P
Paul S. Carter
Researcher at GlaxoSmithKline
Publications - 24
Citations - 2694
Paul S. Carter is an academic researcher from GlaxoSmithKline. The author has contributed to research in topics: Kinase & Serine/threonine-specific protein kinase. The author has an hindex of 14, co-authored 24 publications receiving 2282 citations.
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Journal ArticleDOI
Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription.
Matthew P. Coghlan,Ainsley A. Culbert,Darren Cross,Stacey L. Corcoran,John W. Yates,Nigel J. Pearce,Olivier Lars SmithKline Beecham Pharmaceu. Rausch,Gregory J. Murphy,Paul S. Carter,Lynne Roxbee Cox,David Mills,Murray J. B. Brown,David Haigh,Robert W. Ward,Smith David Glynn,Kenneth J. Murray,Alastair D. Reith,Julie C. Holder +17 more
TL;DR: SB-216763 and SB-415286 are novel, potent and selective cell permeable inhibitors of GSK-3 and represent valuable pharmacological tools with which the role of G SKS-3 in cellular signalling can be further elucidated.
Journal ArticleDOI
Catalytic in vivo protein knockdown by small-molecule PROTACs
Daniel P. Bondeson,Alina Mares,Ian Edward David Smith,Ko Eunhwa,Sebastien Andre Campos,Afjal Hussain Miah,Katie E Mulholland,Natasha Routly,Dennis L. Buckley,Jeffrey L. Gustafson,Nico Zinn,Paola Grandi,Satoko Shimamura,Giovanna Bergamini,Maria Faelth-Savitski,Marcus Bantscheff,Carly S. Cox,Deborah A. Gordon,Ryan R. Willard,John J. Flanagan,Linda N. Casillas,Bartholomew J. Votta,Willem den Besten,Kristoffer Famm,Laurens Kruidenier,Paul S. Carter,John D. Harling,Ian Churcher,Craig M. Crews +28 more
TL;DR: Major improvements to the proteolysis targeting chimeras (PROTACs) method are described, a chemical knockdown strategy in which a heterobifunctional molecule recruits a specific protein target to an E3 ubiquitin ligase, resulting in the target's ubiquitination and degradation.
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The Structure of Phosphorylated GSK-3β Complexed with a Peptide, FRATtide, that Inhibits β-Catenin Phosphorylation
Benjamin D. Bax,Paul S. Carter,Ceri J. Lewis,Angela R. Guy,Angela Bridges,Robert Tanner,Gary Pettman,Chris Mannix,Ainsley A. Culbert,Murray J. B. Brown,Smith David Glynn,Alastair D. Reith +11 more
TL;DR: The Axin binding site on GSK-3 presumably overlaps with that for FRATtide; its proximity to the active site explains how Axin may act as a scaffold protein promoting β-catenin phosphorylation.
Journal ArticleDOI
Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors.
Xiayang Qiu,Cheryl A. Janson,Ward W. Smith,Susan M. Green,Patrick McDevitt,Kyung O. Johanson,Paul S. Carter,Martin Hibbs,Ceri J. Lewis,Alison F Chalker,Andrew P. Fosberry,Judith LaLonde,John M. Berge,Pamela Brown,Catherine S. V. Houge-Frydrych,Richard L. Jarvest +15 more
TL;DR: Crystal structures of this class of potent and specific inhibitors of bacterial tyrosyl‐tRNA synthetases may contribute to the understanding of the catalytic mechanism and provide the structural basis for designing novel antimicrobial agents.
Journal ArticleDOI
The antimicrobial natural product chuangxinmycin and Some synthetic analogues are potent and selective inhibitors of bacterial tryptophanyl tRNA synthetase
Murray J. B. Brown,Paul S. Carter,Ashley E. Fenwick,Andrew P. Fosberry,Dieter Hamprecht,Martin Hibbs,Richard L. Jarvest,Lucy Mensah,Peter Henry Milner,Peter J. O'Hanlon,Andrew J. Pope,Christine M. Richardson,Andrew West,David R. Witty +13 more
TL;DR: The antimicrobial natural product chuangxinmycin has been found to be a potent and selective inhibitor of bacterial tryptophanyl tRNA synthetase (WRS), and its interaction with WRS appears to be highly constrained, as only sterically smaller analogues afforded significant inhibition.