The DOI matches its Crossref record; 91 of the 91 references it cites were found in a registry or an index.
A First Line of Stress Defense: Small Heat Shock Proteins and Their Function in Protein Homeostasis
Open accessAbstract
Small heat shock proteins (sHsps) are virtually ubiquitous molecular chaperones that can prevent the irreversible aggregation of denaturing proteins. To maintain protein homeostasis, sHsps complex with a variety of nonnative proteins in an ATP-independent manner and, in the context of the stress response, form a first line of defense against protein aggregation. In vertebrates they act to maintain the clarity of the eye lens, and in humans sHsp mutations are linked to myopathies and neuropathies. Although found in all domains of life, sHsps are quite diverse and have evolved independently in metazoans, plants and fungi. sHsp monomers range in size from approximately 12 to 42 kDa and are defined by a conserved β-sandwich α-crystallin domain, flanked by variable N- and C-terminal sequences. Most sHsps form large oligomeric ensembles with a broad distribution of different, sphere- or barrel like oligomers, with the size and structure of the oligomers dictated by features of the N- and C-termini. The activity of sHsps is regulated by mechanisms that change the equilibrium distribution in tertiary features and/or quaternary structure of the sHsp ensembles. Cooperation and/or coassembly between different sHsps in the same cellular compartment adds an underexplored level of complexity to sHsp structure and function.
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Cites
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Cellular Handling of Protein Aggregates by Disaggregation Machines
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Mimicking the Cell: Bio-Inspired Functions of Supramolecular Assemblies
Tu, Y., Peng, F., Adawy, A., Men, Y., Abdelmohsen, L. K. E. A., & Wilson, D. A. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00344 · Cited by 316
The Hsp70–Hsp90 Chaperone Cascade in Protein Folding
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Puangmalai, N., Sengupta, U., Bhatt, N., Gaikwad, S., Montalbano, M., Bhuyan, A., Garcia, S., McAllen, S., Sonawane, M., Jerez, C., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101766 · Cited by 68
Metadata
- Authors
- Haslbeck, M., & Vierling, E.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2015-04
- Volume
- 427
- Issue
- 7
- Pages
- 1537-1548
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2098555753
- Cited by
- 606
- References
- 91
- FWCI
- 19.68
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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