The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Structural and Functional Diversities between Members of the Human HSPB, HSPH, HSPA, and DNAJ Chaperone Families
Open accessAbstract
Heat shock proteins (HSPs) were originally identified as stress-responsive proteins required to deal with proteotoxic stresses. Besides being stress-protective and possible targets for delaying progression of protein folding diseases, mutations in chaperones also have been shown to cause disease (chaperonopathies). The mechanism of action of the "classical", stress-inducible HSPs in serving as molecular chaperones preventing the irreversible aggregation of stress-unfolded or disease-related misfolded proteins is beginning to emerge. However, the human genome encodes several members for each of the various HSP families that are not stress-related but contain conserved domains. Here, we have reviewed the existing literature on the various members of the human HSPB (HSP27), HSPH (HSP110), HSPA (HSP70), and DNAJ (HSP40) families. Apart from structural and functional homologies, several diversities between members and families can be found that not only point to differences in client specificity but also seem to serve differential client handling and processing. How substrate specificity and client processing is determined is far from being understood.
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Cites
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Cited by
Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions
Basha, E., O’Neill, H., & Vierling, E. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.11.005 · Cited by 538
A Small Molecule Inhibitor of Inducible Heat Shock Protein 70
Leu, J. I.-J., Pimkina, J., Frank, A., Murphy, M. E., & George, D. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.023 · Cited by 441
Cellular Handling of Protein Aggregates by Disaggregation Machines
Mogk, A., Bukau, B., & Kampinga, H. H. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.004 · Cited by 365
Self-citationFirefly luciferase mutants as sensors of proteome stress
Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219
Proteostasis in cardiac health and disease
Henning, R. H., & Brundel, B. J. J. M. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.89 · Cited by 193
Metadata
- Authors
- Vos, M. J., Hageman, J., Carra, S., & Kampinga, H. H.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-06-17
- Volume
- 47
- Issue
- 27
- Pages
- 7001-7011
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2147770635
- Cited by
- 391
- References
- 50
- FWCI
- 9.80
- Type
- journal article
- Language
- en
- Open access
- green
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- Vos, M. J., Hageman, J., Carra, S., & Kampinga, H. H. (2008). Structural and Functional Diversities between Members of the Human HSPB, HSPH, HSPA, and DNAJ Chaperone Families. Biochemistry. https://doi.org/10.1021/bi800639z
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