C
Christian Schlieker
Researcher at Yale University
Publications - 52
Citations - 3839
Christian Schlieker is an academic researcher from Yale University. The author has contributed to research in topics: Ubiquitin & CLPB. The author has an hindex of 29, co-authored 47 publications receiving 3474 citations. Previous affiliations of Christian Schlieker include University of New South Wales & Heidelberg University.
Papers
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Journal ArticleDOI
Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB
Jimena Weibezahn,Peter Tessarz,Christian Schlieker,Regina Zahn,Zeljka Maglica,Sukyeong Lee,Hanswalter Zentgraf,Eilika Weber-Ban,David A. Dougan,David A. Dougan,Francis T.F. Tsai,Axel Mogk,Bernd Bukau +12 more
TL;DR: The activity switch of BAP to a degrading disaggregase does not support thermotolerance development, demonstrating that cell survival during severe thermal stress requires reactivation of aggregated proteins.
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Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.
Axel Mogk,Christian Schlieker,Kenneth L. Friedrich,Hans-Joachim Schönfeld,Elizabeth Vierling,Bernd Bukau +5 more
TL;DR: It is proposed that sHsp function in cellular protein quality control is to promote rapid resolubilization of aggregated proteins, formed upon severe heat stress, by DnaK or ClpB/DnaK.
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Roles of Individual Domains and Conserved Motifs of the AAA+ Chaperone ClpB in Oligomerization, ATP Hydrolysis, and Chaperone Activity
TL;DR: The results show that ClpB oligomerization is strictly dependent on the presence of the C-terminal domain of the second AAA-domain, while ATP binding to the first AAA-domains stabilized the ClpP oligomer.
Journal ArticleDOI
Substrate recognition by the AAA+ chaperone ClpB.
Christian Schlieker,Jimena Weibezahn,Holger Patzelt,Peter Tessarz,Christine Strub,Kornelius Zeth,Annette H. Erbse,Jens Schneider-Mergener,Jason W. Chin,Peter G. Schultz,Bernd Bukau,Axel Mogk +11 more
TL;DR: This work has identified a substrate-binding site of ClpB that is located at the central pore of the first AAA domain that contributes to substrate binding and its crucial role was confirmed by mutational analysis and direct crosslinking to substrates.
Journal ArticleDOI
Mechanisms, biology and inhibitors of deubiquitinating enzymes
TL;DR: How chemical tools have enabled the discovery of deubiquitinating enzymes, their functional profiling, crystallographic characterization and mechanistic classification and development of molecules for therapeutic purposes are discussed are discussed.