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Tsai Laboratory

Houston, Texas

BCM is an internationally respected medical and research institution known for excellence in education, research and patient care.
Francis Tsai
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Selected Publications

1. Sung, N., Lee, J., Kim, J.-H., Chang, C., Joachimiak, A., Lee, S. and Tsai, F.T.F. (2016) Mitochondrial Hsp90 is a Ligand Activated Molecular Chaperone Coupling ATP Binding to Dimer Closure Through a Coiled-coil Intermediate. Proc. Natl. Acad. Sci. USA. 113:2952-2957. [PubMed]

2. Lee, J., Kim, J.-H., Biter, A.B., Sielaff, B., Lee, S. and Tsai, F.T.F. (2013). Hsp70 is a Potent Activator of the Hsp104 AAA+ Motor. Proc. Natl. Acad. Sci. USA. 110:8513-8518. [PubMed]

3. Biter, A.B., Lee, S., Sung, N. and Tsai, F.T.F. (2012). Structural Basis for Inter-subunit Signaling in a Protein Disaggregating Machine. Proc. Natl. Acad. Sci. USA. 109:12515-12520. [PubMed]

4. Lee, S., Augustin, S., Tatsuta, T., Gerdes, F., Langer, T. and Tsai, F.T.F. (2011). Electron Cryomicroscopy Structure of a Membrane-anchored Mitochondrial AAA Protease. J. Biol. Chem. 286:4404-4411. [PubMed]

5. Sielaff, B., Lee, K.S. and Tsai, F.T.F. (2011). Structural and Functional Conservation of Mycobacterium tuberculosis GroEL Paralogs Suggests that GroEL1 is a Chaperonin. J. Mol. Biol. 405:831-839. [PubMed]

6. Sielaff, B. and Tsai, F.T.F. (2010). The M-domain Controls the Hsp104 Protein-remodeling Activity in an Hsp70/Hsp40-dependent Manner. J. Mol. Biol. 402:30-37. [PubMed]

7. Lee, S., Sielaff, B., Lee, J. and Tsai, F.T.F. (2010). CryoEM Structure of Hsp104 and Its Mechanistic Implication for Protein Disaggregation. Proc. Natl. Acad. Sci. USA. 107:8135-8140. [PubMed]

8. Augustin, S., Gerdes, F., Lee, S., Tsai, F.T.F., Langer, T. and Tatsuta, T. (2009). An Intersubunit Signaling Network Coordinates ATP Hydrolysis by m-AAA Proteases. Mol. Cell 35:574-585. [PubMed]
Commentary by W. Kress and E. Weber-Ban (2009) Mol. Cell 35:545-547. [PubMed]

9. Lee, S., Choi, J.-M. and Tsai, F.T.F. (2007). Visualizing the ATPase Cycle in a Protein Disaggregating Machine: Structural Basis for Substrate Binding by ClpB. Mol. Cell 25:261-271. [PubMed]

10. Haslberger, T., Weibezahn, J., Zahn, R., Lee, S., Tsai, F.T.F., Bukau, B. and Mogk, A. (2007). M Domains Couple the ClpB Threading Motor with the DnaK Chaperone Activity. Mol. Cell 25:247-260. [PubMed]

11. Zhang, J., Simisky, J., Tsai, F.T.F. and Geller, D.S. (2005). A Critical Role of Helix3-helix 5 Interaction in Steroid Hormone Receptor Function. Proc. Natl. Acad. Sci. USA 102:2707-2712. [PubMed]

12. Weibezahn, J., Tessarz, P., Schlieker, C., Zahn, R., Maglica, Z., Lee, S., Zentgraf, H., Weber-Ban, E., Dougan, D., Tsai, F.T.F., Mogk, A. and Bukau, B. (2004). Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation Through the Central Pore of ClpB. Cell 119:653-665. [PubMed]
Commentaries by A.L. Horwich (2004) Cell 119:579-581. [PubMed]; J. Shorter and S.L. Lindquist (2005) Nat. Struct. Mol. Biol. 12:4-6. [PubMed]

13. Lee, S., Sowa, M.E., Watanabe, Y., Sigler, P.B., Chiu, W., Yoshida, M. and Tsai, F.T.F. (2003). The Structure of ClpB: A Molecular Chaperone that Rescues Proteins from an Aggregated State. Cell 115:229-240. [PubMed]
Commentary by A. Mogk and B. Bukau (2004) Curr. Biol. 14:R78-R80. [PubMed]

14. Geller, D.S., Farhi, A., Pinkerton, N., Fradley, M., Moritz, M., Spitzer, A., Meinke, G., Tsai, F.T.F., Sigler, P.B. and Lifton, R.P. (2000). Activating Mineralocorticoid Receptor Mutation in Hypertension Exacerbated by Pregnancy. Science 289:119-123. [PubMed]
Commentary by I. Wickelgren (2000) Science 289:23-26. [PubMed]

15. Tsai, F.T.F. and Sigler, P.B. (2000). Structural Basis of Preinitiation Complex Assembly on Human Pol II Promoters. EMBO J. 19:25-36. [PubMed]
Cited in the "Advanced Information on the Nobel Prize in Chemistry 2006" by L. Thelander. [PDF]

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