The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.
Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions
Open accessAbstract
The small heat shock proteins (sHSPs) and the related α-crystallins (αCs) are virtually ubiquitous proteins that are strongly induced by a variety of stresses, but that also function constitutively in multiple cell types in many organisms. Extensive research demonstrates that a majority of sHSPs and αCs can act as ATP-independent molecular chaperones by binding denaturing proteins and thereby protecting cells from damage due to irreversible protein aggregation. Because of their diverse evolutionary history, their connection to inherited human diseases, and their novel protein dynamics, sHSPs and αCs are of significant interest to many areas of biology and biochemistry. However, it is increasingly clear that no single model is sufficient to describe the structure, function or mechanism of action of sHSPs and αCs. In this review, we discuss recent data that provide insight into of the variety of structures of these proteins, their dynamic behavior, how they recognize substrates, and their many possible cellular roles.
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Cites
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Alpha-crystallin can function as a molecular chaperone.
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Small heat shock proteins are molecular chaperones.
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Cellular strategies for controlling protein aggregation
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Cited by
Heirbaut, M., Lermyte, F., Martin, E. M., Beelen, S., Sobott, F., Strelkov, S. V., & Weeks, S. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.773515 · Cited by 28
Metadata
- Authors
- Basha, E., O’Neill, H., & Vierling, E.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 37
- Issue
- 3
- Pages
- 106-117
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2068262186
- Cited by
- 538
- References
- 75
- FWCI
- 2.11
- Type
- journal article
- Language
- en
- Open access
- green
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