Superoxide accelerates DNA damage by elevating free-iron levels.
about
Oxidative Decay of DNAOxidative-stress resistance mutants of Helicobacter pylori.A small RNA promotes siderophore production through transcriptional and metabolic remodelingRedox pioneer: professor Irwin FridovichWidespread distribution in pathogenic bacteria of di-iron proteins that repair oxidative and nitrosative damage to iron-sulfur centersMicroarray analysis of Pseudomonas aeruginosa reveals induction of pyocin genes in response to hydrogen peroxideStaphylococcal response to oxidative stressWhat really happens in the neutrophil phagosome?The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteinsTwo Distinct Ferritin-like Molecules in Pseudomonas aeruginosa : The Product of the bfrA Gene Is a Bacterial Ferritin (FtnA) and Not a Bacterioferritin (Bfr)Evidence for a novel role of copper-zinc superoxide dismutase in zinc metabolism.Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly.The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species.Oxidative damage is increased in human liver tissue adjacent to hepatocellular carcinomaRyhB small RNA modulates the free intracellular iron pool and is essential for normal growth during iron limitation in Escherichia coliAnalysis of S-nitroso-N-acetylpenicillamine effects on dopamine release in the striatum of freely moving rats: role of endogenous ascorbic acid and oxidative stressRapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and independent transcriptional networksRibonucleotide reductases of Salmonella typhimurium: transcriptional regulation and differential role in pathogenesisProteomic and physiological responses of Kineococcus radiotolerans to copperGlobal transcriptome analysis of Staphylococcus aureus response to hydrogen peroxidePerR acts as a switch for oxygen tolerance in the strict anaerobe Clostridium acetobutylicumBacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressorsContrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletionThe DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureusA potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of Gram-negative bacteriaAn Open and Shut Case: The Interaction of Magnesium with MST EnzymesGeobacter sulfurreducens has two autoregulated lexA genes whose products do not bind the recA promoter: differing responses of lexA and recA to DNA damage.Interaction of Bacillus subtilis Fur (ferric uptake repressor) with the dhb operator in vitro and in vivo.Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible.Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutansCellular defenses against superoxide and hydrogen peroxideIron induces bimodal population development by Escherichia coliMechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator.Role of iron in neurodegenerative diseases.Construction and characterization of transposon insertion mutations in Corynebacterium diphtheriae that affect expression of the diphtheria toxin repressor (DtxR).Knock-out of SO1377 gene, which encodes the member of a conserved hypothetical bacterial protein family COG2268, results in alteration of iron metabolism, increased spontaneous mutation and hydrogen peroxide sensitivity in Shewanella oneidensis MR-1Inhibition of staphylococcal biofilm formation by nitrite.Oxidative inactivation of mitochondrial aconitase results in iron and H2O2-mediated neurotoxicity in rat primary mesencephalic cultures.Oxidative risk for atherothrombotic cardiovascular disease.
P2860
Q22066181-D6F0D24F-775F-4F7E-8419-7DA1F90F2030Q24538998-3C7C9599-F29A-4881-BA36-FD18085B98D3Q24621536-23E6E717-0E23-4590-A97C-F1EE52276EACQ24633721-F273927F-06DA-4ED6-8BBE-B7EFD0ABEC5CQ24657985-257EE8B2-45D5-4C05-98C7-A89CDEE11E56Q24816990-5FE9345B-9366-4F31-9A04-6D0F3AF151DCQ26991866-86A8BAD4-C154-41BA-99F8-428F281A782CQ26995028-60611388-1834-4A51-891E-50C5637B988EQ27443131-0FF7A773-F600-4C02-99C4-F609EE9A7C85Q27667858-5A6EE581-5CF1-4A02-ADE9-E8AC57A33F69Q27934416-71E59F8B-B45E-4AB7-A718-AD1CA79A8771Q27934525-761BB167-9B34-4EB9-BA22-12A83A1B3C18Q27935180-8AD26049-887E-4799-965B-B75AA5EED5D2Q27939493-D6BA75EC-FF35-4B00-8E63-556A482B62FDQ28265837-F4E7C4B3-0F5C-41DE-8BE4-8DE7A3CD882AQ28271605-9E6809DF-38A1-4C84-9185-635E31834FACQ28349970-04E2CF6B-F1F4-406F-A0E6-A5D44EEDD382Q28471595-2A87A227-EB58-4707-934F-338D032EA431Q28474730-AE61F9B3-0627-41BE-965C-52F8F3E02A21Q28475313-F58F0014-E127-46ED-AC85-E9761BAAFD39Q28485590-F673C6AA-1517-4F19-803E-1C49DD1A16B2Q28485887-38309AF7-59E3-49A8-B842-F1ED9E4BC2ADQ28488940-2FBB1E4D-F7B9-4179-9843-1471F0095A92Q28493128-536FCA0D-F77E-4A17-B1C6-788CF5CD963DQ28553511-6D5E69E7-3761-4721-ABB1-075DB9C52CE9Q28611508-3094FB23-3B31-4D3F-A0D4-6A7F7E442E48Q28829605-6585033C-74B7-4CA4-ADFF-1A7F3633CBCAQ29346626-933086DF-12D6-4FE6-BF31-BA9DFBA6910AQ29346693-EA50BEEF-E2B9-4B27-A185-D95E1E29BAD3Q29346706-548FAD64-37EC-4546-A0AF-2AA7AF8FE2E8Q29391695-AFB61A8D-7BD9-4CD8-9BFF-51FD94B5894AQ29615306-185E1111-8EB2-404C-817B-AC0E95BDC313Q30536025-C3AA6314-285E-485C-8CFB-B887F8EB45B4Q30658057-1A10E7AE-8A9D-4BD5-B86A-03F2CF027C3CQ31038817-531B4A7D-3314-4E33-89C6-C1A94161FBB4Q31110538-E6785152-075D-462D-919F-E7E7A29502BCQ33239143-DC8FB23E-CDD4-43DA-BC6E-64E322F73E11Q33295154-C47E2465-1B9A-482E-9CF2-0B430BD2130AQ33504558-BABE179C-5C84-495F-BD36-4816CD3BC24DQ33554184-028F4D21-94BC-48BF-A820-5E48235BDBCE
P2860
Superoxide accelerates DNA damage by elevating free-iron levels.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Superoxide accelerates DNA damage by elevating free-iron levels.
@ast
Superoxide accelerates DNA damage by elevating free-iron levels.
@en
type
label
Superoxide accelerates DNA damage by elevating free-iron levels.
@ast
Superoxide accelerates DNA damage by elevating free-iron levels.
@en
prefLabel
Superoxide accelerates DNA damage by elevating free-iron levels.
@ast
Superoxide accelerates DNA damage by elevating free-iron levels.
@en
P2860
P356
P1476
Superoxide accelerates DNA damage by elevating free-iron levels.
@en
P2093
P2860
P304
13635-13640
P356
10.1073/PNAS.93.24.13635
P407
P577
1996-11-01T00:00:00Z