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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
Large-scale phosphorylation analysis of mouse liver
Villén, J., Beausoleil, S. A., Gerber, S. A., & Gygi, S. P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609836104 · Cited by 730
Mechanisms that regulate adaptor binding to β-integrin cytoplasmic tails
Legate, K. R., & Fässler, R. (2009) · Journal of Cell Science · doi:10.1242/jcs.041624 · Cited by 370
Crippa, V., Sau, D., Rusmini, P., Boncoraglio, A., Onesto, E., Bolzoni, E., Galbiati, M., Fontana, E., Marino, M., Carra, S., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq257 · Cited by 330
Crippa, V., Carra, S., Rusmini, P., Sau, D., Bolzoni, E., Bendotti, C., De Biasi, S., & Poletti, A. (2010) · Autophagy · doi:10.4161/auto.6.7.13042 · Cited by 101
Cited by
A First Line of Stress Defense: Small Heat Shock Proteins and Their Function in Protein Homeostasis
Haslbeck, M., & Vierling, E. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.002 · Cited by 606
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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.
