Uracil interference, a rapid and general method for defining protein-DNA interactions involving the 5-methyl group of thymines: the GCN4-DNA complex.
about
Visna virus dUTPase is dispensable for neuropathogenicity.DNA-binding specificity of NGFI-A and related zinc finger transcription factorsdUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae.Critical base pairs and amino acid residues for protein-DNA interaction between the TyrR protein and tyrP operator of Escherichia coli.Subtle hydrophobic interactions between the seventh residue of the zinc finger loop and the first base of an HGATAR sequence determine promoter-specific recognition by the Aspergillus nidulans GATA factor AreA.X4 and R5 HIV-1 have distinct post-entry requirements for uracil DNA glycosylase during infection of primary cells.dUTPase activity is critical to maintain genetic stability in Saccharomyces cerevisiae.Processing of deoxyuridine mismatches and abasic sites by human immunodeficiency virus type-1 integrase.Fine structure of E. coli RNA polymerase-promoter interactions: alpha subunit binding to the UP element minor groovePermanganate oxidation reactions of DNA: perspective in biological studies.Replication properties of dUTPase-deficient mutants of caprine and ovine lentivirusesAnalysis of DNA binding by a eubacterial zinc finger transcription factorContrasting effects of single stranded DNA binding protein on the activity of uracil DNA glycosylase from Escherichia coli towards different DNA substratesDifferential effects of the incorporation of 1-(2-deoxy-2-fluoro-beta-D-arabinofuranosyl)-5-iodouracil (FIAU) on the binding of the transcription factors, AP-1 and TFIID, to their cognate target DNA sequences.Binding site recognition by Rns, a virulence regulator in the AraC family.African swine fever virus dUTPase is a highly specific enzyme required for efficient replication in swine macrophages.From footprint to toeprint: a close-up of the DnaA box, the binding site for the bacterial initiator protein DnaA.Inefficient excision of uracil from loop regions of DNA oligomers by E. coli uracil DNA glycosylase.Modification interference approach to detect ribose moieties important for the optimal activity of a ribozyme.Uracil-DNA glycosylase as a probe for protein--DNA interactions.Chemical reagents for investigating the major groove of DNA.Rns, a virulence regulator within the AraC family, requires binding sites upstream and downstream of its own promoter to function as an activator.Analysis of the DNA-binding sequence specificity of the archaeal transcriptional regulator Ss-LrpB from Sulfolobus solfataricus by systematic mutagenesis and high resolution contact probing.Identification of binding sites for the group A streptococcal global regulator CovR.Binding of the global response regulator protein CovR to the sag promoter of Streptococcus pyogenes reveals a new mode of CovR-DNA interaction.
P2860
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P2860
Uracil interference, a rapid and general method for defining protein-DNA interactions involving the 5-methyl group of thymines: the GCN4-DNA complex.
description
1992 nî lūn-bûn
@nan
1992 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Uracil interference, a rapid a ...... hymines: the GCN4-DNA complex.
@ast
Uracil interference, a rapid a ...... hymines: the GCN4-DNA complex.
@en
type
label
Uracil interference, a rapid a ...... hymines: the GCN4-DNA complex.
@ast
Uracil interference, a rapid a ...... hymines: the GCN4-DNA complex.
@en
prefLabel
Uracil interference, a rapid a ...... hymines: the GCN4-DNA complex.
@ast
Uracil interference, a rapid a ...... hymines: the GCN4-DNA complex.
@en
P2860
P356
P1476
Uracil interference, a rapid a ...... hymines: the GCN4-DNA complex.
@en
P2860
P304
P356
10.1093/NAR/20.4.771
P407
P577
1992-02-01T00:00:00Z