Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
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Comparison of the DNA association kinetics of the Lac repressor tetramer, its dimeric mutant LacIadi, and the native dimeric Gal repressorRecognition of the four Watson-Crick base pairs in the DNA minor groove by synthetic ligandsGlucocorticoid receptor-glucocorticoid response element binding stimulates nucleosome disruption by the SWI/SNF complexSharing and archiving nucleic acid structure mapping dataSpectral enhancement of proteins: biological incorporation and fluorescence characterization of 5-hydroxytryptophan in bacteriophage lambda cI repressor.Determining the role of missense mutations in the POU domain of HNF1A that reduce the DNA-binding affinity: A computational approach.One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes?Snf2/Swi2-related ATPase Mot1 drives displacement of TATA-binding protein by gripping DNAActivation of gene expression by small molecule transcription factorsDNA-protein interactions: methods for detection and analysis.Classification of RNA structure change by 'gazing' at experimental data.Next generation hairpin polyamides with (R)-3,4-diaminobutyric acid turn unit.Octamerization of lambda CI repressor is needed for effective repression of P(RM) and efficient switching from lysogeny.Combination of native and denaturing PAGE for the detection of protein binding regions in long fragments of genomic DNA.Identifying regulatory elements in eukaryotic genomes.Gel retardation at low pH resolves trp repressor-DNA complexes for quantitative study.Na(+) and K(+) allosterically regulate cooperative DNA binding by the human progesterone receptorStructural heterogeneity in the intrinsically disordered RNA polymerase II C-terminal domain.DNA looping-dependent autorepression of LEE1 P1 promoters by Ler in enteropathogenic Escherichia coli (EPEC).Cyclic polyamides for recognition in the minor groove of DNAMyb protein binds to human immunodeficiency virus 1 long terminal repeat (LTR) sequences and transactivates LTR-mediated transcriptionDNA sequence recognition in the minor groove by crosslinked polyamides: The effect of N-terminal head group and linker length on binding affinity and specificityKinetic trapping of DNA by transcription factor IIIBDNA deformation in nucleoprotein complexes between RNA polymerase, cAMP receptor protein and the lac UV5 promoter probed by singlet oxygen.Triple-helix formation in the antiparallel binding motif of oligodeoxynucleotides containing N(9)- and N(7)-2-aminopurine deoxynucleosidesExpression and purification of recombinant human c-Fos/c-Jun that is highly active in DNA binding and transcriptional activation in vitroFootprint analysis of the RAG protein recombination signal sequence complex for V(D)J type recombination.Nucleic acid fragmentation on the millisecond timescale using a conventional X-ray rotating anode source: application to protein-DNA footprintingAdvances in the study of protein-DNA interaction.Operator binding by lambda repressor heterodimers with one or two N-terminal arms.Repression of deoP2 in Escherichia coli by CytR: conversion of a transcription activator into a repressor.SAFA: semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experimentsDeterminants of bacteriophage 933W repressor DNA binding specificity.ZNF143 mediates basal and tissue-specific expression of human transaldolase.Contributions of distinct quaternary contacts to cooperative operator binding by Mnt repressor.Fast Fenton footprinting: a laboratory-based method for the time-resolved analysis of DNA, RNA and proteinsQuantitative analysis of electrophoresis data: novel curve fitting methodology and its application to the determination of a protein-DNA binding constantDNA sequence selectivity of hairpin polyamide turn unitsCharacterization of a silencer element in the first exon of the human osteocalcin geneFlanking DNA-sequences contribute to the specific binding of cI-repressor and OR1.
P2860
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P2860
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
description
1986 nî lūn-bûn
@nan
1986 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@ast
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@en
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@nl
type
label
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@ast
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@en
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@nl
prefLabel
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@ast
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@en
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@nl
P2093
P1476
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
@en
P2093
P304
P356
10.1016/0076-6879(86)30011-9
P407
P577
1986-01-01T00:00:00Z