UT Health SA Newsroom: Greehey cancer researcher receives UT System’s Rising STARs award

April 10, 2019

David Libich, PhD, assistant professor of biochemistry and structural biology in the Long School of Medicine and faculty member of UT Health’s Greehey Children’s Cancer Research Institute, has received a Rising STARs Award from the UT System. The award for early-career investigators comes with a $250,000 grant. Dr. Libich, who began work here in 2017, […]

YouTube: Experimental Biology TV, WebsEdgeMedicine

April 4, 2019

 "Cancers in children are rare, and the genetics and epigenetic causes are very different from those of adults. Consequently, the study of the etiology and potential therapies for these tumors requires intensive research. The majority of children diagnosed with cancer survive their disease, but the long-term consequences of current treatments lead to lifelong health issues. [...]

PNAS: Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR

February 26, 2019

Samuel A. Kotler, Vitali Tugarinov, Thomas Schmidt, Alberto Ceccon, David S. Libich, Rodolfo Ghirlando, Charles D. Schwieters, and G. Marius Clore Abstract The N-terminal region of the huntingtin protein, encoded by exon-1, comprises an amphiphilic domain (httNT), a polyglutamine (Q n ) tract, and a proline-rich sequence. Polyglutamine expansion results in an aggregation-prone protein responsible for Huntington’s disease. Here, we study the earliest events […]

The Journal of Physical Chemistry Letters: Extensive Sampling of the Cavity of the GroEL Nanomachine by Protein Substrates Probed by Paramagnetic Relaxation Enhancement

June 21, 2018

Marielle A Wälti 1, David S Libich 1, G Marius Clore 1 Abstract The chaperonin GroEL is an 800 kDa nanomachine comprising two heptameric rings, each of which encloses a large cavity or folding chamber. The GroEL cycle involves ATP-dependent capping of the cavity by the cochaperone GroES to create a nanocage in which a single protein molecule can fold. […]

Biochemistry: Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR

February 21, 2017

David S Libich 1, Vitali Tugarinov 1, Rodolfo Ghirlando 1, G Marius Clore 1 Abstract The interaction of two folding intermediate mimetics of the model protein substrate Fyn SH3 with the chaperonin GroEL, a supramolecular foldase/unfoldase machine, has been investigated by 15N relaxation-based nuclear magnetic resonance spectroscopy (lifetime line broadening, dark-state exchange saturation transfer, and relaxation dispersion). The two mimetics comprise C-terminal truncations […]