The DOI matches its Crossref record; 168 of the 168 references it cites were found in a registry or an index.
Heat‐shock proteins as molecular chaperones
Open accessAbstract
Functional proteins within cells are normally present in their native, completely folded form. However, vital processes of protein biogenesis such as protein synthesis and translocation of proteins into intracellular compartments require the protein to exist temporarily in an unfolded or partially folded conformation. As a consequence, regions buried when a polypeptide is in its native conformation become exposed and interact with other proteins causing protein aggregation which is deleterious to the cell. To prevent aggregation as proteins become unfolded, heat‐shock proteins protect these interactive surfaces by binding to them and facilitating the folding of unfolded or nascent polypeptides. In other instances the binding of heat‐shock proteins to interactive surfaces of completely folded proteins is a crucial part of their regulation. As heat shock and other stress conditions cause cellular proteins to become partially unfolded, the ability of heat‐shock proteins to protect cells against the adverse effects of stress becomes a logical extension of their normal function as molecular chaperones.
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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Lindquist, S., & Craig, E. A. (1988) · Annual Review of Genetics · doi:10.1146/annurev.ge.22.120188.003215 · Cited by 5,284
Self-citationLindquist, S. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.005443 · Cited by 4,588
Gething, M.-J., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,123
A C-terminal signal prevents secretion of luminal ER proteins
Munro, S., & Pelham, H. R. B. (1987) · Cell · doi:10.1016/0092-8674(87)90086-9 · Cited by 1,721
Speculations on the functions of the major heat shock and glucose-regulated proteins
Pelham, H. R. B. (1986) · Cell · doi:10.1016/0092-8674(86)90693-8 · Cited by 1,546
Deshaies, R. J., Koch, B. D., Werner-Washburne, M., Craig, E. A., & Schekman, R. (1988) · Nature · doi:10.1038/332800a0 · Cited by 1,472
Self-citationMunro, S., & Pelham, H. R. B. (1986) · Cell · doi:10.1016/0092-8674(86)90746-4 · Cited by 1,449
Cells in Stress: Transcriptional Activation of Heat Shock Genes
Morimoto, R. I. (1993) · Science · doi:10.1126/science.8451637 · Cited by 1,417
Attardi, G., & Schatz, G. (1988) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.04.110188.001445 · Cited by 1,387
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Accelerated evolution and Muller’s Rachet in endosymbiotic bacteria
Moran, N. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2873 · Cited by 1,017
The evolution, function, structure, and expression of the plant sHSPs
Waters, E. R. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ers355 · Cited by 417
Selective Induction of Mitochondrial Chaperones in Response to Loss of the Mitochondrial Genome
Martinus, R. D., Garth, G. P., Webster, T. L., Cartwright, P., Naylor, D. J., Høj, P. B., & Hoogenraad, N. J. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0098h.x · Cited by 351
Parent, L. J., Bennett, R. P., Craven, R. C., Nelle, T. D., Krishna, N. K., Bowzard, J. B., Wilson, C. B., Puffer, B. A., Montelaro, R. C., & Wills, J. W. (1995) · Journal of Virology · doi:10.1128/jvi.69.9.5455-5460.1995 · Cited by 258
Kodavanti, P. R. S., Royland, J. E., Osorio, C., Winnik, W. M., Ortiz, P., Lei, L., Ramabhadran, R., & Alzate, O. (2015) · Environmental Health Perspectives · doi:10.1289/ehp.1408504 · Cited by 45
Metadata
- Authors
- BECKER, J., & CRAIG, E. A.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1994-01
- Volume
- 219
- Issue
- 1-2
- Pages
- 11-23
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2045865115
- Cited by
- 553
- References
- 168
- FWCI
- 16.67
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
