The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference45 articles.
1. Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
2. Getting Newly Synthesized Proteins into Shape
3. Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.
4. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
5. Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor
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