The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
One size does not fit all: The oligomeric states of αB crystallin
Open accessAbstract
Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that delay protein aggregation through interactions with non‐native and aggregate‐prone protein states. This function has been shown to be important to cellular viability and sHSP function/dysfunction is implicated in many diseases, including Alzheimer's and Alexander disease. Though their gene products are small, many sHSPs assemble into a distribution of large oligomeric states that undergo dynamic subunit exchange. These inherent properties present significant experimental challenges for characterizing sHSP oligomers. Of the human sHSPs, αB crystallin is a paradigm example of sHSP oligomeric properties. Advances in our understanding of sHSP structure, oligomeric distribution, and dynamics have prompted the proposal of several models for the oligomeric states of αB. The aim of this review is to highlight characteristics of αB crystallin (αB) that are key to understanding its structure and function. The current state of knowledge, existing models, and outstanding questions that remain to be addressed are presented.
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
Alpha-crystallin can function as a molecular chaperone.
Horwitz, J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10449 · Cited by 1,820
A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy
Vicart, P., Caron, A., Guicheney, P., Li, Z., Prévost, M.-C., Faure, A., Chateau, D., Chapon, F., Tomé, F., Dupret, J.-M., et al. (1998) · Nature Genetics · doi:10.1038/1765 · Cited by 1,079
Crystal structure of a small heat-shock protein
Kim, K. K., Kim, R., & Kim, S.-H. (1998) · Nature · doi:10.1038/29106 · Cited by 888
Some like it hot: the structure and function of small heat-shock proteins
Haslbeck, M., Franzmann, T., Weinfurtner, D., & Buchner, J. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb993 · Cited by 828
Crystal structure and assembly of a eukaryotic small heat shock protein.
van Montfort, R. L. M., Basha, E., Friedrich, K. L., Slingsby, C., & Vierling, E. (2001) · Nature Structural Biology · doi:10.1038/nsb722 · Cited by 718
Stokoe, D., Engel, K., Campbell, D. G., Cohen, P., & Gaestel, M. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81216-9 · Cited by 571
Goldstein, L. E., Muffat, J. A., Cherny, R. A., Moir, R. D., Ericsson, M. H., Huang, X., Mavros, C., Coccia, J. A., Faget, K. Y., Fitch, K. A., et al. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12981-9 · Cited by 363
Sugiyama, Y., Suzuki, A., Kishikawa, M., Akutsu, R., Hirose, T., Waye, M. M. Y., Tsui, S. K. W., Yoshida, S., & Ohno, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1095 · Cited by 296
The small heat-shock protein, αb-crystallin, has a variable quaternary structure
Haley, D. A., Horwitz, J., & Stewart, P. L. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1611 · Cited by 280
Jehle, S., Rajagopal, P., Bardiaux, B., Markovic, S., Kühne, R., Stout, J. R., Higman, V. A., Klevit, R. E., van Rossum, B.-J., & Oschkinat, H. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1891 · Cited by 276
Self-citation
Research works printed but not linked: 15
- 10.1016/j.jmb.2008.10.097 · doi:10.1016/j.jmb.2008.10.097
- Jong W.W., 1981, Molecular and Cellular Biology of the Eye Lens, 221
- 10.1074/jbc.M009004200 · doi:10.1074/jbc.m009004200
- 10.1016/j.exer.2008.07.007 · doi:10.1016/j.exer.2008.07.007
- 10.1002/pro.380 · doi:10.1002/pro.380
- 10.1002/prot.21762 · doi:10.1002/prot.21762
- 10.1046/j.1432-1033.2002.03049.x · doi:10.1046/j.1432-1033.2002.03049.x
- 10.1074/jbc.M404455200 · doi:10.1074/jbc.m404455200
- 10.1021/ja307874r · doi:10.1021/ja307874r
- 10.1021/bi300525x · doi:10.1021/bi300525x
- 10.1016/S0021-9258(18)99902-3 · doi:10.1016/s0021-9258(18)99902-3
- 10.1021/bi0518141 · doi:10.1021/bi0518141
- 10.1073/pnas.0902651106 · DOI
- 10.1111/j.1432-1033.1980.tb04644.x · doi:10.1111/j.1432-1033.1980.tb04644.x
- 10.1021/bi00466a010 · doi:10.1021/bi00466a010
Cited by
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Bülow, A., Keijsers, L., Boele, S., van Roekel, E., & Denissen, J. J. A. (2021) · Developmental Psychology · doi:10.1037/dev0001208 · Cited by 116
Habibović, M., Denollet, J., Cuijpers, P., Spek, V. R. M., van den Broek, K. C., Warmerdam, L., van der Voort, P. H., Herrman, J.-P., Bouwels, L., Valk, S. S. D., et al. (2014) · Psychosomatic Medicine · doi:10.1097/psy.0000000000000096 · Cited by 38
Ethical aspects of clinical research with minors
Bos, W., Tromp, K., Tibboel, D., & Pinxten, W. (2013) · European Journal of Pediatrics · doi:10.1007/s00431-012-1856-8 · Cited by 25
Metadata
- Authors
- Delbecq, S. P., & Klevit, R. E.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2013-01-19
- Volume
- 587
- Issue
- 8
- Pages
- 1073-1080
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2087713518
- Cited by
- 263
- References
- 33
- FWCI
- 15.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- onlinelibrary.wiley.com/termsAndConditions#vor (vor)
- doi.wiley.com/10.1002/tdm_license_1 (tdm, 955 d)
- doi.wiley.com/10.1002/tdm_license_1.1 (tdm, 955 d)
- Funders
- NIH grant (1R01 EY017370)
- NIGMS (2T32 GM008268)
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: One size does not fit all: The oligomeric states of αB crystallin. https://app.cochat.ai/papers/10.1016/j.febslet.2013.01.021
- The paper
- Delbecq, S. P., & Klevit, R. E. (2013). One size does not fit all: The oligomeric states of αB crystallin. FEBS Letters. https://doi.org/10.1016/j.febslet.2013.01.021
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.