Molecular Biology and Genetics / Moleküler Biyoloji ve Genetik

Permanent URI for this collectionhttps://hdl.handle.net/11147/9

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Access type: Open accessAuthor: search.filters.author.Şimşek Papur, Özlenen

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  • Conference Object
    Functional Characterization of Clinically Relevant Novel Mutations in Atp7b Gene Using the Saccharomyces Cerevisiae Model
    (Wiley, 2016) Şimşek Papur, Özlenen; Koç, Ahmet; Terzioğlu, Orhan; Koç, Ahmet; 04.03. Department of Molecular Biology and Genetics; 04. Faculty of Science; 01. Izmir Institute of Technology
    Wilson disease is an autosomal recessive disorder of copper metabolism characterized as neurodegeneration and liver abnormalities. It is caused by defects in the ATP7B gene. ATP7B is responsible for the sequestration of Cu into secretory vesicles, and this function is exhibited by the orthologous Ccc2p in the yeast. We aimed to characterize clinically-relevant novel mutations of p.T788I, p.V1036I and p.R1038G-fsX8 in yeast lacking the CCC2 gene.
  • Article
    Citation - WoS: 8
    Citation - Scopus: 10
    Functional Characterization of New Mutations in Wilson Disease Gene (atp7b) Using the Yeast Model
    (Urban und Fischer Verlag GmbH und Co. KG, 2015) Şimşek Papur, Özlenen; Koç, Ahmet; Koç, Ahmet; 04.03. Department of Molecular Biology and Genetics; 04. Faculty of Science; 01. Izmir Institute of Technology
    The Wilson disease gene, a copper transporting ATPase (Atp7b), is responsible for the sequestration of Cu into secretory vesicles, and this function is exhibited by the orthologous Ccc2p in the yeast. In this study, we aimed to characterize clinically relevant new mutations of human ATP7B (p.T788I, p.V1036I and p.R1038G-fsX83) in yeast lacking the CCC2 gene. Expression of human wild type ATP7B gene in ccc2δ mutant yeast restored the growth deficiency and copper transport activity; however, expression of the mutant forms did not restore the copper transport functions and only partially supported the cell growth. Our data support that p.T788I, p.V1036I and p.R1038G-fsX83 mutations cause functional deficiency in ATP7B functions and suggest that these residues are important for normal ATP7B function.