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Showing 1 to 5 of 5 for “"IA-2"”.

  1. Diabetes mellitus Typ 2 oder Typ LADA- Unterscheidung anhand klinischer Kriterien

    Hall, FlorianLudwig-Maximilians-Universität

    … klinische Unterscheidung des latenten Autoimmundiabetes (LADA) vom Typ 2 Diabetes ist oft problematisch. Deshalb wurde die mögliche Korrelation zwischen klinischen Kriterien und dem Vorkommen von Diabetes-Autoimmunantikörpern untersucht. Von 133 erwachsenen Diabetikern waren 17 (=12,8%) positiv …

    lmu-germany Repository record

  2. T-Zell-Immunität gegen Präproinsulin, Glutamatdecarboxylase 65 und Protein-Tyrosin-Phosphatase-2 in humanem Diabetes mellitus Typ 1

    Plomin, Julia ChristinaUniversität Ulm

    ulm-diss Repository record

  3. The genetic background of gestational diabetes mellitus

    Papadopoulou, AnastasiaDept of Diabetes and Celiac Disease2011

    … determine the genetic background of gestational diabetes (GDM) and to examine how specific genes affect the development of diabetes post partum. In the DiPiS (Diabetes Prediction in Skåne) study we typed for HLA-DQB1 alleled, the transcription factor 7-like 2(TCF7L2) rs7903146, rs12255372 and …

    lund Repository record

  4. Aspects of autoantibody epitopes in type 1 diabetes

    Skärstrand, HannaDepartment of Clinical Sciences, Lund University2014

    Type 1 diabetes (T1D) is strongly associated with autoantibodies against insulin (IAA), glutamic acid decarboxylase 65 (GADA), insulinoma-associated protein 2 (IA-2A) and the most recently identified zinc T8 transporter (ZnT8A). Together or alone, they are important both to predict T1D and to …

    lund Repository record

  5. The Role of [beta]2-Syntrophin Phosphorylation in Secretory Granule Exocytosis

    Schubert, SandraTechnische Universität Dresden

    … membrane protein of the SGs named ICA512/IA-2 binds the PDZ domain of b2-syntrophin,which in turn binds to the F-actin-binding protein utrophin. These data also indicate that stimulation of SG exocytosis affects the phosphorylation of b2-syntrophin,hence altering its binding to …

    qucosa-diss