Continuous asr for flexible incremental dialogue

Spoken dialogue systems provide a convenient way for users to interact with a machine using only speech. However, they often rely on a rigid turn taking regime in which a voice activity detection (VAD) module is used to determine when the user is speaking and decide when is an appropriate time for the system to respond. This paper investigates replacing the VAD and discrete utterance recogniser of a conventional turn-taking system with a continuously operating recogniser that is always listening, and using the recogniser 1-best path to guide turn taking. In this way, a flexible framework for incremental dialogue management is possible. Experimental results show that it is possible to remove the VAD component and successfully use the recogniser best path to identify user speech, with more robustness to noise, potentially smaller latency times, and a reduction in overall recognition error rate compared to using the conventional approach. © 2013 IEEE.

Interfacial immobilization of monoclonal antibody and detection of human prostate-specific antigen.

Antibody orientation and its antigen binding efficiency at interface are of particular interest in many immunoassays and biosensor applications. In this paper, spectroscopic ellipsometry (SE), neutron reflection (NR), and dual polarization interferometry (DPI) have been used to investigate interfacial assembly of the antibody [mouse monoclonal anti-human prostate-specific antigen (anti-hPSA)] at the silicon oxide/water interface and subsequent antigen binding. It was found that the mass density of antibody adsorbed at the interface increased with solution concentration and adsorption time while the antigen binding efficiency showed a steady decline with increasing antibody amount at the interface over the concentration range studied. The amount of antigen bound to the interfacial immobilized antibody reached a maximum when the surface-adsorbed amount of antibody was around 1.5 mg/m(2). This phenomenon is well interpreted by the interfacial structural packing or crowding. NR revealed that the Y-shaped antibody laid flat on the interface at low surface mass density with a thickness around 40 Å, equivalent to the short axial length of the antibody molecule. The loose packing of the antibody within this range resulted in better antigen binding efficiency, while the subsequent increase of surface-adsorbed amount led to the crowding or overlapping of antibody fragments, hence reducing the antigen binding due to the steric hindrance. In situ studies of antigen binding by both NR and DPI demonstrated that the antigen inserted into the antibody layer rather than forming an additional layer on the top. Stability assaying revealed that the antibody immobilized at the silica surface remained stable and active over the monitoring period of 4 months. These results are useful in forming a general understanding of antibody interfacial behavior and particularly relevant to the control of their activity and stability in biosensor development.