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Timothy Street

Associate Professor of Biochemistry
Timothy  Street
tstreet@brandeis.edu
781-736-4961
Rosenstiel Basic Medical Sciences Research Center, 648A

Departments/Programs

Biochemistry
Rosenstiel Basic Medical Sciences Research Center

Degrees

The Johns Hopkins University, Ph.D.
University of California, Berkeley, B.S.

Expertise

Protein folding and misfolding
Molecular chaperones
Hsp90 molecular chaperone
Insulin family of growth factors

Profile

Please visit my new faculty profile page here.

The 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.

Courses Taught

BCBP 200b Reading in Macromolecular Structure-Function Analysis
BCBP 266a Advanced Topics in Protein Folding
BCBP 296a Master's Lab Rotation I
BCBP 296b Master's Lab Rotation I
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

Dean's Mentoring Award (2020)

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)

Scholarship

Hoxie RS, Street TO.. "Hsp90 chaperones have an energetic hot-spot for binding inhibitors.." Protein Sci. 29. 10 (2021): 2101-2111.

Halpin, J. C., Jangi. R., and Street, T. O.. "Multi-mapping confounds ribosome profiling analysis: A case-study of the Hsp90 molecular chaperone.." Proteins: Structure Function and Bioinformatics (2020).

Huang, B., Freidman, L. J., Sun, M., Gelles, J., and Street, T. O.. "Conformational cycling within the closed state of Grp94, an Hsp90-family chaperone." J Mol Biol 429. (2019): 3312-3323.

Sun, M., Kotler, J. L. M., Liu, S., and Street, T. O.. "The ER chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation.." Journal of Biological Chemistry 294. (2019): 6387-639.

Halpin JC, Street TO. "Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms." J Mol Biol 429. 19 (2017): 2918-2930.

Jin Y, Hoxie RS, Street TO. "Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity." Protein Sci 26. 6 (2017): 2209-2215.

Liu S, Street TO.. "5'-N-ethylcarboxamidoadenosine is not a paralog-specific Hsp90 inhibitor." Protein Science 25. 12 (2017): 2209-2215.

Turman DL, Nathanson JT, Stockbridge RB, Street TO, Miller C.. "Two-sided block of a dual-topology F- channel.." Proc Natl Acad Sci U S A 112. 18 (2017): 5697-701.

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.



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