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Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiaeUnscrambling an egg: protein disaggregation by AAA+ proteinsMolecular Basis for the Unique Role of the AAA+ Chaperone ClpV in Type VI Protein SecretionHead-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregationThe Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation.Coordination of translational control and protein homeostasis during severe heat stress.Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationAdaptor protein controlled oligomerization activates the AAA+ protein ClpCQuantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing.Signature of protein unfolding in chemical exchange saturation transfer imaging.Trigger Factor and DnaK possess overlapping substrate pools and binding specificities.Aggregation-induced changes in the chemical exchange saturation transfer (CEST) signals of proteins.Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coliCellular strategies for controlling protein aggregation.Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology.MecA, an adaptor protein necessary for ClpC chaperone activity.Mechanisms of protein folding: molecular chaperones and their application in biotechnology.Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretionAAA+ proteins and substrate recognition, it all depends on their partner in crime.Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition.Prolonged starvation drives reversible sequestration of lipid biosynthetic enzymes and organelle reorganization in Saccharomyces cerevisiaeMolecular chaperones: structure of a protein disaggregase.Broad yet high substrate specificity: the challenge of AAA+ proteins.Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils.A PDZ switch for a cellular stress response.Novel insights into the mechanism of chaperone-assisted protein disaggregation.The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies.Common and specific mechanisms of AAA+ proteins involved in protein quality control.Principles of general and regulatory proteolysis by AAA+ proteases in Escherichia coli.Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation.Tubules and donuts: a type VI secretion story.Integrating protein homeostasis strategies in prokaryotes.Chaperone networks in protein disaggregation and prion propagation.Deadly syringes: type VI secretion system activities in pathogenicity and interbacterial competition.Spatially organized aggregation of misfolded proteins as cellular stress defense strategy.Role of sHsps in organizing cytosolic protein aggregation and disaggregation.Bacterial and Yeast AAA+ Disaggregases ClpB and Hsp104 Operate through Conserved Mechanism Involving Cooperation with Hsp70.Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus.
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wetenschapper
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Axel Mogk
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P106
P31
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0000-0003-3674-5410