An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein

scientific article published on January 1994

An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein is …
instance of (P31):
scholarly articleQ13442814

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P932PMC publication ID394787
P698PubMed publication ID8306957

P2093author name stringB Demple
E Hidalgo
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Untwist and shout: a heavy metal-responsive transcriptional regulatorQ36074033
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Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coliQ36145766
A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress.Q36179934
Genetic analysis of transcriptional activation and repression in the Tn21 mer operonQ36180026
soxR, a locus governing a superoxide response regulon in Escherichia coli K-12Q36254384
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Regulation of bacterial oxidative stress genesQ36468273
Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulonQ37083624
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Recent developments in the field of iron-sulfur proteins.Q37920968
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Prooxidant states and tumor promotionQ39492603
The regulation of transcription initiation in bacteriaQ39850560
Saccharomyces cerevisiae has distinct adaptive responses to both hydrogen peroxide and menadioneQ39940619
Two-stage control of an oxidative stress regulon: the Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory geneQ39940686
Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidationQ40323852
Molecular characterization of the soxRS genes of Escherichia coli: two genes control a superoxide stress regulonQ40506211
Regulating the fate of mRNA: the control of cellular iron metabolismQ40851091
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Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coliQ41332825
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Allosteric underwinding of DNA is a critical step in positive control of transcription by Hg-MerRQ42617709
The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimerQ43534036
Generation of EPR-detectable nitrosyl-iron complexes in tumor target cells cocultured with activated macrophages.Q43551018
Comparison of regulatory and structural regions of genes of tryptophan metabolismQ46000867
Potent intracellular oxidative stress exerted by the carcinogen 4-nitroquinoline-N-oxide.Q53479294
Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydrataseQ53782091
The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex.Q54361808
Inducible repair of oxidative DNA damage in Escherichia coliQ54492754
An iron-sulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli.Q54662227
The mammalian ultraviolet response is triggered by activation of src tyrosine kinasesQ60621256
Characterization of the FNR protein of Escherichia coli , an iron-binding transcriptional regulatorQ68314718
Saccharomyces cerevisiae has an inducible response to menadione which differs from that to hydrogen peroxideQ70661329
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectironQ677
P304page(s)138-146
P577publication date1994-01-01
P1433published inThe EMBO JournalQ1278554
P1476titleAn iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein
P478volume13

Reverse relations

cites work (P2860)
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