Framework For The Rapid Development And Deployment Of Customized Industrial Robotic Applications

Automation and industrial robots enable today's enterprises to increase productivity. Due to current challenges, such as a shortage of skilled workers, the trend is toward using industrial robots more and more in high-mix low-volume production. For this, enterprises must be able to develop and deploy robotic applications for various products, variants, and tasks easily and quickly. In previous works, we demonstrated the increased flexibility and efficiency of robot programming via a skills-based software framework. In this paper, we expand this framework by considering the overall development and deployment procedure of robotic applications. In addition to modular programming, we address the development of the necessary hardware for the robotic application. Here, we focus on the design of the gripper system. As an exemplary use case we present the handling and testing of variant-rich electronic products. Finally, based on the introduced framework, we show our first implementation results to realize this use case

Identification of the variant Ala335Val of MED25 as responsible for CMT2B2: molecular data, functional studies of the SH3 recognition motif and correlation between wild-type MED25 and PMP22 RNA levels in CMT1A animal models

Charcot-Marie-Tooth (CMT) disease is a clinically and genetically heterogeneous disorder. All mendelian patterns of inheritance have been described. We identified a homozygous p.A335V mutation in the MED25 gene in an extended Costa Rican family with autosomal recessively inherited Charcot-Marie-Tooth neuropathy linked to the CMT2B2 locus in chromosome 19q13.3. MED25, also known as ARC92 and ACID1, is a subunit of the human activator-recruited cofactor (ARC), a family of large transcriptional coactivator complexes related to the yeast Mediator. MED25 was identified by virtue of functional association with the activator domains of multiple cellular and viral transcriptional activators. Its exact physiological function in transcriptional regulation remains obscure. The CMT2B2-associated missense amino acid substitution p.A335V is located in a proline-rich region with high affinity for SH3 domains of the Abelson type. The mutation causes a decrease in binding specificity leading to the recognition of a broader range of SH3 domain proteins. Furthermore, Med25 is coordinately expressed with Pmp22 gene dosage and expression in transgenic mice and rats. These results suggest a potential role of this protein in the molecular etiology of CMT2B2 and suggest a potential, more general role of MED25 in gene dosage sensitive peripheral neuropathy pathogenesis