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This article focuses on the composition practices of three single moms across academic ranks and single mom identities in order to expand our understanding in Composition and Rhetoric of how composing processes are influenced by lived experience and material circumstances. Drawing on composition process research, I argue for the need to give greater attention to the individual composing practices of those with marginalized identities in order to strengthen our work in Comp/Rhet as teachers, mentors, and colleagues. Written in a style that combines testimonios and analysis, this article pushes and expands our understanding of what counts as composition practice, why composition practice does not happen, and how composition practices in and out of the classroom can be valuable resources.

Many existing works have made great strides towards reducing racial bias in face recognition. However, most of these methods attempt to rectify bias that manifests in models during training instead of directly addressing a major source of the bias, the dataset itself. Exceptions to this are BUPT-Balancedface/RFW and Fairface, but these works assume that primarily training on a single race or not racially balancing the dataset are inherently disadvantageous. We demonstrate that these assumptions are not necessarily valid. In our experiments, training on only African faces induced less bias than training on a balanced distribution of faces and distributions skewed to include more African faces produced more equitable models. We additionally notice that adding more images of existing identities to a dataset in place of adding new identities can lead to accuracy boosts across racial categories. Our code is available at https://github.com/j-alex-hanson/rethinking-race-face-datasets., Accepted as an oral paper to the Human-centric Trustworthy Computer Vision (HTCV 2021) workshop at ICCV 2021; 17 pages, 9 figures, 6 tables

The complex disorder Cantu syndrome (CS) arises from gain-of-function mutations in either KCNJ8 or ABCC9, the genes encoding the Kir6.1 and SUR2 subunits of ATP-sensitive potassium (KATP) channels, respectively. Recent reports indicate that such mutations can increase channel activity by multiple molecular mechanisms. In this study, we determined the mechanism by which KATP function is altered by several substitutions in distinct structural domains of SUR2: D207E in the intracellular L0-linker and Y985S, G989E, M1060I, and R1154Q/R1154W in TMD2. We engineered substitutions at their equivalent positions in rat SUR2A (D207E, Y981S, G985E, M1056I, and R1150Q/R1150W) and investigated functional consequences using macroscopic rubidium (86Rb+) efflux assays and patch-clamp electrophysiology. Our results indicate that D207E increases KATP channel activity by increasing intrinsic stability of the open state, whereas the cluster of Y981S/G985E/M1056I substitutions, as well as R1150Q/R1150W, augmented Mg-nucleotide activation. We also tested the responses of these channel variants to inhibition by the sulfonylurea drug glibenclamide, a potential pharmacotherapy for CS. None of the D207E, Y981S, G985E, or M1056I substitutions had a significant effect on glibenclamide sensitivity. However, Gln and Trp substitution at Arg-1150 significantly decreased glibenclamide potency. In summary, these results provide additional confirmation that mutations in CS–associated SUR2 mutations result in KATP gain-of-function. They help link CS genotypes to phenotypes and shed light on the underlying molecular mechanisms, including consequences for inhibitory drug sensitivity, insights that may inform the development of therapeutic approaches to manage CS.

The complex disorder Cantu syndrome (CS) arises from gain-of-function mutations in either KCNJ8 or ABCC9, the genes encoding the Kir6.1 and SUR2 subunits of ATP-sensitive potassium (KATP) channels, respectively. Recent reports indicate that such mutations can increase channel activity by multiple molecular mechanisms. In this study, we determined the mechanism by which KATP function is altered by several substitutions in distinct structural domains of SUR2: D207E in the intracellular L0-linker and Y985S, G989E, M1060I, and R1154Q/R1154W in TMD2. We engineered substitutions at their equivalent positions in rat SUR2A (D207E, Y981S, G985E, M1056I, and R1150Q/R1150W) and investigated functional consequences using macroscopic rubidium (86Rb+) efflux assays and patch-clamp electrophysiology. Our results indicate that D207E increases KATP channel activity by increasing intrinsic stability of the open state, whereas the cluster of Y981S/G985E/M1056I substitutions, as well as R1150Q/R1150W, augmented Mg-nucleotide activation. We also tested the responses of these channel variants to inhibition by the sulfonylurea drug glibenclamide, a potential pharmacotherapy for CS. None of the D207E, Y981S, G985E, or M1056I substitutions had a significant effect on glibenclamide sensitivity. However, Gln and Trp substitution at Arg-1150 significantly decreased glibenclamide potency. In summary, these results provide additional confirmation that mutations in CS–associated SUR2 mutations result in KATP gain-of-function. They help link CS genotypes to phenotypes and shed light on the underlying molecular mechanisms, including consequences for inhibitory drug sensitivity, insights that may inform the development of therapeutic approaches to manage CS.