Ted Jardetzky
Academic Appointments
- Professor, Structural Biology
- Member, Stanford Cancer Institute
- Member, Bio-X
Key Documents
Contact Information
- Academic Offices
Personal Information Email Tel (650) 498-4179
Professional Overview
Honors and Awards
- Fellow, American Academy of Microbiology (2008)
- NIH Merit Award, NIAID/NIH (2001-2011)
- Research Scholar, Leukemia and Lymphoma Society (2001-2006)
- Investigator Award, Cancer Research Institute (1999-2003)
- Pew Scholar in the Biomedical Sciences, Pew Foundation (1996-2001)
Professional Education
| Ph.D.: | University of Basel, Swizterland, Biophysical Chemistry (1986) |
| B.S.: | Stanford University, Chemistry (1982) |
Graduate & Fellowship Program Affiliations
Scientific Focus
Current Research Interests
The Jardetzky laboratory is studying the structures and mechanisms of macromolecular complexes important in viral pathogenesis, allergic hypersensitivities and the regulation of cellular growth and differentiation, with an interest in uncovering novel conceptual approaches to intervening in disease processes. Ongoing research projects include studies of paramyxovirus and herpesvirus entry mechanisms, IgE-receptor structure and function and TGF-beta ligand signaling pathways.
Publications
- A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion. Virology. 2013; (1): 118-26
- A time-resolved fluorescence resonance energy transfer assay suitable for high-throughput screening for inhibitors of immunoglobulin E-receptor interactions. Anal Biochem. 2012; (2): 84-9
- Accelerated disassembly of IgE-receptor complexes by a disruptive macromolecular inhibitor. Nature. 2012; (7425): 613-7
- An engineered disulfide bond reversibly traps the IgE-Fc3-4 in a closed, nonreceptor binding conformation. J Biol Chem. 2012; (43): 36251-7
- Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering. Proc Natl Acad Sci U S A. 2012; (39): E2625-34
- Inhibin α-subunit N terminus interacts with activin type IB receptor to disrupt activin signaling. J Biol Chem. 2012; (11): 8060-70
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