A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding.

Saved in:
Bibliographic Details
Title: A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding.
Authors: Pflug A; Structure, Biophysics and Fragment-Based Lead Generation, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K., Schimpl M; Structure, Biophysics and Fragment-Based Lead Generation, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K., Nissink JWM; Oncology R&D, AstraZeneca, Cambridge, U.K., Overman RC; Discovery Biology, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K., Rawlins PB; Structure, Biophysics and Fragment-Based Lead Generation, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K., Truman C; Mechanistic Biology and Profiling, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K., Underwood E; Discovery Biology, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K., Warwicker J; Discovery Biology, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K., Winter-Holt J; Oncology R&D, AstraZeneca, Cambridge, U.K., McCoull W; Oncology R&D, AstraZeneca, Cambridge, U.K.
Source: The Biochemical journal [Biochem J] 2020 Nov 27; Vol. 477 (22), pp. 4443-4452.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Published by Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 2984726R Publication Model: Print Cited Medium: Internet ISSN: 1470-8728 (Electronic) Linking ISSN: 02646021 NLM ISO Abbreviation: Biochem J Subsets: MEDLINE
Database: MEDLINE Ultimate
Be the first to leave a comment!
You must be logged in first