MicroScale Thermophoresis as a Tool to Study Protein-peptide Interactions in the Context of Large Eukaryotic Protein Complexes.
MicroScale Thermophoresis: A Rapid and Precise Method to Quantify Protein–Nucleic Acid Interactions in Solution.
The monoclonal S9.6 antibody exhibits highly variable binding affinities towards different R-loop sequences.
Aptatope mapping of the binding site of a progesterone aptamer on the steroid ring structure.
The Composition of the Arabidopsis RNA Polymerase II Transcript Elongation Complex Reveals the Interplay between Elongation and mRNA Processing Factors.
The characterization and validation of 17β-estradiol binding aptamers.
The Arabidopsis THO/TREX component TEX1 functionally interacts with MOS11 and modulates mRNA export and alternative splicing events.
Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis.
Aptamer Binding Studies Using MicroScale Thermophoresis.
Studying small molecule–aptamer interactions using MicroScale Thermophoresis (MST).
ß-Conglutin dual aptamers binding distinct aptatopes.
Synonymous variants in HTRA1 implicated in AMD susceptibility impair its capacity to regulate TGF-β signaling.
Review: Studying epigenetic interactions using MicroScale Thermophoresis (MST).
In vitro Selection and Interaction Studies of a DNA Aptamer Targeting Protein A.
A Plasmodium Falciparum Bromodomain Protein Regulates Invasion Gene Expression.
The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation.
Mechanisms of in vivo binding site selection of the hematopoietic master transcription factor PU.1.
Large-scale organization of ribosomal DNA chromatin is regulated by Tip5.
Arabidopsis DEAD-Box RNA Helicase UAP56 Interacts with Both RNA and DNA as well as with mRNA Export Factors.
Df31 protein and snoRNAs maintain accessible higher-order structures of chromatin.