In-person undergraduate research experiences (UREs) promote students' integration into careers in life science research. In 2020, the COVID-19 pandemic prompted institutions hosting summer URE programs to offer them remotely, raising questions about whether undergraduates who participate in remote research can experience scientific integration and whether they might perceive doing research less favorably (i.e.
View Article and Find Full Text PDFThe COVID-19 pandemic shut down undergraduate research programs across the United States. A group of 23 colleges, universities, and research institutes hosted remote undergraduate research programs in the life sciences during Summer 2020. Given the unprecedented offering of remote programs, we carried out a study to describe and evaluate them.
View Article and Find Full Text PDFResearch within interprofessional education (IPE) indicates health professional students hold stereotypes of other health professions at all stages within their academic journey. IPE can minimize negative stereotypes and influence a student's willingness and readiness to collaborate with others. This article explores undergraduate pre-health student stereotypes of various health professionals at the beginning and end of a six-week summer academic enrichment program, which included IPE.
View Article and Find Full Text PDFAs literature indicates, historic racism and implicit bias throughout academia have been profound metrics leading to a lack of diversity, as related to people from underrepresented groups according to race and ethnicity, among biomedical sciences graduate students in U.S. universities.
View Article and Find Full Text PDFThe NEDD4-2 (neural precursor cell-expressed developmentally down-regulated 4-2) HECT ligase catalyzes polyubiquitin chain assembly by an ordered two-step mechanism requiring two functionally distinct E2∼ubiquitin-binding sites, analogous to the trimeric E6AP/UBE3A HECT ligase. This conserved catalytic mechanism suggests that NEDD4-2, and presumably all HECT ligases, requires oligomerization to catalyze polyubiquitin chain assembly. To explore this hypothesis, we examined the catalytic mechanism of NEDD4-2 through the use of biochemically defined kinetic assays examining rates of I-labeled polyubiquitin chain assembly and biophysical techniques.
View Article and Find Full Text PDFThe mechanism of Nedd4-2 has been quantitatively explored for the first time using biochemically defined kinetic assays examining rates of I-polyubiquitin chain assembly as a functional readout. We demonstrate that Nedd4-2 exhibits broad specificity for E2 paralogs of the Ubc4/5 clade to assemble Lys-linked polyubiquitin chains. Full-length Nedd4-2 catalyzes free I-polyubiquitin chain assembly by hyperbolic Michaelis-Menten kinetics with respect to Ubc5B∼ubiquitin thioester concentration ( = 44 ± 6 nm; = 0.
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