Emily R. Derbyshire, Associate Professor of Chemistry

Contact Info:

Office Location:	3218 FFSC
Office Phone:	(919) 660-1511
Email Address:
Web Page:	http://derbylab.org/

Teaching (Fall 2024):

• CHEM 517.01, MOLECULES IN LIFE AND DISEASE Synopsis

  FFSC 2237, TuTh 10:05 AM-11:20 AM

Education:

Ph.D.	University of California, Berkeley	2008
B.S.	Trinity College	2002

Research Interests:

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 – forward and reverse chemical genetics – to dissecting biological pathways and identifying small molecules with potential therapeutic value. Our interdisciplinary collaborative program integrates both novel and established methods to address target identification, one of the most challenging aspects of malaria drug discovery. Our lab’s goal is to globally interrogate parasite biology by using chemical biology, molecular biology, and biochemistry to characterize the roles of essential proteins.

Keywords:

Actinomycetales • Adenosine Triphosphate • Adenylate Cyclase • Alcohols • Alkanes • Alkylation • Allosteric Regulation • Allosteric Site • Amino Acid Sequence • Animals • Anopheles • Anthraquinones • Anti-Bacterial Agents • Antimalarials • Antineoplastic Agents • Ants • Artemisinins • Atovaquone • Bacillus subtilis • Base Sequence • Binding Sites • Caenorhabditis elegans • Carbon Monoxide • Catalytic Domain • Cell Line, Tumor • Cells, Cultured • Chemistry, Pharmaceutical • Chlamydomonas reinhardtii • Chloroquine • Computer Simulation • Crystallography, X-Ray • Cyclic GMP • Cysteine • Cytokinesis • Dimerization • Drug Design • Drug Discovery • Drug Evaluation, Preclinical • Drug Resistance, Microbial • Drug Screening Assays, Antitumor • Electron Spin Resonance Spectroscopy • Electron Transport Complex III • Electrons • Enzyme Activation • Enzyme Activators • Escherichia coli • Ferrous Compounds • Glutamine • Guanosine Triphosphate • Guanylate Cyclase • Heme • Hemeproteins • Hep G2 Cells • High-Throughput Screening Assays • Humans • Hydroxides • Indazoles • Indicators and Reagents • Inhibitory Concentration 50 • Insect Vectors • Iron • Isocyanates • Isoenzymes • Kinetics • Life Cycle Stages • Ligands • Liver • Malaria • Malaria, Falciparum • Male • Mice • Mice, Inbred C57BL • Microbial Sensitivity Tests • Models, Biological • Models, Chemical • Models, Molecular • Molecular Sequence Data • Mutagenesis, Site-Directed • Mutant Proteins • Mutation • Nitric Oxide • Nitric Oxide Synthase • Nitrosation • Nitroso Compounds • Nucleotides • Organophosphonates • Oxidation-Reduction • Oxygen • Parasitic Sensitivity Tests • PC12 Cells • Phosphorylation • Piperidines • Plasmodium berghei • Plasmodium falciparum • Plasmodium malariae • Porphyrins • Protein Binding • Protein Conformation • Protein Isoforms • Protein Multimerization • Protein Structure, Quaternary • Protein Structure, Tertiary • Protein Subunits • Quinazolines • Quinazolinones • Rats • Receptors, Cytoplasmic and Nuclear • Recombinant Fusion Proteins • Reproducibility of Results • Saccharomyces cerevisiae • Sequence Alignment • Sequence Homology, Amino Acid • Signal Transduction • Solubility • Spectrophotometry • Spectrophotometry, Ultraviolet • Spectroscopy, Electron Energy-Loss • Spectrum Analysis, Raman • Spodoptera • Sporozoites • Structure-Activity Relationship • Substrate Specificity • Sulfhydryl Compounds • Symbiosis • Temperature • Thermoanaerobacter • Thiazepines • Treatment Outcome • Tyrosine • Vibrio cholerae

Recent Publications   (More Publications)

1. Mansfield, CR; Quan, B; Chirgwin, ME; Eduful, B; Hughes, PF; Neveu, G; Sylvester, K; Ryan, DH; Kafsack, BFC; Haystead, TAJ; Leahy, JW; Fitzgerald, MC; Derbyshire, ER, Selective targeting of Plasmodium falciparum Hsp90 disrupts the 26S proteasome., Cell Chem Biol (March, 2024), pp. S2451-9456(24)00082-5 [doi]  [abs]
2. Schroeder, EA; Toro-Moreno, M; Raphemot, R; Sylvester, K; Colón, IC; Derbyshire, ER, Toxoplasma and Plasmodium associate with host Arfs during infection., edited by Blader, IJ, mSphere, vol. 9 no. 3 (March, 2024), pp. e0077023, American Society for Microbiology [doi]  [abs]
3. Ong, HW; de Silva, C; Avalani, K; Kwarcinski, F; Mansfield, CR; Chirgwin, M; Truong, A; Derbyshire, ER; Zutshi, R; Drewry, DH, Characterization of 2,4-Dianilinopyrimidines Against Five P. falciparum Kinases PfARK1, PfARK3, PfNEK3, PfPK9, and PfPKB., ACS medicinal chemistry letters, vol. 14 no. 12 (December, 2023), pp. 1774-1784 [doi]  [abs]
4. D'Ambrosio, HK; Keeler, AM; Derbyshire, ER, Examination of Secondary Metabolite Biosynthesis in Apicomplexa., Chembiochem : a European journal of chemical biology, vol. 24 no. 17 (September, 2023), pp. e202300263 [doi]  [abs]
5. Keeler, AM; Petruzziello, PE; Boger, EG; D'Ambrosio, HK; Derbyshire, ER, Exploring the Chain Release Mechanism from an Atypical Apicomplexan Polyketide Synthase., Biochemistry, vol. 62 no. 17 (September, 2023), pp. 2677-2688 [doi]  [abs]