Tom L. Blundell
University of Cambridge
716 Papers
8.7K Citations
Tom L. Blundell is an academic researcher from University of Cambridge. The author has contributed to research in topics: Protein structure & Biology. The author has an hindex of 86, co-authored 687 publications. Previous affiliations of Tom L. Blundell include Agricultural and Food Research Council & University of Oxford.
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Papers
Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif
TL;DR: Comparison of the available structural data for BRCA1 BRCT domains in complex with phosphopeptides is compared in order to gain a more complete understanding of the interaction between phosphopePTides and BRC a1-BRCT domains.
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Structural biology of DNA repair: spatial organisation of the multicomponent complexes of nonhomologous end joining.
Takashi Ochi,Bancinyane L. Sibanda,Qian Wu,Dimitri Y. Chirgadze,Victor M. Bolanos-Garcia,Tom L. Blundell +5 more
TL;DR: It is described how a combination of methods—X-ray crystallography, electron microscopy and small angle X-ray scattering—can give insights into the transient multicomponent complexes that mediate NHEJ.
The deubiquitylating enzyme UCHL3 regulates Ku80 retention at sites of DNA damage.
Ryotaro Nishi,Ryotaro Nishi,Paul W. G. Wijnhoven,Paul W. G. Wijnhoven,Yusuke Kimura,Misaki Matsui,Rebecca Konietzny,Qian Wu,Keisuke Nakamura,Tom L. Blundell,Benedikt M. Kessler +10 more
TL;DR: UCHL3 facilitates cellular viability after DSB induction by antagonizing Ku80 ubiquitylation to enhance Ku80 retention at sites of damage, and this phosphorylation destabilizes UCHL3, despite having no effect on its catalytic activity.
Small-Molecule Inhibitors That Target Protein–Protein Interactions in the RAD51 Family of Recombinases
Duncan Scott,Anthony G. Coyne,Ashok R. Venkitaraman,Tom L. Blundell,Chris Abell,Marko Hyvönen +5 more
TL;DR: This study reports the development of indole‐based fragments that bind in a shallow surface pocket of a humanised surrogate of RAD51, an ATP‐dependent recombinase that plays a key role in the repair of double‐strand DNA breaks.
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Structure-guided fragment-based drug discovery at the synchrotron: screening binding sites and correlations with hotspot mapping.
Sherine E. Thomas,P.M. Collins,Rory Hennell James,Rory Hennell James,Vitor Mendes,Sitthivut Charoensutthivarakul,Chris J Radoux,Chris Abell,Anthony G. Coyne,R. Andres Floto,R. Andres Floto,Frank von Delft,Tom L. Blundell +12 more
TL;DR: Advances in X-ray fragment screening and the challenge of identifying sites where fragments not only bind but can be chemically elaborated while retaining their positions and binding modes are discussed.
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