Jose M. Barral, MD, PhD Professor and Vice Chair for Operations
Department of Neuroscience & Cell Biology
- Associate Dean for Academic Affairs,
- Graduate School of Biomedical Sciences
- 429C Levin Hall
- Route: 1050 | Tel: 409-747-2180 | Fax: (409) 747-2200 | email@example.com
Education and Training
MD from ITESM, Monterrey, Mexico
PhD in Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas
Post-Doctoral in Biochemistry, Max Planck Institute for Biochemistry, Germany
Basic Science Research: A major goal of my research is to understand the mechanisms and molecules that allow efficient protein folding in vivo. My efforts are focused on: (1) expanding our methodological arsenal to study the relationship between protein synthesis and folding in various model systems and (2) interrogating how protein misfolding leads to disease states, with particular emphasis on neurodegeneration.
Medical and Graduate Education: My main interests are: (1) curriculum design to integrate foundational and clinical sciences based on contextual and causal relationships; and (2) streamlining methodologies to allow efficient incorporation of active learning methodologies into medical and graduate school curricula.
Barral, J.M., Hutagalung, A.H., Brinker, A., Hartl, F.U., Epstein, H.F. Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 295: 669-671, 2002.
Agashe, V.R., Guha, S., Chang, H.-C., Genevaux, P., Hayer-Hartl, M., Stemp, M., Georgopoulos, C., Hartl, F.U. and Barral, J.M. Function of trigger factor and DnaK in multi-domain protein folding: Increase in yield at the expense of folding speed. Cell 117:199-209, 2004.
Hoppe, T., Cassata, G., Barral, J.M., Springer, W., Hutagalung, A.H., Epstein, H.F. and Baumeister, R. Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans. Cell 118:337-349, 2004.
Kaiser, C.M., Chang, H.C., Agashe, V.R., Lakshmipathy, S.K., Etchells, S., Hayer-Hartl, M., Hartl, F.U. and Barral, J.M. Real time observation of Trigger factor function on translating ribosomes. Nature 444:455-460, 2006.
Spencer, P.S., Siller, E., Anderson, J.F. and Barral, J.M. Silent substitutions predictably alter translation elongation rates and protein folding efficiencies. J. Mol. Biol. 422:328-335, 2012.
Barral, J.M. and Buck, E. What, how and why is problem-based learning in medical education; ASBMB Today 12:34-3, 2013.
Zhou, M., Guo, J., Cha, J., Chae, M., Chen, S., Barral, J.M., Sachs, M.S. and Liu, Y. Non-optimal codon usage determines the expression, structure and function of a circadian clock protein. Nature 495:111-115, 2013.
Kim, S.J., Yoon, J.S., Shishido, H. Yang, Z., Rooney, L., Barral, J.M. and Skach, W.R. Translational tuning optimizes nascent protein folding in cells. Science 348:444-448, 2015.