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Showing 1 to 8 of 8 for “"RhoGEF"”.

  1. Activated RhoA Positively Regulates Exchange Activity of PDZ-RhoGEF

    … activation of the protein. The RGS subfamily of RhoGEFs (RGS-RhoGEFs) act as direct mediators of RhoA activation in response to stimulation of the heterotrimeric G12 and G13 proteins by hormone receptors. RhoGEFs usually bind most tightly to the nucleotide free form of RhoA, which represents the …

    utswmed Repository record for Activated RhoA Positively Regulates Exchange Activity of PDZ-RhoGEF (opens in a new tab)

  2. From Cell Shape to Body Shape: Epithelial Morphogenesis in Drosophila melanogaster

    … by Rho guanine nucleotide exchange factors (RhoGEFs) play an important role in this process. The present thesis investigates the mechanisms that control activation and specificity of the GTPase Rho1 by DRhoGEF2 during morphogenesis of the Drosophila embryonic epidermis. DRhoGEF2 is the …

    lund Repository record for From Cell Shape to Body Shape: Epithelial Morphogenesis in Drosophila melanogaster (opens in a new tab)

  3. Rho GTPase Signaling Modulates Neurotransmission in Caenorhabditis elegans

    … Kalirin and Trio ortholog UNC-73 contains two RhoGEF domains that specifically activate either Rac or Rho GTPases, respectively. The RhoGEF1 domain and the Rac pathway are required for axon guidance in neuronal development, while the RhoGEF2 domain is involved in the control of locomotion, …

    ohiolink Repository record for Rho GTPase Signaling Modulates Neurotransmission in Caenorhabditis elegans (opens in a new tab)

  4. Stretch-Dependant Tonic Force Maintenance in Rabbit Epigastric Artery

    … Colchicine incubation has been shown to release RhoGEF, a RhoA activator, and resulted in increased tonic force and MLC-p which were both inhibited by a ROK inhibitor.Additionally, KC1-stimulation appeared to activate MAPK and ROK pathways, while stretch alone activated a yet undetermined …

    vcu Repository record for Stretch-Dependant Tonic Force Maintenance in Rabbit Epigastric Artery (opens in a new tab)

  5. Molecular mechanisms of mammalian cell survival and differentiation

    … understood. In Chapter 2, I identified XPLN, a RhoGEF, as an endogenous inhibitor of mTORC2 kinase activity towards Akt. Furthermore, I showed that the GEF activity of XPLN is dispensable for its regulation of mTORC2 and Akt, whereas an N-terminal 125-amino acid fragment of XPLN is both …

    uiuc Repository record for Molecular mechanisms of mammalian cell survival and differentiation (opens in a new tab)

  6. Identification and characterization of genetic interactors of the Rho Guanine-nucleotide exchange factor Pebble in <em>Drosophila</em>

    The gene pebble (pbl) encodes a Rho GEF required for the migration of mesoderm cells during Drosophila gastrulation. The spreading of mesoderm cells is controlled by the FGF signalling pathway acting through the FGF receptor Heartless (Htl). Pbl represents an important downstream component of this …

    dundee Repository record for Identification and characterization of genetic interactors of the Rho Guanine-nucleotide exchange factor Pebble in <em>Drosophila</em> (opens in a new tab)

  7. Regulation of rho guanine nucleotide exchange factors through lipid binding and phosphorylation

    Submission published under a 24 month embargo labeled 'U of I Access', the embargo will last until 2027-08-01

    uiuc Repository record for Regulation of rho guanine nucleotide exchange factors through lipid binding and phosphorylation (opens in a new tab)

  8. Redefining the specificity of phosphoinositide-binding by human PH domain-containing proteins

    … containing Dbl-homology (DH) domain, called RhoGEFs, which are known for conserved DH-PH domain structures. While the DH domain is responsible for GEF activity, the function of the PH domain in RhoGEFs is not well-understood. In Chapter 4, I have investigated the role of phosphoinositide …

    uiuc Repository record for Redefining the specificity of phosphoinositide-binding by human PH domain-containing proteins (opens in a new tab)