Joseph Thibault

Background: Artificial intelligence (AI) offers exciting possibilities; however, AI is a double-edged sword. The adoption of this technology offers many benefits but also presents risks to academic integrity and appropriately prepared graduates. Many of today's nurse educators are from generations that are unlikely to possess an understanding of AI. This article provides fundamental knowledge needed to understand the current state of AI in nursing and offers recommendations to nurse educators on ways to responsibly incorporate AI technologies into nursing curricula. Method: AI literature from PubMed, CINAHL, and Google Scholar was reviewed and synthesized. Results: Definitions, explanations, and applications to nursing education are outlined. Recommendations are made for AI implementation, along with ideas to avoid potential AI-enabled plagiarism and academic dishonesty. Conclusion: As professionals, nurse educators should understand the basics of AI and be able to judge the appropriateness of integration and also recognize opportunities to embrace future application. [ J Nurs Educ . 2023;62(12):716–720.]

Polysialic acid, a homopolymer of alpha2,8-linked sialic acid expressed on the neural cell adhesion molecule (NCAM), is thought to play critical roles in neural development. Two highly homologous polysialyltransferases, ST8Sia II and ST8Sia IV, which belong to the sialyltransferase gene family, synthesize polysialic acid on NCAM. By contrast, ST8Sia III, which is moderately homologous to ST8Sia II and ST8Sia IV, adds oligosialic acid to itself but very inefficiently to NCAM. Here, we report domains of polysialyltransferases required for NCAM recognition and polysialylation by generating chimeric enzymes between ST8Sia IV and ST8Sia III or ST8Sia II. We first determined the catalytic domain of ST8Sia IV by deletion mutants. To identify domains responsible for NCAM polysialylation, different segments of the ST8Sia IV catalytic domain, identified by the deletion experiments, were replaced with corresponding segments of ST8Sia II and ST8Sia III. We found that larger polysialic acid was formed on the enzymes themselves (autopolysialylation) when chimeric enzymes contained the carboxyl-terminal region of ST8Sia IV. However, chimeric enzymes that contain only the carboxyl-terminal segment of ST8Sia IV and the amino-terminal segment of ST8Sia III showed very weak activity toward NCAM, even though they had strong activity in polysialylating themselves. In fact, chimeric enzymes containing the amino-terminal portion of ST8Sia IV fused to downstream sequences of ST8Sia III inhibited NCAM polysialylation in vitro, although they did not polysialylate NCAM. These results suggest that in polysialyltransferases the NCAM recognition domain is distinct from the polysialylation domain and that some chimeric enzymes may act as a dominant negative enzyme for NCAM polysialylation.