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Oxidative stress, protein damage and repair in bacteria.
Primary tabs
Document type | Article de périodique (Journal article) – Synthèse de littérature |
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Publication date | 2017 |
Language | Anglais |
Journal information | "Nature Reviews. Microbiology" - Vol. 15, no.7, p. 385-396 (2017) |
Peer reviewed | yes |
Publisher | Nature Publishing Group ((United Kingdom) London) |
issn | 1740-1526 |
e-issn | 1740-1534 |
Publication status | Publié |
Affiliations |
UCL
- SSS/DDUV - Institut de Duve UCL - SSS/DDUV/BCHM - Biochimie-Recherche métabolique |
MESH Subject | Bacteria ; Cell Membrane ; Cell Wall ; Cysteine ; Methionine ; Oxidation-Reduction ; Oxidative Stress ; Proteins ; Reactive Oxygen Species ; Sulfur |
Links |
- Imlay James A., The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium, 10.1038/nrmicro3032
- Flannagan Ronald, Heit Bryan, Heinrichs David, Antimicrobial Mechanisms of Macrophages and the Immune Evasion Strategies of Staphylococcus aureus, 10.3390/pathogens4040826
- Winterbourn Christine C., Kettle Anthony J., Redox Reactions and Microbial Killing in the Neutrophil Phagosome, 10.1089/ars.2012.4827
- Hurst James K., What really happens in the neutrophil phagosome?, 10.1016/j.freeradbiomed.2012.05.008
- Nyström Thomas, Role of oxidative carbonylation in protein quality control and senescence, 10.1038/sj.emboj.7600599
- 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, 10.1038/nchembio.133
- Feeney Maria B., Schöneich Christian, Tyrosine Modifications in Aging, 10.1089/ars.2012.4595
- Thurlkill Richard L., Grimsley Gerald R., Scholtz J. Martin, Pace C. Nick, pK values of the ionizable groups of proteins, 10.1110/ps.051840806
- Winterbourn Christine C., Hampton Mark B., Thiol chemistry and specificity in redox signaling, 10.1016/j.freeradbiomed.2008.05.004
- Nagy Péter, Kinetics and Mechanisms of Thiol–Disulfide Exchange Covering Direct Substitution and Thiol Oxidation-Mediated Pathways, 10.1089/ars.2012.4973
- Paulsen Candice E., Carroll Kate S., Cysteine-Mediated Redox Signaling: Chemistry, Biology, and Tools for Discovery, 10.1021/cr300163e
- Roos Goedele, Messens Joris, Protein sulfenic acid formation: From cellular damage to redox regulation, 10.1016/j.freeradbiomed.2011.04.031
- Imlay James A., Cellular Defenses against Superoxide and Hydrogen Peroxide, 10.1146/annurev.biochem.77.061606.161055
- Davies Michael J., The oxidative environment and protein damage, 10.1016/j.bbapap.2004.08.007
- Lavine T. F., J. Biol. Chem., 169, 477 (1947)
- Lee Byung Cheon, Gladyshev Vadim N., The biological significance of methionine sulfoxide stereochemistry, 10.1016/j.freeradbiomed.2010.11.008
- Vogt Walther, Oxidation of methionyl residues in proteins: Tools, targets, and reversal, 10.1016/0891-5849(94)00158-g
- Schöneich Christian, Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease, 10.1016/j.bbapap.2004.09.009
- Buxton George V., Greenstock Clive L., Helman W. Phillips, Ross Alberta B., Critical Review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals (⋅OH/⋅O− in Aqueous Solution, 10.1063/1.555805
- Pattison David I., Davies Michael J., Absolute Rate Constants for the Reaction of Hypochlorous Acid with Protein Side Chains and Peptide Bonds, 10.1021/tx0155451
- Padmaja S., Squadrito G.L., Lemercier J.-N., Cueto R., Pryor William A., Rapid oxidation of dl-selenomethionine by peroxynitrite, 10.1016/0891-5849(96)00132-3
- Collet Jean-Francois, Messens Joris, Structure, Function, and Mechanism of Thioredoxin Proteins, 10.1089/ars.2010.3114
- Arts Isabelle S., Vertommen Didier, Baldin Francesca, Laloux Géraldine, Collet Jean-François, Comprehensively Characterizing the Thioredoxin InteractomeIn VivoHighlights the Central Role Played by This Ubiquitous Oxidoreductase in Redox Control, 10.1074/mcp.m115.056440
- Collet Jean-Francois, D'Souza Jonathan Conrad, Jakob Ursula, Bardwell James C. A., Thioredoxin 2, an Oxidative Stress-induced Protein, Contains a High Affinity Zinc Binding Site, 10.1074/jbc.m307818200
- Ritz Daniel, Patel Hiten, Doan Bernard, Zheng Ming, Åslund Fredrik, Storz Gisela, Beckwith Jon, Thioredoxin 2 Is Involved in the Oxidative Stress Response inEscherichia coli, 10.1074/jbc.275.4.2505
- Storz G, Tartaglia L., Ames B., Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation, 10.1126/science.2183352
- Ritz Daniel, Beckwith Jon, Roles of Thiol-Redox Pathways in Bacteria, 10.1146/annurev.micro.55.1.21
- Fernandes Aristi Potamitou, Holmgren Arne, Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System, 10.1089/152308604771978354
- Vlamis-Gardikas Alexios, The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisited, 10.1016/j.bbagen.2008.03.013
- Iwema Thomas, Picciocchi Antoine, Traore Daouda A. K., Ferrer Jean-Luc, Chauvat Franck, Jacquamet Lilian, Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin, 10.1021/bi900440m
- Newton Gerald, Fahey Robert, Mycothiol biochemistry, 10.1007/s00203-002-0469-4
- Newton Gerald L, Rawat Mamta, La Clair James J, Jothivasan Vishnu Karthik, Budiarto Tanya, Hamilton Chris J, Claiborne Al, Helmann John D, Fahey Robert C, Bacillithiol is an antioxidant thiol produced in Bacilli, 10.1038/nchembio.189
- Delaye Luis, Becerra Arturo, Orgel Leslie, Lazcano Antonio, Molecular Evolution of Peptide Methionine Sulfoxide Reductases (MsrA and MsrB): On the Early Development of a Mechanism That Protects Against Oxidative Damage, 10.1007/s00239-005-0281-2
- Brot N., Weissbach L., Werth J., Weissbach H., Enzymatic reduction of protein-bound methionine sulfoxide., 10.1073/pnas.78.4.2155
- Rahman M. A., J. Biol. Chem., 267, 15549 (1992)
- Grimaud Régis, Ezraty Benjamin, Mitchell Jennifer K., Lafitte Daniel, Briand Claudette, Derrick Peter J., Barras Frédéric, Repair of Oxidized Proteins : IDENTIFICATION OF A NEW METHIONINE SULFOXIDE REDUCTASE, 10.1074/jbc.m105509200
- Lin Z., Johnson L. C., Weissbach H., Brot N., Lively M. O., Lowther W. T., Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function, 10.1073/pnas.0703774104
- Ezraty B., Bos J., Barras F., Aussel L., Methionine Sulfoxide Reduction and Assimilation in Escherichia coli: New Role for the Biotin Sulfoxide Reductase BisC, 10.1128/jb.187.1.231-237.2005
- Kryukov G. V., Kumar R. A., Koc A., Sun Z., Gladyshev V. N., Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase, 10.1073/pnas.072603099
- Sharov Victor S., Ferrington Deborah A., Squier Thomas C., Schöneich Christian, Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase, 10.1016/s0014-5793(99)00888-1
- Moskovitz Jackob, Poston J. Michael, Berlett Barbara S., Nosworthy Neil J., Szczepanowski Roman, Stadtman Earl R., Identification and Characterization of a Putative Active Site for Peptide Methionine Sulfoxide Reductase (MsrA) and Its Substrate Stereospecificity, 10.1074/jbc.275.19.14167
- Boschi-Muller Sandrine, Olry Alexandre, Antoine Mathias, Branlant Guy, The enzymology and biochemistry of methionine sulfoxide reductases, 10.1016/j.bbapap.2004.09.016
- Boschi-Muller Sandrine, Azza Saïd, Branlant Guy, E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide, 10.1110/ps.10701
- Kumar R. Abhilash, Koc Ahmet, Cerny Ronald L., Gladyshev Vadim N., Reaction Mechanism, Evolutionary Analysis, and Role of Zinc inDrosophilaMethionine-R-sulfoxide Reductase, 10.1074/jbc.m203496200
- Kim Hwa-Young, Gladyshev Vadim N, Different Catalytic Mechanisms in Mammalian Selenocysteine- and Cysteine-Containing Methionine-R-Sulfoxide Reductases, 10.1371/journal.pbio.0030375
- Russel M., J. Biol. Chem., 261, 14997 (1986)
- Boschi-Muller Sandrine, Branlant Guy, Methionine sulfoxide reductase: Chemistry, substrate binding, recycling process and oxidase activity, 10.1016/j.bioorg.2014.07.002
- Lee Tae-Hyung, Kim Hwa-Young, An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide, 10.1016/j.abb.2008.07.028
- Coudevylle Nicolas, Antoine Mathias, Bouguet-Bonnet Sabine, Mutzenhardt Pierre, Boschi-Muller Sandrine, Branlant Guy, Cung Manh-Thong, Solution Structure and Backbone Dynamics of the Reduced Form and an Oxidized Form of E. coli Methionine Sulfoxide Reductase A (MsrA): Structural Insight of the MsrA Catalytic Cycle, 10.1016/j.jmb.2006.11.042
- Ranaivoson Fanomezana M., Antoine Mathias, Kauffmann Brice, Boschi-Muller Sandrine, Aubry André, Branlant Guy, Favier Frédérique, A Structural Analysis of the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidis, 10.1016/j.jmb.2008.01.021
- Ranaivoson Fanomezana M., Neiers Fabrice, Kauffmann Brice, Boschi-Muller Sandrine, Branlant Guy, Favier Frédérique, Methionine Sulfoxide Reductase B Displays a High Level of Flexibility, 10.1016/j.jmb.2009.08.073
- Lowther W. T., Nat. Struct. Biol., 9, 348 (2002)
- Mahawar Manish, Tran ViLinh, Sharp Joshua S., Maier Robert J., Synergistic Roles ofHelicobacter pyloriMethionine Sulfoxide Reductase and GroEL in Repairing Oxidant-damaged Catalase, 10.1074/jbc.m111.223677
- Benoit S. L., Bayyareddy K., Mahawar M., Sharp J. S., Maier R. J., Alkyl Hydroperoxide Reductase Repair by Helicobacter pylori Methionine Sulfoxide Reductase, 10.1128/jb.01001-13
- Khor Hui Koon, Fisher Mark T., Schöneich Christian, Potential Role of Methionine Sulfoxide in the Inactivation of the Chaperone GroEL by Hypochlorous Acid (HOCl) and Peroxynitrite (ONOO–), 10.1074/jbc.m310045200
- Abulimiti Abuduaini, Qiu Xiaolei, Chen Jing, Liu Yang, Chang Zengyi, Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants, 10.1016/s0006-291x(03)00685-5
- Levine R. L., Mosoni L., Berlett B. S., Stadtman E. R., Methionine residues as endogenous antioxidants in proteins, 10.1073/pnas.93.26.15036
- Ezraty Benjamin, Grimaud Régis, Hassouni Mohammed El, Moinier Daniéle, Barras Frédéric, Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli, 10.1038/sj.emboj.7600172
- Luirink J., EMBO J., 13, 2289 (1994)
- Ulbrandt Nancy D, Newitt John A, Bernstein Harris D, The E. coli Signal Recognition Particle Is Required for the Insertion of a Subset of Inner Membrane Proteins, 10.1016/s0092-8674(00)81839-5
- Leverrier Pauline, Vertommen Didier, Collet Jean-François, Contribution of proteomics toward solving the fascinating mysteries of the biogenesis of the envelope ofEscherichia coli, 10.1002/pmic.200900461
- Silhavy T. J., Kahne D., Walker S., The Bacterial Cell Envelope, 10.1101/cshperspect.a000414
- Depuydt Matthieu, Messens Joris, Collet Jean-Francois, How Proteins Form Disulfide Bonds, 10.1089/ars.2010.3575
- Bardwell James C.A., McGovern Karen, Beckwith Jon, Identification of a protein required for disulfide bond formation in vivo, 10.1016/0092-8674(91)90532-4
- Bader Martin, Muse Wilson, Ballou David P, Gassner Christian, Bardwell James C.A, Oxidative Protein Folding Is Driven by the Electron Transport System, 10.1016/s0092-8674(00)81016-8
- Kadokura Hiroshi, Beckwith Jon, Detecting Folding Intermediates of a Protein as It Passes through the Bacterial Translocation Channel, 10.1016/j.cell.2009.07.030
- Shevchik V. E., EMBO J., 13, 2007 (1994)
- Dutton R. J., Boyd D., Berkmen M., Beckwith J., Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation, 10.1073/pnas.0804621105
- Depuydt M., Leonard S. E., Vertommen D., Denoncin K., Morsomme P., Wahni K., Messens J., Carroll K. S., Collet J.-F., A Periplasmic Reducing System Protects Single Cysteine Residues from Oxidation, 10.1126/science.1179557
- Mainardi Jean-Luc, Hugonnet Jean-Emmanuel, Rusconi Filippo, Fourgeaud Martine, Dubost Lionel, Moumi Angèle Nguekam, Delfosse Vanessa, Mayer Claudine, Gutmann Laurent, Rice Louis B., Arthur Michel, Unexpected Inhibition of Peptidoglycan LD-Transpeptidase fromEnterococcus faeciumby the β-Lactam Imipenem, 10.1074/jbc.m704286200
- Denoncin Katleen, Vertommen Didier, Arts Isabelle S., Goemans Camille V., Rahuel-Clermont Sophie, Messens Joris, Collet Jean-François, A New Role forEscherichia coliDsbC Protein in Protection against Oxidative Stress, 10.1074/jbc.m114.554055
- Arts Isabelle S., Gennaris Alexandra, Collet Jean-François, Reducing systems protecting the bacterial cell envelope from oxidative damage, 10.1016/j.febslet.2015.04.057
- Rietsch A, Bessette P, Georgiou G, Beckwith J, Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin., 10.1128/jb.179.21.6602-6608.1997
- Rietsch A., Belin D., Martin N., Beckwith J., An in vivo pathway for disulfide bond isomerization in Escherichia coli, 10.1073/pnas.93.23.13048
- Katzen Federico, Beckwith Jon, Transmembrane Electron Transfer by the Membrane Protein DsbD Occurs via a Disulfide Bond Cascade, 10.1016/s0092-8674(00)00180-x
- Williamson Jessica A, Cho Seung-Hyun, Ye Jiqing, Collet Jean-Francois, Beckwith Jonathan R, Chou James J, Structure and multistate function of the transmembrane electron transporter CcdA, 10.1038/nsmb.3099
- Skaar E. P., Tobiason D. M., Quick J., Judd R. C., Weissbach H., Etienne F., Brot N., Seifert H. S., The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species, 10.1073/pnas.152334799
- Olry Alexandre, Boschi-Muller Sandrine, Marraud Michel, Sanglier-Cianferani Sarah, Van Dorsselear Alain, Branlant Guy, Characterization of the Methionine Sulfoxide Reductase Activities of PILB, a Probable Virulence Factor from Neisseria meningitidis , 10.1074/jbc.m112350200
- Brot Nathan, Collet Jean-François, Johnson Lynnette C., Jönsson Thomas J., Weissbach Herbert, Lowther W. Todd, The Thioredoxin Domain ofNeisseria gonorrhoeaePilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases, 10.1074/jbc.m604971200
- Saleh Malek, Bartual Sergio G., Abdullah Mohammed R., Jensch Inga, Asmat Tauseef M., Petruschka Lothar, Pribyl Thomas, Gellert Manuela, Lillig Christopher H., Antelmann Haike, Hermoso Juan A., Hammerschmidt Sven, Molecular architecture ofStreptococcus pneumoniaesurface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence : Pneumococcal surface oxidative resistance system, 10.1002/emmm.201202435
- Gennaris Alexandra, Ezraty Benjamin, Henry Camille, Agrebi Rym, Vergnes Alexandra, Oheix Emmanuel, Bos Julia, Leverrier Pauline, Espinosa Leon, Szewczyk Joanna, Vertommen Didier, Iranzo Olga, Collet Jean-François, Barras Frédéric, Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons, 10.1038/nature15764
- Brokx Stephen J., Rothery Richard A., Zhang Guijin, Ng Derek P., Weiner Joel H., Characterization of anEscherichia coliSulfite Oxidase Homologue Reveals the Role of a Conserved Active Site Cysteine in Assembly and Function†, 10.1021/bi050621a
- Juillan-Binard Céline, Picciocchi Antoine, Andrieu Jean-Pierre, Dupuy Jerome, Petit-Hartlein Isabelle, Caux-Thang Christelle, Vivès Corinne, Nivière Vincent, Fieschi Franck, A Two-component NADPH Oxidase (NOX)-like System in Bacteria Is Involved in the Electron Transfer Chain to the Methionine Sulfoxide Reductase MsrP, 10.1074/jbc.m116.752014
- Loschi Lodovica, Brokx Stephen J., Hills Tanya L., Zhang Glen, Bertero Michela G., Lovering Andrew L., Weiner Joel H., Strynadka Natalie C. J., Structural and Biochemical Identification of a Novel Bacterial Oxidoreductase, 10.1074/jbc.m408876200
- Melnyk Ryan A., Youngblut Matthew D., Clark Iain C., Carlson Hans K., Wetmore Kelly M., Price Morgan N., Iavarone Anthony T., Deutschbauer Adam M., Arkin Adam P., Coates John D., Novel Mechanism for Scavenging of Hypochlorite Involving a Periplasmic Methionine-Rich Peptide and Methionine Sulfoxide Reductase, 10.1128/mbio.00233-15
- Vlamis-Gardikas Alexios, Potamitou Aristi, Zarivach Raz, Hochman Ayala, Holmgren Arne, Characterization ofEscherichia coliNull Mutants for Glutaredoxin 2, 10.1074/jbc.m111024200
- Kosower Nechama S., Kosower Edward M., Wertheim Bilha, Correa Walter S., Diamide, a new reagent for the intracellular oxidation of glutathione to the disulfide, 10.1016/0006-291x(69)90850-x
- Lin Kan, O'Brien Kathryn M., Trujillo Carolina, Wang Ruojun, Wallach Joshua B., Schnappinger Dirk, Ehrt Sabine, Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant Defense, 10.1371/journal.ppat.1005675
- Uziel O., Borovok I., Schreiber R., Cohen G., Aharonowitz Y., Transcriptional Regulation of the Staphylococcus aureus Thioredoxin and Thioredoxin Reductase Genes in Response to Oxygen and Disulfide Stress, 10.1128/jb.186.2.326-334.2004
- Marteyn Benoit, Domain Francis, Legrain Pierre, Chauvat Franck, Cassier-Chauvat Corinne, The thioredoxin reductase-glutaredoxins-ferredoxin crossroad pathway for selenate tolerance inSynechocystisPCC6803, 10.1111/j.1365-2958.2008.06550.x
- Pasternak C., Assemat K., Clement-Metral J. D., Klug G., Thioredoxin is Essential for Rhodobacter Sphaeroides Growth by Aerobic and Anaerobic Respiration, 10.1099/00221287-143-1-83
- Scharf C., J. Bacteriol., 180, 1869 (1998)
- Navarro F., Florencio F. J., The Cyanobacterial Thioredoxin Gene Is Required for Both Photoautotrophic and Heterotrophic Growth, 10.1104/pp.111.4.1067
- Kuhns Lisa G., Wang Ge, Maier Robert J., Comparative Roles of the Two Helicobacter pylori Thioredoxins in Preventing Macromolecule Damage, 10.1128/iai.00232-15
- Potter Adam J., Kidd Stephen P., Edwards Jennifer L., Falsetta Megan L., Apicella Michael A., Jennings Michael P., McEwan Alastair G., Thioredoxin Reductase Is Essential for Protection ofNeisseria gonorrhoeaeagainst Killing by Nitric Oxide and for Bacterial Growth during Interaction with Cervical Epithelial Cells, 10.1086/595737
- Kraemer P. S., Mitchell A., Pelletier M. R., Gallagher L. A., Wasnick M., Rohmer L., Brittnacher M. J., Manoil C., Skerett S. J., Salama N. R., Genome-Wide Screen in Francisella novicida for Genes Required for Pulmonary and Systemic Infection in Mice, 10.1128/iai.00978-08
- Rocha E. R., Tzianabos A. O., Smith C. J., Thioredoxin Reductase Is Essential for Thiol/Disulfide Redox Control and Oxidative Stress Survival of the Anaerobe Bacteroides fragilis, 10.1128/jb.00714-07
- Ortenberg R., Gon S., Porat A., Beckwith J., Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli, 10.1073/pnas.0401965101
- Russel M, Model P, Holmgren A, Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis., 10.1128/jb.172.4.1923-1929.1990
- Toledano Michel B., Kumar Chitranshu, Le Moan Natacha, Spector Dan, Tacnet Frédérique, The system biology of thiol redox system in Escherichia coli and yeast: Differential functions in oxidative stress, iron metabolism and DNA synthesis, 10.1016/j.febslet.2007.07.002
- Crooke Helen, Cole Jeff, The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain, 10.1111/j.1365-2958.1995.tb02287.x
- Mavridou Despoina A.I., Ferguson Stuart J., Stevens Julie M., The interplay between the disulfide bond formation pathway and cytochromecmaturation inEscherichia coli, 10.1016/j.febslet.2012.04.055
- Metheringham R., Mol. Gen. Genet., 253, 95 (1996)
- Beckett Caroline S., Loughman Jennifer A., Karberg Katherine A., Donato Gina M., Goldman William E., Kranz Robert G., Four genes are required for the system II cytochromec biogenesis pathway inBordetella pertussis, a unique bacterial model : A bacterial model for system II cytochromecsynthesis, 10.1046/j.1365-2958.2000.02174.x
- Liu Yang-Wei, Kelly David J., Cytochromecbiogenesis inCampylobacter jejunirequires cytochromec6(CccA; Cj1153) to maintain apocytochrome cysteine thiols in a reduced state for haem attachment : Cytochromescbiogenesis and function inC. jejuni, 10.1111/mmi.13008
- Braun M., Thony-Meyer L., Cytochrome c Maturation and the Physiological Role of c-Type Cytochromes in Vibrio cholerae, 10.1128/jb.187.17.5996-6004.2005
- Page M. D., Saunders N. F. W., Ferguson S. J., Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis, 10.1099/00221287-143-10-3111
- Hiniker Annie, Collet Jean-Francois, Bardwell James C. A., Copper Stress Causes anin VivoRequirement for theEscherichia coliDisulfide Isomerase DsbC, 10.1074/jbc.m505742200
- Missiakas D., EMBO J., 14, 3415 (1995)
- Leverrier Pauline, Declercq Jean-Paul, Denoncin Katleen, Vertommen Didier, Hiniker Annie, Cho Seung-Hyun, Collet Jean-François, Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC, 10.1074/jbc.m111.224865
- Kumar Pradeep, Sannigrahi Soma, Scoullar Jessica, Kahler Charlene M., Tzeng Yih-Ling, Characterization of DsbD in Neisseria meningitidis : DsbD is essential for N. meningitidis, 10.1111/j.1365-2958.2011.07546.x
- Vertommen D., Mol. Microbiol., 67, 336 (2008)
- Denoncin Katleen, Vertommen Didier, Paek Eunok, Collet Jean-François, The Protein-disulfide Isomerase DsbC Cooperates with SurA and DsbA in the Assembly of the Essential β-Barrel Protein LptD, 10.1074/jbc.m110.119321
- Missiakas D., EMBO J., 13, 2013 (1994)
- An Ruisheng, Sreevatsan Srinand, Grewal Parwinder S, Moraxella osloensis Gene Expression in the Slug Host Deroceras reticulatum, 10.1186/1471-2180-8-19
- Guo W., Cui Y.-p., Li Y.-r., Che Y.-z., Yuan L., Zou L.-f., Zou H.-s., Chen G.-y., Identification of seven Xanthomonas oryzae pv. oryzicola genes potentially involved in pathogenesis in rice, 10.1099/mic.0.050419-0
- Vincent-Sealy L. V., Thomas J. D., Commander P., Salmond G. P. C., Erwinia carotovora DsbA mutants: evidence for a periplasmic-stress signal transduction system affecting transcription of genes encoding secreted proteins, 10.1099/13500872-145-8-1945
- Zhao C., Hartke A., La Sorda M., Posteraro B., Laplace J.-M., Auffray Y., Sanguinetti M., Role of Methionine Sulfoxide Reductases A and B of Enterococcus faecalis in Oxidative Stress and Virulence, 10.1128/iai.00165-10
- Denkel Luisa A., Horst Sarah A., Rouf Syed Fazle, Kitowski Vera, Böhm Oliver M., Rhen Mikael, Jäger Timo, Bange Franz-Christoph, Methionine Sulfoxide Reductases Are Essential for Virulence of Salmonella Typhimurium, 10.1371/journal.pone.0026974
- Dhandayuthapani S., Blaylock M. W., Bebear C. M., Rasmussen W. G., Baseman J. B., Peptide Methionine Sulfoxide Reductase (MsrA) Is a Virulence Determinant in Mycoplasma genitalium, 10.1128/jb.183.19.5645-5650.2001
- Vattanaviboon P., Seeanukun C., Whangsuk W., Utamapongchai S., Mongkolsuk S., Important Role for Methionine Sulfoxide Reductase in the Oxidative Stress Response of Xanthomonas campestris pv. phaseoli, 10.1128/jb.187.16.5831-5836.2005
- Moskovitz J, Rahman M A, Strassman J, Yancey S O, Kushner S R, Brot N, Weissbach H, Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage., 10.1128/jb.177.3.502-507.1995
- Romsang A., Atichartpongkul S., Trinachartvanit W., Vattanaviboon P., Mongkolsuk S., Gene Expression and Physiological Role of Pseudomonas aeruginosa Methionine Sulfoxide Reductases during Oxidative Stress, 10.1128/jb.00167-13
- Trivedi Raj Narayan, Agarwal Pranjali, Kumawat Manoj, Pesingi Pavan Kumar, Gupta Vivek Kumar, Goswami Tapas Kumar, Mahawar Manish, Methionine sulfoxide reductase A (MsrA) contributes to Salmonella Typhimurium survival against oxidative attack of neutrophils, 10.1016/j.imbio.2015.07.011
- Dhandayuthapani Subramanian, Jagannath Chinnaswamy, Nino Celina, Saikolappan Sankaralingam, Sasindran Smitha J., Methionine sulfoxide reductase B (MsrB) of Mycobacterium smegmatis plays a limited role in resisting oxidative stress, 10.1016/s1472-9792(09)70008-3
- Atack J. M., Kelly D. J., Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni, 10.1099/mic.0.2008/019711-0
- Lee Warren L., Gold Benjamin, Darby Crystal, Brot Nathan, Jiang Xiuju, de Carvalho Luiz Pedro S., Wellner Daniel, St. John Gregory, Jacobs Jr William R., Nathan Carl, Mycobacterium tuberculosisexpresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochlorite, 10.1111/j.1365-2958.2008.06548.x
- Pericone C. D., Overweg K., Hermans P. W. M., Weiser J. N., Inhibitory and Bactericidal Effects of Hydrogen Peroxide Production by Streptococcus pneumoniae on Other Inhabitants of the Upper Respiratory Tract, 10.1128/iai.68.7.3990-3997.2000
- Hassouni M. E., Chambost J. P., Expert D., Van Gijsegem F., Barras F., The minimal gene set member msrA, encoding peptide methionine sulfoxide reductase, is a virulence determinant of the plant pathogen Erwinia chrysanthemi, 10.1073/pnas.96.3.887
- Das Kishore, De la Garza Georgina, Maffi Shivani, Saikolappan Sankaralingam, Dhandayuthapani Subramanian, Methionine Sulfoxide Reductase A (MsrA) Deficient Mycoplasma genitalium Shows Decreased Interactions with Host Cells, 10.1371/journal.pone.0036247
- Singh Vineet K., Vaish Manisha, Johansson Trintje R., Baum Kyle R., Ring Robert P., Singh Saumya, Shukla Sanjay K., Moskovitz Jackob, Significance of Four Methionine Sulfoxide Reductases in Staphylococcus aureus, 10.1371/journal.pone.0117594
- Wizemann T. M., Moskovitz J., Pearce B. J., Cundell D., Arvidson C. G., So M., Weissbach H., Brot N., Masure H. R., Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens., 10.1073/pnas.93.15.7985
- Alamuri Praveen, Maier Robert J., Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen Helicobacter pylori : Msr in H. pylori, 10.1111/j.1365-2958.2004.04190.x
- Beloin Christophe, Valle Jaione, Latour-Lambert Patricia, Faure Philippe, Kzreminski Mickaël, Balestrino Damien, Haagensen Janus A. J., Molin Søren, Prensier Gérard, Arbeille Brigitte, Ghigo Jean-Marc, Global impact of mature biofilm lifestyle on Escherichia coli K-12 gene expression : Mature biofilm formation in E. coli, 10.1046/j.1365-2958.2003.03865.x
- Hitchcock Andrew, Jones Michael A., Hall Stephen J., Myers Jonathan D., Kelly David J., Mulholland Francis, Roles of the twin-arginine translocase and associated chaperones in the biogenesis of the electron transport chains of the human pathogen Campylobacter jejuni, 10.1099/mic.0.042788-0
- Chiarugi Paola, Cirri Paolo, Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction, 10.1016/s0968-0004(03)00174-9
- Tanner John J., Parsons Zachary D., Cummings Andrea H., Zhou Haiying, Gates Kent S., Redox Regulation of Protein Tyrosine Phosphatases: Structural and Chemical Aspects, 10.1089/ars.2010.3611
- Rhee S. G., CELL SIGNALING: H2O2, a Necessary Evil for Cell Signaling, 10.1126/science.1130481
- Mongkolsuk Skorn, Helmann John D., Regulation of inducible peroxide stress responses, 10.1046/j.1365-2958.2002.03015.x
- Antelmann Haike, Helmann John D., Thiol-Based Redox Switches and Gene Regulation, 10.1089/ars.2010.3400
- Storz Gisela, Imlayt James A, Oxidative stress, 10.1016/s1369-5274(99)80033-2
- Choi Hee-Jung, Kim Seung-Jun, Mukhopadhyay Partha, Cho Sayeon, Woo Joo-Rang, Storz Gisela, Ryu Seong-Eon, Structural Basis of the Redox Switch in the OxyR Transcription Factor, 10.1016/s0092-8674(01)00300-2
- Zheng M., Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation, 10.1126/science.279.5357.1718
- Gebendorfer Katharina M., Drazic Adrian, Le Yan, Gundlach Jasmin, Bepperling Alexander, Kastenmüller Andreas, Ganzinger Kristina A., Braun Nathalie, Franzmann Titus M., Winter Jeannette, Identification of a Hypochlorite-specific Transcription Factor fromEscherichia coli, 10.1074/jbc.m111.287219
- Drazic Adrian, Miura Haruko, Peschek Jirka, Le Yan, Bach Nina C., Kriehuber Thomas, Winter Jeannette, Methionine oxidation activates a transcription factor in response to oxidative stress, 10.1073/pnas.1300578110
- Drazic Adrian, Gebendorfer Katharina M., Mak Stefanie, Steiner Andrea, Krause Maike, Bepperling Alexander, Winter Jeannette, Tetramers Are the Activation-competent Species of the HOCl-specific Transcription Factor HypT, 10.1074/jbc.m113.521401
Bibliographic reference | Ezraty, Benjamin ; Gennaris, Alexandra ; Barras, Frédéric ; Collet, Jean-François. Oxidative stress, protein damage and repair in bacteria.. In: Nature Reviews. Microbiology, Vol. 15, no.7, p. 385-396 (2017) |
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Permanent URL | http://hdl.handle.net/2078.1/203845 |