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Borschel, W. F.

Publications and source records attributed to Borschel, W. F..

2 recordsLinked to original sources

CalFluxTools: An R package for analysis of high-throughput calcium oscillation screening data

Whole plate detection of calcium flux signals using fluorescence is a powerful technology for monitoring oscillatory activity of excitable cells in a high throughput fashion that sees broad applications in neurotoxicity and cardiotoxicity research. However, analysis of calcium oscillation profiles can output more than 60 peak kinetic parameters, which makes manual data analysis challenging. We have created the CalFluxTools R package, an automated pipeline for parsing plate data for 384 well plates, generating quality control metrics and plots, and performing data analysis, including T-tests, Z-score analysis, and machine learning prediction of compound toxicity values. CalFluxTools requires a plate map and experimental manifest that includes parameter filtration specifications, as well as data in the ".statall" format. CalFluxTools runs in less than a minute on a Macbook Pro with a 2.6 GHz 6-Core Intel Core i7 processor.

bioinformatics↗

Conformational ensemble of the human TRPV3 ion channel

Transient receptor potential vanilloid channel 3 (TRPV3), a member of the thermosensitive TRP (thermoTRPV) channels, is activated by warm temperatures and serves as a key regulator of normal skin physiology through the release of pro-inflammatory messengers. Mutations in trpv3 have been identified as the cause of the congenital skin disorder, Olmsted syndrome. Unlike other members of the thermoTRPV channel family, TRPV3 sensitizes upon repeated simulation, yet a lack of structural information about the channel precludes a molecular-level understanding of TRPV3 sensitization and gating. Here, we present the cryo-electron microscopy structures of apo and sensitized human TRPV3, as well as several structures of TRPV3 in the presence of the common thermoTRPV agonist 2-aminoethoxydiphenyl borate (2-APB). Our results show -to-{pi}-helix transitions in the S6 during sensitization, and suggest a critical role for the S4-S5 linker {pi}-helix during ligand gating.

biochemistry↗