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Travis L. Rodkey

Researcher at University of Texas Health Science Center at Houston

Publications -  5
Citations -  392

Travis L. Rodkey is an academic researcher from University of Texas Health Science Center at Houston. The author has contributed to research in topics: Lipid bilayer fusion & Signal transduction. The author has an hindex of 5, co-authored 5 publications receiving 347 citations. Previous affiliations of Travis L. Rodkey include University of Texas at Austin & Rice University.

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Signal integration by lipid-mediated spatial cross talk between Ras nanoclusters.

TL;DR: It is concluded that phosphatidylserine maintains the lateral segregation of diverse lipid-based assemblies on the plasma membrane and that lateral connectivity between spatially remote lipid assemblies offers important previously unexplored opportunities for signal integration and signal processing.
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Caveolae regulate the nanoscale organization of the plasma membrane to remotely control Ras signaling

TL;DR: Caveolae transduce mechanical stress into plasma membrane lipid alterations that disrupt Ras organization in an isoform-specific manner and modulate downstream signal transduction.
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Another surprise from Metformin: novel mechanism of action via K-Ras influences endometrial cancer response to therapy

TL;DR: Metformin inhibited cell proliferation, induced apoptosis, and decreased tumor growth in preclinical endometrial cancer models, with the greatest response observed in cells harboring activating mutations in K-Ras, revealing a novel mechanism of action for metformin.
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Munc18a Scaffolds SNARE Assembly to Promote Membrane Fusion

TL;DR: In vitro fusion assays suggest that Munc18a binds to the Syntaxin1a NRD and H3 domain within the assembled t-SNARE complex, positioning them for productive VAMP2 binding.
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The polybasic juxtamembrane region of Sso1p is required for SNARE function in vivo.

TL;DR: The results suggest that the sequence of the juxtamembrane region of Sso1p is vital for function in vivo, independent of the ability of these proteins to direct membrane fusion.