Daniel Martinez Molina

TL;DR: This cellular thermal shift assay (CETSA) is based on the biophysical principle of ligand-induced thermal stabilization of target proteins and validated drug binding for a set of important clinical targets and monitored processes of drug transport and activation, off-target effects and drug resistance in cancer cell lines, as well as drug distribution in tissues.

TL;DR: The cellular thermal shift assay (CETSA) allows studies of target engagement of drug candidates in a cellular context, herein exemplified with experimental data on the human kinases p38α and ERK1/2.

TL;DR: Thermal profiling of cellular proteomes enables the differential assessment of protein ligand binding and other protein modifications, providing an unbiased measure of drug-target occupancy for multiple targets and facilitating the identification of markers for drug efficacy and toxicity.

TL;DR: A recently developed, label-free, biophysical assay, the cellular thermal shift assay (CETSA), which facilitates the direct assessment of TE in cells and tissues at various stages of drug development, and also reveals biochemical events downstream of drug binding and therefore provides a promising means of establishing mechanistic biomarkers.

TL;DR: The structure of CorA supports an efflux system involving dehydration and rehydration of divalent metal ions potentially mediated by a ring of conserved aspartate residues at the cytoplasmic entrance and a carbonyl funnel at the periplasmic side of the pore.