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Beyer, I.

Publications and source records attributed to Beyer, I..

2 recordsLinked to original sources

Bio-inspired augmented reality: an interactive, digital twin of C. elegans

This work presents a digital twin of the nematode Caenorhabditis elegans (C. elegans), an organism whose biology has been extensively studied. The digital twin can emulate neuronal activity and the corresponding muscle activity, and performs basic locomotion movement. The underlying mathematical model of C. elegans can be realized directly as an electronic circuit and is additionally implemented as a ready-to-use simulation in software. We implemented the digital twin in augmented reality (AR) as a novel format that extends the content of a traditional paper with an interactive visualization in the real world. The figures in the paper are the anchor point for the AR that can be accessed by the readers via an open-source app, which is freely available for tablets, phones, and AR glasses. This enables immersive experiences of the three-dimensional visualization in the real world from a perspective chosen by the reader, supplementing the traditional, flat figure layout of the paper. For researchers, the digital twin further provides a useful tool that is highly relevant and versatile for future developments. At the same time, its manifold possibilities for scientific outreach also aim at making the topic more engaging for a broader audience.

bioengineering↗

An uncommon phosphorylation mode regulates the activity and protein-interactions of N-acetylglucosamine kinase

While the function of protein phosphorylation in eukaryotic cell signaling is well established, the role of a closely related modification, protein pyrophosphorylation, is just starting to surface. A recent study has identified several targets of endogenous protein pyrophosphorylation in mammalian cell lines, including N-acetylglucosamine kinase (NAGK). Here, a detailed functional analysis of NAGK phosphorylation and pyrophosphorylation on serine 76 (S76) has been conducted. This analysis was enabled by using amber codon suppression to obtain phosphorylated pS76-NAGK, which was subsequently converted to site-specifically pyrophosphorylated NAGK (ppS76-NAGK) with a phosphorimidazolide regent. A significant reduction in GlcNAc kinase activity was observed upon phosphorylation, and near-complete inactivation upon pyrophosphorylation. The formation of ppS76-NAGK proceeded via an ATP-dependent autocatalytic process, and once formed, ppS76-NAGK displayed notable stability towards dephosphorylation in mammalian cell lysates. Proteomic examination unveiled a distinct set of protein-protein interactions for ppS76-NAGK, suggesting an alternative function, independent of its kinase activity. Overall, a significant regulatory role of pyrophosphorylation on NAGK activity was uncovered, providing a strong incentive to investigate the influence of this unusual phosphorylation mode on other kinases.

biochemistry↗