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Joseph A. Szule

Researcher at Texas A&M University

Publications -  20
Citations -  634

Joseph A. Szule is an academic researcher from Texas A&M University. The author has contributed to research in topics: Synaptic vesicle & Vesicle. The author has an hindex of 10, co-authored 16 publications receiving 559 citations. Previous affiliations of Joseph A. Szule include University of Calgary & Brock University.

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The Effects of Acyl Chain Length and Saturation of Diacylglycerols and Phosphatidylcholines on Membrane Monolayer Curvature

TL;DR: The second messenger, diacylglycerol (DAG), introduces negative curvature in phospholipid monolayers and strongly induces the lamellar to reverse hexagonal phase transition, which is critical for the induction of the H(II) phase by DOG.
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Macromolecular connections of active zone material to docked synaptic vesicles and presynaptic membrane at neuromuscular junctions of mouse.

TL;DR: Electron tomography was used to view macromolecules composing active zone material (AZM) in axon terminals at mouse neuromuscular junctions to support the hypothesis that AZM regulates vesicle docking and fusion.
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Regulation of synaptic vesicle docking by different classes of macromolecules in active zone material.

TL;DR: Vesicle movement toward and maintenance at docking sites on the presynaptic membrane are directed by an orderly succession of stable interactions between the vesicles and distinct classes of AZM macromolecules positioned at different distances from the membrane.
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Revisiting the role of SNAREs in exocytosis and membrane fusion.

TL;DR: While SNARE proteins are essential to the physiology of exocytosis, assay limitations often prevent definitive conclusions concerning the molecular mechanism of membrane fusion, the SNAREs are more likely to function upstream as modulators or priming factors of fusion.
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Calcium-triggered Membrane Fusion Proceeds Independently of Specific Presynaptic Proteins

TL;DR: A stage-specific preparation is used to test the roles of SNAREs, synaptotagmin, and SNARE-binding proteins in the mechanism of Ca2+-triggered membrane fusion, indicating a more direct involvement of other proteins inThe triggered fusion pathway.