Bibliometric analysis for characterization of oil production in Brazilian territory

Scientometrics - The theme related to the oil production in the Brazilian territory is not limited to the extraction means, distribution and use of this product, and involves political, cultural...     

Personalized technology-enhanced training for people with cognitive impairment

Universal Access in the Information Society - Today, ICT technology offers mobile, customized user-friendly environments to support learning and stimulate an individual’s potential. However,...     

Synthesis,characterization and rheological properties of multiblock associative copolymers by RAFT technique

Polymer Bulletin - Preparation of associating multiblock copolymer electrolytes mediated by radical addition–fragmentation chain transfer (RAFT) technique has been evaluated and reported in...     

Solid-Phase Synthesis of Substrate-Based Dipeptides and Heterocyclic Pseudo-dipeptides as Potential NO Synthase Inhibitors

More than 160 arginine analogues modified on the C-terminus via either an amide bond or a heterocyclic moiety (1,2,4-oxadiazole, 1,3,4-oxadiazole and 1,2,4-triazole) were prepared as potential inhibitors of NO synthases (NOS). A methodology involving formation of a thiocitrulline intermediate linked through its side-chain on a solid support followed by modification of its carboxylate group was developed. Finally, the side-chain thiourea group was either let unchanged, S-alkylated (Me, Et) or guanidinylated (Me, Et) to yield respectively after TFA treatment the corresponding thiocitrulline, S-Me/Et-isothiocitrulline and N-Me/Et-arginine substrate analogues. They all were tested against three recombinant NOS isoforms. Several compounds containing a S-Et- or a S-Me-Itc moiety and mainly belonging to both the dipeptide-like and 1,2,4-oxadiazole series were shown to inhibit nNOS and iNOS with IC₅₀ in the 1–50 μM range. Spectral studies confirmed that these new compounds interacted at the heme active site. The more active compounds were found to inhibit intra-cellular iNOS expressed in RAW264.7 and INS-1 cells with similar efficiency than the reference compounds L-NIL and SEIT.     

Plasmin-Induced Activation of Human Platelets Is Modulated by Thrombospondin-1, Bona Fide Misfolded Proteins and Thiol Isomerases

Inflammatory processes are triggered by the fibrinolytic enzyme plasmin. Tissue-type plasminogen activator, which cleaves plasminogen to plasmin, can be activated by the cross-β-structure of misfolded proteins. Misfolded protein aggregates also represent substrates for plasmin, promoting their degradation, and are potent platelet agonists. However, the regulation of plasmin-mediated platelet activation by misfolded proteins and vice versa is incompletely understood. In this study, we hypothesize that plasmin acts as potent agonist of human platelets in vitro after short-term incubation at room temperature, and that the response to thrombospondin-1 and the bona fide misfolded proteins Eap and SCN⁻-denatured IgG interfere with plasmin, thereby modulating platelet activation. Plasmin dose-dependently induced CD62P surface expression on, and binding of fibrinogen to, human platelets in the absence/presence of plasma and in citrated whole blood, as analyzed by flow cytometry. Thrombospondin-1 pre-incubated with plasmin enhanced these plasmin-induced platelet responses at low concentration and diminished them at higher dose. Platelet fibrinogen binding was dose-dependently induced by the C-terminal thrombospondin-1 peptide RFYVVMWK, Eap or NaSCN-treated IgG, but diminished in the presence of plasmin. Blocking enzymatically catalyzed thiol-isomerization decreased plasmin-induced platelet responses, suggesting that plasmin activates platelets in a thiol-dependent manner. Thrombospondin-1, depending on the concentration, may act as cofactor or inhibitor of plasmin-induced platelet activation, and plasmin blocks platelet activation induced by misfolded proteins and vice versa, which might be of clinical relevance.     

Corrosion behavior of porous magnesium coated by plasma electrolytic oxidation in simulated body fluid

Porous magnesium has a great potential to be used as degradable bone scaffolds. In this study, porous magnesium with 35% percolating porosity has been successfully fabricated through powder metallurgy route utilizing space holders. The intrinsic mechanical properties of the porous magnesium were measured by nanoindentation testing and analyzed with the Oliver–Pharr method. Afterward, a ceramic coating on the surface of the porous magnesium was performed by plasma electrolytic oxidation (PEO) treatment in a silicate‐based solution. The morphology and composition results of the PEO coatings indicated that it is possible to apply a homogenous and adhesive ceramic coating layer on all free surface of the porous magnesium through PEO method. The protective performance of the PEO coatings was evaluated using by potentiodynamic polarization and electrochemical impedance spectroscopy tests in simulated body fluid. The results revealed the PEO coating significantly improves biocorrosion resistance of the porous magnesium. Therefore, it can be used as an effective method to control the degradation rate of porous magnesium implants in the human body.     

Phase portraits of Abel quadratic differential systems of second kind with symmetries

We provide normal forms and the global phase portraits on the Poincaré disk of the Abel quadratic differential equations of the second kind having a symmetry with respect to an axis or to the origin. Moreover, we also provide the bifurcation diagrams for these global phase portraits.