Analysis of protein-DNA interactions using surface plasmon resonance.
about
Specific DNA recognition mediated by a type IV pilinInvestigation of DNA sequence recognition by a streptomycete MarR family transcriptional regulator through surface plasmon resonance and X-ray crystallographySurface plasmon resonance: a versatile technique for biosensor applicationsAn integrated model of transcription factor diffusion shows the importance of intersegmental transfer and quaternary protein structure for target site finding.Real-Time Analysis of Specific Protein-DNA Interactions with Surface Plasmon Resonance.The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures.A general method for discovering inhibitors of protein-DNA interactions using photonic crystal biosensorsReverse engineering the yeast RNR1 transcriptional control systemHigh-affinity immobilization of proteins using biotin- and GST-based coupling strategiesExperimental strategies for studying transcription factor-DNA binding specificities.Space-induced bifurcation in repression-based transcriptional circuits.Analysis of the leakage of gene repression by an artificial TetR-regulated promoter in cyanobacteria.Direct Transcriptional Effects of Apolipoprotein EThe effects of magnetic fields exposure on relative permittivity of saline solutions measured by a high resolution SPR system.A capture approach for supercoiled plasmid DNA using a triplex-forming oligonucleotide.DNA methylation presents distinct binding sites for human transcription factors.Discovery and verification of functional single nucleotide polymorphisms in regulatory genomic regions: current and developing technologiesDynamic SPR monitoring of yeast nuclear protein binding to a cis-regulatory elementDissecting the oligonucleotide binding properties of a disordered chaperone protein using surface plasmon resonance.Precise temporal control of the eye regulatory gene Pax6 via enhancer-binding site affinity.Specificity of Atonal and Scute bHLH factors: analysis of cognate E box binding sites and the influence of Senseless.HNRNPA1 interacts with a 5'-flanking distal element of interleukin-6 and upregulates its basal transcription.Using competition assays to quantitatively model cooperative binding by transcription factors and other ligands.
P2860
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P2860
Analysis of protein-DNA interactions using surface plasmon resonance.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Analysis of protein-DNA interactions using surface plasmon resonance.
@ast
Analysis of protein-DNA interactions using surface plasmon resonance.
@en
type
label
Analysis of protein-DNA interactions using surface plasmon resonance.
@ast
Analysis of protein-DNA interactions using surface plasmon resonance.
@en
prefLabel
Analysis of protein-DNA interactions using surface plasmon resonance.
@ast
Analysis of protein-DNA interactions using surface plasmon resonance.
@en
P1476
Analysis of protein-DNA interactions using surface plasmon resonance.
@en
P2093
Christian Speck
Jerzy Majka
P577
2007-01-01T00:00:00Z