31, no.2, 193-211.
Stohl, Elizabeth A., Criss, Alison K., Seifert, H. Steven. The transcriptome response of Neisseria gonorrhoeae to hydrogen peroxide reveals genes with previously uncharacterized roles in oxidative damage protection. Molecular microbiology, vol.58, no.2, 520-532.
Strube, Katja, de Vries, Simon, Cramm, Rainer. Formation of a Dinitrosyl Iron Complex by NorA, a Nitric Oxide-binding Di-iron Protein from Ralstonia eutropha H16. The Journal of biological chemistry, vol.282, no.28, 20292-20300.
Touati, D, Jacques, M, Tardat, B, Bouchard, L, Despied, S. Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase. Journal of bacteriology, vol.177, no.9, 2305-2314.
Traoré, Daouda A. K., El Ghazouani, Abdelnasser, Ilango, Sougandi, Dupuy, Jérôme, Jacquamet, Lilian, Ferrer, Jean-Luc, Caux-Thang, Christelle, Duarte, Victor, Latour, Jean-Marc. Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis. Molecular microbiology, vol.61, no.5, 1211-1219.
Traoré, Daouda A K, Ghazouani, Abdelnasser El, Jacquamet, Lilian, Borel, Franck, Ferrer, Jean-Luc, Lascoux, David, Ravanat, Jean-Luc, Jaquinod, Michel, Blondin, Geneviève, Caux-Thang, Christelle, Duarte, Victor, Latour, Jean-Marc. Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein. Nature chemical biology, vol.5, no.1, 53-59.
Tucker, Nicholas P., D'Autréaux, Benoît, Studholme, David J., Spiro, Stephen, Dixon, Ray. DNA Binding Activity of theEscherichia coliNitric Oxide Sensor NorR Suggests a Conserved Target Sequence in Diverse Proteobacteria. Journal of bacteriology, vol.186, no.19, 6656-6660.
Tucker, Nicholas P., Ghosh, Tamaswati, Bush, Matthew, Zhang, Xiaodong, Dixon, Ray. Essential roles of three enhancer sites in σ 54 -dependent transcription by the nitric oxide sensing regulatory protein NorR. Nucleic acids research, vol.38, no.4, 1182-1194.
Tucker, Nicholas P., D'Autréaux, Benoît, Yousafzai, Faridoon K., Fairhurst, Shirley A., Spiro, Stephen, Dixon, Ray. Analysis of the Nitric Oxide-sensing Non-heme Iron Center in the NorR Regulatory Protein. The Journal of biological chemistry, vol.283, no.2, 908-918.
Varghese, Shery, Wu, Amy, Park, Sunny, Imlay, Karin R. C., Imlay, James A.. Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli. Molecular microbiology, vol.64, no.3, 822-830.
Velayudhan, Jyoti, Castor, Margaret, Richardson, Anthony, Main-Hester, Kara L., Fang, Ferric C.. The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence. Molecular microbiology, vol.63, no.5, 1495-1507.
Venugopal, Aditya, Bryk, Ruslana, Shi, Shuangping, Rhee, Kyu, Rath, Poonam, Schnappinger, Dirk, Ehrt, Sabine, Nathan, Carl. Virulence of Mycobacterium tuberculosis Depends on Lipoamide Dehydrogenase, a Member of Three Multienzyme Complexes. Cell host & microbe, vol.9, no.1, 21-31.
Voskuil, Martin I., Bartek, Iona L., Visconti, Kevin, Schoolnik, Gary K.. The Response of Mycobacterium Tuberculosis to Reactive Oxygen and Nitrogen Species. Frontiers in microbiology, vol.2, 105-.
Wang, Yanling, Dunn, Anne K., Wilneff, Jacqueline, McFall-Ngai, Margaret J., Spiro, Stephen, Ruby, Edward G.. Vibrio fischeri flavohaemoglobin protects against nitric oxide during initiation of the squid–Vibrio symbiosis. Molecular microbiology, vol.78, no.4, 903-915.
Wen, Yao-Tseng, Tsou, Chih-Cheng, Kuo, Hsin-Tzu, Wang, Jie-Siou, Wu, Jiunn-Jong, Liao, Pao-Chi. Differential Secretomics of Streptococcus pyogenes Reveals a Novel Peroxide Regulator (PerR)-regulated Extracellular Virulence Factor Mitogen Factor3 (MF3). Molecular & cellular proteomics : MCP, vol.10, no.9, M110.007013-.
Wu, Hsing-Ju, Seib, Kate L., Srikhanta, Yogitha N., Kidd, Stephen P., Edwards, Jennifer L., Maguire, Tina L., Grimmond, Sean M., Apicella, Michael A., McEwan, Alastair G., Jennings, Michael P.. PerR controls Mn-dependent resistance to oxidative stress in Neisseria gonorrhoeae. Molecular microbiology, vol.60, no.2, 401-416.
Yang, J., Duan, X., Landry, A.P., Ding, H.. Oxygen is required for the l-cysteine-mediated decomposition of protein-bound dinitrosyl-iron complexes. Free radical biology & medicine, vol.49, no.2, 268-274.
Yuhara, Satoshi, Komatsu, Harunobu, Goto, Hiroyuki, Ohtsubo, Yoshiyuki, Nagata, Yuji, Tsuda, Masataka. Pleiotropic roles of iron-responsive transcriptional regulator Fur in Burkholderia multivorans. Microbiology, vol.154, no.6, 1763-1774.
J Bacteriol Zheng M 4639 181 1999 10.1128/JB.181.15.4639-4643.1999
Zheng, Ming, Wang, Xunde, Templeton, Lori J., Smulski, Dana R., LaRossa, Robert A., Storz, Gisela. DNA Microarray-Mediated Transcriptional Profiling of the Escherichia coli Response to Hydrogen Peroxide. Journal of bacteriology, vol.183, no.15, 4562-4570.
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