549 research outputs found
TripleSent: a triple store of events associated with their prototypical sentiment
The current generation of sentiment analysis
systems is limited in their real-world applicability because they
cannot detect utterances that implicitly carry positive or negative
sentiment. We present early stage research ideas to address this
inability with the development of a dynamic triple store of events
associated with their prototypical sentiment
Interaction of prothrombin with factor Va-phospholipid complexes
The effects of factor Va and the phospholipid-binding fragment of factor Va [factor Va light chain (LC), Mr 80000] on the binding of prothrombin, factor X, and factor Xa to phospholipid vesicles are reported. Equilibrium binding experiments were performed that utilized large-volume vesicles, which can be removed from the bulk solution by centrifugation. Factor Va decreased the dissociation constant of the prothrombin-phospholipid complex 50-fold, from 2.0 X 10(-7) M to 4.0 X 10(-9) M. For the factor X-phospholipid complex the decrease was 60-fold (1.8 X 10(-7) M to 3.0 X 10(-9) M) and for factor Xa, 160-fold (1.6 X 10(-7) M to 1.0 X 10(-9) M). The ratios of moles of protein bound to moles of total added factor Va at saturation of phospholipid-bound factor Va indicate an 1:1 stoichiometric complex of either factor Xa, factor X, or prothrombin and phospholipid-bound factor Va. In the presence of factor Va LC, the dissociation constants of factor Xa- and prothrombin-phospholipid complexes were increased, while the maximal protein-binding capacities of the vesicles were not affected by factor Va LC. The data suggest a competitive interaction between factor Xa and factor Va LC binding as well as between prothrombin and factor Va LC binding at the phospholipid surface. From this, it is concluded that the phospholipid-binding fragment of factor Va alone does not serve as the binding site for interactions of factor Xa and prothrombin with factor Va
Tactility Trialing: Exploring Materials to Inform Tactile Experience Design
Although materials of tangible interaction designs largely determine their user experience, material choices are often steered by practical motives. This paper presents ‘tactility trialing’, an approach to explore tactile experiences of materials to inform the design of tangible artifacts. Through experience formulation, material selection, artifact creation and short user studies, designers and design-researchers are enabled to make informed decisions on the materials to be used in order to evoke the intended experience. The approach is illustrated through two case studies of student work. Tactility trialing helped them in getting acquainted with tactile material qualities in practice, and with the applicability of material characteristics such as resilience and hardness in design
Design of the physical exercise during Adjuvant Chemotherapy Effectiveness Study (PACES): a randomized controlled trial to evaluate effectiveness and cost-effectiveness of physical exercise in improving physical fitness and reducing fatigue
Design of the physical exercise during Adjuvant Chemotherapy Effectiveness Study (PACES): a randomized controlled trial to evaluate effectiveness and cost-effectiveness of physical exercise in improving physical fitness and reducing fatigue
Interaction of bovine blood clotting factor Va and its subunits with phosolipid vesicles
Thrombin-activated factor Va and factor Va subunit binding to large-volume vesicles was investigated by a technique based on the separation by centrifugation of phospholipid-bound protein from the bulk solution. This technique allows the direct measurement of free-protein concentration. It is concluded that the phospholipid binding site on factor Va is located on a basic factor Va subunit with Mr 80 000 (factor Va-LC). The effects of phospholipid vesicle composition, calcium concentration, pH, and ionic strength on the equilibrium constants of factor Va- and factor Va-LC-phospholipid interaction were studied. Factor Va and factor Va-LC binding to phospholipid requires the presence of negatively charged phospholipids. It is further demonstrated that the following occur: (a) Calcium ions compete with factor Va and factor Va-LC for phospholipid-binding sites. (b) The dissociation constant of protein-phospholipid interaction increases with the ionic strength, whereas the maximum protein-binding capacity of the phospholipid vesicle was not affected by ionic strength. (c) The dissociation constant for factor Va-phospholipid interaction depends on pH when the vesicle consists of phosphatidic acid. It is concluded that factor Va-phospholipid interaction is primarily electrostatic in nature, where positively charged groups on the protein directly interact with the phosphate group of net negatively charged phospholipids. The results suggest that factor Va, like factor Xa and prothrombin, has the characteristics of an extrinsic membrane protein
Functional properties of factor Va subunits after proteolytic alterations by activated protein C
Effect of low versus high intensity physical exercise during chemotherapy on physical fitness, fatigue and chemotherapy completion rates:Results of a randomized, controlled trial
- …