{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T21:08:15Z","timestamp":1777324095656,"version":"3.51.4"},"reference-count":24,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":8070,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell Motility"],"published-print":{"date-parts":[[1983,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Talin is a recently identified cytoskeletal protein with a polypeptide molecular weight of 215,000 daltons. In cultured fibroblasts talin has been localized by immunofluorescence in adhesion plaques (focal contacts), in the ruffling membranes and leading lamellae of the cell periphery, and in fibrillar patterns that align with microfilament bundles and\/or with cell surface fibronectin. These cellular locations suggest that the protein could function either in the attachment of microfilaments to the plasma membane or in the organization of microfilaments close to membrane attachment sites. Cell transformation by viruses such as Rous sarcoma virus disrupts the normal organization of talin, and in most transformed cells talin appears distributed diffusely through the cytoplasm. In a few cells talin is detected in doughnut\u2010shaped aggregates, as a ring surrounding a central core of actin. The significance of these structures is uncertain, but in some cells the individual structures will condense to form much larger aggregates with a striking appearance when viewed by immunofluoresence microscopy.<\/jats:p>","DOI":"10.1002\/cm.970030509","type":"journal-article","created":{"date-parts":[[2005,4,11]],"date-time":"2005-04-11T19:33:39Z","timestamp":1113248019000},"page":"405-417","source":"Crossref","is-referenced-by-count":122,"title":["Talin: A cytoskeletal component concentrated in adhesion plaques and other sites of actin\u2010membrane interaction"],"prefix":"10.1002","volume":"3","author":[{"given":"Keith","family":"Burridge","sequence":"first","affiliation":[]},{"given":"Laurie","family":"Connell","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.77.2.980"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"2753","DOI":"10.1016\/S0021-9258(17)40522-9","article-title":"Selective association of spectrin with the cytoplasmic surface of human erythrocyte plasma membranes","volume":"252","author":"Bennett V.","year":"1977","journal-title":"J. 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