Ellen Yeh
Academic Appointments
- Assistant Professor, Pathology
- Member, Child Health Research Institute
- Assistant Professor, Microbiology & Immunology
- Assistant Professor, Biochemistry
Key Documents
Contact Information
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Clinical Offices
Pathology 269 Campus Dr. CCSR 3245B Stanford, CA 94305 Tel Work (650) 736-0062 Fax (650) 736-0073Practices at Stanford Hospital and Clinics and Lucile Packard Children's Hospital
Professional Overview
Clinical Focus
- Anatomic/Clinical Pathology
- Clinical Microbiology
Honors and Awards
- Early Career Independence Award (DP5), NIH (2012-2017)
- Career Award for Medical Scientists, Burroughs-Wellcome Fund (2012-2017)
- Medical Scientist Training Program (MSTP), NIH (2001-2008)
Professional Education
| Residency: | Stanford Hospital & Clinics CA (2011) |
| Medical Education: | Harvard Medical School MA (2008) |
| MD: | Harvard Medical School, Medicine (2008) |
| PhD: | Harvard Medical School, Biophysics (2006) |
| BA: | Harvard University, Biochemical Sciences (2001) |
Graduate & Fellowship Program Affiliations
Scientific Focus
Current Research Interests
The chemistry and biology of the unique plastid organelle, the apicoplast, in malaria parasites
Malaria caused by Plasmodium spp parasites has an enormous disease burden that disproportionately affects the worlds poorest and youngest. New anti-malarials with novel drug mechanisms are desperately needed in the face of existing or emerging drug resistance to all available therapies. Investigation of Plasmodium biology offers both the potential for important biomedical impact and an opportunity to explore fascinating eukaryotic biology. Given the challenges of genetic and other approaches to studying this complex organism, the development of chemical tools will be especially critical in pushing forward basic research.
My research focuses on the apicoplast, a prokaryotically-derived plastid organelle unique to Plasmodium (and other pathogenic Apicomplexa parasites) and a key anti-malarial drug target. My laboratory's goal is to elucidate apicoplast biology, function, and role in pathogenesis with the ultimate goal of realizing the potential of the apicoplast as a therapeutic target. In a major step toward this goal, my previous work has demonstrated that the sole essential function of the apicoplast in blood-stage P. falciparum parasites is the biosynthesis of isoprenoid precursors. As such, I was able to generate parasites completely devoid of this essential organelle but chemically rescued by supplementation of the growth media with isopentenyl pyrophosphate (IPP), the pathway product. Chemical rescue and apicoplast(-) parasites are innovative tools for investigating apicoplast biology and for advancing apicoplast-directed drug and vaccine development. Our research takes advantage of these new tools and our newfound understanding of apicoplast function to explore a variety of topics, including protein trafficking to the apicoplast and the protein "prenylome" in Plasmodium. We employ a variety of methods but have a particular focus on the use of chemical tools to overcome the current challenges in studying this organelle. Our exploration of the Plasmodium apicoplast are likely to reveal both unique biology and targets for anti-malarial drug development.
Publications
- Chemical rescue of malaria parasites lacking an apicoplast defines organelle function in blood-stage Plasmodium falciparum. PLoS Biol. 2011; (8): e1001138
- Immediate incubation reduces indeterminate results for QuantiFERON-TB Gold in-tube assay. J Clin Microbiol. 2010; (8): 2672-6
- Preferential lower respiratory tract infection in swine-origin 2009 A(H1N1) influenza. Clin Infect Dis. 2010; (3): 391-4
- Real-time PCR testing for mecA reduces vancomycin usage and length of hospitalization for patients infected with methicillin-sensitive staphylococci. J Clin Microbiol. 2010; (3): 785-90
- Hair sheep blood, citrated or defibrinated, fulfills all requirements of blood agar for diagnostic microbiology laboratory tests. PLoS One. 2009; (7): e6141
- Characterization of the aminocarboxycyclopropane-forming enzyme CmaC. Biochemistry. 2007; (2): 359-68
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