End-to-End Evaluation in Simultaneous Translation

This paper presents the end-to-end evaluation of an automatic simultaneous translation system, built with state-of-the-art components. It shows whether, and for which situations, such a system might be advantageous when compared to a human interpreter. Using speeches in English translated into Spanish, we resent the evaluation procedure and we discuss the results both for the recognition and translation components as well as for the overall system. Even if the translation process remains the Achilles’ heel of the system, the results show that the system can keep at least half of the information, becoming potentially useful for final users

Genome variations: Effects on the robustness of neuroevolved control for swarm robotics systems

Manual design of self-organized behavioral control for swarms of robots is a complex task. Neuroevolution has proved a viable alternative given its capacity to automatically synthesize controllers. In this paper, we introduce the concept of Genome Variations (GV) in the neuroevolution of behavioral control for robotic swarms. In an evolutionary setup with GV, a slight mutation is applied to the evolving neural network parameters before they are copied to the robots in a swarm. The genome variation is individual to each robot, thereby generating a slightly heterogeneous swarm. GV represents a novel approach to the evolution of robust behaviors, expected to generate more stable and robust individual controllers, and bene t swarm behaviors that can deal with small heterogeneities in the behavior of other members in the swarm. We conduct experiments using an aggregation task, and compare the evolved solutions to solutions evolved under ideal, noise-free conditions, and to solutions evolved with traditional sensor noise.info:eu-repo/semantics/acceptedVersio

Comparison of Recombinant Human Haptocorrin Expressed in Human Embryonic Kidney Cells and Native Haptocorrin

Haptocorrin (HC) is a circulating corrinoid binding protein with unclear function. In contrast to transcobalamin, the other transport protein in blood, HC is heavily glycosylated and binds a variety of cobalamin (Cbl) analogues. HC is present not only in blood but also in various secretions like milk, tears and saliva. No recombinant form of HC has been described so far. We report the expression of recombinant human HC (rhHC) in human embryonic kidney cells. We purified the protein with a yield of 6 mg (90 nmol) per litre of cell culture supernatant. The isolated rhHC behaved as native HC concerning its spectral properties and ability to recognize both Cbl and its baseless analogue cobinamide. Similar to native HC isolated from blood, rhHC bound to the asialoglycoprotein receptor only after removal of terminal sialic acid residues by treatment with neuraminidase. Interestingly, rhHC, that compared to native HC contains four excessive amino acids (…LVPR) at the C-terminus, showed subtle changes in the binding kinetics of Cbl, cobinamide and the fluorescent Cbl conjugate CBC. The recombinant protein has properties very similar to native HC and although showing slightly different ligand binding kinetics, rhHC is valuable for further biochemical and structural studies

Sequence-definition in stiff conjugated oligomers

Abstract The concept of sequence-definition in the sense of polymer chemistry is introduced to conjugated, rod-like oligo(phenylene ethynylene)s via an iterative synthesis procedure. Specifically, monodisperse sequence-defined trimers and pentamers were prepared via iterative Sonogashira cross-coupling and deprotection. The reaction procedure was extended to tetra- and pentamers for the first time yielding a monodisperse pentamer with 18% and a sequence-defined pentamer with 3.2% overall yield. Furthermore, three novel trimers with a 9H-fluorene building block at predefined positions within the phenylene ethynylene chain were synthesised in 23–52% overall yields. Hence, it was confirmed that a functionality of interest can be incorporated selectively at a pre-defined position of these monodisperse oligomers. All respective intermediate structures were fully characterised by proton and carbon NMR, mass spectrometry, size-exclusion chromatography, and IR spectroscopy. Additionally, thermal and optical transitions are reported for the different oligomers

Agricultural Knowledge, Science and Technology: Investment and economic returns

The IAASTD is a promising starting point and provides the opportunity for a rational and holistic discussion on the future of agriculture with the cooperation of all stakeholders involved. It presents a clear message: Business as usual is not an option! A thorough and radical overhaul of present international and national agricultural policies is necessary to meet the challenges of the future. The IAASTD does not offer so called “silver bullet“ solutions, in fact it warns us against believing such solutions exist. Instead, it provides a comprehensive and interdisciplinary analysis of the state of agriculture and a wide range of promising approaches.Peer reviewe

A Yeast Model of FUS/TLS-Dependent Cytotoxicity

FUS/TLS is a nucleic acid binding protein that, when mutated, can cause a subset of familial amyotrophic lateral sclerosis (fALS). Although FUS/TLS is normally located predominantly in the nucleus, the pathogenic mutant forms of FUS/TLS traffic to, and form inclusions in, the cytoplasm of affected spinal motor neurons or glia. Here we report a yeast model of human FUS/TLS expression that recapitulates multiple salient features of the pathology of the disease-causing mutant proteins, including nuclear to cytoplasmic translocation, inclusion formation, and cytotoxicity. Protein domain analysis indicates that the carboxyl-terminus of FUS/TLS, where most of the ALS-associated mutations are clustered, is required but not sufficient for the toxicity of the protein. A genome-wide genetic screen using a yeast over-expression library identified five yeast DNA/RNA binding proteins, encoded by the yeast genes ECM32, NAM8, SBP1, SKO1, and VHR1, that rescue the toxicity of human FUS/TLS without changing its expression level, cytoplasmic translocation, or inclusion formation. Furthermore, hUPF1, a human homologue of ECM32, also rescues the toxicity of FUS/TLS in this model, validating the yeast model and implicating a possible insufficiency in RNA processing or the RNA quality control machinery in the mechanism of FUS/TLS mediated toxicity. Examination of the effect of FUS/TLS expression on the decay of selected mRNAs in yeast indicates that the nonsense-mediated decay pathway is probably not the major determinant of either toxicity or suppression.Fidelity Biosciences (Firm)Fidelity Biosciences (Firm) (Research Inititative)ALS Therapy AllianceNational Institutes of Health (U.S.) (NIH 1RC1NS06839)National Institutes of Health (U.S.) (NIH U01NS05225-03)National Institutes of Health (U.S.) (NIH R01NS050557-05)National Institutes of Health (U.S.) (NIH 1RC2NS070342-01)Pierre L. de Bourgknecht ALS Research FoundationNational Science Foundation (U.S.) (NS614192