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Randal Halfmann

B.S., Genetics, Texas A&M University
Ph.D., Biology, Massachusetts Institute of Technology

Portrait of Randal Halfmann

Why are innate immune signaling pathways structured in such a way that our cells are literally waiting to die?

Research Areas

Development and Regeneration, Genetics and Genomics, Molecular and Cell Biology, Systems Biology

Courses Taught

Cell Biology; Laboratory Rotation; Thesis Laboratory



American Cancer Society Research Scholar


Basil O’Connor Starter Scholar


National Institute of Health Director’s Early Independence Award


Sara and Frank McKnight Fellow, UT Southwestern Medical Center


National Science Foundation Graduate Research Fellow

Randal Halfmann, Ph.D., is an Associate Investigator at the Stowers Institute. Halfmann joined the Institute in 2015.

Born in a rural west Texas, Halfmann received his B.S. in genetics in 2004 from Texas A&M University on an agricultural scholarship earned during his participation in the Future Farmers of America (FFA). He earned a Ph.D. in biology at the Massachusetts Institute of Technology (MIT) in 2010 in the lab of renowned biologist Susan Lindquist, Ph.D. Rather than pursuing a postdoctoral position, Halfmann accepted an independent scientific position at the University of Texas Southwestern Medical Center before joining the Institute in 2015.

The Halfmann Lab investigates the physics governing protein folding, aggregation, and phase transitions that drive gene regulation, cell signaling, and ultimately aging. Specifically, the lab is interested in how energetically unfavorable conditions that govern phase transitions, or the energy required to overcome a disordered liquid protein solution into a solid, ordered protein assembly, arise and how they control intracellular protein activity in time and space. Halfmann and his team combine physics and cell biology to understand the how cells overcome energy barriers to form prions and amyloids.

The lab has and is continuing to develop novel technologies to study protein self-assembly in living cells at high spatial and temporal resolution. They hope to be able to answer scientific inquiries surrounding protein sequence governs development, cellular adaptation, memory, and aging.

Featured Publications

Pathologic polyglutamine aggregation begins with a self-poisoning polymer crystal

Kandola T, Venkatesan S, Zhang J, Lerbakken B, Schulze AV, Blanck JF, Wu J, Unruh J, Berry P, Lange JJ, Box A, Cook M, Sagui C, Halfmann R. eLife 2023;12:RP86939. doi: 10.7554/eLife.86939.

A nucleation barrier spring-loads the CBM signalosome for binary activation

Rodriguez Gama A, Miller T, Lange JJ, Unruh JR, Halfmann R. eLife. 2022;11:e79826. doi: 10.7554/eLife.79826.

Quantifying nucleation in vivo reveals the physical basis of prion-like phase behavior

Khan T, Kandola TS, Wu J, Venkatesan S, Ketter E, Lange JJ, Rodriguez Gama A, Box A, Unruh JR, Cook M, Halfmann R. Mol Cell. 2018;71:155-168.e157.

A self-perpetuating repressive state of a viral replication protein blocks superinfection by the same virus

Zhang XF, Sun R, Guo Q, Zhang S, Meulia T, Halfmann R, Li D, Qu F. PLoS Pathog. 2017;13:e1006253. doi: 1006210.1001371/journal.ppat.1006253.

Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation

Cai X, Chen J, Xu H, Liu S, Jiang QX, Halfmann R, Chen ZJ. Cell. 2014;156:1207-1222.

Heritable remodeling of yeast multicellularity by an environmentally responsive prion

Holmes DL, Lancaster AK, Lindquist S, Halfmann R. Cell. 2013;153:153-165.

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