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[Tadeo Lentz]

SmartEnabled by default, AMATI VIOLA's Smart fingering mode intelligently chooses the most realistic fingering for the notes played. As an example, when playing a chromatic passage, the Smart mode chooses to play the notes on the same string when possible, just as a real violaist would do, yielding realistic results. In contrast, when playing a motif moving around different strings in the same area of the fingerboard, fingering on different strings is preferred intelligently and realistically.

Yummy Bakery's pancakes are "hot" and end up on the shelves of virtually every major retail chain in Belgium. The secret behind this success? Using the authentic ingredients and preparation method on a baking plate. A recipe that perfectly combines with digitalization as CTRL Engineering successfully demonstrated. Besides 7 to 8% raw material savings, the automation of dough dosing with control technology from Beckhoff also helped provide data for ongoing process optimization.

Annie Alderweireldt's life in Bruges didn't always revolve around pancakes. But when her pregnancy forced her to stop working in 1984, they did give her an outlet. "She started experimenting in the kitchen until she had the recipe for the perfect pancake, using the neighbors as guinea pigs," says her daughter Sara Geldhof, who runs the business with her brother Tom today. "She then went to the local bakers and butchers in Dudzele near Bruges to market her pancakes." A snowball effect, because before she knew it, they were on the shelves of convenience stores and the big supermarket chains also discovered her. "Mom's arm pouring the dough onto the baking plate over and over again in the same fluid motion with a ladle ... that was actually our first machine. But at some point that was no longer feasible. So we built a carousel that worked semi-automatically at least," Sara Geldhof recalls.

In 1995, they had the opportunity to purchase a piece of land in an industrial park in Bruges. A first industrial pancake machine went up and running there. But authenticity was still as hard-won as ever. Sara Geldhof explains: "We achieved the typical taste by opting to prepare via griddle. Compared to using infrared technology, the pancake is then seared immediately, so the dough inside stays soft and creamy. In addition, only natural ingredients enter the recipe, no preservatives or colorings, just pure nature." A philosophy that Yummy Bakery also applies to their new products. For example, they already have organic pancakes in the product range and are working behind the scenes on the first vegan pancakes. "And will continue do so until the taste is completely right," Sara Geldhof says. What started with the industrial production of traditional pancakes from Bruges, now also serves current trends, for example with motif pancakes for Halloween.

The acquisition of a second production hall followed eight years ago. Maybe a happy twist of fate, because only a year and a half ago, Yummy Bakery could use the space to increase its production capacity from 10,000 to 22,500 pancakes per hour. And still the growth curve is going up: last year, sales increased 25%. "We couldn't ignore automation and digitalization anymore if we wanted to keep up with our growth. We are all about fresh products, so everything we produce goes straight out the door. In the past, you could manage that with a good team that had all the necessary know-how in their heads. Today, though, you have to secure that knowledge using technology. The goal is to create a complete digital flow that improves our process stability and minimizes repetitive work for our employees." To achieve this, Yummy Bakery partnered with CTRL Engineering who have a background in automotive. "In automotive production lines, the goal is zero errors. Because profit margins are limited, the entire process is completely purged of inaccuracies. We want to introduce these principles to other sectors as well. Together we look for ways how our customers' processes can be improved to produce more with the same machines and people. What we offer is efficiency as a service," Managing Director Pieter Meseure summarizes the mission of the company.

Although Yummy Bakery and CTRL Engineering both wanted to set the bar high, they decided to start small. "We started looking for the low-hanging fruit. Something that would give us immediate profit, so that we had more resources to take the next steps in digitalization," says Pieter Meseure. The lack of stability in the weight of the pancakes was the first item on the agenda. Mathieu Dutr, Director of Innovation and Business Development at CTRL Engineering, explained: "We were wondering, if we can save 10% overweight, what impact would that have on the bottom line? A calculation pointed to an ROI of less than a year. That was a no-brainer!" Until then, dosing had been done pneumatically, that is, depending on the recipe, operators would have to adjust the compressed air flow rate manually. As a result, a pack of pancakes with a nominal weight of 500 g could weigh between 500 g and 560 g. CTRL Engineering used virtual engineering to see how they could best address the problem and what hardware would suit the specifications they found.

In terms of digitalization,this is just the tip of the iceberg for Yummy Bakery. The next step? "Automating quality inspection at the end of the packaging line by adding vision capabilities. We are just waiting for the OCR functionality to be introduced. Behind the scenes, Beckhoff is already training a machine learning model to recognize even more fonts. The potential profits from that should in turn serve to eventually install a second production line in the new building, adding another 50% of capacity. Then we can transfer all production facilities from the first building to here and repeat the process until we achieve one perfect, digital flow," Pieter Meseure concludes with an outlook into the future.

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The receptor tyrosine kinase MET is essential for embryonic development of vertebrates and the healing of skin wounds in adults. In addition MET signaling is subverted during infection by the facultative intracellular pathogen Listeria monocytogenes, which induces its own uptake into non-phagocytic cells upon MET activation. The surface associated protein InlB functions as bacterial MET agonist by specifically binding to the MET extracellular domain. Structurally, InlB does not resemble the endogenous MET ligand hepatocyte growth factor/scatter factor (HGF/SF). However, the cellular response to MET stimulation by InlB is very similar to that elicited by HGF/SF.

We try to understand the mechanism of ligand-induced MET activation at the molecular level. To this end we solved crystal structures of the complex formed by InlB and the MET ectodomain. (Niemann et al. 2007). The structure revealed that the binding site for InlB does not overlap with that previously described for the β-chain of HGF/SF. MET dimerization is brought about by a small, low-affinity contact formed by the back-sides of two InlB molecules in the 2:2 complex. (Ferraris et al. 2010). As discussed in a recent review, this is reminiscent of MET activation by the HGF/SF splice variant NK1 (Niemann 2013). In cooperation with Prof. Heilemann (Frankfurt) we now use single-molecule fluorescence microscopy to study InlB mediated MET dimerization on cells. (Dietz et al. 2013).

InlB is a multi-domain protein. MET only interacts with the N-terminal internalin domain of InlB, but the other InlB domains contribute to full activation of the MET receptor. We investigate the function of the central domain of InlB called B-repeat. We solved its crystal structure revealing an ubiquitin-like β-grasp fold and we showed that the B-repeat is required for InlB to induce cell motility. (Ebbes et al. 2011). The InlB B-repeat probably binds to a host cell receptor other than MET. Currently, we try to identify this receptor.

MET is a target structure of medical importance due to its role in tissue regeneration. MET agonists could serve as protein therapeutics, e.g. to stimulate wound healing. The structure of the 2:2 InlB/MET signaling active complex, allowed the rational design of a potent MET agonist. (Ferraris et al. 2010; Kolditz et al. 2013; bottom figure).

Resembling a macromolecular syringe, type III secretion systems are multi-protein complexes used by various Gram-negative pathogens to inject effector proteins directly into the host cell cytoplasm. Hydrophobic so-called translocator proteins form the necessary pore in the host cell membrane. Within in the bacterial cytosol, these translocators bind to a chaperone, which itself is not exported. In contrast to classic chaperones, T3S chaperones do not bind or hydrolyze nucleotides.

We solved the first crystal structure of a T3S translocator chaperone, the Yersinia enterocolitica protein SycD. ( Bttner et al. 2008). SycD forms a curved structure consisting of three tetratrico peptide repeats (TPRs). A second structure of SycD in complex with a chaperone-binding peptide derived from the translocator protein YopD shows that the concave face of the curved TPR fold serves as binding site for YopD. ( Schreiner et al. 2012).

In addition to the translocators YopB and YopD, SycD binds to several other T3S proteins enabling it to exert regulatory functions. Currently, we investigate the interaction of SycD with several Y. enterocolitica T3S proteins in vitro. in vitro.

The gastric pathogen H. pylori employs a type IV secretion system (T4SS) to inject the oncogenic effector protein CagA into the stomach epithelium of its human host. The T4SS protein CagL localizes to the T4SS pilus and is essential for injection of CagA into host cells. CagL harbors a RGD motif that probably mediates binding to host cell integrins.

We solved the crystal structure of H. pylori CagL. (Barden et al. 2013). An elongated three-helix bundle forms the structural core of CagL, to which the N-terminal helix is associated only loosely. Structure comparisons suggest that CagL is a H. pylori specific protein. The RGD motif is exposed at the protein surface and thus accessible for interaction with a receptor molecule. In contrast to previously characterized RGD motifs, the RGD motif of CagL is not located in an extended or flexible loop structure but in the middle of a long helix.

We now investigate the molecular basis of the interaction between CagL and host cell receptors.

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