169 research outputs found

    Navigation and interaction in a real-scale digital mock-up using natural language and user gesture

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    This paper tries to demonstrate a very new real-scale 3D system and sum up some firsthand and cutting edge results concerning multi-modal navigation and interaction interfaces. This work is part of the CALLISTO-SARI collaborative project. It aims at constructing an immersive room, developing a set of software tools and some navigation/interaction interfaces. Two sets of interfaces will be introduced here: 1) interaction devices, 2) natural language (speech processing) and user gesture. The survey on this system using subjective observation (Simulator Sickness Questionnaire, SSQ) and objective measurements (Center of Gravity, COG) shows that using natural languages and gesture-based interfaces induced less cyber-sickness comparing to device-based interfaces. Therefore, gesture-based is more efficient than device-based interfaces.FUI CALLISTO-SAR

    Plexin-B2 Negatively Regulates Macrophage Motility, Rac, and Cdc42 Activation

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    Plexins are cell surface receptors widely studied in the nervous system, where they mediate migration and morphogenesis though the Rho family of small GTPases. More recently, plexins have been implicated in immune processes including cell-cell interaction, immune activation, migration, and cytokine production. Plexin-B2 facilitates ligand induced cell guidance and migration in the nervous system, and induces cytoskeletal changes in overexpression assays through RhoGTPase. The function of Plexin-B2 in the immune system is unknown. This report shows that Plexin-B2 is highly expressed on cells of the innate immune system in the mouse, including macrophages, conventional dendritic cells, and plasmacytoid dendritic cells. However, Plexin-B2 does not appear to regulate the production of proinflammatory cytokines, phagocytosis of a variety of targets, or directional migration towards chemoattractants or extracellular matrix in mouse macrophages. Instead, Plxnb2−/− macrophages have greater cellular motility than wild type in the unstimulated state that is accompanied by more active, GTP-bound Rac and Cdc42. Additionally, Plxnb2−/− macrophages demonstrate faster in vitro wound closure activity. Studies have shown that a closely related family member, Plexin-B1, binds to active Rac and sequesters it from downstream signaling. The interaction of Plexin-B2 with Rac has only been previously confirmed in yeast and bacterial overexpression assays. The data presented here show that Plexin-B2 functions in mouse macrophages as a negative regulator of the GTPases Rac and Cdc42 and as a negative regulator of basal cell motility and wound healing

    Spectral reflectance properties of zeolites and remote sensing implications

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    The 0.3- to 26-μm reflectance spectra of a suite of 28 zeolites were measured and analyzed to derive spectral-compositional-structural relationships. Below ~7 μm, the spectra are largely dominated by absorption features associated with zeolitic water. At longer wavelengths, the spectra are dominated by absorption features associated with the aluminosilicate framework. The spectra exhibit a number of systematic variations which can be used for both structurl and compositional determinations. These include: (1) distinguishing different structural groups on the basis of wavelength position variations associated with absorption features in the 8.5- to 26-μm region that are related to differences in the structure of the aluminosilicate framework; (2) determining the major cation which is present (Ca, Na, K) and the associated electronic environment of the zeolitic water on the basis of how these cations hydrogen bond to the water molecules in the void spaces and consequently affect water-related absorption band positions, particularly in the 1.4, 1.9, and 2.0- to 2.5-μm regions; (3) determining the Al:(Al + Si) ratio and SCFM chemical index on the basis of absorption features in the 7- to 26-μm region which are most sensitive to these compositional variations; and (4) identifying ironbearing zeolites on the basis of absorption features in the 0.35- to 0.9-μm region. The wavelength position and number of H2O-associated absorption bands are sensitive to factors such as the type of major cation, degree of hydrogen bonding, and size of the void space, all of which are somewhat interrelated.This study was supported by a research grant from the Natural Sciences and Engineering Research Council of Canada, a contract from the Canadian Space Agency Space Science Program, a discretionary grant from the University of Winnipeg (to E.A.C.), and the Louise McBee Scholarship of the Georgia Association for Women in Education, University of Georgia (to P.M.A.).This study was supported by a research grant from the Natural Sciences and Engineering Research Council of Canada, a contract from the Canadian Space Agency Space Science Program, a discretionary grant from the University of Winnipeg (to E.A.C.), and the Louise McBee Scholarship of the Georgia Association for Women in Education, University of Georgia (to P.M.A.).https://agupubs.onlinelibrary.wiley.com/doi/abs/10.1029/2000JE00146

    Immune plexins and semaphorins: old proteins, new immune functions

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    Plexins and semaphorins are a large family of proteins that are involved in cell movement and response. The importance of plexins and semaphorins has been emphasized by their discovery in many organ systems including the nervous (Nkyimbeng-Takwi and Chapoval, 2011; McCormick and Leipzig, 2012; Yaron and Sprinzak, 2012), epithelial (Miao et al., 1999; Fujii et al., 2002), and immune systems (Takamatsu and Kumanogoh, 2012) as well as diverse cell processes including angiogenesis (Serini et al., 2009; Sakurai et al., 2012), embryogenesis (Perala et al., 2012), and cancer (Potiron et al., 2009; Micucci et al., 2010). Plexins and semaphorins are transmembrane proteins that share a conserved extracellular semaphorin domain (Hota and Buck, 2012). The plexins and semaphorins are divided into four and eight subfamilies respectively based on their structural homology. Semaphorins are relatively small proteins containing the extracellular semaphorin domain and short intra-cellular tails. Plexins contain the semaphorin domain and long intracellular tails (Hota and Buck, 2012). The majority of plexin and semaphorin research has focused on the nervous system, particularly the developing nervous system, where these proteins are found to mediate many common neuronal cell processes including cell movement, cytoskeletal rearrangement, and signal transduction (Choi et al., 2008; Takamatsu et al., 2010). Their roles in the immune system are the focus of this review
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