D
Drake S. Eggleston
Researcher at GlaxoSmithKline
Publications - 133
Citations - 4236
Drake S. Eggleston is an academic researcher from GlaxoSmithKline. The author has contributed to research in topics: Crystal structure & Ring (chemistry). The author has an hindex of 28, co-authored 133 publications receiving 3996 citations. Previous affiliations of Drake S. Eggleston include Smith, Kline & French & Laboratory of Molecular Biology.
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Journal ArticleDOI
Type IIA topoisomerase inhibition by a new class of antibacterial agents.
Benjamin D. Bax,Pan F. Chan,Drake S. Eggleston,Drake S. Eggleston,Andrew P. Fosberry,Daniel R. Gentry,Fabrice Gorrec,Fabrice Gorrec,Ilaria Giordano,Michael M. Hann,Alan Joseph Hennessy,Martin Hibbs,Jianzhong Huang,Emma J. Jones,Jo J. Jones,Kristin K. Brown,Ceri J. Lewis,Earl May,Earl May,Martin R. Saunders,Onkar M. P. Singh,Claus Spitzfaden,Carol Shen,Anthony Shillings,Andrew J. Theobald,Alexandre Wohlkonig,Alexandre Wohlkonig,Neil D. Pearson,Michael N. Gwynn +28 more
TL;DR: This work provides new insights into the mechanism of topoisomerase action and a platform for structure-based drug design of a new class of antibacterial agents against a clinically proven, but conformationally flexible, enzyme class.
Journal ArticleDOI
Structure and redox properties of the water-oxidation catalyst [(bpy)2(OH2)RuORu(OH2)(bpy)2]4+
John Gilbert,Drake S. Eggleston,Wyatt R. Murphy,Daniel A. Geselowitz,Susan W. Gersten,Derek J. Hodgson,Thomas J. Meyer +6 more
Journal ArticleDOI
Crystal structure of human cytochrome P450 2D6.
Paul Rowland,Frank E. Blaney,Martin G. Smyth,Jo J. Jones,Vaughan R. Leydon,Amanda K. Oxbrow,Ceri J. Lewis,Mike Tennant,Sandeep Modi,Drake S. Eggleston,Richard J. Chenery,Angela Bridges +11 more
TL;DR: The crystal structure of human 2D6 helps to explain how Asp-301, Glu-216, and Phe-483 can act as substrate binding residues and suggests that the role of PHe-120 is to control the orientation of the aromatic ring found in most substrates with respect to the heme.
ComponentDOI
Design, synthesis, and kinetic evaluation of high-affinity fkbp ligands and the x-ray crystal-structures of their complexes with fkbp12.
Dennis A. Holt,Juan I. Luengo,Dennis S. Yamashita,Hye-Ja Oh,Arda L. Konialian,H.‐K. Yen,Leonard W. Rozamus,Martin Brandt,Mary J. Bossard,Mark Alan Levy,Drake S. Eggleston,Jun Liang,L.W Schultz,T.J Stout,Jon Clardy +14 more
TL;DR: In this article, the design and synthesis of high affinity FKBP12 ligands is described, which can inhibit the cis-trans-peptidylprolyl isomerase (rotamase) activity with an inhibition constant as low as 1 nM, yet they possess remarkable structural simplicity relative to FK506 and rapamycin.