β-Fur-2-yl-α-halogenacrylonitrile. V [1] Darstellung von β-(5-Nitro-fur-2-yl)-α-azidoacrylonitril und β-(5-Nitro-fur-2-yl)-α-aminoacrylonitril

β-Fur-2-yl-α-halogenacrylonitriles. V. Preparation of β-(5-Nitro-fur-2-yl)-α-azidoacrylonitrile and β-(5-Nitro-fur-2-yl)-α-aminoacrylonitrile β-(5-Nitro-fur-2-yl)-α-chloroacrylonitrile ( 1 ) reacts with sodium azide to yield β-(5-nitro-fur-2-yl)-α-azidoacrylonitrile ( 2 ). By Staudinger-reaction β-(5-nitro-fur-2-yl)-α-aminoacrylonitrile ( 5 ) is formed. The ¹H- and ¹³C-n.m.r. spectra of E/Z isomers are discussed.     

SMTIBEA: a hybrid multi-objective optimization algorithm for configuring large constrained software product lines

Software and Systems Modeling - A key challenge to software product line engineering is to explore a huge space of various products and to find optimal or near-optimal solutions that satisfy all...     

Er+ medium energy ion implantation into lithium niobate

Erbium-doped lithium niobate (Er:LiNbO₃) is a prospective photonics component, operating at 1.5 μm, which could find its use chiefly as an optical amplifier or waveguide laser. In this study, we have focused on the properties of the optically active Er:LiNbO₃ layers, which are fabricated by medium energy ion implantation under various experimental conditions. Erbium ions were implanted at energies of 330 and 500 keV with fluences of 1.0 × 10¹⁵, 2.5 × 10¹⁵ and 1.0 × 10¹⁶ cm^?2 into LiNbO₃ single-crystalline cuts of various orientations. The as-implanted samples were annealed in air at 350 °C for 5 h. The depth distribution and diffusion profiles of the implanted Er were measured by Rutherford Backscattering Spectroscopy (RBS) using 2 MeV He⁺ ions. The projected range R_P and projected range straggling ΔR_P were calculated employing the SRIM code. The damage distribution and structural changes were described using the RBS/channelling method. Changes of the lithium concentration depth distribution were studied by Neutron Depth Profiling (NDP). The photoluminescence spectra of the samples were measured to determine whether the emission was in the desired region of 1.5 μm. The obtained data made it possible to reveal the relations between the structural changes of erbium-implanted lithium niobate and its luminescence properties important for photonics applications.     

Characterization of a class of spatially interconnected systems (ladder circuits) using two-dimensional systems theory

Multidimensional Systems and Signal Processing - This paper considers a class of spatially interconnected systems formed by ladder circuits using two-dimensional systems theory. The individual...     

CD4-CD8-C.B-17 SCID thymocytes enter the CD4+CD8+ stage in the presence of neonatally grafted T cells

Our previous studies in iron-loaded rat heart cells showed that in vitro iron loading results in peroxidative injury, manifested in a marked decrease in rate and amplitude of heart cell contractility and rhythmicity, which is correctable by treatment with deferoxamine (DF). In the present studies we explored the role of mitochondrial damage in myocardial iron toxicity. Iron loading by 24-hour incubation with 0.36 mmol/L ferric ammonium citrate resulted in a decrease in the activity of nicotinamide adenine dinucleotide (NADH)-cytochrome c oxidoreductase (complex I+III) to 35.3%+/-11.2% of the value in untreated controls; of succinate-cytochrome c oxidoreductase (complex II+III) to 57.4%+/-3.1%; and of succinate dehydrogenase to 63.5%+/-12.6% (p < 0.001 in all cases). The decrease in activity of other mitochondrial enzymes, including NADH-ferricyanide reductase, succinate ubiquinone oxidoreductase (complex II), cytochrome c oxidase (complex IV), and ubiquinol cytochrome c oxidoreductase (complex III), was less impressive and ranged from 71.5%+/-15.8% to 91.5%+/-14.6% of controls. That the observed loss of respiratory enzyme activity was a specific effect of iron toxicity was clearly demonstrated by the complete restoration of enzyme activities by in vitro iron chelation therapy. Sequential treatment with iron and doxorubicin caused a loss of complex I+III and complex II+III activity that was greater than that seen with either agent alone but was only partially correctable by DF treatment. Alterations in cellular adenosine triphosphate measurements paralleled very closely the changes observed in respiratory complex activity. These findings demonstrate for the first time the impairment of cardiac mitochondrial respiratory enzyme activity caused by iron loading at conditions formerly shown to produce severe abnormalities in contractility and rhythmicity.