Innovación pedagógica para el aprendizaje de la Administración en la Facultad de Cs. Económicas y Sociales de la UNMDP. Prácticas pre profesionales en organizaciones de la sociedad civil y de la economía solidaria

Desde el año 2005 se implementaron en la Facultad de Ciencias Económicas y Sociales de la UNMDP, Prácticas Profesionales Comunitarias como requisito curricular obligatorio de sus Planes de Estudios; con 30 hs. de intervención por cada estudiante acompañadas por un Seminario de conceptualización y su correspondiente evaluación. Su implementación es regida por la OCA Nº 1211/09. Desde el año 2008, han recorrido el Seminario y realizado la Práctica más de 300 estudiantes que se han involucrado con cerca de 373 instituciones (ONG, Cooperativas, Sociedades de Fomento, entre otros) concretando al menos 27.570 horas de Prácticas con destacados resultados, no solo en la dimensión del aprendizaje sino también en la intervención comunitaria. En esta oportunidad analizaremos las conclusiones de los estudiantes, en particular de la Lic. en Administración, a la luz de las modificaciones metodológicas que se realizaron en el programa del Seminario durante el período 2013-2014.Fil: Huergo, María Consuelo. Universidad Nacional de Mar del Plata. Facultad de Ciencias Económicas y Sociales; Argentina.Fil: Morasso, M. C. Universidad Nacional de Mar del Plata. Facultad de Ciencias Económicas y Sociales; Argentina

bilateral robot therapy based on haptics and reinforcement learning feasibility study of a new concept for treatment of patients after stroke

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A dominant mutation etiologic for human tricho-dento-osseous syndrome impairs the ability of DLX3 to downregulate ΔNp63α.

The homeodomain transcription factors play crucial roles in many developmental processes ranging from organization of the body plan to differentiation of individual tissues. The homeodomain protein Distal-less-3 (DLX3) has an essential role in epidermal stratification and development of ectodermal appendages, placenta and bones. A four-nucleotide deletion in the human DLX3 gene is etiologic for the human hereditary tricho-dento-osseous (TDO) ectodermal dysplasia, a dominant syndrome characterized by abnormalities in hair, nails, teeth, and bones. We have previously demonstrated that DLX3 gene expression induces degradation of ΔNp63α, a specific product of the TP63 gene, a master regulator of multi-layered epithelia. Here we show that the DLX3(TDO) mutant protein is unable to promote ΔNp63α protein degradation and impairs the expression of cell cycle regulatory proteins and skin differentiation markers. However, we found that in cell expressing equal amounts of mutant and wild-type DLX3, ΔNp63α protein level is efficiently regulated implying that genetic heterozygosity at the DLX3 locus protects TDO patients from developing severe p63-associated skin defects

Immobilization of γ-Glutamyl Transpeptidase from Equine Kidney for the Synthesis of Kokumi Compounds

γ-Glutamyl transpeptidase from equine kidney (ekGGT, E.C. 2.3.2.2) is an intrinsic membrane enzyme which transfers the γ-glutamyl moiety of glutathione to amino acids and peptides, thus producing γ-glutamyl derivatives. An immobilization study of ekGGT was carried out with the aim to develop a robust biocatalyst for the synthesis of γ-glutamyl amino acids which are known as kokumi compounds. Heterofunctional octyl-glyoxyl-agarose resulted in a high immobilization yield and activity recovery (93 % and 88 %, respectively). Immobilized ekGGT retained more than 95 % activity under reaction conditions (Tris-HCl, pH 9, 0.05 M) after 6 days, whereas the residual activity after 6 reaction cycles (18 days) was 85 %. The synthesis of γ-glutamylmethionine catalyzed by octyl-glyoxyl-agarose-ekGGT afforded the product in 42 % yield (101 mg). The immobilized ekGGT was characterized by Raman spectroscopy. The immobilization protocol developed for ekGGT could be of general applicability to membrane proteins

Towards a Universal Method for the Stable and Clean Functionalization of Inert Perfluoropolymer Nanoparticles : Exploiting Photopolymerizable Amphiphilic Diacetylenes

Highly fluorinated materials are being widely investigated due to a number of peculiar properties, which are potentially useful for various applications, including use as lubricants, anti-adhesive films, and substitutes for biological fluids for biomedical utilization. However, at present such potential is still poorly exploited. One of the major drawbacks that hampers the rapid development of nanoscale fluoro-hybrid devices is the remarkable inertness of perfluoropolymeric materials that lack reactive functionalities, as they do not offer any functional groups that can be employed to covalently anchor organic molecules on their surface. In this paper, a convenient method for the stable biofunctionalization of strongly unreactive perfluoropolymer nanoparticles (PnPs) is reported. PnPs are easily coated with newly synthesized asymmetric diacetylenic monomer compounds (ADMs), thanks to PnP's high propensity to interact with hydrophobic moieties. Once monomerically adsorbed onto PnPs, such suitably designed ADMs enable the formation of a robust polymeric shell around the perfluoroelastomer core via a clean UV-promoted localized photopolymerization. Given the peculiar optical characteristics of PnPs, the coating of the particles can be monitored step by step using light scattering, which also allows estimation of the fraction of reacted monomers by competitive adsorption with smaller particles. The potential of this method for the biofunctionalization of PnPs is demonstrated with representative proteins and carbohydrates. Among them, the extension to avidin-biotin technology may broaden the scope and applicability of this strategy to potentially a large number of molecules of biomedical interest. Making the unreactive reactive: A smart method for the biofunctionalization of strongly inert perfluoropolymer nanoparticles (PnPs) is presented, using a stable coating with novel diacetylenic compounds followed by clean UV photopolymerization to generate reactive functionalities on the PnP surface. This method further allows fine tuning of the amount of conjugated biomolecules, which can be sensitively and straightforwardly quantified

Immobilization of γ-Glutamyl Transpeptidase from Equine Kidney for the Synthesis of kokumi Compounds

\u3b3-Glutamyl transpeptidase from equine kidney (ekGGT, E.C. 2.3.2.2) is an intrinsic membrane enzyme which transfers the \u3b3-glutamyl moiety of glutathione to amino acids and peptides, thus producing \u3b3-glutamyl derivatives. An immobilization study of ekGGT was carried out with the aim to develop a robust biocatalyst for the synthesis of \u3b3-glutamyl amino acids which are known as kokumi compounds. Heterofunctional octyl-glyoxyl-agarose resulted in a high immobilization yield and activity recovery (93 % and 88 %, respectively). Immobilized ekGGT retained more than 95 % activity under reaction conditions (Tris-HCl, pH 9, 0.05 M) after 6 days, whereas the residual activity after 6 reaction cycles (18 days) was 85 %. The synthesis of \u3b3-glutamylmethionine catalyzed by octyl-glyoxyl-agarose-ekGGT afforded the product in 42 % yield (101 mg). The immobilized ekGGT was characterized by Raman spectroscopy. The immobilization protocol developed for ekGGT could be of general applicability to membrane proteins

Attentive Learning of Sequential Handwriting Movements: A Neural Network Model

Defense Advanced research Projects Agency and the Office of Naval Research (N00014-95-1-0409, N00014-92-J-1309); National Science Foundation (IRI-97-20333); National Institutes of Health (I-R29-DC02952-01)