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Christian Schlieker
Christian Schlieker
Bestätigte E-Mail-Adresse bei yale.edu - Startseite
Titel
Zitiert von
Zitiert von
Jahr
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
J Weibezahn, P Tessarz, C Schlieker, R Zahn, Z Maglica, S Lee, ...
Cell 119 (5), 653-665, 2004
5362004
Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
A Mogk, C Schlieker, KL Friedrich, HJ Schönfeld, E Vierling, B Bukau
Journal of Biological Chemistry 278 (33), 31033-31042, 2003
3542003
Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity
A Mogk, C Schlieker, C Strub, W Rist, J Weibezahn, B Bukau
Journal of Biological Chemistry 278 (20), 17615-17624, 2003
3032003
Substrate recognition by the AAA+ chaperone ClpB
C Schlieker, J Weibezahn, H Patzelt, P Tessarz, C Strub, K Zeth, A Erbse, ...
Nature structural & molecular biology 11 (7), 607-615, 2004
2692004
Mechanisms, biology and inhibitors of deubiquitinating enzymes
KR Love, A Catic, C Schlieker, HL Ploegh
Nature chemical biology 3 (11), 697-705, 2007
2592007
The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER
R Ernst, B Mueller, HL Ploegh, C Schlieker
Molecular cell 36 (1), 28-38, 2009
2342009
Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology
C Schlieker, B Bukau, A Mogk
Journal of biotechnology 96 (1), 13-21, 2002
2162002
Characterization of a trap mutant of the AAA+ chaperone ClpB
J Weibezahn, C Schlieker, B Bukau, A Mogk
Journal of Biological Chemistry 278 (35), 32608-32617, 2003
1802003
A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae
C Schlieker, GA Korbel, LM Kattenhorn, HL Ploegh
Journal of virology 79 (24), 15582-15585, 2005
1732005
Regulation of Torsin ATPases by LAP1 and LULL1
C Zhao, RSH Brown, AR Chase, MR Eisele, C Schlieker
Proceedings of the National Academy of Sciences 110 (17), E1545-E1554, 2013
1502013
Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes
C Schlieker, WA Weihofen, E Frijns, LM Kattenhorn, R Gaudet, HL Ploegh
Molecular cell 25 (5), 677-687, 2007
1322007
Novel insights into the mechanism of chaperone-assisted protein disaggregation
J Weibezahn, C Schlieker, P Tessarz, A Mogk, B Bukau
Walter de Gruyter 386 (8), 739-744, 2005
1322005
Angiostatin formation involves disulfide bond reduction and proteolysis in kringle 5 of plasmin
P Stathakis, AJ Lay, M Fitzgerald, C Schlieker, LJ Matthias, PJ Hogg
Journal of Biological Chemistry 274 (13), 8910-8916, 1999
1251999
A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway
CD Schlieker, AG Van der Veen, JR Damon, E Spooner, HL Ploegh
Proceedings of the National Academy of Sciences 105 (47), 18255-18260, 2008
1182008
Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier
AG Van der Veen, K Schorpp, C Schlieker, L Buti, JR Damon, E Spooner, ...
Proceedings of the National Academy of Sciences 108 (5), 1763-1770, 2011
1112011
ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria
C Schlieker, H Zentgraf, P Dersch, A Mogk
Walter de Gruyter 386 (11), 1115-1127, 2005
1102005
Enzymatic blockade of the ubiquitin-proteasome pathway
R Ernst, JHL Claessen, B Mueller, S Sanyal, E Spooner, AG van der Veen, ...
PLoS biology 8 (3), e1000605, 2011
1032011
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
C Schlieker, I Tews, B Bukau, A Mogk
FEBS letters 578 (3), 351-356, 2004
962004
The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations
PL Tsai, C Zhao, E Turner, C Schlieker
Elife 5, e16011, 2016
872016
The mechanism of Torsin ATPase activation
RSH Brown, C Zhao, AR Chase, J Wang, C Schlieker
Proceedings of the National Academy of Sciences 111 (45), E4822-E4831, 2014
862014
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