abstract: This study exmaines the effect of in-vehicle infotainment display depth on driving performance. More features are being built into infotainment displays, allowing drivers to complete a greater number of secondary tasks while driving. However, the complexity of completing these tasks can take attention away from the primary task of driving, which may present safety risks. Tasks become more time consuming as the items drivers wish to select are buried deeper in a menu’s structure. Therefore, this study aims to examine how deeper display structures impact driving performance compared to more shallow structures. Procedure. Participants complete a lead car following task, where they follow a lead car and attempt to maintain a time headway (TH) of 2 seconds behind the lead car at all times, while avoiding any collisions. Participants experience five conditions where they are given tasks to complete with an in-vehicle infotainment system. There are five conditions, each involving one of five displays with different structures: one-layer vertical, one-layer horizontal, two-layer vertical, two-layer horizontal, and three-layer. Brake Reaction Time (BRT), Mean Time Headway (MTH), Time Headway Variability (THV), and Time to Task Completion (TTC) are measured for each of the five conditions. Results. There is a significant difference in MTH, THV, and TTC for the three-layer condition. There is a significant difference in BRT for the two-layer horizontal condition. There is a significant difference between one- and two-layer displays for all variables, BRT, MTH, THV, and TTC. There is also a significant difference between one- and three-layer displays for TTC. Conclusions. Deeper displays negatively impact driving performance and make tasks more time consuming to complete while driving. One-layer displays appear to be optimal, although they may not be practical for in-vehicle displays. / Dissertation/Thesis / Masters Thesis Human Systems Engineering 2018

In the dynamic arena of display technology, augmented reality (AR) displays represent a pivotal advancement, seamlessly bridging the digital and physical worlds. This dissertation delves into the realm of AR display technologies, spotlighting the challenges and limitations of current systems, including transparent and near-eye displays, and proposes innovative solutions to enhance user experience and display performance. With a focus on overcoming issues such as diffraction-induced image blur, the trade-off between resolution and field of view (FoV) in near-eye displays, and FoV constraints in waveguide-based displays, this research introduces new evaluation methods, optimization techniques, and system designs. First, the dissertation presents a quantitative evaluation of diffraction effects on background objects, leading to the development of a pixel structure optimization method aimed at reducing diffraction in transparent displays with small aperture ratios. This advancement promises to enhance image clarity and visibility, addressing one of the key challenges in the deployment of AR technology for transparent displays. Next, we introduce a novel Maxwellian-type foveated AR system that leverages a single light engine. This system employs a temporal polarization-multiplexing method to encode both high-resolution foveal and low-resolution peripheral images through the same light engine. With the aid of polarization-selective lenses, this system effectively separates the two views, delivering a wide FoV and high angular resolution in the foveal region, effectively minimizing the resolution-FoV compromise in near-eye displays. Furthermore, the dissertation conducts a detailed analysis of FoV limitations in single-layer waveguides, proposing a strategic combination of a gradient-pitch polarization volume grating (PVG) with a butterfly exit-pupil expansion (EPE) scheme. This approach aims to extend the FoV in single-layer waveguides towards the theoretical full-color limit. This research addresses pivotal challenges in waveguide-based AR technology, marking a significant step towards realizing more immersive and user-friendly AR systems.

ITC/USA 2009 Conference Proceedings / The Forty-Fifth Annual International Telemetering Conference and Technical Exhibition / October 26-29, 2009 / Riviera Hotel & Convention Center, Las Vegas, Nevada / The Common Display System (CDS) will provide all NAVAIRWD sites with a flexible Range real-time situational awareness and telemetry display/processing capability. CDS will have an extensible framework enabling all sites to quickly and conveniently develop Range unique plugins to accommodate new requirements or functionality not presently found in the applications common core plug-ins. Range unique plug-ins are separate and distinct from the application's common core engine.

Recent guidelines recommend oxygen saturation (SpO(2)) levels of 90%-95% for preterm neonates on supplemental oxygen but it is difficult to discern such levels with current pulse oximetry sonifications. We tested (1) whether adding levels of tremolo to a conventional log-linear pulse oximetry sonification would improve identification of SpO(2) ranges, and (2) whether adding a beacon reference tone to conventional pulse oximetry confuses listeners about the direction of change. Participants using the Tremolo (94%) or Beacon (81%) sonifications identified SpO(2) range significantly more accurately than participants using the LogLinear sonification (52%). The Beaton sonification did not confuse participants about direction of change. The Tremolo sonification may have advantages over the Beacon sonification for monitoring SpO(2) of preterm neonates, but both must be further tested with clinicians in clinically representative scenarios, and with different levels of ambient noise and distractions. Crown Copyright (C) 2016 Published by Elsevier Ltd. All rights reserved.

Interferon regulatory factor 1 (IRF-1) is a tumour suppressor protein and transcription factor. It has been shown to modulate target gene expression in response to stimuli, which include viral infection and DNA damage, and to be down-regulated in several forms of cancer. This thesis details the development of an intrabody, an intracellular antibody, that binds specifically to endogenous IRF-1. The binding of the intrabody to IRF-1 enhanced transcription from IRF-1-responsive reporter gene constructs and endogenous promoters, thus it was shown to activate IRF-1. Intrabody binding also increased the rate at which IRF-1 was degraded, suggesting that the intrabody epitope may be regulating both IRF-1 activity and turnover. These results were supported point mutation within the intrabody epitope (P325 to A) as the resultant mutant also displayed both a higher transcriptional activity and increased rate of degradation. In an effort to understand the mechanisms which regulate IRF-1 activity a search for novel IRF-1-interacting proteins was carried out using phage peptide display. This in vitro technique enables the identification of peptides able to bind a specific target protein. The sequence of these peptides can then be used to search protein databases for homologous, full-length proteins that could also bind the target protein. This led to the identification of an IRF-1-binding peptide that held sequence similar to a region of Zinc Finger 350 (ZNF350), a transcription factor involved in regulating the DNA damage response. Subsequently, endogenous ZNF350 and IRF-1 were co-immunoprecipitated from a human cancer cell line. The extreme C-terminus of IRF-1 was shown to be sufficient for an interaction with ZNF350, although a second, more N-terminal site was also shown to be essential for a stable intracellular interaction. This data sheds new light on the role of the extreme C-terminus of IRF-1 in modulating the protein‟s activity. This study also provides new and IRF-1-specific molecular tools, in the form of intrabodies and IRF-1-binding peptides, which could be used in the future to further characterise the activity and regulation of this tumour suppressor protein.

International Telemetering Conference Proceedings / October 23-26, 2000 / Town & Country Hotel and Conference Center, San Diego, California / This paper will provide details on planned upgrades to the Advanced Data Acquisition and Processing System (ADAPS) Real-Time / Post Flight Processing (RT/PFP) telemetry processor. The ADAPS RT/PFP is used to process real-time telemetry at the Air Force Flight Test Center (AFFTC). The ADAPS telemetry processor is based on the L3 Communications O/S90 telemetry pre-processing system. New modifications to the ADAPS telemetry processor will provide increased processing capability, increased data throughput, and higher reliability.

International Telemetering Conference Proceedings / October 23-26, 2000 / Town & Country Hotel and Conference Center, San Diego, California / The strip-chart recorder has evolved from a simple pen-writing instrument to an instrumentation platform. Today's Telemetry Recording Workstations not only provide a permanent hard copy of telemetry data, but also offer high resolution videographic displays with real-time point-of-writing representation, the ability to efficiently store data digitally, and customizable user interfaces. Host control and digital data transfer can be achieved using Ethernet networks, making the instrument an integral part of a telemetry system. The Telemetry Recording Workstation is a fundamental instrument for any telemetry application or installation, due to its abilities to display, print and store real-time data.

<p>In affinity protein biotechnology the selective bindingbetween a chosen protein and an interacting biomolecule isutilized for a variety of applications including bioseparation,detection and therapy. Traditionally, affinity proteinsrecruited for such applications have been derived from naturalproteins or immunoglobulins generated via immunization routes.More recently, advances in the construction and handling oflarge collections of proteins(denoted libraries) generated invitro have opened up for new routes for the development ofaffinity proteins with desired properties.</p><p>In this study, phage display selection technology was usedfor the isolation of novel human CD28 (hCD28)-specific affinityproteins from a protein library constructed by combinatorialprotein engineering of a 58 aa protein domain (Z) derived fromstaphylococcal protein A (SPA). From selections using hCD28 asa target molecule, several hCD28-specific affinity proteins(denoted affibodies) could be identified and analysis of theisolated affibody variants revealed a high degree of sequencehomology between the different clones. The biosensor analysisshowed that all variants bound to hCD28 with micromolardissociation constants (KD) and no significant cross-reactivitytowards the structurally related T-cell receptor hCTLA-4 couldbe observed. The apparent binding affinity for hCD28 of one ofthe isolated affibodies was further improved through fusion toa human Fc fragment fusion partner, resulting in a homodimericversion of the affibody ligand showing avidity effects uponhCD28 binding. Further, a co-culture experiment involvingJurkat T-cells and CHO cell lines tranfected to express eitherhuman CD80 or LFA-3 on the cell surface showed that apreincubation of Jurkat cells with one of the affibody variantsresulted in a specific concentration-dependent inhibition ofthe CD80 induced IL-2 production. This indicates that thisaffibody binds to hCD28 and specifically interferes with theco-stimulation signal mediated via hCD28 and hCD80. ACD28-specific binding protein could have potential as an agentfor various immunotherapy applications. In a second study, anaffinity protein-based strategy was investigated forsite-specific anchoring of proteins onto cellulose for woodfiber engineering purposes. Here, affinity proteins derivedfrom different sources were used for the assembly of acellulosome-like complex for specific and reversible anchoringof affinity domain-tagged reporter proteins to acellulose-anchored fusion protein. A fusion protein between acellulose binding module (Cel6A CBM1) derived from the fungalTrichoderma reesei and a five-domain staphylococcal protein A(SPA) moiety was constructed to serve as a platform for thedocking of reporter proteins produced as fusion to two copiesof a SPA-binding affibody affinity protein (denoted ZSPA-1),selected by phage display technology from a Z domain basedprotein library. In a series of experiments, involving repeatedwashing and low pH elutions, affinity tagged Enhanced GreenFluorescent Protein (EGFP) and Fusarium solani pisi lipasecutinase reporter proteins were both found to be specificallydirected from solution to a region of a cellulose-based filterpaper where the SPA-CBM fusion protein previously had beenpositioned. This showed that the cellulose-anchored SPA-Cel6ACBM1 fusion protein had been stably anchored to the surfacewith retained binding activity and that the interaction betweenSPA and the ZSPA-1 affibody domain was selective.</p><p>phage display, combinatorial, selection, CD28, cellulosome,cellulose, affibody</p>

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