Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
about
Nanostructures for peroxidasesAntimicrobial strategies centered around reactive oxygen species--bactericidal antibiotics, photodynamic therapy, and beyondIron Binding at Specific Sites within the Octameric HbpS Protects Streptomycetes from Iron-Mediated Oxidative StressInterdependence of tetrapyrrole metabolism, the generation of oxidative stress and the mitigative oxidative stress responseRedox regulation by reversible protein S-thiolation in bacteriaDNA Phosphorothioate Modification Plays a Role in Peroxides Resistance in Streptomyces lividansReactive oxygen species do not contribute to ObgE*-mediated programmed cell deathAuranofin exerts broad-spectrum bactericidal activities by targeting thiol-redox homeostasisManaging oxidative stresses in Shewanella oneidensis: intertwined roles of the OxyR and OhrR regulons.The Distinct Transcriptional Response of the Midgut of Amblyomma sculptum and Amblyomma aureolatum Ticks to Rickettsia rickettsii Correlates to Their Differences in Susceptibility to InfectionAntibiotics induce redox-related physiological alterations as part of their lethality.CodY Regulates Thiol Peroxidase Expression as Part of the Pneumococcal Defense Mechanism against H2O2 Stress.Genomic analysis reveals key aspects of prokaryotic symbiosis in the phototrophic consortium "Chlorochromatium aggregatum".Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetECharacterization of a Mycobacterium tuberculosis nanocompartment and its potential cargo proteinsNicotinamide nucleotide transhydrogenase (Nnt) links the substrate requirement in brain mitochondria for hydrogen peroxide removal to the thioredoxin/peroxiredoxin (Trx/Prx) system.Disruption of the S41 peptidase gene in mycoplasma mycoides capri impacts proteome profile, H(2)O(2) production, and sensitivity to heat shockDissecting a complex chemical stress: chemogenomic profiling of plant hydrolysatesA long-chain flavodoxin protects Pseudomonas aeruginosa from oxidative stress and host bacterial clearance.Molecular stress responses to nano-sized zero-valent iron (nZVI) particles in the soil bacterium Pseudomonas stutzeri.Genomic and proteomic evidences unravel the UV-resistome of the poly-extremophile Acinetobacter sp. Ver3.Impaired cell envelope resulting from arcA mutation largely accounts for enhanced sensitivity to hydrogen peroxide in Shewanella oneidensis.Unraveling the Mechanism for the Viability Deficiency of Shewanella oneidensis oxyR Null Mutant.Antibacterial Properties and Mechanism of Activity of a Novel Silver-Stabilized Hydrogen Peroxide.Distinct Responses of Mycobacterium smegmatis to Exposure to Low and High Levels of Hydrogen PeroxideMechanisms of group A Streptococcus resistance to reactive oxygen species.A Kinetic Platform to Determine the Fate of Hydrogen Peroxide in Escherichia coliEndogenous hydrogen peroxide increases biofilm formation by inducing exopolysaccharide production in Acinetobacter oleivorans DR1Transcriptional Profiling of Coxiella burnetii Reveals Extensive Cell Wall Remodeling in the Small Cell Variant Developmental Form.KatG, the Bifunctional Catalase of Xanthomonas citri subsp. citri, Responds to Hydrogen Peroxide and Contributes to Epiphytic Survival on Citrus Leaves.Sequence analysis, expression profiles and function of thioredoxin 2 and thioredoxin reductase 1 in resistance to nucleopolyhedrovirus in Helicoverpa armigera.Exposure of Bacterial Biofilms to Electrical Current Leads to Cell Death Mediated in Part by Reactive Oxygen SpeciesCurrent status and emerging role of glutathione in food grade lactic acid bacteria.Insights into the Function of a Second, Nonclassical Ahp Peroxidase, AhpA, in Oxidative Stress Resistance in Bacillus subtilis.NADPH oxidase-derived H2O2 subverts pathogen signaling by oxidative phosphotyrosine conversion to PB-DOPA.Adaptive strategies and pathogenesis of Clostridium difficile from in vivo transcriptomicsGimme shelter: how Vibrio fischeri successfully navigates an animal's multiple environments.An anaerobic bacterium, Bacteroides thetaiotaomicron, uses a consortium of enzymes to scavenge hydrogen peroxide.Developmental transitions of Coxiella burnetii grown in axenic media.Fenton chemistry at aqueous interfaces.
P2860
Q26782807-B4C6C0F7-A825-4CC3-9B7B-293FAD825070Q27001203-6801A837-4516-4242-841A-46D9E9882FDFQ27679887-0C9596B0-4F7C-47D9-AD04-25AFB3FDBF83Q28081940-CD74C11A-D4EE-4C3A-94E1-E5FA6E634DF4Q28083854-36C4FA56-DFEC-4AF4-AD70-F3EE3AC73882Q28828407-9A444D1A-6775-4B12-A50B-E6FE45199FC1Q28829944-B0143755-C2F0-4952-88B4-24380EC1A140Q29013419-387AACF8-2354-42E7-96AF-CDBCD7549285Q29346668-8F56FA6A-366A-4777-882E-5B7BCD06460DQ33615318-82312599-FE19-4A3C-82C3-707CBEA284E0Q33665248-276ABD31-C826-4744-B523-9CA1DA748DCCQ33723696-1C288481-01ED-440E-924D-A476FCA26711Q33742621-9F59C498-3261-4F91-A822-001DB9D33CACQ33828236-BF178049-6B6F-4EC3-B458-348E85EB82D4Q34073938-3E7BC40B-5312-4F16-8397-00E334B5145CQ34075997-34608FA5-85C8-4FFE-8613-9AF7D70A10B6Q34540121-A3FA3F28-0876-4770-B7E6-7359A11E874BQ34775204-32A7D17E-8847-4EB8-A84B-02B26D1B822BQ35097157-98FB3D0D-88CC-4646-9B29-DAFD9385C326Q35107883-4D68C1C9-8C49-4609-94D9-6C5E2B669B06Q35521947-D3E89176-2C23-4F2A-97FF-A1EC4FE2D310Q35608810-D9241DCE-51D9-4B52-9E3F-9DE6E7CFE646Q35682355-EAE2CEAE-0CCC-4439-99A0-09A0C5224449Q35685926-6D03D433-73DB-4D19-89F0-BC17960D4285Q35725724-EA60B518-8546-4791-B175-A73E7F2A2326Q35804730-1552406B-7C62-467B-89DC-B5519A52CC29Q35834574-A97C3673-6FDE-4F19-954A-FA98169EE638Q35925591-2A348E99-D55B-46AF-B784-9E7C168A7E95Q35933639-9BCC90CC-90C7-44A3-A9C6-9D75A2E32E12Q35962253-CC9FC3A9-9D03-4659-B60A-87D99CF1B978Q36209216-8B405F09-B0DF-473E-8B36-08736427230FQ36228373-FA8E3961-2388-4EC4-AE90-E71ABEBFE76CQ36292837-61E40402-C186-4192-9C66-505638C47ED7Q36709442-8A5D6A58-AEE0-4B3C-8F2F-698AACDDC11EQ37264155-AB1D9B80-42C7-4BAC-9053-33D06C8A4BD3Q37264629-CD8673F7-7DB2-42A1-B6C4-A3A9A498D924Q37349385-9161ADAF-D2D9-4F1E-B618-E298D8CDB259Q37438939-CA398781-C493-4BEB-98DB-0AE675951A58Q37494948-2D351934-91BD-45B4-BB34-8E89B80AA831Q37495159-D24DC1E3-D1AE-4D97-8295-BE48B65A6A8D
P2860
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
@ast
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
@en
type
label
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
@ast
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
@en
prefLabel
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
@ast
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
@en
P2860
P1476
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
@en
P2093
James Imlay
Surabhi Mishra
P2860
P304
P356
10.1016/J.ABB.2012.04.014
P407
P577
2012-05-16T00:00:00Z