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Emily Derbyshire

Assistant Professor of Chemistry and Molecular Genetics and Micriobiology
(919) 660-1511
Research Interest: 
Enzymology
Microbiology and virology
Molecular structure
Research Summary: 
Multidisciplinary research group that addresses global health problems usiing the interface of chemistry and biology.
Research Description: 

Parasites infect millions 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, have successfully eluded our defense mechanisms since they first infected us tens of thousands of years ago.

The Derbyshire Lab uses chemical probes and biological methods to uncover novel aspects of malaria parasite biology with the ultimate aim of identifying druggable targets. Projects range from the biochemical and structural elucidation of essential malaria proteins and developing assays for phenotypic and target-based screens – forward and reverse chemical genetics – to dissecting biological pathways. Our collaborative interdisciplinary program integrates both novel and established methods to address target identification, which is one of the most challenging aspects of malaria drug discovery. Our lab’s goal is to globally interrogate parasite biology by using molecular biology, biochemistry, chemical biology and parasitology.

Publications: 
Chemical interrogation of the malaria kinome.
Derbyshire ER, Zuzarte-Luís V, Magalhães AD, Kato N, Sanschagrin PC, Wang J, Zhou W, Miduturu CV, Mazitschek R, Sliz P, Mota MM, Gray NS, Clardy J.
Chembiochem. 2014. 15:1920-30.

Dihydroquinazolinone inhibitors of proliferation of blood and liver stage malaria parasites.
Derbyshire ER, Min J, Guiguemde WA, Clark JA, Connelly MC, Magalhães AD, Guy RK, Clardy J.
Antimicrob Agents Chemother. 2014. 58:1516-22.

Characterization of Plasmodium liver stage inhibition by halofuginone.
Derbyshire ER, Mazitschek R, Clardy J.
ChemMedChem. 2012. 7:844-9.

Liver-stage malaria parasites vulnerable to diverse chemical scaffolds.
Derbyshire ER, Prudêncio M, Mota MM, Clardy J.
Proc Natl Acad Sci U S A. 2012. 109:8511-6.

A nitric oxide/cysteine interaction mediates the activation of soluble guanylate cyclase.
Fernhoff NB, Derbyshire ER, Marletta MA.
Proc Natl Acad Sci U S A. 2009. 106:21602-7.