Ontology highlight
ABSTRACT:
SUBMITTER: Cho KF
PROVIDER: S-EPMC6978363 | biostudies-literature | 2020 Jan
REPOSITORIES: biostudies-literature
Cho Kelvin F KF Ma Taylur P TP Rose Christopher M CM Kirkpatrick Donald S DS Yu Kebing K Blake Robert A RA
Nature communications 20200123 1
The ability to quantitatively measure a small molecule's interactions with its protein target(s) is crucial for both mechanistic studies of signaling pathways and in drug discovery. However, current methods to achieve this have specific requirements that can limit their application or interpretation. Here we describe a complementary target-engagement method, HIPStA (Heat Shock Protein Inhibition Protein Stability Assay), a high-throughput method to assess small molecule binding to endogenous, un ...[more]