UWB Localization in a Smart Factory: Augmentation Methods and Experimental Assessment

The advent of the fourth industrial revolution (Industry 4.0) aims at increasing automation and efficiency in manufacturing processes by the adoption of information and communication technologies. Several of the proposed solutions rely on precise localization of material, equipment, or operators. This article investigates the employment of ultrawideband (UWB) real-time location systems (RTLS) in a factory environment and proposes an augmentation technique to mitigate the impairments that arise in such a complex scenario. A Bayesian filtering method is developed to jointly track the motion dynamics and the time-varying visibility conditions of the UWB antennas, with particle-based implementation to deal with the nonlinearity of the UWB measurements. Laboratory tests and industrial experiments are carried out to evaluate the performance of three commercial off-the-shelf UWB technologies: Decawave, Sewio, and Ubisense. The experimental data are then used to calibrate and test the developed filtering technique, showing that it is possible to significantly reduce the positioning error originating from dense multipath and NLOS effects by jointly tracking the target dynamics and visibility conditions

Insulin binding to its receptor induces a conformational change in the receptor C-terminus.

International audienceAntibodies against peptides corresponding to sequences in the C-terminus of the insulin receptor beta-subunit were used to approach the putative role of this receptor domain in signal generation. Two sequences were chosen and correspond to peptide C1, comprising amino acids 1309-1326, and peptide C2, comprising amino acids 1294-1317. The two antibodies produced distinct immunoprecipitation patterns as a function of the insulin receptor form and recognized changes in the insulin receptor molecule induced by ligand binding and autophosphorylation. Both antipeptides, anti-C1 and anti-C2, showed an important decrease in their recognition capacity for the receptor occupied by insulin when compared to the empty receptor. Further, anti-C1 had a lower affinity for the phosphorylated receptor compared to the unphosphorylated receptor and failed to recognize a fraction of the phosphoreceptor population. In contrast, anti-C2 had similar affinities for the phosphorylated and unphosphorylated receptors but was unable to interact with part of the unphosphorylated receptors. Finally, using immunoblotting of the receptor to analyze the denatured molecules, we showed that the phosphorylation-induced changes detected by anti-C1 are retained, suggesting that they are likely not of a conformational nature. In contrast, the insulin-induced changes in the receptor molecule disappear with receptor denaturation which points to their reversible nature. We conclude from these data that (i) antipeptides against the receptor C-terminal sequence are able to distinguish between phosphorylated and unphosphorylated receptor forms and (ii) binding of insulin to its receptor leads to a reversible, phosphorylation-independent, and possibly conformational change at the level of the receptor C-terminal domain

Bioresponsive pseudoGlucosinolates (psGSLs) release Isothiocyanates (ITCs) in the Presence of Nitroreductases

Glucosinolates (GSLs) are secondary metabolites produced as part of an herbivore defence system in plants of the order Brassicales. GSLs release isothiocyanates (ITCs) upon activation by the myrosinase. Beyond their herbivore feeding deterrent properties, these ITCs have multiple interesting bioactivities. However, their release is limited by the presence of myrosinase. Here, we report the concept of pseudoglucosinolates (psGSLs) hijacking the natural release mechanism of GSLs for the release of ITCs and adapting it to nitroreductase as triggering enzymes. We provide the proof-of-concept for nitroreductase-responsive psGSLs and demonstrate their potential for peptide labelling and ITC-prodrug approaches