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

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

Change of Antiferromagnetic Structure near a Quantum Critical Point in CeRh1-xCoxIn5

The elastic neutron scattering experiments were carried out on the solid solutions CeRh_{1-x}Co_xIn_5 to clarify the nature of the antiferromagnetic (AF) state in the vicinity of the quantum critical point (QCP): x_c ~0.8. The incommensurate AF order with the wave vector of q_h=(1/2,1/2,~0.3) observed in pure CeRhIn_5 is weakly suppressed upon doping with Co, and a commensurate q_c=(1/2,1/2,1/2) and an incommensurate q_1=(1/2,1/2,~0.42) AF structures evolve at intermediate Co concentrations. These AF orders are enhanced at x=0.7, and furthermore the q_h AF order vanishes. These results suggest that the AF correlations with the q_c and q_1 modulations are significantly enhanced in the intermediate x range, and may be connected with the evolution of the superconductivity observed above x~0.3.Comment: 5 pages, 5 figures, accepted for publication in Phys. Rev.

A Dual Binding Mode for RhoGTPases in Plexin Signalling

A novel binding site for RhoGTPases on the intracellular region of plexins induces a trimeric ligand—receptor arrangement that appears crucial for plexin function

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

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

Immune plexins and semaphorins: old proteins, new immune functions

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