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.
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Showing 1 to 7 of 7 for “"Pleckstrin Homology domain"”.
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Analysis of the Interaction and Functional Determinants of Arc and Its Regulation of Dynamin
… studies show Arc interacts with the proline-rich domain of dynamin and not the pleckstrin homology domain. All together, these results provide a mechanism to explain the previously reported role of Arc in glutamate receptor internalization.
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A screen for phosphatidylinositol 3,4-bisphosphate and other 3-phosphoinositide effector proteins
… proteins. The identification of tandem pleckstrin homology domain containing protein-1 (TAPP-1) and protein kinase B (PKB) among a multitude of proteins expressing known lipid binding domains (LBDs) demonstrates the utility of this strategy. Analysis of other similarly, isotopically …
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Phosphatidylinositol 3-phosphate binding properties and autoinhibition mechanism of Phafin2
… Phafins are modular with an N-terminal PH (Pleckstrin Homology) domain followed by a central FYVE (Fab1, YOTB, Vac1, and EEA1) domain. Both the Phafin2 PH and FYVE domains bind phosphatidylinositol 3-phosphate [PtdIns(3)P], a phosphoinositide mainly found in endosomal and lysosomal …
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Protein-Protein Interactions and Muscle cell Signaling Via Syntrophin
… Oligomerization was localized to the N-terminal pleckstrin homology domain (PH1) or adjacent sequences; the second, C-terminal PH2 domain did not show oligomerization. PH1 was found to se lf-associate and calmodulin or Ca<sup>2+</sup> chelating agents such as EGTA could effectively prevent this …
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Targeting Ph Domain Proteins For Cancer Therapy
… critical to new and promising targeted therapy. Pleckstrin Homology (PH) domain proteins are one of the biggest protein families in the human proteome. However, no drugs have been achieved to the late development stages, let alone getting to the market. Thus, a deeper understanding of this …
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Redefining the specificity of phosphoinositide-binding by human PH domain-containing proteins
… I have examined the binding characteristics of Pleckstrin Homology (PH) domain, a lipid-binding domain, with phosphoinositides (phosphatidylinositol phosphates or PIPs), an important class of regulatory phospholipids. PH domains are presumed to bind PIPs, but specific interaction with and …