about
Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoStructural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMRStructure and function of the molecular chaperone Trigger Factor.Chaperone action at the single-molecule level.Alternative modes of client binding enable functional plasticity of Hsp70.Mechanism of regulation of the bifunctional histidine kinase NtrB in Escherichia coli.Genome-scale co-evolutionary inference identifies functions and clients of bacterial Hsp90Monitoring protein misfolding by site-specific labeling of proteins in vivoCo-translational mechanisms of protein maturation.SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational foldingGlobal profiling of SRP interaction with nascent polypeptides.Analyzing the Complex Regulatory Landscape of Hfq - an Integrative, Multi-Omics Approach.Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding.Role for ribosome-associated complex and stress-seventy subfamily B (RAC-Ssb) in integral membrane protein translation.Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity.Protein Folding Mediated by Trigger Factor and Hsp70: New Insights from Single-Molecule Approaches.Operon structure and cotranslational subunit association direct protein assembly in bacteria.Reshaping of the conformational search of a protein by the chaperone trigger factor.Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding.Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK.Systemic control of protein synthesis through sequestration of translation and ribosome biogenesis factors during severe heat stressTrigger Factor Reduces the Force Exerted on the Nascent Chain by a Cotranslationally Folding ProteinCotranslational assembly of protein complexes in eukaryotes revealed by ribosome profiling.A chemical kinetic basis for measuring translation initiation and elongation rates from ribosome profiling data.Low temperature of GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor DnaKThe C-terminal tail of the bacterial translocation ATPase SecA modulates its activityConcerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide foldingCell Biology. Finding nascent proteins the right homeMechanisms of Cotranslational Maturation of Newly Synthesized ProteinsMonitoring Cell-Type-Specific Gene Expression Using Ribosome Profiling In Vivo During Cardiac Hemodynamic StressGPD1 Specifically Marks Dormant Glioma Stem Cells with a Distinct Metabolic Profile
P50
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P50
description
researcher
@en
wetenschapper
@nl
name
Günter Kramer
@en
Günter Kramer
@nl
type
label
Günter Kramer
@en
Günter Kramer
@nl
prefLabel
Günter Kramer
@en
Günter Kramer
@nl
P106
P31
P496
0000-0001-7552-8393