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Witchuda Saengsawang

Researcher at Mahidol University

Publications -  26
Citations -  493

Witchuda Saengsawang is an academic researcher from Mahidol University. The author has contributed to research in topics: Medicine & Internal medicine. The author has an hindex of 9, co-authored 19 publications receiving 391 citations. Previous affiliations of Witchuda Saengsawang include University of Illinois at Chicago & University of Wisconsin-Madison.

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Synaptic Regulation of Microtubule Dynamics in Dendritic Spines by Calcium, F-Actin, and Drebrin

TL;DR: It is shown that in hippocampal neurons from male and female mice, the majority of microtubules enter spines from highly localized sites at the base of spines in response to synapse-specific calcium transients that promote microtubule entry into active spines.
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Regulation of ubiquitin-dependent cargo sorting by multiple endocytic adaptors at the plasma membrane

TL;DR: It is demonstrated that multiple plasma membrane endocytic adaptors function redundantly to regulate clathrin-mediated endocytosis and to recruit components of the endosomal sorting complex required for transport (ESCRT) machinery to the cell surface to direct the sorting of ubiquitin-modified substrates.
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Heterotrimeric G-Proteins Interact Directly with Cytoskeletal Components to Modify Microtubule-Dependent Cellular Processes

TL;DR: The role of tubulin and microtubules in directly mediating effects of heterotrimeric G-proteins on neuronal outgrowth, shape and differentiation and their role in synaptic plasticity is reviewed.
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The F-BAR Protein CIP4 Inhibits Neurite Formation by Producing Lamellipodial Protrusions

TL;DR: This is the first study to demonstrate that an F-BAR protein functions differently in neuronal versus nonneuronal cells and induces lamellipodial protrusions instead of invaginations or filopodia-like structures.
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Structural model of a complex between the heterotrimeric G protein, Gsα, and tubulin

TL;DR: Structural models explain the able of tubulin to facilitate GTP exchange on Galpha and the ability of Galpha to activate tubulin GTPase.