Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster.
about
The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathwayATP-dependent RecG helicase is required for the transcriptional regulator OxyR function in Pseudomonas speciesRedox Signaling through DNAElectrochemistry of the [4Fe4S] Cluster in Base Excision Repair Proteins: Tuning the Redox Potential with DNA.DNA-mediated charge transport in redox sensing and signalingThe N-terminal domain of human DNA helicase Rtel1 contains a redox active iron-sulfur cluster.Mycobacterium tuberculosis DinG is a structure-specific helicase that unwinds G4 DNA: implications for targeting G4 DNA as a novel therapeutic approach.8-Oxo-7,8-dihydroguanine: links to gene expression, aging, and defense against oxidative stressFanconi anemia group J mutation abolishes its DNA repair function by uncoupling DNA translocation from helicase activity or disruption of protein-DNA complexes.Molecular and cellular functions of the FANCJ DNA helicase defective in cancer and in Fanconi anemiaTwo novel PIWI families: roles in inter-genomic conflicts in bacteria and Mediator-dependent modulation of transcription in eukaryotes.Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress.Escherichia coli enterobactin synthesis and uptake mutants are hypersensitive to an antimicrobial peptide that limits the availability of iron in addition to blocking Holliday junction resolutionSubunit D of RNA polymerase from Methanosarcina acetivorans contains two oxygen-labile [4Fe-4S] clusters: implications for oxidant-dependent regulation of transcription.DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster.DNA charge transport within the cell.Chemistry of nitrosyliron complexes supported by a β-diketiminate ligandConnecting Replication and Repair: YoaA, a Helicase-Related Protein, Promotes Azidothymidine Tolerance through Association with Chi, an Accessory Clamp Loader Protein.Stimulation of Escherichia coli DNA damage inducible DNA helicase DinG by the single-stranded DNA binding protein SSB.Iron chelators with topoisomerase-inhibitory activity and their anticancer applications.The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: a proposal for an evolutionary driving forceModulation of the structure, catalytic activity, and fidelity of African swine fever virus DNA polymerase X by a reversible disulfide switch.Strand-specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility.Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide.The XPD helicase: XPanDing archaeal XPD structures to get a grip on human DNA repair.Grip it and rip it: structural mechanisms of DNA helicase substrate binding and unwinding.DNA Charge Transport: from Chemical Principles to the Cell.The 'liaisons dangereuses' between iron and antibiotics.Mechanistic and biological considerations of oxidatively damaged DNA for helicase-dependent pathways of nucleic acid metabolism.DNA-mediated signaling by proteins with 4Fe-4S clusters is necessary for genomic integrity.A role for [Fe4S4] clusters in tRNA recognition--a theoretical study.Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.Staphylococcus aureus DinG, a helicase that has evolved into a nuclease.Genetic analysis of Escherichia coli RadA: functional motifs and genetic interactions.A Redox Role for the [4Fe4S] Cluster of Yeast DNA Polymerase δ.Analysis of differences in oxygen sensitivity of Fe-S clusters.The helicase DinG responds to stress due to DNA double strand breaks.Life without Fe-S clusters.Nitric Oxide Modulates Endonuclease III Redox Activity by a 800 mV Negative Shift upon [FeS] Cluster Nitrosylation
P2860
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P2860
Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Redox control of the DNA damag ...... y via its iron-sulfur cluster.
@en
type
label
Redox control of the DNA damag ...... y via its iron-sulfur cluster.
@en
prefLabel
Redox control of the DNA damag ...... y via its iron-sulfur cluster.
@en
P2093
P2860
P356
P1476
Redox control of the DNA damag ...... y via its iron-sulfur cluster.
@en
P2093
Binbin Ren
Huangen Ding
Xuewu Duan
P2860
P304
P356
10.1074/JBC.M807943200
P407
P50
P577
2008-12-12T00:00:00Z