| scholarly article | Q13442814 |
| P6179 | Dimensions Publication ID | 1016935127 |
| P356 | DOI | 10.1038/NSMB856 |
| P698 | PubMed publication ID | 15543158 |
| P5875 | ResearchGate publication ID | 8184126 |
| P2093 | author name string | Cheolju Lee | |
| Gisela Storz | |||
| Seong Eon Ryu | |||
| Seung Jun Kim | |||
| Myeong-Hee Yu | |||
| Sang Chul Lee | |||
| Partha Mukhopadhyay | |||
| Woo-Sung Ahn | |||
| Soon Mi Lee | |||
| P2860 | cites work | Structural basis of the redox switch in the OxyR transcription factor | Q27631186 |
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| How to flip the (redox) switch | Q35015887 | ||
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| P433 | issue | 12 | |
| P304 | page(s) | 1179-1185 | |
| P577 | publication date | 2004-11-14 | |
| P1433 | published in | Nature Structural & Molecular Biology | Q1071739 |
| P1476 | title | Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path | |
| P478 | volume | 11 |
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| Q36845536 | Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys peroxide sensor. |
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| Q37874952 | Iron homeostasis and management of oxidative stress response in bacteria |
| Q26827753 | Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways |
| Q38780589 | Legionella pneumophila OxyR Is a Redundant Transcriptional Regulator That Contributes to Expression Control of the Two-Component CpxRA System |
| Q36425513 | Light-Mediated Sulfenic Acid Generation from Photocaged Cysteine Sulfoxide |
| Q28084963 | Mitochondria: Much ado about nothing? How dangerous is reactive oxygen species production? |
| Q35879792 | Mitochondrial ROS Metabolism: 10 Years Later |
| Q46441615 | Molecular mechanism of oxidative stress perception by the Orp1 protein |
| Q35220672 | Mutational analysis to define an activating region on the redox-sensitive transcriptional regulator OxyR. |
| Q36637889 | Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance |
| Q39005654 | Myeloperoxidase targets oxidative host attacks to Salmonella and prevents collateral tissue damage |
| Q47673498 | On the interactions among zinc availability and responses to ozone stress in durum wheat seedlings |
| Q37168354 | Oxidant sensing by reversible disulfide bond formation |
| Q27675617 | Oxidation-sensing Regulator AbfR Regulates Oxidative Stress Responses, Bacterial Aggregation, and Biofilm Formation in Staphylococcus epidermidis |
| Q34922146 | Oxidative stress enhances cephalosporin resistance of Enterococcus faecalis through activation of a two-component signaling system |
| Q38222588 | Oxidative stress response in Pseudomonas putida |
| Q35611511 | Oxidative stress, redox regulation and diseases of cellular differentiation |
| Q36459359 | Oxidization without substrate unfolding triggers proteolysis of the peroxide-sensor, PerR. |
| Q64120797 | Oxidized OxyR Up-Regulates Expression to Suppress Plating Defects of and Catalase-Deficient Strains |
| Q42030587 | OxyR2 Functions as a Three-state Redox Switch to Tightly Regulate Production of Prx2, a Peroxiredoxin of Vibrio vulnificus. |
| Q41697394 | OxyR2 Modulates OxyR1 Activity and Vibrio cholerae Oxidative Stress Response. |
| Q37679721 | PerR vs OhrR: selective peroxide sensing in Bacillus subtilis |
| Q35031166 | Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis |
| Q36482028 | Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity. |
| Q36281008 | Peroxide-sensing transcriptional regulators in bacteria |
| Q27668121 | Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia |
| Q36334693 | Prediction of reversible disulfide based on features from local structural signatures |
| Q30367869 | Prediction of reversibly oxidized protein cysteine thiols using protein structure properties |
| Q39103477 | Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product. |
| Q34853615 | Proline metabolism increases katG expression and oxidative stress resistance in Escherichia coli |
| Q28829133 | Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding |
| Q27935085 | Proximity-based protein thiol oxidation by H2O2-scavenging peroxidases |
| Q29617340 | ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis |
| Q36198016 | Redox active thiol sensors of oxidative and nitrosative stress |
| Q33578637 | Redox regulatory mechanisms in cellular stress responses |
| Q36756386 | Redox-based regulation of signal transduction: principles, pitfalls, and promises |
| Q28114970 | Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function |
| Q61818422 | Redoxins as gatekeepers of the transcriptional oxidative stress response |
| Q35865019 | Regulation of the protein disulfide proteome by mitochondria in mammalian cells |
| Q34378257 | Regulatory role of tetR gene in a novel gene cluster of Acidovorax avenae subsp. avenae RS-1 under oxidative stress |
| Q41824230 | Regulatory roles for IscA and SufA in iron homeostasis and redox stress responses in the cyanobacterium Synechococcus sp. strain PCC 7002. |
| Q34514368 | Role of oxyR in the oral anaerobe Porphyromonas gingivalis |
| Q39451853 | S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics |
| Q27305361 | Spatially-resolved intracellular sensing of hydrogen peroxide in living cells |
| Q27678878 | Staphylococcus aureus CymR Is a New Thiol-based Oxidation-sensing Regulator of Stress Resistance and Oxidative Response |
| Q30374300 | Structural details of the OxyR peroxide-sensing mechanism |
| Q27676699 | Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR |
| Q59199785 | Structural snapshots of OxyR reveal the peroxidatic mechanism of H2O2 sensing |
| Q27678886 | Structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form |
| Q27680170 | Structures of thePorphyromonas gingivalisOxyR regulatory domain explain differences in expression of the OxyR regulon inEscherichia coliandP. gingivalis |
| Q36901967 | Synergistic effects of ascorbate and sorafenib in hepatocellular carcinoma: New insights into ascorbate cytotoxicity |
| Q42375356 | The Methanogen-Specific Transcription Factor MsvR Regulates the fpaA-rlp-rub Oxidative Stress Operon Adjacent to msvR in Methanothermobacter thermautotrophicus |
| Q59065588 | The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation |
| Q36869996 | The Pseudomonas aeruginosa multidrug efflux regulator MexR uses an oxidation-sensing mechanism. |
| Q26774284 | The Roles of Peroxiredoxin and Thioredoxin in Hydrogen Peroxide Sensing and in Signal Transduction |
| Q35095921 | The YaaA protein of the Escherichia coli OxyR regulon lessens hydrogen peroxide toxicity by diminishing the amount of intracellular unincorporated iron |
| Q42405417 | The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core |
| Q35370790 | The functions of crucial cysteine residues in the arsenite methylation catalyzed by recombinant human arsenic (III) methyltransferase |
| Q29346930 | The hdhA gene encodes a haloacid dehalogenase that is regulated by the LysR-type regulator, HdhR, in Sinorhizobium meliloti. |
| Q46408244 | The hydrogen peroxide hypersensitivity of OxyR2 in Vibrio vulnificus depends on conformational constraints. |
| Q38570138 | The impact of thiol peroxidases on redox regulation |
| Q35602469 | The induction of two biosynthetic enzymes helps Escherichia coli sustain heme synthesis and activate catalase during hydrogen peroxide stress |
| Q28492604 | The major catalase gene (katA) of Pseudomonas aeruginosa PA14 is under both positive and negative control of the global transactivator OxyR in response to hydrogen peroxide |
| Q49845791 | The myeloperoxidase: a fine strategist facing pathogenic infections |
| Q27025122 | The redox biochemistry of protein sulfenylation and sulfinylation |
| Q37511905 | The role of redox mechanisms in cell signalling |
| Q39798896 | The stringent response controls catalases in Pseudomonas aeruginosa and is required for hydrogen peroxide and antibiotic tolerance |
| Q28259282 | The structural basis of XRCC1-mediated DNA repair |
| Q27661691 | The structure of a reduced form of OxyR from Neisseria meningitidis |
| Q35040525 | Thiol-based redox switches and gene regulation |
| Q38365541 | Thiol-based redox switches in prokaryotes |
| Q36199932 | Transcription Factors That Defend Bacteria Against Reactive Oxygen Species |
| Q91623270 | Transcription of cis Antisense Small RNA MtlS in Vibrio cholerae Is Regulated by Transcription of Its Target Gene, mtlA |
| Q36613750 | Translocation as a means of disseminating lipid hydroperoxide-induced oxidative damage and effector action |
| Q46771146 | Use of a genetically encoded hydrogen peroxide sensor for whole cell screening of enzyme activity. |
| Q54971401 | Using in vivo oxidation status of one- and two-component redox relays to determine H2O2 levels linked to signaling and toxicity. |
| Q36147012 | Why do bacteria use so many enzymes to scavenge hydrogen peroxide? |
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