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

Ahmed, Ikhlas M MRofe, AdamHenry, Martyn CWest, EricJamieson, CraigMcEwan, Iain JBeveridge, Rebecca2025-01-232025-01-232025-01Ahmed, I M M, Rofe, A, Henry, M C, West, E, Jamieson, C, McEwan, I J & Beveridge, R 2025, '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, vol. 34, no. 1, e5254. https://doi.org/10.1002/pro.52540961-8368PubMedCentral: PMC11635395https://hdl.handle.net/2164/24916136834732engSDG 3 - Good Health and Well-beingReceptors, Androgen/chemistryIntrinsically Disordered Proteins/chemistryHumansProtein DomainsIon Mobility SpectrometryMass SpectrometryProtein ConformationProtein BindingR MedicineBiochemistryMolecular BiologySupplementary DataRIon mobility mass spectrometry unveils conformational effects of drug lead EPI-001 on the intrinsically disordered N-terminal domain of the androgen receptorJournal article10.1002/pro.5254http://www.scopus.com/inward/record.url?scp=85211613819&partnerID=8YFLogxK341