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Defining the glycan destruction signal for endoplasmic reticulum-associated degradation.

• Erin M. Quan, Yukiko Kamiya, +4 authors Jonathan S. Weissman
• Molecular cell
• 2008

The endoplasmic reticulum (ER) must target potentially toxic misfolded proteins for retrotranslocation and proteasomal degradation while avoiding destruction of productive folding intermediates. For… (More)

M domains couple the ClpB threading motor with the DnaK chaperone activity.

• Tobias Haslberger, Jimena Weibezahn, +4 authors Axel Mogk
• Molecular cell
• 2007

The AAA(+) chaperone ClpB mediates the reactivation of aggregated proteins in cooperation with the DnaK chaperone system. ClpB consists of two AAA domains that drive the ATP-dependent threading of… (More)

Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.

• Axel Mogk, Christian Schlieker, Christine Strub, Wolfgang Rist, Jimena Weibezahn, Bernd Bukau
• The Journal of biological chemistry
• 2003

ClpB of Escherichia coli is an ATP-dependent ring-forming chaperone that mediates the resolubilization of aggregated proteins in cooperation with the DnaK chaperone system. ClpB belongs to the… (More)

Substrate recognition by the AAA+ chaperone ClpB

• Christian Schlieker, Jimena Weibezahn, +9 authors Axel Mogk
• Nature Structural &Molecular Biology
• 2004

The AAA+ protein ClpB cooperates with the DnaK chaperone system to solubilize and refold proteins from an aggregated state. The substrate-binding site of ClpB and the mechanism of ClpB-dependent… (More)

Characterization of a trap mutant of the AAA+ chaperone ClpB.

• Jimena Weibezahn, Christian Schlieker, Bernd Bukau, Axel Mogk
• The Journal of biological chemistry
• 2003

The AAA+ protein ClpB mediates the solubilization of protein aggregates in cooperation with the DnaK chaperone system (KJE). The order of action of ClpB and KJE on aggregated proteins is unknown. We… (More)

Broad yet high substrate specificity: the challenge of AAA+ proteins.

• Axel Mogk, David A Dougan, Jimena Weibezahn, Christian Schlieker, Kursad Turgay, Bernd Bukau
• Journal of structural biology
• 2004

AAA+ proteins remodel target substrates in an ATP-dependent manner, an activity that is of central importance for a plethora of cellular processes. While sharing a similar hexameric structure AAA+… (More)

Unscrambling an egg: protein disaggregation by AAA+ proteins

• Jimena Weibezahn, Bernd Bukau, Axel Mogk
• Microbial cell factories
• 2004

Aprotein quality control system, consisting of molecular chaperones and proteases, controls the folding status of proteins and prevents the aggregation of misfolded proteins by either refolding or… (More)

Novel insights into the mechanism of chaperone-assisted protein disaggregation.

• Jimena Weibezahn, Christian Schlieker, Peter Tessarz, Axel Mogk, Bernd Bukau
• Biological chemistry
• 2005

Cell survival under severe thermal stress requires the activity of a bi-chaperone system, consisting of the ring-forming AAA+ chaperone ClpB (Hsp104) and the DnaK (Hsp70) chaperone system, which acts… (More)

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