{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T19:34:30Z","timestamp":1772134470046,"version":"3.50.1"},"reference-count":22,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2010,10,14]],"date-time":"2010-10-14T00:00:00Z","timestamp":1287014400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2011,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>We describe results from a mutational analysis of the region of the dentin sialophosphoprotein (DSPP) gene encoding dentin phosphoprotein (DPP) in 12 families with dominantly inherited dentin diseases. In eight families (five mutations in the N-terminal third of DPP), the clinical and radiologic features were uniform and compatible with dentin dysplasia type II (DD-II) with major clinical signs in the deciduous dentition. In the other families (four mutations in the more C-terminal part), the permanent teeth also were affected, and the diseases could be classified as variants of dentinogenesis imperfecta. Attrition was not prominent, but periapical infections were common. Discoloring with varying intensity was evident, and pulps and root canals were obliterated in the permanent dentition. All mutations caused a frameshift that replaced the Ser-Ser-Asx repeat by a code for a hydrophobic downstream sequence of approximately original length. We conclude that frameshift mutations in DSPP explain a significant part of dentin diseases. Furthermore, we propose that the location of the mutation is reflected in the phenotypic features as a gradient from DD-II to more severe disease that does not conform to the classic definitions of DI-II. \u00a9 2011 American Society for Bone and Mineral Research.<\/jats:p>","DOI":"10.1002\/jbmr.276","type":"journal-article","created":{"date-parts":[[2010,10,14]],"date-time":"2010-10-14T19:38:18Z","timestamp":1287085098000},"page":"873-880","source":"Crossref","is-referenced-by-count":33,"title":["Frameshift mutations in dentin phosphoprotein and dependence of dentin disease phenotype on mutation location"],"prefix":"10.1093","volume":"26","author":[{"given":"Pekka","family":"Nieminen","sequence":"first","affiliation":[{"name":"Department of Oral and Maxillofacial Diseases, Helsinki University Central Hospital, Helsinki, Finland"},{"name":"Institute of Dentistry, Biomedicum, University of Helsinki, Helsinki, Finland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lisa","family":"Papagiannoulis-Lascarides","sequence":"additional","affiliation":[{"name":"Department of Paediatric Dentistry, School of Dentistry, University of Athens, Athens, Greece"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Janna","family":"Waltimo-Siren","sequence":"additional","affiliation":[{"name":"Institute of Dentistry, Biomedicum, University of Helsinki, Helsinki, Finland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P\u00e4ivi","family":"Ollila","sequence":"additional","affiliation":[{"name":"Institute of Dentistry, University of Oulu, Oulu, Finland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sara","family":"Karjalainen","sequence":"additional","affiliation":[{"name":"Institute of Dentistry, University of Turku, Turku, 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