Rosenstiel Basic Medical Sciences Research Center, 648A
DegreesThe Johns Hopkins University, Ph.D.
University of California, Berkeley, B.S.
ExpertiseProtein folding and misfolding
Hsp90 molecular chaperone
Insulin family of growth factors
ProfileThe balance of protein folding and degradation is one of the most fundamental activities of the cell, and is a critical point of intervention in cancer, metabolic, and aging diseases. Molecular chaperones are the central players that regulate the cell's repertoire of folded proteins, and as a consequence chaperones influence virtually every cellular process under both healthy and disease conditions. Despite their central influence, the functional mechanisms of many chaperones are poorly understood. Work in my lab is focused on revealing these mechanisms.
|BCBP||296a||Master's Lab Rotation I|
|BCBP||296b||Master's Lab Rotation I|
|BCBP||297a||Master's Lab Research I|
|BCBP||297b||Master's Lab Research II|
|BCBP||300a||Introduction to Research in Biochemistry and Biophysics I|
|BCBP||300b||Introduction to Research in Biochemistry and Biophysics II|
|BCHM||104b||Physical Chemistry of Macromolecules II|
Awards and Honors
Member of Protein Folding Consortium (2013)
Damon Runyon Cancer Research Foundation Fellowship. (2009)
Burroughs-Wellcome Predoctoral Training Fellowship. (2004)
High honors in physics from UC Berkeley (2001)
Year abroad at Cambridge University. (1999)
Jackson Halpin, Bin Huang, Ming Sun, Timothy Street. "Crowding Activates Heat Shock Protein 90." Journal of Biological Chemistry (2016).
Street TO, X. Zeng, R. Pellarin, M. Bonomi, A. Sali, MJS. Kelly, F. Chu, DA. Agard. "Elucidating the mechanism of substrate recognition by the Hsp90 molecular chaperone." J. Mol. Biol. N/A. N/A (2014): N/A.