个人简介

PhD - University of California, Berkeley BS - Trinity College

研究领域

Biomolecular Structure and Function/Biological/Analytical

Parasites infect billions of humans each year and cause several major diseases, largely in underserved populations in developing parts of the world. Malaria, in particular, is a leading cause of deaths worldwide, and its causative agents, Plasmodium parasites, are crafty as they have successfully eluded our defense mechanisms since they first infected us tens of thousands of years ago. They have several different developmental stages and two hosts: mosquitoes and humans. Despite increased efforts at treating and suppressing the disease around the globe, its impact is increasing due to the parasites?? ability to rapidly mutate and develop resistance to first-line antimalarial drugs. Malaria parasites can synthesize over 5,000 proteins, but the functions of these predicted proteins, along with which ones are important at which developmental stage, are largely unknown. The combination of unexplored biology, poorly understood host-parasite relations, and the burden of morbidity and mortality offer multiple opportunities to conduct research with practical implications. Research in the Derbyshire laboratory uses chemical tools and biological methods to uncover novel aspects of malaria parasite biology with the ultimate aim of identifying druggable targets. Projects range from developing assays for phenotypic and target-based screens ?C forward and reverse chemical genetics ?C to dissecting biological pathways and

近期论文

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Derbyshire, E.R., Clardy, J. Closing in on a New Treatment for Sleeping Sickness. eLife 2013, 2, e01042. Insight. Carr, G., Derbyshire, E.R., Caldera, E., Currie, C.R., Clardy, J. Antibiotic and Antimalarial Quinones from Fungus-Growing Ant-Associated Pseudonocardia sp. Journal of Natural Products 2012, 75, 1806-1809. Gunn, A., Derbyshire, E.R., Marletta, M.A., Britt, R.D. Conformationally Distinct Five-Coordinate Heme-NO Complexes of Soluble Guanylate Cyclase Elucidated by Multifrequency EPR. Biochemistry 2012, 51, 8384-8390. Fernhoff, N.B., Derbyshire, E.R., Underbakke E.S., Marletta, M.A. Heme-Assisted S-nitrosation Desensitizes Ferric Soluble Guanylate Cyclase to Nitric Oxide. Journal of Biological Chemistry 2012, 287, 43053-43062. Derbyshire, E.R., Mazitschek, R., Clardy, J. Halofuginone Inhibition of Liver Stage Malaria. ChemMedChem 2012, 7, 844-849: Selected as Very Important Paper. Featured on Cover. Derbyshire, E.R., Prudencio, M., Mota, M.M., Clardy, J. Liver-Stage Malaria Parasites Vulnerable to Diverse Chemical Scaffolds. Proceedings of the National Academy Science 2012, 109, 8511-8516. Derbyshire, E.R., Marletta, M.A. Structure and Regulation of Soluble Guanylate Cyclase. Annual Review in Biochemistry 2012, 81, 533-539. Review article. Dong, C.K., Urgaonkar, S., Cortese, J.F., Gamo, F.J., Garcia-Bustos, J.F., Lafuente, M.J., Patel, V., Ross, L., Coleman, B.I., Derbyshire, E.R., Clish, C.B., Serrano, A.E., Cromwell, M., Barker, R.H. Jr, Dvorin, J.D., Duraisingh, M.T., Wirth, D.F., Clardy, J., Mazitschek, R. Identification and Validation of Tetracyclic Benzothiazepines as Plasmodium falciparum Cytochrome bc1 Inhibitors. Chemistry & Biology 2011, 18, 1602-1610. Derbyshire, E.R., Mota, M.M., Clardy, J. The Next Opportunity in Anti-Malaria Drug Discovery: The Liver Stage. PLoS Pathogens 2011, 7, e1002178. Review article. Derbyshire, E.R., Winter, M.B.,* Ibrahim, M.,* Deng, S., Spiro, T.G., Marletta, M.A. Probing Domain Function in Soluble Guanylate Cyclase. Biochemistry 2011, 50, 4281-4290: Featured article. Ibrahim, M., Derbyshire, E.R., Soldatova, A.V., Marletta, M.A., Spiro, T.G. Soluble Guanylate Gyclase is Activated Differently by Excess NO and YC-1: Resonance Raman Spectroscopic Evidence. Biochemistry 2010, 49, 4864-4871. Ibrahim, M., Derbyshire, E.R., Marletta, M.A., Spiro, T.G. Probing Soluble Guanylate Cyclase Activation by CO and YC-1 Using Resonance Raman Spectroscopy. Biochemistry 2010, 49, 3815-3823. Derbyshire, E.R., Deng, S., Marletta, M.A. Incorporation of Tyrosine and Glutamine Residues into the Soluble Guanylate Cyclase Heme Distal Pocket Alters NO and O2 Binding. Journal of Biological Chemistry 2010, 285, 17471-17478. Fernhoff, N.B.,* Derbyshire, E.R.,* Marletta, M.A. A Nitric Oxide/Cysteine Interaction Mediates the Activation of Soluble Guanylate Cyclase. Proceedings of the National Academy Science 2009, 106, 21602-21607. Derbyshire, E.R., Fernhoff, N.B., Deng, S., Marletta, M.A. Nucleotide Regulation of Soluble Guanylate Cyclase Substrate Specificity. Biochemistry 2009, 48, 7519-7524. Derbyshire, E.R., Marletta, M.A. Biochemistry of Soluble Guanylate Cyclase. Handbook of Experimental Pharmacology 2009, 191, 17-31. Book chapter. Winger, J.A., Derbyshire, E.R., Lamers, M.H., Marletta, M.A., Kuriyan, J. The Crystal Structure of the Catalytic Domain of a Eukaryotic Guanylate Cyclase. BMC Structural Biology 2008, 8, 42: Highly accessed article. Derbyshire, E.R., Gunn, A., Ibrahim, M., Spiro, T.G., Britt, R.D., Marletta, M.A. Characterization of Two Different 5-Coordinate Soluble Guanylate Cyclase Ferrous Nitrosyl Complexes. Biochemistry 2008, 47, 3892-3899. Derbyshire, E.R., Marletta, M.A. Nitric Oxide: Biological Targets. Wiley Encyclopedia of Chemical Biology 2008, 4, 1-8. Book chapter. Derbyshire, E.R., Marletta, M.A. Butyl Isocyanide as a Probe of the Activation Mechanism of Soluble Guanylate Cyclase: Investigating the Role of Non-Heme Nitric Oxide. Journal of Biological Chemistry 2007, 282, 35741-35748.