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Niels Bradshaw

Assistant Professor of Biochemistry
Niels  Bradshaw
niels@brandeis.edu
781-736-2309
Volen National Center for Complex Systems, 416

Departments/Programs

Biochemistry

Degrees

University of California, San Francisco, Ph.D.
University of Chicago, B.A.

Expertise

Regulation of protein phosphatases and the evolution of cellular signaling. Bacterial stress responses and community behavior.

Profile

I study how cells sense cellular and environmental conditions to appropriately grow, divide, survive, and coordinate their behaviors in communities. Reversible phosphorylation of proteins is a fundamental mechanism cells use to control their physiology; I use genetics, cell biology, mechanistic enzymology, and structural biology to identify how phosphatases achieve regulation and specificity, and how kinases and phosphatases work together to controll signaling. We address these questions in two major biological systems: 1) Phosphatases that control stress responses, developmental programs, and community behavior in bacteria. 2) Phosphatases that control human signaling pathways that drive cancer and other diseases.

Courses Taught

BCHM 103b Advanced Biochemistry: Cellular Information Transfer Mechanisms

Scholarship

Ho, Kristin and Bradshaw, Niels. "A conserved allosteric element controls specificity and activity of functionally divergent PP2C phosphatases from B. subtilis." Journal of Biological Chemistry (2021).

Bradshaw, N., Levdikov, V. M., Zimanyi, C. M., Gaudet, R., Wilkinson, A. J., and Losick, R.. "A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases.." eLife 6. e6211 (2017).

DeFrancesco, A.S., Masloboeva, N., Syed, A.K., Deloughery, A., Bradshaw, N., Li, G.-W., Gilmore, M.S., Walker, S., and Losick, R.. "Genome-wide screen for genes involved in eDNA release during biofilm formation by Staphylococcus aureus.." PNAS 114. 28 (2017): E5969-E5978.

Bradshaw, N. & Losick, R.. "Asymmetric division triggers cell-specific gene expression through coupled capture and stabilization of a phosphatase.." eLife 4. (2015): e08145.



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