Lee, J., Kim, J.-H., Biter, A.B., Sielaff, B., Lee, S.* and Tsai, F.T.F. (2013). Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor. Proc. Natl. Acad. Sci. USA. 110: 8513-8518. [PubMed] (*Co-corresponding author)
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. Structural 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] (*Co-corresponding author)
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]
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]
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]
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] (*Co-corresponding author)
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]
Lee, S., Sowa, M.E., Choi, J.-M. and Tsai, F.T.F. (2004). The ClpB/Hsp104 molecular chaperone - a protein disaggregating machine. J. Structural 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]
