Ion mobility mass spectrometry unveils conformational effects of drug lead EPI-001 on the intrinsically disordered N-terminal domain of the androgen receptor.

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第一作者： Ikhlas M M,Ahmed

第一单位： Department of Pure and Applied Chemistry, University of Strathclyde, Glasgow, UK.

作者： Ikhlas M M,Ahmed ^[1] ; Adam,Rofe ^[2] ; Martyn C,Henry ^[1] ; Eric,West ^[2] ; Craig,Jamieson ^[1] ; Iain J,McEwan ^[2] ; Rebecca,Beveridge ^[1]

作者单位： Department of Pure and Applied Chemistry, University of Strathclyde, Glasgow, UK. ^[1] Institute of Medical Sciences, School of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, UK. ^[2]

关键词 EPI‐001 androgen receptor intrinsically disordered proteins ion mobility mass spectrometry native mass spectrometry prostate cancer protein–drug interactions

主题词受体, 雄激素(Receptors, Androgen);人类(Humans);质谱分析法(Mass Spectrometry);蛋白质构象(Protein Conformation);蛋白质结合(Protein Binding)

DOI 10.1002/pro.5254

PMID 39665260

发布时间 2025-02-12

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Protein science

2025年34卷1期

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Ion mobility mass spectrometry unveils conformational effects of drug lead EPI-001 on the intrinsically disordered N-terminal domain of the androgen receptor.

Protein science

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Protein science

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Ion mobility mass spectrometry unveils conformational effects of drug lead EPI-001 on the intrinsically disordered N-terminal domain of the androgen receptor.

Protein science

相似文献

Protein science

相关期刊

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