Chaperones in concert: Orchestrating co-translational protein folding in the cell
In this issue of Molecular Cell, Roeselová et al.1 provide insights into co-translational folding of a multidomain protein in bacteria, revealing how the chaperones Trigger Factor, DnaJ, and DnaK work together to facilitate the folding of nascent chains. In this issue of Molecular Cell, Roeselová et...
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Veröffentlicht in: | Molecular cell 2024-07, Vol.84 (13), p.2403-2404 |
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description | In this issue of Molecular Cell, Roeselová et al.1 provide insights into co-translational folding of a multidomain protein in bacteria, revealing how the chaperones Trigger Factor, DnaJ, and DnaK work together to facilitate the folding of nascent chains.
In this issue of Molecular Cell, Roeselová et al.1 provide insights into co-translational folding of a multidomain protein in bacteria, revealing how the chaperones Trigger Factor, DnaJ, and DnaK work together to facilitate the folding of nascent chains. |
doi_str_mv | 10.1016/j.molcel.2024.06.018 |
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subjects | Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism HSP40 Heat-Shock Proteins - genetics HSP40 Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism Protein Biosynthesis Protein Folding |
title | Chaperones in concert: Orchestrating co-translational protein folding in the cell |
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