Towards a collaborative experience to generate knowledge: Use of gamification in robotics for Good Agricultural Practices

Currently gamification strategies are implemented in the most diverse fields. This paper discusses the design of gamification environment on a collaborative wiki on good agricultural practices. The aim of the project is to present a gamification design is complemented by a robotic interface, aimed at increasing customizing the experience from a cooperative community context. The robot interface also presents the possibility of containing a living organism, linked to the actions of the wiki.Laboratorio de Investigación y Formación en Informática Avanzad

Towards a collaborative experience to generate knowledge: Use of gamification in robotics for Good Agricultural Practices

Currently gamification strategies are implemented in the most diverse fields. This paper discusses the design of gamification environment on a collaborative wiki on good agricultural practices. The aim of the project is to present a gamification design is complemented by a robotic interface, aimed at increasing customizing the experience from a cooperative community context. The robot interface also presents the possibility of containing a living organism, linked to the actions of the wiki.Laboratorio de Investigación y Formación en Informática Avanzad

Towards a collaborative experience to generate knowledge: Use of gamification in robotics for Good Agricultural Practices

Currently gamification strategies are implemented in the most diverse fields. This paper discusses the design of gamification environment on a collaborative wiki on good agricultural practices. The aim of the project is to present a gamification design is complemented by a robotic interface, aimed at increasing customizing the experience from a cooperative community context. The robot interface also presents the possibility of containing a living organism, linked to the actions of the wiki.Laboratorio de Investigación y Formación en Informática Avanzad

Disulfide bond reduction and exchange in C4 domain of von Willebrand factor undermines platelet binding

Background The von Willebrand factor (VWF) is a key player in regulating hemostasis through adhesion of platelets to sites of vascular injury. It is a large, multi-domain, mechano-sensitive protein that is stabilized by a net of disulfide bridges. Binding to platelet integrin is achieved by the VWF-C4 domain, which exhibits a fixed fold, even under conditions of severe mechanical stress, but only if critical internal disulfide bonds are closed. Objective To determine the oxidation state of disulfide bridges in the C4 domain of VWF and implications for VWF’s platelet binding function. Methods We combined classical molecular dynamics and quantum mechanical simulations, mass spectrometry, site-directed mutagenesis, and platelet binding assays. Results We show that 2 disulfide bonds in the VWF-C4 domain, namely the 2 major force-bearing ones, are partially reduced in human blood. Reduction leads to pronounced conformational changes within C4 that considerably affect the accessibility of the integrin-binding motif, and thereby impair integrin-mediated platelet binding. We also reveal that reduced species in the C4 domain undergo specific thiol/disulfide exchanges with the remaining disulfide bridges, in a process in which mechanical force may increase the proximity of specific reactant cysteines, further trapping C4 in a state of low integrin-binding propensity. We identify a multitude of redox states in all 6 VWF-C domains, suggesting disulfide bond reduction and swapping to be a general theme. Conclusions Our data suggests a mechanism in which disulfide bonds dynamically swap cysteine partners and control the interaction of VWF with integrin and potentially other partners, thereby critically influencing its hemostatic function

Conservando tiburones con ciencia ciudadana

El proyecto se gesta en colaboración de los proyectos de investigación y preservación de condrictios “Análisis poblacional y migratorio del cazón (Galeorhinus galeus) en el Atlántico Sudoccidental” y “Filogeografía aplicada a la conservación del gatopardo (Notorynchus pectorosus, Chondrichthyes) en el Mar Argentino” de la Facultad de Ciencias Naturales y Museo de la UNLP.Facultad de Informátic

Conservando tiburones con ciencia ciudadana

El proyecto se gesta en colaboración de los proyectos de investigación y preservación de condrictios “Análisis poblacional y migratorio del cazón (Galeorhinus galeus) en el Atlántico Sudoccidental” y “Filogeografía aplicada a la conservación del gatopardo (Notorynchus pectorosus, Chondrichthyes) en el Mar Argentino” de la Facultad de Ciencias Naturales y Museo de la UNLP.Facultad de Informátic

Conservando tiburones con ciencia ciudadana

El proyecto se gesta en colaboración de los proyectos de investigación y preservación de condrictios “Análisis poblacional y migratorio del cazón (Galeorhinus galeus) en el Atlántico Sudoccidental” y “Filogeografía aplicada a la conservación del gatopardo (Notorynchus pectorosus, Chondrichthyes) en el Mar Argentino” de la Facultad de Ciencias Naturales y Museo de la UNLP.Facultad de Informátic

Autoregulation of von Willebrand factor function by a disulfide bond switch

Force-dependent binding of platelet glycoprotein Ib (GPIb) receptors to plasma von Willebrand factor (VWF) plays a key role in hemostasis and thrombosis. Previous studies have suggested that VWF activation requires force-induced exposure of the GPIb binding site in the A1 domain that is autoinhibited by the neighboring A2 domain. However, the biochemical basis of this “mechanopresentation” remains elusive. From a combination of protein chemical, biophysical, and functional studies, we find that the autoinhibition is controlled by the redox state of an unusual disulfide bond near the carboxyl terminus of the A2 domain that links adjacent cysteine residues to form an eight-membered ring. Only when the bond is cleaved does the A2 domain bind to the A1 domain and block platelet GPIb binding. Molecular dynamics simulations indicate that cleavage of the disulfide bond modifies the structure and molecular stresses of the A2 domain in a long-range allosteric manner, which provides a structural explanation for redox control of the autoinhibition. Significantly, the A2 disulfide bond is cleaved in ~75% of VWF subunits in healthy human donor plasma but in just ~25% of plasma VWF subunits from heart failure patients who have received extracorporeal membrane oxygenation support. This suggests that the majority of plasma VWF binding sites for platelet GPIb are autoinhibited in healthy donors but are mostly available in heart failure patients. These findings demonstrate that a disulfide bond switch regulates mechanopresentation of VWF.: This study was supported by grants from the National Health and Medical Research Council of Australia (P.J.H.), Royal College of Pathologists Foundation Kanematsu/Novo Nordisk Research Award (F.P. and L.J.), Diabetes Australia Research Trust grant G179720 and Sydney Medical School Early-Career Researcher Kickstart Grant (L.J.), National Heart Foundation of Australia Postdoctoral Fellowship (101285) (L.J.) and British Heart Foundation Intermediate Basic Science Research Fellowship (FS/11/51/28920) (B.M.L.), Deutsche Forschungsgemeinschaft (research unit FOR 1543 to C.A.-S., C.B., and F.G.), the Center for Modelling and Simulation in the Biosciences postdoctoral program of the Heidelberg University (A.B.), and the Klaus Tschira Foundation (F.G.). B.L. was supported by the Dutch Thrombosis Foundation through grant number 2016-03.

Betalain, Acid Ascorbic, Phenolic Contents and Antioxidant Properties of Purple, Red, Yellow and White Cactus Pears

Commercialization of cactus pears based on their antioxidant properties can generate competitive advantages, and these can turn into business opportunities and the development of new products and a high-value ingredient for the food industry. This work evaluated the antioxidant activities (1,1-diphenyl-2-picrylhydrazyl radical-scavenging, protection against oxidation of a β-carotene-linoleic acid emulsion, and iron (II) chelation), the content of total phenolic compounds, ascorbic acid, betacyanin, betaxanthin and the stability of betacyanin pigments in presence of Cu (II)-dependent hydroxyl radicals (OH•), in 18 cultivars of purple, red, yellow and white cactus pear from six Mexican states. Our results indicated that the antiradical activities from yellow and white cactus pear cultivars were not significantly different (p < 0.05) and were lower than the average antiradical activities in red and purple cultivars. The red cactus pear from the state of Zacatecas showed the highest antioxidant activity. The free radical scavenging activity for red cactus pears was significantly correlated (p < 0.05) to the concentration of total phenolic compounds (R2 = 0.90) and ascorbic acid (R2 = 0.86). All 18 cultivars of cactus pears studied showed significant chelating activity of ferrous ions. The red and purple cactus pears showed a great stability when exposed to OH•

The Promigratory Activity of the Matricellular Protein Galectin-3 Depends on the Activation of PI-3 Kinase

Expression of galectin-3 is associated with sarcoma progression, invasion and metastasis. Here we determined the role of extracellular galectin-3 on migration of sarcoma cells on laminin-111. Cell lines from methylcholanthrene-induced sarcomas from both wild type and galectin-3−/− mice were established. Despite the presence of similar levels of laminin-binding integrins on the cell surface, galectin-3−/− sarcoma cells were more adherent and less migratory than galectin-3+/+ sarcoma cells on laminin-111. When galectin-3 was transiently expressed in galectin-3−/− sarcoma cells, it inhibited cell adhesion and stimulated the migratory response to laminin in a carbohydrate-dependent manner. Extracellular galectin-3 led to the recruitment of SHP-2 phosphatase to focal adhesion plaques, followed by a decrease in the amount of phosphorylated FAK and phospho-paxillin in the lamellipodia of migrating cells. The promigratory activity of extracellular galectin-3 was inhibitable by wortmannin, implicating the activation of a PI-3 kinase dependent pathway in the galectin-3 triggered disruption of adhesion plaques, leading to sarcoma cell migration on laminin-111