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William L. Duax
Researcher at Hauptman-Woodward Medical Research Institute
Publications - 242
Citations - 4457
William L. Duax is an academic researcher from Hauptman-Woodward Medical Research Institute. The author has contributed to research in topics: Crystal structure & Hydrogen bond. The author has an hindex of 36, co-authored 242 publications receiving 4372 citations. Previous affiliations of William L. Duax include Woodward, Inc. & University at Buffalo.
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Journal ArticleDOI
Structure of human estrogenic 17β-hydroxysteroid dehydrogenase at 2.20 å resolution
Debashis Ghosh,Vladimir Z. Pletnev,Dao-Wei Zhu,Zdislaw Wawrzak,William L. Duax,Walter Pangborn,Fernand Labrie,Sheng-Xiang Lin +7 more
TL;DR: The structure of the active site provides a rational basis for designing more specific inhibitors of this breast cancer associated enzyme and a model for steroid and cofactor binding as well as for the estrone to estradiol transition state is proposed.
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Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family.
Debashis Ghosh,Charles M. Weeks,Pawel Grochulski,William L. Duax,Mary Erman,Robert L. Rimsay,James C. Orr +6 more
TL;DR: The x-ray structure of a short-chain dehydrogenase, the bacterial holo 3 alpha,20 beta-hydroxysteroid dehydrogen enzyme, is described at 2.6 A resolution and the architecture of the postulated active site is consistent with the observed stereospecificity of the enzyme and the fact that the tetramer is the active form.
Journal ArticleDOI
The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases
TL;DR: In this paper, the authors further refined the structure of the short-chain dehydrogenase with its cofactor, nicotinamide adenine dinucleotide (NAD), and solvent molecules, at the same resolution.
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Mechanism of ion exchange in crystalline zirconium phosphates. I. Sodium ion exchange of .alpha.-zirconium phosphate
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The Conducting Form of Gramicidin a is a Right-Handed Double-Stranded Double Helix.
TL;DR: The x-ray crystal structures of the right-handed double-stranded double-helical dimers (DSDH) reported here agree with 15N-NMR and CD data on the functional gramicidin D channel in lipid bilayers and demonstrate single-file ion transfer through the channels.