bioRxiv Science⌕ Search

Biology subjects

Goss, D.

Publications and source records attributed to Goss, D..

2 recordsLinked to original sources

Spurring and Siloing: Identity Navigation in Scientific Writing Among Asian Early-Career Researchers

Scientific writing and publication are critical sites where students must navigate between personal identities and presumed scientific objectivity. For non-white student researchers, particularly those stereotyped as "model minorities," this process involves complex negotiations. This qualitative study examines how Asian and Asian American students navigate ethnic and cultural identities within scientific writing processes. Using an integrated theoretical framework combining cultural community wealth, narrative identity, and border crossing, we analyzed how participants deployed cultural resources while navigating institutional expectations. Drawing on interviews with 23 student participants who engaged with the [Blinded Journal], we identified two primary approaches: "spurring," wherein ethnic and cultural backgrounds catalyze research questions, and "siloing," wherein these identities are deliberately compartmentalized during writing. Findings reveal that while participants drew upon familial capital to inform research interests, most practiced disciplinary compartmentalization and adhered to perceived scientific norms. This tension demonstrates how students negotiate cultural scripts while developing professional identities. Our findings suggest that science educators could help students recognize their cultural backgrounds as valuable epistemic resources rather than sources of bias, explicitly address the myth of value-neutral science, and provide models of how scientists integrate personal and cultural perspectives into rigorous scientific work.

scientific communication and education↗

Recruitment of human eIF4G1 or DAP5 to the 5’ untranslated regions of a subset of cellular mRNAs drives cap-independent translation

During unfavorable human cellular conditions (e.g., tumor hypoxia, viral infection, etc.), canonical, cap-dependent mRNA translation is suppressed. Nonetheless, a subset of physiologically important mRNAs (e.g., HIF-1, FGF-9, and p53) is still translated by an unknown, cap-independent mechanism. Additionally, expression levels of eIF4G and its homolog, death associated protein 5 (DAP5), are elevated. Using fluorescence anisotropy binding studies, luciferase reporter-based in vitro translation assays, and mutational analyses, here we demonstrate that eIF4GI and DAP5 specifically bind to the 5 UTRs of these cap-independently translated mRNAs. Surprisingly, we find that the eIF4E binding domain of eIF4GI increases not only the binding affinity, but also the selectivity among these mRNAs. We further demonstrate that the affinities of eIF4GI and DAP5 binding to these 5 UTRs correlate with the efficiency with which these factors drive cap-independent translation of these mRNAs. Integrating the results of our binding and translation assays, we show that eIF4GI and/or DAP5 are critical for recruitment of a specific subset of mRNAs to the ribosome and provide mechanistic insight into their cap-independent translation.

biophysics↗