The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Large Potentials of Small Heat Shock Proteins
Abstract
Modern classification of the family of human small heat shock proteins (the so-called HSPB) is presented, and the structure and properties of three members of this family are analyzed in detail. Ubiquitously expressed HSPB1 (HSP27) is involved in the control of protein folding and, when mutated, plays a significant role in the development of certain neurodegenerative disorders. HSPB1 directly or indirectly participates in the regulation of apoptosis, protects the cell against oxidative stress, and is involved in the regulation of the cytoskeleton. HSPB6 (HSP20) also possesses chaperone-like activity, is involved in regulation of smooth muscle contraction, has pronounced cardioprotective activity, and seems to participate in insulin-dependent regulation of muscle metabolism. HSPB8 (HSP22) prevents accumulation of aggregated proteins in the cell and participates in the regulation of proteolysis of unfolded proteins. HSPB8 also seems to be directly or indirectly involved in regulation of apoptosis and carcinogenesis, contributes to cardiac cell hypertrophy and survival and, when mutated, might be involved in development of neurodegenerative diseases. All small heat shock proteins play important “housekeeping” roles and regulate many vital processes; therefore, they are considered as attractive therapeutic targets.
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Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
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Large-scale phosphorylation analysis of mouse liver
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Mechanisms that regulate adaptor binding to β-integrin cytoplasmic tails
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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
Cooray, S. N., Gobbetti, T., Montero-Melendez, T., McArthur, S., Thompson, D., Clark, A. J. L., Flower, R. J., & Perretti, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308253110 · Cited by 299
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
Oral proteasome inhibitor with strong preclinical efficacy in myeloma models
Park, J., Park, E., Jung, C.-K., Kang, S.-W., Kim, B. G., Jung, Y., Kim, T. H., Lim, J.-Y., Lee, S.-E., Min, C.-K., et al. (2016) · BMC Cancer · doi:10.1186/s12885-016-2285-2 · Cited by 9
Metadata
- Authors
- Mymrikov, E. V., Seit-Nebi, A. S., & Gusev, N. B.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2011-10
- Volume
- 91
- Issue
- 4
- Pages
- 1123-1159
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W1987220770
- Cited by
- 409
- References
- 5
- FWCI
- 2.28
- Type
- journal article
- Language
- en
- Open access
- closed
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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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