P
Paul A. Bates
Researcher at Francis Crick Institute
Publications - 238
Citations - 14094
Paul A. Bates is an academic researcher from Francis Crick Institute. The author has contributed to research in topics: Crystal structure & Hydrogen bond. The author has an hindex of 61, co-authored 233 publications receiving 12829 citations. Previous affiliations of Paul A. Bates include Durham University & Barcelona Supercomputing Center.
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Journal ArticleDOI
Genomic architecture and evolution of clear cell renal cell carcinomas defined by multiregion sequencing
Marco Gerlinger,Stuart Horswell,James Larkin,Andrew Rowan,Max Salm,Ignacio Varela,Rosalie Fisher,Nicholas McGranahan,Nicholas Matthews,Claudio R. Santos,Pierre Martinez,Benjamin Phillimore,Sharmin Begum,Adam Rabinowitz,Bradley Spencer-Dene,Sakshi Gulati,Paul A. Bates,Gordon Stamp,Lisa Pickering,Martin Gore,David Nicol,Steven Hazell,P. Andrew Futreal,Aengus Stewart,Charles Swanton,Charles Swanton +25 more
TL;DR: It was found that 73–75% of identified ccRCC driver aberrations were subclonal, confounding estimates of driver mutation prevalence, and the proportion of C>T transitions at CpG sites increased during tumor progression.
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Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM.
TL;DR: Fourteen models were constructed and analyzed for the comparative modeling section of Critical Assessment of Techniques for Protein Structure Prediction (CASP4), and there now is a convergence of algorithms for comparative modeling and fold recognition, particularly in the region of remote homology.
Journal ArticleDOI
Global topological features of cancer proteins in the human interactome
Pall F. Jonsson,Paul A. Bates +1 more
TL;DR: It is shown that cancer proteins contain a high ratio of highly promiscuous structural domains, i.e., domains with a high propensity for mediating protein interactions, reflecting the central roles of proteins, whose mutations lead to cancer.
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Structure of the AAA ATPase p97.
Xiaodong Zhang,Anthony Shaw,Paul A. Bates,Richard H. Newman,Brent E. Gowen,Elena V. Orlova,Michael A. Gorman,Hisao Kondo,Pawel Dokurno,John M. Lally,Gordon A. Leonard,Hemmo Meyer,Marin van Heel,Paul S. Freemont +13 more
TL;DR: Two structures are reported: a crystal structure of the N-terminal and D1 ATPase domains of murine p97 and a cryoelectron microscopy structure of full-length rat p97, showing that the D1 and D2 hexamers pack in a tail-to-tail arrangement, and that the N domain is flexible.
Journal ArticleDOI
Reversal of DNA alkylation damage by two human dioxygenases
TL;DR: Two human AlkB homologs are identified, ABH2 and ABH3, by sequence and fold similarity, functional assays, and complementation of the E. coli alkB mutant phenotype, which does not appear to correlate with cell proliferation but tissue distributions are different.