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Christian Schlieker - Publications

Molecular Biophysics and Biochemistry Yale University, New Haven, CT 
Protein Folding and Dynamics; Structural Biology

31 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Laudermilch E, Schlieker C. Torsin ATPases: structural insights and functional perspectives. Current Opinion in Cell Biology. 40: 1-7. PMID 26803745 DOI: 10.1016/  0.96
2015 Rose AE, Brown RS, Schlieker C. Torsins: not your typical AAA+ ATPases. Critical Reviews in Biochemistry and Molecular Biology. 1-18. PMID 26592310 DOI: 10.3109/10409238.2015.1091804  0.96
2015 Speltz EB, Brown RS, Hajare HS, Schlieker C, Regan L. A designed repeat protein as an affinity capture reagent. Biochemical Society Transactions. 43: 874-80. PMID 26517897 DOI: 10.1042/BST20150091  0.96
2015 Turner EM, Brown RS, Laudermilch E, Tsai PL, Schlieker C. The Torsin Activator LULL1 Is Required for Efficient Growth of Herpes Simplex Virus 1. Journal of Virology. 89: 8444-52. PMID 26041288 DOI: 10.1128/JVI.01143-15  0.96
2014 Brown RS, Zhao C, Chase AR, Wang J, Schlieker C. The mechanism of Torsin ATPase activation. Proceedings of the National Academy of Sciences of the United States of America. 111: E4822-31. PMID 25352667 DOI: 10.1073/pnas.1415271111  0.96
2014 Rose AE, Zhao C, Turner EM, Steyer AM, Schlieker C. Arresting a Torsin ATPase reshapes the endoplasmic reticulum. The Journal of Biological Chemistry. 289: 552-64. PMID 24275647 DOI: 10.1074/jbc.M113.515791  0.96
2013 Zhao C, Brown RS, Chase AR, Eisele MR, Schlieker C. Regulation of Torsin ATPases by LAP1 and LULL1. Proceedings of the National Academy of Sciences of the United States of America. 110: E1545-54. PMID 23569223 DOI: 10.1073/pnas.1300676110  0.96
2013 Sehrawat S, Koenig PA, Kirak O, Schlieker C, Fankhauser M, Ploegh HL. A catalytically inactive mutant of the deubiquitylase YOD-1 enhances antigen cross-presentation. Blood. 121: 1145-56. PMID 23243279 DOI: 10.1182/blood-2012-08-447409  0.96
2012 Rose A, Schlieker C. Alternative nuclear transport for cellular protein quality control. Trends in Cell Biology. 22: 509-14. PMID 22858153 DOI: 10.1016/j.tcb.2012.07.003  0.96
2011 Ernst R, Claessen JH, Mueller B, Sanyal S, Spooner E, van der Veen AG, Kirak O, Schlieker CD, Weihofen WA, Ploegh HL. Enzymatic blockade of the ubiquitin-proteasome pathway. Plos Biology. 8: e1000605. PMID 21468303 DOI: 10.1371/journal.pbio.1000605  0.96
2011 Van der Veen AG, Schorpp K, Schlieker C, Buti L, Damon JR, Spooner E, Ploegh HL, Jentsch S. Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier. Proceedings of the National Academy of Sciences of the United States of America. 108: 1763-70. PMID 21209336 DOI: 10.1073/pnas.1014402108  0.96
2010 Rose A, Schlieker C. DNA repair: Blocking ubiquitin transfer. Nature. 466: 929-30. PMID 20725029 DOI: 10.1038/466929a  0.96
2009 Ernst R, Mueller B, Ploegh HL, Schlieker C. The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Molecular Cell. 36: 28-38. PMID 19818707 DOI: 10.1016/j.molcel.2009.09.016  0.96
2008 Schlieker CD, Van der Veen AG, Damon JR, Spooner E, Ploegh HL. A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway. Proceedings of the National Academy of Sciences of the United States of America. 105: 18255-60. PMID 19017811 DOI: 10.1073/pnas.0808756105  0.96
2007 Love KR, Catic A, Schlieker C, Ploegh HL. Mechanisms, biology and inhibitors of deubiquitinating enzymes. Nature Chemical Biology. 3: 697-705. PMID 17948018 DOI: 10.1038/nchembio.2007.43  0.96
2007 Gredmark S, Schlieker C, Quesada V, Spooner E, Ploegh HL. A functional ubiquitin-specific protease embedded in the large tegument protein (ORF64) of murine gammaherpesvirus 68 is active during the course of infection. Journal of Virology. 81: 10300-9. PMID 17634221 DOI: 10.1128/JVI.01149-07  0.96
2007 Schlieker C, Weihofen WA, Frijns E, Kattenhorn LM, Gaudet R, Ploegh HL. Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Molecular Cell. 25: 677-87. PMID 17349955 DOI: 10.1016/j.molcel.2007.01.033  0.96
2005 Schlieker C, Zentgraf H, Dersch P, Mogk A. ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria. Biological Chemistry. 386: 1115-27. PMID 16307477 DOI: 10.1515/BC.2005.128  0.96
2005 Schlieker C, Korbel GA, Kattenhorn LM, Ploegh HL. A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae. Journal of Virology. 79: 15582-5. PMID 16306630 DOI: 10.1128/JVI.79.24.15582-15585.2005  0.96
2005 Weibezahn J, Schlieker C, Tessarz P, Mogk A, Bukau B. Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biological Chemistry. 386: 739-44. PMID 16201868 DOI: 10.1515/BC.2005.086  0.96
2004 Schlieker C, Tews I, Bukau B, Mogk A. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. Febs Letters. 578: 351-6. PMID 15589844 DOI: 10.1016/j.febslet.2004.11.051  0.96
2004 Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, Weber-Ban EU, Dougan DA, Tsai FT, Mogk A, Bukau B. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell. 119: 653-65. PMID 15550247 DOI: 10.1016/j.cell.2004.11.027  0.96
2004 Schlieker C, Weibezahn J, Patzelt H, Tessarz P, Strub C, Zeth K, Erbse A, Schneider-Mergener J, Chin JW, Schultz PG, Bukau B, Mogk A. Substrate recognition by the AAA+ chaperone ClpB. Nature Structural & Molecular Biology. 11: 607-15. PMID 15208691 DOI: 10.1038/nsmb787  0.96
2004 Schlieker C, Mogk A, Bukau B. A PDZ switch for a cellular stress response. Cell. 117: 417-9. PMID 15137934 DOI: 10.1016/S0092-8674(04)00453-2  0.96
2004 Mogk A, Dougan D, Weibezahn J, Schlieker C, Turgay K, Bukau B. Broad yet high substrate specificity: the challenge of AAA+ proteins. Journal of Structural Biology. 146: 90-8. PMID 15037240 DOI: 10.1016/j.jsb.2003.10.009  0.96
2003 Strub C, Schlieker C, Bukau B, Mogk A. Poly-L-lysine enhances the protein disaggregation activity of ClpB. Febs Letters. 553: 125-30. PMID 14550559 DOI: 10.1016/S0014-5793(03)00985-2  0.96
2003 Weibezahn J, Schlieker C, Bukau B, Mogk A. Characterization of a trap mutant of the AAA+ chaperone ClpB. The Journal of Biological Chemistry. 278: 32608-17. PMID 12805357 DOI: 10.1074/jbc.M303653200  0.96
2003 Mogk A, Schlieker C, Friedrich KL, Schönfeld HJ, Vierling E, Bukau B. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. The Journal of Biological Chemistry. 278: 31033-42. PMID 12788951 DOI: 10.1074/jbc.M303587200  0.96
2003 Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. The Journal of Biological Chemistry. 278: 17615-24. PMID 12624113 DOI: 10.1074/jbc.M209686200  0.96
2002 Schlieker C, Bukau B, Mogk A. Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology. Journal of Biotechnology. 96: 13-21. PMID 12142139 DOI: 10.1016/S0168-1656(02)00033-0  0.96
1999 Stathakis P, Lay AJ, Fitzgerald M, Schlieker C, Matthias LJ, Hogg PJ. Angiostatin formation involves disulfide bond reduction and proteolysis in kringle 5 of plasmin. The Journal of Biological Chemistry. 274: 8910-6. PMID 10085135 DOI: 10.1074/jbc.274.13.8910  0.96
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