The DinG protein from Escherichia coli is a structure-specific helicase.
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The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathwayYbiB from Escherichia coli, the Defining Member of the Novel TrpD2 Family of Prokaryotic DNA-binding Proteins.Structure of the DNA Repair Helicase XPDATP-dependent RecG helicase is required for the transcriptional regulator OxyR function in Pseudomonas speciesEnzymatic activities and DNA substrate specificity of Mycobacterium tuberculosis DNA helicase XPBFANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner.Mycobacterium tuberculosis DinG is a structure-specific helicase that unwinds G4 DNA: implications for targeting G4 DNA as a novel therapeutic approach.Replication fork reversal after replication-transcription collision.The SOS Regulatory Network.Identification of two DNA helicases UvrD and DinG as suppressors for lethality caused by mutant cspA mRNAsTwo novel PIWI families: roles in inter-genomic conflicts in bacteria and Mediator-dependent modulation of transcription in eukaryotes.Biochemical characterization of Warsaw breakage syndrome helicase.DNA charge transport within the cell.DNA repair and genome maintenance in Bacillus subtilis.Connecting Replication and Repair: YoaA, a Helicase-Related Protein, Promotes Azidothymidine Tolerance through Association with Chi, an Accessory Clamp Loader Protein.Replication-transcription conflicts in bacteria.Stimulation of Escherichia coli DNA damage inducible DNA helicase DinG by the single-stranded DNA binding protein SSB.Welcome the family of FANCJ-like helicases to the block of genome stability maintenance proteins.Tolerance of Escherichia coli to fluoroquinolone antibiotics depends on specific components of the SOS response pathway.FANCJ helicase operates in the Fanconi Anemia DNA repair pathway and the response to replicational stress.Genome dynamics in major bacterial pathogens.Nitrosyl iron complexes--synthesis, structure and biology.DNA-mediated signaling by proteins with 4Fe-4S clusters is necessary for genomic integrity.Staphylococcus aureus DinG, a helicase that has evolved into a nuclease.Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster.The helicases DinG, Rep and UvrD cooperate to promote replication across transcription units in vivoGenetic analysis of Escherichia coli RadA: functional motifs and genetic interactions.Evidence for the role of Mycobacterium tuberculosis RecG helicase in DNA repair and recombination.The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-double-stranded DNA junction.The helicase DinG responds to stress due to DNA double strand breaks.
P2860
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P2860
The DinG protein from Escherichia coli is a structure-specific helicase.
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The DinG protein from Escherichia coli is a structure-specific helicase.
@en
The DinG protein from Escherichia coli is a structure-specific helicase.
@nl
type
label
The DinG protein from Escherichia coli is a structure-specific helicase.
@en
The DinG protein from Escherichia coli is a structure-specific helicase.
@nl
prefLabel
The DinG protein from Escherichia coli is a structure-specific helicase.
@en
The DinG protein from Escherichia coli is a structure-specific helicase.
@nl
P2860
P356
P1476
The DinG protein from Escherichia coli is a structure-specific helicase.
@en
P2093
Oleg N Voloshin
R Daniel Camerini-Otero
P2860
P304
18437-18447
P356
10.1074/JBC.M700376200
P407
P577
2007-04-06T00:00:00Z