Ribosome-tethered molecular chaperones: the first line of defense against protein misfolding?
- 1 April 2003
- journal article
- review article
- Published by Elsevier in Current Opinion in Microbiology
- Vol. 6 (2) , 157-162
- https://doi.org/10.1016/s1369-5274(03)00030-4
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded ProteinScience, 2002
- Folding of Newly Translated Proteins In Vivo: The Role of Molecular ChaperonesAnnual Review of Biochemistry, 2001
- Implications of macromolecular crowding for protein assemblyPublished by Elsevier ,2000
- The fundamentals of protein folding: bringing together theory and experimentCurrent Opinion in Structural Biology, 1999
- The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome–nascent chain complexThe EMBO Journal, 1998
- The Hsp70 and Hsp60 Chaperone MachinesCell, 1998
- Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein foldingThe EMBO Journal, 1997
- Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.Proceedings of the National Academy of Sciences, 1996
- Protein folding: local structures, domains, subunits, and assembliesBiochemistry, 1991
- Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shieldingJournal of Molecular Biology, 1967