{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T10:43:04Z","timestamp":1788432184350,"version":"build-2803163510"},"reference-count":62,"publisher":"Portland Press Ltd.","issue":"4","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2016,8,15]]},"abstract":"<jats:p>There is a family of proteins from parasitic worms which combine N-terminal EF-hand domains with C-terminal dynein light chain-like domains. Data are accumulating on the biochemistry and cell biology of these proteins. However, little is known about their functions in\u00a0vivo. Schistosoma mansoni expresses 13 family members (SmTAL1\u2013SmTAL13). Three of these (SmTAL1, SmTAL2 and SmTAL3) have been subjected to biochemical analysis which demonstrated that they have different molecular properties. Although their overall folds are predicted to be similar, small changes in the EF-hand domains result in differences in their ion binding properties. Whereas SmTAL1 and SmTAL2 are able to bind calcium (and some other) ions, SmTAL3 appears to be unable to bind any divalent cations. Similar biochemical diversity has been seen in the CaBP proteins from Fasciola hepatica. Four family members are known (FhCaBP1\u20134). All of these bind to calcium ions. However, FhCaBP4 dimerizes in the presence of calcium ions, FhCaBP3 dimerizes in the absence of calcium ions and FhCaBP2 dimerizes regardless of the prevailing calcium ion concentration. In both the SmTAL and FhCaBP families, the proteins also differ in their ability to bind calmodulin antagonists and related drugs. Interestingly, SmTAL1 interacts with praziquantel (the drug of choice for treating schistosomiasis). The pharmacological significance (if any) of this finding is unknown.<\/jats:p>","DOI":"10.1042\/bst20150270","type":"journal-article","created":{"date-parts":[[2016,8,15]],"date-time":"2016-08-15T12:27:21Z","timestamp":1471264041000},"page":"1005-1010","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["A mysterious family of calcium-binding proteins from parasitic worms"],"prefix":"10.1042","volume":"44","author":[{"given":"Charlotte\u00a0M.","family":"Thomas","sequence":"first","affiliation":[{"name":"School of Biological Sciences, Queen's University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast BT9 7BL, U.K."},{"name":"Institute for Global Food Security, Queen's University Belfast, 18-30 Malone Road, Belfast BT9 5BN, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David\u00a0J.","family":"Timson","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, Queen's University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast BT9 7BL, U.K."},{"name":"School of Pharmacy and Biomolecular Sciences, University of Brighton, Huxley Building, Lewes Road, Brighton BN2 4GJ, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2016,8,15]]},"reference":[{"key":"2021111719500664900_B1","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1016\/0092-8674(95)90408-5","article-title":"Calcium signaling","volume":"80","author":"Clapham","year":"1995","journal-title":"Cell"},{"key":"2021111719500664900_B2","doi-asserted-by":"publisher","first-page":"7261","DOI":"10.1021\/jp048838m","article-title":"Solvation of calcium ion in polar solvents:\u2009 an X-ray diffraction and ab initio study","volume":"108","author":"Megyes","year":"2004","journal-title":"J. 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