News
22 June 2022
The switch-like nature of the immune system
Immune cells respond to danger in an “all-or-none” fashion via protein aggregation
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B.S., Genetics, Texas A&M University
Ph.D., Biology, Massachusetts Institute of Technology
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
Honors
2020
American Cancer Society Research Scholar
2017
Basil O’Connor Starter Scholar
2011
National Institute of Health Director’s Early Independence Award
2011
Sara and Frank McKnight Fellow, UT Southwestern Medical Center
2004
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.
News
22 June 2022
Immune cells respond to danger in an “all-or-none” fashion via protein aggregation
Read Article
News
01 September 2020
Several researchers at the Stowers Institute received award notifications during the past few months, including investigators, a postdoctoral researcher, and predoctoral researchers.
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News
06 April 2020
Assistant Investigator Randal Halfmann, PhD, was awarded a four-year grant from the NIH National Institute of General Medical Sciences.
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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.
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.
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.