D
Dana E. Vanderwall
Researcher at Research Triangle Park
Publications - 22
Citations - 2338
Dana E. Vanderwall is an academic researcher from Research Triangle Park. The author has contributed to research in topics: Cleavage (embryo) & Two-dimensional nuclear magnetic resonance spectroscopy. The author has an hindex of 16, co-authored 22 publications receiving 2223 citations. Previous affiliations of Dana E. Vanderwall include University of Maryland, College Park & Massachusetts Institute of Technology.
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Journal ArticleDOI
Thousands of chemical starting points for antimalarial lead identification
Francisco-Javier Gamo,Laura M. Sanz,J. Vidal,Cristina de Cozar,Emilio Alvarez,J.L. Lavandera,Dana E. Vanderwall,Darren V. S. Green,Vinod Kumar,Samiul Hasan,James R. Brown,Catherine E. Peishoff,Lon R. Cardon,Jose F. Garcia-Bustos +13 more
TL;DR: Chemical structures and associated data suggest several novel mechanisms of antimalarial action, such as inhibition of protein kinases and host–pathogen interaction related targets.
Journal ArticleDOI
Atomic Structure of PDE4: Insights into Phosphodiesterase Mechanism and Specificity
Robert X. Xu,Anne M. Hassell,Dana E. Vanderwall,Millard H. Lambert,William D. Holmes,Michael A. Luther,Warren J. Rocque,Michael V. Milburn,Yingdong Zhao,Hengming Ke,Robert T. Nolte +10 more
TL;DR: The three-dimensional structure of the catalytic domain of phosphodiesterase 4B2B to 1.77 angstrom resolution suggests the mechanism of action and basis for specificity and will provide a framework for structure-assisted drug design for members of the phosphodiedterase family.
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Bleomycins : a structural model for specificity, binding, and double strand cleavage
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Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram.
Robert X. Xu,Warren J. Rocque,Millard H. Lambert,Dana E. Vanderwall,Michael A. Luther,Robert T. Nolte +5 more
TL;DR: In this paper, the crystal structures of the catalytic domain of PDE4B with AMP, 8-Br-AMP and rolipram were determined using X-ray anomalous difference data.
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6-Ethynylthieno[3,2-d]- and 6-ethynylthieno[2,3-d]pyrimidin-4-anilines as tunable covalent modifiers of ErbB kinases.
Edgar R. Wood,Lisa M. Shewchuk,Byron Ellis,Perry Scott Brignola,Ronald L. Brashear,Thomas R. Caferro,Scott Howard Dickerson,Hamilton D. Dickson,Kelly Horne Donaldson,Michael D. Gaul,Robert J. Griffin,Anne M. Hassell,Barry R. Keith,Robert J. Mullin,Kimberly G. Petrov,Michael J. Reno,David W. Rusnak,Sarva M. Tadepalli,John C. Ulrich,Craig D. Wagner,Dana E. Vanderwall,Alex G. Waterson,Jon D. Williams,Wendy L. White,David E. Uehling +24 more
TL;DR: Several ErbB family enzyme and cell potent 6-ethynyl thienopyrimidine kinase inhibitors were found to form covalent adducts with EGFR, which has a conserved cysteine near the ATP binding pocket.