Publications by authors named "Timothy L Dosey"

Article Synopsis
  • Cation channels from the transient receptor potential (TRP) family play crucial roles by responding to various stimuli that affect their gate opening.
  • Previous research has struggled to clarify how the gates of these channels interact, particularly focusing on extracellular loops called 'pore turrets' in the TRPV subfamily.
  • Our study utilized structural analysis of rat TRPV2 to show the significance of the pore turret, revealing both fully open and partially open states and suggesting that lipid binding can influence the lower gate and interact with the upper gate through the pore turret.
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Viroporins are small virus-encoded ion channel proteins. Most viroporins are monovalent selective cation channels, with few showing the ability to conduct divalent cations, like calcium (Ca). Nevertheless, some viroporins are known to disrupt host cell Ca homeostasis, which is critical for virus replication and pathogenesis.

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Background: Presently, there is no effective treatment for the lethal muscle wasting disease Duchenne muscular dystrophy (DMD). Here we show that increased sphingosine-1-phoshate (S1P) through direct injection or via the administration of the small molecule 2-acetyl-4(5)-tetrahydroxybutyl imidazole (THI), an S1P lyase inhibitor, has beneficial effects in acutely injured dystrophic muscles of mdx mice.

Methods: We treated mdx mice with and without acute injury and characterized the histopathological and functional effects of increasing S1P levels.

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Hypoxia Inducible Factor (HIF) signaling pathway is important for tumor cells with limited oxygen supplies, as it is shown to be involved in the process of proliferation and angiogenesis. Given its pivotal role in cancer biology, robust assays for tracking changes in HIF expression are necessary for understanding its regulation in cancer as well as developing therapies that target HIF signaling. Here we report a novel HIF reporter construct containing tandem repeats of minimum HIF binding sites upstream of eYFP coding sequence.

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