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

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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
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  Data: A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding.
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  Data: <searchLink fieldCode="AU" term="%22Pflug+A%22">Pflug A</searchLink>; Structure, Biophysics and Fragment-Based Lead Generation, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22Schimpl+M%22">Schimpl M</searchLink>; Structure, Biophysics and Fragment-Based Lead Generation, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22Nissink+JWM%22">Nissink JWM</searchLink>; Oncology R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22Overman+RC%22">Overman RC</searchLink>; Discovery Biology, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22Rawlins+PB%22">Rawlins PB</searchLink>; Structure, Biophysics and Fragment-Based Lead Generation, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22Truman+C%22">Truman C</searchLink>; Mechanistic Biology and Profiling, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22Underwood+E%22">Underwood E</searchLink>; Discovery Biology, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22Warwicker+J%22">Warwicker J</searchLink>; Discovery Biology, Discovery Sciences, R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22Winter-Holt+J%22">Winter-Holt J</searchLink>; Oncology R&D, AstraZeneca, Cambridge, U.K.<br /><searchLink fieldCode="AU" term="%22McCoull+W%22">McCoull W</searchLink>; Oncology R&D, AstraZeneca, Cambridge, U.K.
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  Data: <searchLink fieldCode="JN" term="%222984726R%22">The Biochemical journal</searchLink> [Biochem J] 2020 Nov 27; Vol. 477 (22), pp. 4443-4452.
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  Data: Journal Article; Research Support, Non-U.S. Gov't
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Published+by+Portland+Press+on+behalf+of+the+Biochemical+Society%22">Published by Portland Press on behalf of the Biochemical Society </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>2984726R <i>Publication Model: </i>Print <i>Cited Medium: </i>Internet <i>ISSN: </i>1470-8728 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2202646021%22">02646021 </searchLink><i>NLM ISO Abbreviation: </i>Biochem J <i>Subsets: </i>MEDLINE
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        Value: 10.1042/BCJ20200735
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              Text: 2020 Nov 27
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