Deuerling, Elke
Elke Deuerling researcher
VIAF ID: 36145067047866630366 (Personal)
Permalink: http://viaf.org/viaf/36145067047866630366
Preferred Forms
- 100 1 _ ‡a Deuerling, Elke
- 100 1 _ ‡a Deuerling, Elke
- 100 0 _ ‡a Elke Deuerling ‡c researcher
4xx's: Alternate Name Forms (1)
5xx's: Related Names (3)
- 510 2 _ ‡a Bayreuth, Universiẗat
- 510 2 _ ‡a Universität Konstanz ‡b Fakultät für Biologie ‡e Affiliation
- 510 2 _ ‡a Universität Konstanz ‡b Fakultät für Biologie
Works
Title | Sources |
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amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes | |
C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity | |
Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli | |
Concerted action of the ribosome and the associated chaperone Trigger Factor confines nascent polypeptide folding | |
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 | |
Deciphering molecular details of the RAC-ribosome interaction by EPR spectroscopy | |
Directed PCR-free engineering of highly repetitive DNA sequences | |
Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli | |
Early Scanning of Nascent Polypeptides inside the Ribosomal Tunnel by NAC | |
Extra N-Terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1 | |
Fluorescence-based monitoring of ribosome assembly landscapes | |
Fluorosomen werfen Licht auf Ribosomenproduktion | |
ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion | |
ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift | |
Functional dissection of trigger factor and DnaK interactions with nascent polypeptides and thermally denatured proteins | |
High yield expression of catalytically active USP18 using a trigger factor fusion system. - | |
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis | |
Insights into the Aggregation Mechanism of PolyQ Proteins with Different Glutamine Repeat Lengths | |
L23 protein functions as a chaperone docking site on the ribosome | |
Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK | |
Macrolides : the plug is out | |
Mechanismen der Proteinfaltung Molekulare Chaperone und ihr biotechnologisches Potential | |
Mechanisms of protein folding molecular chaperones and their application in biotechnology | |
Molecular basis of the TRAP complex function in ER protein biogenesis | |
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 | |
NAC controls cotranslational N-terminal methionine excision in eukaryotes | |
nascent polypeptide-associated complex is a key regulator of proteostasis | |
Not4-dependent translational repression is important for cellular protein homeostasis in yeast | |
principle of antagonism ensures protein targeting specificity at the endoplasmic reticulum | |
Ribosome-associated chaperones as key players in proteostasis | |
Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation | |
Structural Analysis of the Ribosome-associated Complex (RAC) Reveals an Unusual Hsp70/Hsp40 Interaction | |
Target-directed proteolysis at the ribosome | |
Trigger factor and DnaK cooperate in folding of newly synthesized proteins | |
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 flexibility | |
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 |