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Stefanie A. Baril on Muck Rack

Stefanie A. Baril

As seen in: Nature, American Chemical Society, Drug Metabolism and Disposition (ASPET)
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Articles

The role of ATP-binding Cassette subfamily B member 6 in the inner ear - Nature Communications

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By Stefanie A. Baril, Katie Wilson, Yu Fukuda, Tomoka Gose, Alexander G. Myasnikov, Jian Zuo, Ravi Kalathur, Michael Taylor, Megan L. O’Mara
| Nature Verified
Abstract ABCB6 has been implicated in dyschromatosis universalis hereditaria, a condition characterized by hyperpigmented and hypopigmented skin macules. Dyschromatosis universalis hereditaria can also present with hearing loss. Dyschromatosis universalis hereditaria-associated mutations in ABCB6 have been reported, but the role of this protein in the inner ear has not been studied.
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Publisher Correction: The net electrostatic potential and hydration of ABCG2 affect substrate transport - Nature Communications

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By Tomoka Gose, Yu Fukuda, Stefanie A. Baril, Anang A. Shelat
| Nature Verified
Correction to: Nature Communications https://doi.org/10.1038/s41467-023-40610-5, published online 18 August 2023 In this article the author name Megan L. O’Mara was incorrectly written as Megan L. O’ Mara. The original article has been corrected.
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The net electrostatic potential and hydration of ABCG2 affect substrate transport - Nature Communications

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By Tomoka Gose, Yu Fukuda, Stefanie A. Baril, Anang A. Shelat
| Nature Verified
Abstract ABCG2 is a medically important ATP-binding cassette transporter with crucial roles in the absorption and distribution of chemically-diverse toxins and drugs, reducing the cellular accumulation of chemotherapeutic drugs to facilitate multidrug resistance in cancer. ABCG2’s capacity to transport both hydrophilic and hydrophobic compounds is not well understood. Here we assess the molecular basis for substrate discrimination by the binding pocket.
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