The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Abstract
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent protein misfolding and aggregation in the crowded environment of the cell. Nascent chain–binding chaperones, including trigger factor, Hsp70, and prefoldin, stabilize elongating chains on ribosomes in a nonaggregated state. Folding in the cytosol is achieved either on controlled chain release from these factors or after transfer of newly synthesized proteins to downstream chaperones, such as the chaperonins. These are large, cylindrical complexes that provide a central compartment for a single protein chain to fold unimpaired by aggregation. Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.
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Citations
Cites
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188
Self-citationMacromolecular crowding: an important but neglected aspect of the intracellular environment
Ellis, R. J. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00172-x · Cited by 1,153
Implications of macromolecular crowding for protein assembly
Minton, A. P. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00045-7 · Cited by 649
Polypeptide Flux through Bacterial Hsp70
Teter, S. A., Houry, W. A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., & Hartl, F. U. (1999) · Cell · doi:10.1016/s0092-8674(00)80787-4 · Cited by 424
Self-citation
Cited by
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Recombinant protein expression in Escherichia coli: advances and challenges
Rosano, G. L., & Ceccarelli, E. A. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00172 · Cited by 2,556
Protein degradation and protection against misfolded or damaged proteins.
Goldberg, A. L. (2003) · Nature · doi:10.1038/nature02263 · Cited by 2,088
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
Young, J. C., Hoogenraad, N. J., & Hartl, F. U. (2003) · Cell · doi:10.1016/s0092-8674(02)01250-3 · Cited by 915
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Metadata
- Authors
- Hartl, F. U., & Hayer-Hartl, M.
- Venue
- Science
- Published
- 2002-03-08
- Volume
- 295
- Issue
- 5561
- Pages
- 1852-1858
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2096966529
- Cited by
- 3,347
- References
- 4
- FWCI
- 70.41
- Type
- journal article
- Language
- en
- Open access
- closed
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