Publications

Zhao, C., Brown, R.S.H., Chase, A.R., Eisele, M.R., and Schlieker, C. (2013) Regulation of Torsin ATPases by LAP1 and LULL1. PNAS, in press.
Rose, A., Schlieker, C. (2012) Alternative nuclear transport for cellular protein quality control. Trends in Cell Biology 22, 509-14. doi: 10.1016/j.tcb.2012.07.003.
Ernst, R., Claessen, J.H., Mueller, B., Sanyal, S., Spooner, E., van der Veen, A.G., Kirak, O., Schlieker, C.D., Weihofen, W.A., and Ploegh, H.L. (2011) Enzymatic blockade of the ubiquitin-proteasome pathway. PLoS Biol 8, e1000605.
Van der Veen, A.G., Schorpp, K., Schlieker, C., Buti, L., Damon, J.R., Spooner, E., Ploegh, H.L., and Jentsch, S. (2011) Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier. Proc Natl Acad Sci U S A 108, 1763-1770.
Rose, A., and Schlieker, C. (2010) DNA repair: Blocking ubiquitin transfer. Nature 466, 929-930.
Ernst, R., Mueller, B., Ploegh, H.L., and Schlieker, C. (2009) The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol Cell 36, 28-38.
Schlieker, C.D., Van der Veen, A.G., Damon, J.R., Spooner, E., and Ploegh, H.L. (2008) A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway. Proc Natl Acad Sci U S A 105, 18255-18260.
Love, K.R., Catic, A., Schlieker, C., and Ploegh, H.L. (2007) Mechanisms, biology and inhibitors of deubiquitinating enzymes. Nat Chem Biol 3, 697-705.
Gredmark, S., Schlieker, C., Quesada, V., Spooner, E., and Ploegh, H.L. (2007). A functional ubiquitin-specific protease embedded in the large tegument protein (ORF64) of murine gammaherpesvirus 68 is active during the course of infection. J Virol 81, 10300-10309.
Schlieker, C., Weihofen, W.A., Frijns, E., Kattenhorn, L.M., Gaudet, R., and Ploegh, H.L. (2007). Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Mol Cell 25, 677-687.
Schlieker, C., Zentgraf, H., Dersch, P., and Mogk, A. (2005). ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria. Biol Chem 386, 1115-1127.
Schlieker, C., Korbel, G.A., Kattenhorn, L.M., and Ploegh, H.L. (2005). A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae. J Virol 79, 15582-15585.
Weibezahn, J., Schlieker, C., Tessarz, P., Mogk, A., and Bukau, B. (2005). Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol Chem 386, 739-744.
Schlieker, C., Tews, I., Bukau, B., and Mogk, A. (2004). Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. FEBS Lett578, 351-356.
Weibezahn, J., Tessarz, P., Schlieker, C., Zahn, R., Maglica, Z., Lee, S., Zentgraf, H., Weber-Ban, E.U., Dougan, D.A., Tsai, F.T., et al. (2004). Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119, 653-665.
Schlieker, C., Weibezahn, J., Patzelt, H., Tessarz, P., Strub, C., Zeth, K., Erbse, A., Schneider-Mergener, J., Chin, J.W., Schultz, P.G., et al. (2004). Substrate recognition by the AAA+ chaperone ClpB. Nat Struct Mol Biol 11, 607-615.
Schlieker, C., Mogk, A., and Bukau, B. (2004). A PDZ switch for a cellular stress response. Cell 117, 417-419.
Mogk, A., Dougan, D., Weibezahn, J., Schlieker, C., Turgay, K., and Bukau, B. (2004). Broad yet high substrate specificity: the challenge of AAA+ proteins. J Struct Biol 146, 90-98.
Strub, C., Schlieker, C., Bukau, B., and Mogk, A. (2003). Poly-L-lysine enhances the protein disaggregation activity of ClpB. FEBS Lett 553, 125-130.
Weibezahn, J., Schlieker, C., Bukau, B., and Mogk, A. (2003). Characterization of a trap mutant of the AAA+ chaperone ClpB. J Biol Chem 278, 32608-32617.
Mogk, A., Schlieker, C., Friedrich, K.L., Schonfeld, H.J., Vierling, E., and Bukau, B. (2003). Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem 278, 31033-31042.
Mogk, A., Schlieker, C., Strub, C., Rist, W., Weibezahn, J., and Bukau, B. (2003). Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J Biol Chem 278, 17615-17624./a>
Schlieker, C., Bukau, B., and Mogk, A. (2002). Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology. J Biotechnol 96, 13-21.
Stathakis, P., Lay, A.J., Fitzgerald, M., Schlieker, C., Matthias, L.J., and Hogg, P.J. (1999). Angiostatin formation involves disulfide bond reduction and proteolysis in kringle 5 of plasmin. J Biol Chem 274, 8910-8916.