{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T12:50:24Z","timestamp":1789563024710,"version":"build-2803163510"},"reference-count":50,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2015,7,23]],"date-time":"2015-07-23T00:00:00Z","timestamp":1437609600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 HL054860"],"award-info":[{"award-number":["R01 HL054860"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[2015,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:sec><jats:label\/><jats:p>Nonerythroid alpha spectrin (\u03b1IISp) interacts in the nucleus with an array of different proteins indicating its involvement in a number of diverse functions. However, the significance of these interactions and their functional importance has been a relatively unexplored area. The best documented role of nuclear \u03b1IISp is in DNA repair where it is critical for repair of DNA interstrand cross\u2010links (ICLs), acting as a scaffold recruiting proteins to sites of damage in genomic and telomeric DNA. A deficiency in \u03b1IISp can importantly impact DNA ICL repair as is seen in cells from patients with the genetic disorder, Fanconi anemia (FA), where loss of \u03b1IISp leads to not only defects in repair of both genomic and telomeric DNA but also to telomere dysfunction and chromosome instability. This previously unexplored link between \u03b1IISp and telomere function is important in developing an understanding of maintenance of genomic stability after ICL damage. In FA cells, these defects in chromosome instability after ICL damage can be corrected when levels of \u03b1IISp are returned to normal by knocking down \u03bc\u2010calpain, a protease which cleaves \u03b1IISp. These studies suggest a new direction for correcting a number of the phenotypic defects in FA and could serve as a basis for therapeutic intervention. More in depth, examination of the interactions of \u03b1IISp with other proteins in the nucleus is of major importance in development of insights into the interacting key elements involved in the diverse processes occurring in the nucleus and the consequences loss of \u03b1IISp has on them. J. Cell. Biochem. 116: 1816\u20131830, 2015. \u00a9 2015 Wiley Periodicals, Inc.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jcb.25123","type":"journal-article","created":{"date-parts":[[2015,3,10]],"date-time":"2015-03-10T11:24:38Z","timestamp":1425986678000},"page":"1816-1830","source":"Crossref","is-referenced-by-count":12,"title":["Functional Significance of Nuclear \u03b1 Spectrin"],"prefix":"10.1002","volume":"116","author":[{"given":"Muriel W.","family":"Lambert","sequence":"first","affiliation":[{"name":"Department of Pathology and Laboratory Medicine, New Jersey Medical School Rutgers, The State University of New Jersey 185 South Orange Avenue Newark New Jersey 07103"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2015,7,23]]},"reference":[{"key":"e_1_2_12_2_1","doi-asserted-by":"crossref","first-page":"18595","DOI":"10.1016\/S0021-9258(17)44793-4","article-title":"Calmodulin\u2010binding proteins in the nuclei of quiescent and 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