Contact information
William Bradshaw
Postdoctoral Scientist - Structural Biology
William received his PhD from the University of Bath, where he worked with Professor Ravi Acharya, studying the structure of proteins found in the S-layer of the "superbug" Clostridioides difficile using X-ray crystallography. He joined the CMD as a postdoctoral researcher in 2018 and works on the structures of a range of proteins that have been implicated in inflammation in the brain in Alzheimer's disease. As part of this work, he has completed five crystallographic fragment screens at Diamond Light Source, determining 256 structures with small molecules bound. He has also determined other structures of proteins implicated in Alzheimer’s in ligand-bound and apo forms, combining these with complementary techniques to improve understanding of their functions, mechanisms and structural dynamics with an aim of working towards small molecule probes.
Recent publications
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Binding-Site Purification of Actives (B-SPA) Enables Efficient Large-Scale Progression of Fragment Hits by Combining Multi-Step Array Synthesis With HT Crystallography.
Journal article
Grosjean H. et al, (2025), Angew Chem Int Ed Engl
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The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures.
Journal article
Bradshaw WJ. et al, (2024), Structure, 32, 2337 - 2351.e4
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Regulation of inositol 5-phosphatase activity by the C2 domain of SHIP1 and SHIP2.
Journal article
Bradshaw WJ. et al, (2024), Structure, 32, 453 - 466.e6
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Discovery of FERM domain protein-protein interaction inhibitors for MSN and CD44 as a potential therapeutic approach for Alzheimer's disease.
Journal article
Du Y. et al, (2023), J Biol Chem, 299
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Regulation of inositol 5-phosphatase activity by the C2 domain of SHIP1 and SHIP2
Preprint
Bradshaw WJ. et al, (2023)
