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Weather Update

BCM Family Medicine on Kirby is without electrical power. Patients with appointments on Tuesday at this location will be moved to Baylor Medicine on the McNair Campus:  7200 Cambridge St, 7th floor, Suite 7B. Patients will be contacted. For questions, call 713-798-7700.

Francis Tsai Lab

Tsai Lab Publications (Selected)

Master
Content

Lee, S., Lee, S.B., Sung, N., Xu, W.W., Chang, C., Kim, H.E., Catic, A. and Tsai, F.T.F. (2023). Structural Basis of Impaired Disaggregase Function in the Oxidation-sensitive SKD3 Mutant Causing 3-Methylglutaconic Aciduria. Nature Commun. 14:2028. [Pubmed] [News]

Lee, G., Kim, R.S., Lee, S.B., Lee, S. and Tsai, F.T.F. (2022). Deciphering the Mechanism and Function of Hsp100 Unfoldases from Protein Structure. Biochem. Soc. Trans. 50:1725-36. [PubMed]

Mercado, J.M., Lee, S., Chang, C., Sung, N., Soong, L., Catic, A. and Tsai, F.T.F. (2022). Atomic Structure of the Leishmania spp. Hsp100 N-domain. Proteins 6:1242-6 [Pubmed

Tsai, J.T., Sung, N., Lee, J., Chang, C., Lee, S., and Tsai, F.T.F. (2019) Crystal Structure of the YcjX Stress Protein Reveals a Ras-like GTP-binding Protein. J. Mol. Biol. 431:3179-90. [Pubmed]

Lee, S., Roh, S.H., Lee, J., Sung, N., Liu, J. and Tsai, F.T.F. (2019) Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation. Cell Rep. 26:29-36 [PubMed]

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]

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]

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]

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]

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]

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]

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]

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]

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]

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]