Elke Deuerling researcher
Deuerling, Elke
VIAF ID: 36145067047866630366 (Personal)
Permalink: http://viaf.org/viaf/36145067047866630366
Preferred Forms
- 100 1 _ ‡a Deuerling, Elke
- 100 0 _ ‡a Elke Deuerling ‡c researcher
4xx's: Alternate Name Forms (1)
5xx's: Related Names (2)
- 510 2 _ ‡a Bayreuth, Universiẗat
- 510 2 _ ‡a Universität Konstanz ‡b Fakultät für Biologie
Works
Title | Sources |
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Chaperone-assisted folding of newly synthesized proteins in the cytosol | |
Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli | |
A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains | |
Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy | |
DafA cycles between the DnaK chaperone system and translational machinery | |
Directed PCR-free engineering of highly repetitive DNA sequences | |
Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli. | |
Elke Deuerling: winner of the 2005 FEBS Letters Award for Young Scientists [interview by Tine Walma]. | |
Extra N-terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1 | |
Insights into the Aggregation Mechanism of PolyQ Proteins with Different Glutamine Repeat Lengths. | |
L23 protein functions as a chaperone docking site on the ribosome | |
Macrolides: the plug is out. | |
Mechanisms of protein folding: molecular chaperones and their application in biotechnology | |
Molecular mechanism and structure of Trigger Factor bound to the translating ribosome | |
Multivalent contacts of the Hsp70 Ssb contribute to its architecture on ribosomes and nascent chain interaction | |
The nascent polypeptide-associated complex is a key regulator of proteostasis | |
Not4-dependent translational repression is important for cellular protein homeostasis in yeast | |
The principle of antagonism ensures protein targeting specificity at the endoplasmic reticulum | |
Ribosome Assembly as Antimicrobial Target | |
Ribosome-associated chaperones as key players in proteostasis | |
Structural analysis of the ribosome-associated complex (RAC) reveals an unusual Hsp70/Hsp40 interaction | |
Target-directed proteolysis at the ribosome | |
Three-state equilibrium of Escherichia coli trigger factor | |
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities | |
Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor | |
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. | |
Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli | |
Validation of a fluorescence-based screening concept to identify ribosome assembly defects in Escherichia coli | |
Vms1: A Cytosolic CAT-Tailing Antagonist to Protect Mitochondria. |