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Showing 1 to 4 of 4 for “"Sec23"”.

  1. Principles of COPII Coat Assembly

    … stages. The inner coat comprises the Sar1-Sec23/Sec24 heterotrimeric complex and is recruited through the activation of the Sar1 GTPase. Sar1 regulates the assembly/disassembly cycle of the coat, Sec23 acts as its GTPase activating protein (GAP), whereas Sec24 is involved in selecting …

    cambridge Repository record for Principles of COPII Coat Assembly (opens in a new tab)

  2. From the Endoplasmic Reticulum to the Golgi Apparatus : In Vitro and In Vivo Approaches to Understanding COPII Vesicle Function in Plant Cells

    … Sar1p and the heterodimeric protein complexes Sec23/24 and Sec13/31. COPII mediated sorting occur when protein cargoes exit the ER. Although the principles of ER-to-GA transport organization in plant cells are supposed to be similar to those in yeast and mammalian systems, evidence in support …

    heid-diss Repository record for From the Endoplasmic Reticulum to the Golgi Apparatus : In Vitro and In Vivo Approaches to Understanding COPII Vesicle Function in Plant Cells (opens in a new tab)

  3. Defining the Cellular and Molecular Basis of Spondyloepiphyseal dysplasia tarda

    … proteins: the small GTPase Sar1, the inner coat (Sec23/Sec24) and the outer layer (Sec13/31). The efficiency of COPII cycling is dispensable for the transport of small soluble cargoes or trans- membrane cargoes, yet is mandatory for the exit of “extra-size” proteins, such as procollagens. To …

    the-open-u Repository record for Defining the Cellular and Molecular Basis of Spondyloepiphyseal dysplasia tarda (opens in a new tab)

  4. P125, A COPII INTERACTING PROTEIN

    … is a protein of 125 kDa that interacts with Sec23A, a component of the COPII coat. It was found to participate in the organization of ER exit sites (Tani et al., 1999; Shimoi et al., 2005). In this current study, using GST-pulldown and mass spectrometry analysis, p125A is also identified as …

    nus Repository record for P125, A COPII INTERACTING PROTEIN (opens in a new tab)