Ontology highlight
ABSTRACT:
SUBMITTER: Subramanian G
PROVIDER: S-EPMC7536819 | biostudies-literature | 2020 Mar
REPOSITORIES: biostudies-literature
Subramanian Govindan G Vairagoundar Rajendran R Bowen Scott J SJ Roush Nicole N Zachary Theresa T Javens Christopher C Williams Tracey T Janssen Ann A Gonzales Andrea A
RSC medicinal chemistry 20200110 3
<i>In silico</i> virtual screening followed by <i>in vitro</i> biochemical, biophysical, and cellular screening resulted in the identification of distinctly different <i>h</i>TrkA kinase domain inhibitor scaffolds. X-ray structural analysis of representative inhibitors bound to <i>h</i>TrkA kinase domain defined the binding mode and rationalized the mechanism of action. Preliminary assessment of the sub-type selectivity against the closest <i>h</i>TrkB isoform, and early ADME guided the progress ...[more]