Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
Results
Showing 1 to 5 of 5 for “"Disabled-2"”.
-
Membrane binding properties of Disabled-2
Disabled-2 (Dab2) is an adapter protein that interacts with cell membranes and it is involved in several biological processes including endocytosis and platelet aggregation. During endocytosis, the Dab2 phosphotyrosine-binding (PTB) domain mediates protein binding to phosphatidylinositol …
-
Structural basis for sulfatide recognition by Disabled-2
Disabled-2 (Dab2) is an adaptor protein that plays critical roles in various biological processes, including protein endocytosis, platelet activation and aggregation, tumor growth, and development. In platelets, Dab2 associates with membrane sulfatide at the platelet surface, modulating platelet …
-
Disabled-2 regulates platelet heterotypic and homotypic aggregation through sulfatide binding
… clotting factors and regulators of aggregation. Disabled-2 (Dab2) is a negative regulator of platelet aggregation released from platelet α-granules. Dab2 binds to the αIIbβ3 integrin, through the PTB domain, and blocks fibrin binding to the integrin which serves as the major cause of …
-
Sulfatides mediate Disabled-2 membrane localization and stability during platelet aggregation
… negative regulators in platelet aggregation is Disabled-2 (Dab2), a modular protein that is released upon platelet activation to the extracellular platelet surface.3 Dab2 inhibits platelet aggregation through its phosphotyrosine-binding (PTB) domain by competing with fibrinogen for ï ¡IIï ¢3 …
-
Studies of the cell biological function of the Amyloid Precursor Protein (APP) family in Drosophila melanogaster and mammals
… novel putative interaction partners, Numb and Disabled-2, were identified. The interacting domain of APP was mapped, and binding was verified by biochemical analysis. The results obtained with the Drosophila model system for cell adhesion properties of APP family proteins were extended to an in …