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Bart L. Staker
Researcher at Center for Infectious Disease Research and Policy
Publications - 96
Citations - 4992
Bart L. Staker is an academic researcher from Center for Infectious Disease Research and Policy. The author has contributed to research in topics: Structural genomics & Topoisomerase. The author has an hindex of 26, co-authored 86 publications receiving 4461 citations. Previous affiliations of Bart L. Staker include Seattle Children's Research Institute & deCODE genetics.
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Journal ArticleDOI
The mechanism of topoisomerase I poisoning by a camptothecin analog
Bart L. Staker,Kathryn Hjerrild,Michael D. Feese,Craig A. Behnke,Alex B. Burgin,Lance Stewart +5 more
TL;DR: The x-ray crystal structure of human topoisomerase I covalently joined to double-stranded DNA and bound to the clinically approved anticancer agent Topotecan suggests that there are at least two classes of mutations that can produce a drug-resistant enzyme.
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ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
Paul Towler,Bart L. Staker,Sridhar Prasad,Saurabh Menon,Jin Tang,Thomas F. Parsons,Dominic Ryan,Martin Fisher,David Williams,Natalie A. Dales,Michael A. Patane,Michael W. Pantoliano +11 more
TL;DR: The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence that offers insights regarding the action of residues involved in catalysis and substrate specificity.
Journal ArticleDOI
Structures of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex
Bart L. Staker,Michael D. Feese,Mark Cushman,Yves Pommier,David E. Zembower,L. Stewart,Alex B. Burgin +6 more
TL;DR: X-ray crystal structures of the human top1-DNA complex bound with camptothecin and representative members of the indenoisoquinoline and indolocarbazole classes of top1 poisons are reported to aid the rational design of completely novel structural classes of anticancer drugs.
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Design of phosphodiesterase 4D (PDE4D) allosteric modulators for enhancing cognition with improved safety
Alex B. Burgin,Olafur T. Magnusson,Jasbir Singh,Pam Witte,Bart L. Staker,Jon Mar Bjornsson,Margret Thorsteinsdottir,Sigrun Hrafnsdottir,Timothy J. Hagen,Alex S. Kiselyov,Lance Stewart,Mark E. Gurney +11 more
TL;DR: Seven co-crystal structures of PDE4 and bound inhibitors are presented that show the regulatory domain closed across the active site, thereby revealing the structural basis of Pde4 regulation, and small-molecule allosteric modulators are designed that do not completely inhibit enzymatic activity.
Journal ArticleDOI
Specific Btk inhibition suppresses B cell– and myeloid cell–mediated arthritis
Julie Di Paolo,Tao Huang,Mercedesz Balazs,James Barbosa,James Barbosa,Kai H. Barck,Brandon J. Bravo,Richard A.D. Carano,James W. Darrow,Douglas R. Davies,Laura DeForge,Lauri Diehl,Ronald E. Ferrando,Steven L. Gallion,Anthony M. Giannetti,Peter Gribling,Vincent Hurez,Vincent Hurez,Sarah G. Hymowitz,Randall Mark Jones,Kropf Jeffrey E,Wyne P. Lee,Patricia Maciejewski,Scott A. Mitchell,Hong Rong,Bart L. Staker,J. Andrew Whitney,Sherry Yeh,Wendy B. Young,Christine Yu,Juan Zhang,Karin Reif,Kevin S. Currie +32 more
TL;DR: CGI1746 is described, a small-molecule Btk inhibitor chemotype with a new binding mode that stabilizes an inactive nonphosphorylated enzyme conformation that decreases cytokine levels within joints and ameliorates disease.