1 Ocak 2010 Dergi makalesi Açık Erişim

Alanay, Yasemin; Avaygan, Hrispima; Camacho, Natalia; Utine, G. Eda; Boduroglu, Koray; Aktas, Dilek; Alikasifoglu, Mehmet; Tuncbilek, Ergul; Orhan, Diclehan; Bakar, Filiz Tiker; Zabel, Bernard; Superti-Furga, Andrea; Bruckner-Tuderman, Leena; Curry, Cindy J. R.; Pyott, Shawna; Byers, Peter H.; Eyre, David R.; Baldridge, Dustin; Lee, Brendan; Merrill, Amy E.; Merrill, Amy E.

Dublin Core

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  <dc:creator>Alanay, Yasemin</dc:creator>
  <dc:creator>Avaygan, Hrispima</dc:creator>
  <dc:creator>Camacho, Natalia</dc:creator>
  <dc:creator>Utine, G. Eda</dc:creator>
  <dc:creator>Boduroglu, Koray</dc:creator>
  <dc:creator>Aktas, Dilek</dc:creator>
  <dc:creator>Alikasifoglu, Mehmet</dc:creator>
  <dc:creator>Tuncbilek, Ergul</dc:creator>
  <dc:creator>Orhan, Diclehan</dc:creator>
  <dc:creator>Bakar, Filiz Tiker</dc:creator>
  <dc:creator>Zabel, Bernard</dc:creator>
  <dc:creator>Superti-Furga, Andrea</dc:creator>
  <dc:creator>Bruckner-Tuderman, Leena</dc:creator>
  <dc:creator>Curry, Cindy J. R.</dc:creator>
  <dc:creator>Pyott, Shawna</dc:creator>
  <dc:creator>Byers, Peter H.</dc:creator>
  <dc:creator>Eyre, David R.</dc:creator>
  <dc:creator>Baldridge, Dustin</dc:creator>
  <dc:creator>Lee, Brendan</dc:creator>
  <dc:creator>Merrill, Amy E.</dc:creator>
  <dc:creator>Merrill, Amy E.</dc:creator>
  <dc:date>2010-01-01</dc:date>
  <dc:description>Osteogenesis imperfecta is a clinically and genetically heterogeneous brittle bone disorder that results from defects in the synthesis, structure, or posttranslational modification of type I procollagen. Dominant forms of OI result from mutations in COL1A1 or COL1A2, which encode the chains of the type I procollagen heterotrimer. The mildest form of OI typically results from diminished synthesis of structurally normal type 1 procollagen, whereas moderately severe to lethal forms of OI usually result from structural defects in one of the type 1 procollagen chains. Recessively inherited OI, usually phenotypically severe, has recently been shown to result from defects in the prolyl-3-hydroxylase complex that lead to the absence of a single 3-hydroxyproline at residue 986 of the alpha 1 (I) triple helical domain. We studied a cohort of five consanguineous Turkish families, originating from the Black Sea region of Turkey, with moderately severe recessively inherited OI and identified a novel locus for OI on chromosome 17. In these families, and in a Mexican-American family, homozygosity for mutations in FKBP10, which encodes FKBP65, a chaperone that participates in type 1 procollagen folding, was identified. Further, we determined that FKBP10 mutations affect type I procollagen secretion. These findings identify a previously unrecognized mechanism in the pathogenesis of OI.</dc:description>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/25305</dc:identifier>
  <dc:identifier>oai:zenodo.org:25305</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>AMERICAN JOURNAL OF HUMAN GENETICS 86(4) 551-559</dc:source>
  <dc:title>Mutations in the Gene Encoding the RER Protein FKBP65 Cause Autosomal-Recessive Osteogenesis Imperfecta</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
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