A Framework to Redesign Nursing Undergraduate Curriculum: One Program's Journey.

Background: Transitioning to the updated version of The Essentials has been a significant shift in nursing education, aimed at reversing national trends of declining new graduate competence. This article describes the curriculum revision journey undertaken by one program to align with the updated version of The Essentials.

Method: The university's Center for Teaching Excellence guided the redesign process using a structured, faculty-led, data-informed approach.

Severe Acute Respiratory Syndrome Coronavirus 2 Omicron Subvariant Neutralization Following a Primary Vaccine Series of NVX-CoV2373 and BNT162b2 Monovalent Booster Vaccine.

We evaluated the immunologic response to a novel vaccine regimen that included 2 doses of NVX-CoV2373 (Novavax) followed by 1 dose of BNT162b2 (Pfizer-BioNTech) monovalent booster vaccine. A durable neutralizing antibody response to Omicron BA.4/BA.

Characterization and structural study of a novel β-N-acetylgalactosaminidase from Niabella aurantiaca.

We report here the identification, characterization and three-dimensional (3D) structure determination of NaNga, a newly identified β-N-acetylgalactosaminidase from the Gram-negative soil bacterium Niabella aurantiaca DSM 17617. When recombinantly expressed in Escherichia coli, the enzyme selectively cleaved 4-nitrophenyl-N-acetyl-β-d-galactosamine (pNP-β-d-GalpNAc). The X-ray crystal structure of the protein was refined to 2.

Glucuronan lyases from family PL7 use a Tyr/Tyr β-elimination catalytic mechanism for glucuronan breakdown.

TpPL7A and TpPL7B, members of CAZy family PL7, act as β-glucuronan lyases. TpPL7A diverges by lacking the catalytic histidine, identified as the Brønsted base in PL7 alginate lyases. Our research, including TpPL7A's crystal structure, and mutagenesis studies, reveals a shared -β-elimination mechanism with a single tyrosine serving as both base and acid catalyst.

Three alginate lyases provide a new gut isolate with the ability to grow on alginate.

Humans consume alginate in the form of seaweed, food hydrocolloids, and encapsulations, making the digestion of this mannuronic acid (M) and guluronic acid (G) polymer of key interest for human health. To increase knowledge on alginate degradation in the gut, a gene catalog from human feces was mined for potential alginate lyases (ALs). The predicted ALs were present in nine species of the Bacteroidetes phylum, of which two required supplementation of an -acting AL, expected to mimic cross-feeding in the gut.