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Open access

Shi-Fan Han, Rui-Fang Zhu, Jia Xue, Qi Yu, Yan-Bing Su and Xiu-Juan Wang


This study proposes the establishment of a knowledge-system ontology in the nursing field. It uses advanced data mining techniques, digital publishing technologies, and new media concepts to comprehensively integrate and deepen nursing knowledge and to aggregate sources of knowledge in specialized technical fields. This study applies all forms of media and transmission channels, such as personal computers and mobile devices, to establish a knowledge-transmission system that provides knowledge services such as knowledge search, update retrieval, evaluation, questions and answers (Q&As), online viewing, information subscription, expert services, push notifications, review forums, and online learning. In doing so, this study creates an authoritative and foundational knowledge service engine for the nursing field, which provides convenient, flexible, and comprehensive knowledge services to members of the nursing industry in a digital format.

Open access

Lu-Lu Wang, Shi-Ying Lu, Pan Hu, Bao-Quan Fu, Yan-Song Li, Fei-Fei Zhai, Dan-Di Ju, Shi-Jun Zhang, Bing Su, Yu Zhou, Zeng-Shan Liu and Hong-Lin Ren


Introduction: Peroxiredoxin 6 (Prdx6) is a bifunctional protein with glutathione peroxidase activity and phospholipase A2 activity. Previous studies have shown a significant positive correlation between the intracellular survival ability of Brucella and Prdx6. Here, the Prdx6 enzyme with a single activity was constructed to facilitate study of the relationship between the single function of Prdx6 and Brucella infection.

Material and Methods: The target open reading frame (ORF) DNAs of Prdx6 with a single active centre were prepared using gene splicing by overlap extension PCR (SOE-PCR), and the recombinant eukaryotic expression plasmids inserted by Prdx6 with the single activity centre were constructed and transfected into murine Raw264.7 macrophages. The glutathione peroxidase activity and phospholipase A2 activity of the constructed Prdx6 were examined.

Results: The core centres (Ser32 and Cys47) of Prdx6 were successfully mutated by changing the 94th nucleotide from T to G and the 140th nucleotide from G to C in the two enzyme activity cores, respectively. The constructed recombinant plasmids of Prdx6 with the single active centre were transfected into murine macrophages showing the expected single functional enzyme activity, which MJ33 or mercaptosuccinate inhibitors were able to inhibit.

Conclusion: The constructed mutants of Prdx6 with the single activity cores will be a benefit to further study of the biological function of Prdx6 with different enzyme activity.