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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

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Delbecq, Scott P., Klevit, Rachel E.·2013·FEBS Letters

Abstract

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.

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Research works printed but not linked: 15

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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
Funders
  • NIH grant (1R01 EY017370)
  • NIGMS (2T32 GM008268)

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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

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