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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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Publications

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]

Biter, A.B., Lee, J., Sung, N., Tsai, F.T.F. and Lee, S. (2012). Functional Analysis of Conserved Cis- and Trans-elements in the Hsp104 Protein Disaggregating Machine. J. Struct. Biol. 179:172-180. [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., 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]

Lee, S. and Tsai, F.T.F. (2010). Molecular Motors and Machines. ACA RefleXions 3:33.

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]

Sielaff, B., Lee, K.S. and Tsai, F.T.F. (2010). Crystallization and Preliminary X-ray Crystallographic Analysis of a GroEL1 Fragment from Mycobacterium tuberculosis H37Rv. Acta Crystallogr. F. 66:418-420. [PubMed]

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]

Lee, S. and Tsai, F.T.F. (2007). Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-terminal Fragment of the Yeast Prion-remodeling Factor Hsp104. Acta Crystallogr. F 63:784-786. [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]

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]

Zhang, J., Tsai, F.T.F. and Geller, D.S. (2006). Differential Interaction of RU486 with the Progesterone and Glucocorticoid Receptors. J. Mol. Endocrinol. 37:163-173. [PubMed]

Rees, I., Lee, S., Kim, H. and Tsai, F.T.F. (2006). The E3 Ubiquitin Ligase CHIP Binds the Androgen Receptor in a Phosphorylation-dependent Manner. Biochim. Biophys. Acta. 1764:1073-1079. [PubMed]

Lee, S. and Tsai, F.T.F. (2005). Molecular Chaperones in Protein Quality Control. J. Biochem. Mol. Biol. 38:259-265. [PubMed]

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]

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]
Commentary by A.L. Horwich (2004) Cell 119:579-581. [PubMed]
Commentary by J. Shorter and S.L. Lindquist (2005) Nat. Struct. Mol. Biol. 12:4-6.
[PubMed]

Lee, S., Sowa, M.E., Choi, J.-M. and Tsai, F.T.F. (2004). The ClpB/Hsp104 Molecular Chaperone - A Protein Disaggregating Machine. J. Struct. Biol. 146:99-105. [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]

Lee, S., Hisayoshi, M., Yoshida, M. and Tsai, F.T.F. (2003). Crystallization and Preliminary X-ray Crystallographic Analysis of the Hsp100 Chaperone ClpB from Thermus thermophilus. Acta Crystallogr. D 59:2334-2336. [PubMed]

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]

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]

Tsai, F.T.F., Littlefield, O., Kosa, P.F., Cox, J.M., Schepartz, A. and Sigler, P.B. (1998). Polarity of Transcription on Pol II and Archaeal Promoters: Where is the "One-way Sign" and How is it Read? Cold Spring Harb. Symp. Quant. Biol. 63:53-61. [PubMed]

Tsai, F.T.F., Singh, O.M.P., Skarzynski, T., Wonacot, A.J., Weston, S., Tucker, A., Pauptit, R.A., Breeze, A.L., Poyser, J.P., O'Brien, R., Ladbury, J.E. and Wigley. D.B. (1997). The High-resolution Crystal Structure of a 24-kDa Gyrase B Fragment from E. coli Complexed with One of the Most Potent Coumarin Inhibitors, Clorobiocin. Proteins 28:41-52. [PubMed]

Tsai, F.T.F., Subramanya, H.S., Brannigan, J.A., Wilkinson, A.J., and Wigley, D.B. (1996). Crystallization and Preliminary Crystallographic Analysis of the DNA Gyrase B Protein from B. steraothermophilus. Acta Crystallogr. D 52:1216-1218. [PubMed]

Lewis, R.J., Tsai, F.T.F. and Wigley, D.B. (1996). Molecular Mechanisms of Drug Inhibition of DNA Gyrase. BioEssays 18:661-671. [PubMed]

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