"Footprint" titrations yield valid thermodynamic isotherms
about
Structural mass spectrometry of proteins using hydroxyl radical based protein footprintingUse of a zinc-finger consensus sequence framework and specificity rules to design specific DNA binding proteinsUnfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry.Classification of RNA structure change by 'gazing' at experimental data.Na(+) and K(+) allosterically regulate cooperative DNA binding by the human progesterone receptorCyclic polyamides for recognition in the minor groove of DNADNA sequence recognition in the minor groove by crosslinked polyamides: The effect of N-terminal head group and linker length on binding affinity and specificityReal-time characterization of intermediates in the pathway to open complex formation by Escherichia coli RNA polymerase at the T7A1 promoterSAFA: semi-automated footprinting analysis software for high-throughput quantification of nucleic acid footprinting experimentsZNF143 mediates basal and tissue-specific expression of human transaldolase.Orientation of the tRNA anticodon in the ribosomal P-site: quantitative footprinting with U33-modified, anticodon stem and loop domainsMapping the kinetic barriers of a Large RNA molecule's folding landscape.Flanking DNA-sequences contribute to the specific binding of cI-repressor and OR1.Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function.A genetic network that balances two outcomes utilizes asymmetric recognition of operator sites.Interaction of drugs with branched DNA structures.AlgR-binding sites within the algD promoter make up a set of inverted repeats separated by a large intervening segment of DNA.Progestin regulated miRNAs that mediate progesterone receptor action in breast cancer.Thermodynamic dissection of estrogen receptor-promoter interactions reveals that steroid receptors differentially partition their self-association and promoter binding energetics.Glucocorticoid receptor-promoter interactions: energetic dissection suggests a framework for the specificity of steroid receptor-mediated gene regulation.From steroid receptors to cytokines: the thermodynamics of self-associating systemsHigh-throughput single-nucleotide structural mapping by capillary automated footprinting analysis.Mapping functional regions of transcription factor TFIIIA.Cooperative binding mode of the inhibitors of R6K replication, pi dimers.Informatics challenges in structured RNA.Local kinetic measures of macromolecular structure reveal partitioning among multiple parallel pathways from the earliest steps in the folding of a large RNA molecule.Dissection of androgen receptor-promoter interactions: steroid receptors partition their interaction energetics in parallel with their phylogenetic divergence.Thermodynamic dissection of progesterone receptor interactions at the mouse mammary tumor virus promoter: monomer binding and strong cooperativity dominate the assembly reaction.Design of artificial sequence-specific DNA bending ligands.Mechanism of strand-specific smooth muscle alpha-actin enhancer interaction by purine-rich element binding protein B (Purbeta).Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters.The sequence specificity of homeodomain-DNA interaction.Exhaustive Enumeration of Kinetic Model Topologies for the Analysis of Time-Resolved RNA Folding.Binding site size limit of the 2:1 pyrrole-imidazole polyamide-DNA motif.Semi-automated, single-band peak-fitting analysis of hydroxyl radical nucleic acid footprint autoradiograms for the quantitative analysis of transitions.Steroid receptor-DNA interactions: toward a quantitative connection between energetics and transcriptional regulationOligonucleotide-mediated triple helix formation using an N3-protonated deoxycytidine analog exhibiting pH-independent binding within the physiological range.Analysis of a glucocorticoid-estrogen receptor chimera reveals that dimerization energetics are under ionic controlMeasurement of the binding of transcription factor Sp1 to a single GC box recognition sequenceRate enhancements in the DNase I footprinting experiment
P2860
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P2860
"Footprint" titrations yield valid thermodynamic isotherms
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年学术文章
@wuu
1986年学术文章
@zh-cn
1986年学术文章
@zh-hans
1986年学术文章
@zh-my
1986年学术文章
@zh-sg
1986年學術文章
@yue
1986年學術文章
@zh
1986年學術文章
@zh-hant
name
"Footprint" titrations yield valid thermodynamic isotherms
@en
"Footprint" titrations yield valid thermodynamic isotherms.
@nl
type
label
"Footprint" titrations yield valid thermodynamic isotherms
@en
"Footprint" titrations yield valid thermodynamic isotherms.
@nl
prefLabel
"Footprint" titrations yield valid thermodynamic isotherms
@en
"Footprint" titrations yield valid thermodynamic isotherms.
@nl
P2093
P2860
P356
P1476
"Footprint" titrations yield valid thermodynamic isotherms
@en
P2093
D F Senear
G K Ackers
M Brenowitz
P2860
P304
P356
10.1073/PNAS.83.22.8462
P407
P577
1986-11-01T00:00:00Z