{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T07:48:37Z","timestamp":1790927317525,"version":"4.1.0"},"reference-count":49,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2024,2,29]],"date-time":"2024-02-29T00:00:00Z","timestamp":1709164800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Alpha-B-crystallin, a member of the small heat shock family of proteins, has been implicated in a variety of cardiomyopathies and in normal cardiac homeostasis. It is known to function as a molecular chaperone, particularly for desmin, but also interacts with a wide variety of additional proteins. The molecular chaperone function is also enhanced by signal-dependent phosphorylation at specific residues under stress conditions. Naturally occurring mutations in CRYAB, the gene that encodes alpha-B-crystallin, have been suggested to alter ionic intermolecular interactions that affect dimerization and chaperone function. These mutations have been associated with myofibrillar myopathy, restrictive cardiomyopathy, and hypertrophic cardiomyopathy and promote pathological hypertrophy through different mechanisms such as desmin aggregation, increased reductive stress, or activation of calcineurin\u2013NFAT signaling. This review will discuss the known mechanisms by which alpha-B-crystallin functions in cardiac homeostasis and the pathogenesis of cardiomyopathies and provide insight into potential future areas of exploration.<\/jats:p>","DOI":"10.3390\/ijms25052826","type":"journal-article","created":{"date-parts":[[2024,2,29]],"date-time":"2024-02-29T05:59:19Z","timestamp":1709186359000},"page":"2826","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Role of the Alpha-B-Crystallin Protein in Cardiomyopathic Disease"],"prefix":"10.3390","volume":"25","author":[{"given":"Andres","family":"Thorkelsson","sequence":"first","affiliation":[{"name":"Tufts University School of Medicine, Tufts University, Boston, MA 02111, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3065-8498","authenticated-orcid":false,"given":"Michael T.","family":"Chin","sequence":"additional","affiliation":[{"name":"Tufts University School of Medicine, Tufts University, Boston, MA 02111, USA"},{"name":"Molecular Cardiology Research Institute, Tufts Medical Center, Boston, MA 02111, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,2,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.molcel.2010.10.006","article-title":"The Heat Shock Response: Life on the Verge of Death","volume":"40","author":"Richter","year":"2010","journal-title":"Mol. 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