ILC Communications Workshop

ILC Communications Workshop -- Vancouver July, 2006 The LCSGA Communications Committee is planning a half-day workshop for the afternoon of July 18, 2006 in conjunction with the Vancouver Linear Collider Workshop. The goal of this workshop is to understand and come to agreement on a inspirational, consistent, credible, sustainable and differentiating ILC communications strategy for building a consensus of support for the ILC both inside and outside the HEP community. ILC scientists and staff will be giving talks and communicating with scientific (both HEP and non-HEP) audiences. These talks must be clear, credible and consistent while demonstrating purposes and importance of the ILC. Workshop outcomes include clarifying primary ILC audiences and needs, communications goals, obstacles to successful communications, and mitigation strategies to ensure we achieve our communication goals. A pre-workshop survey will be distributed to participants. Please reply as it will significantly help us prepare for the workshop. Subsequent to this workshop the communications team will develop and maintain up-to-date presentation outlines, tools, materials and resources to assist ILC presenters throughout the world. The LCSGA Communication Committee members are Jonathan Bagger, Jim Brau, Neil Calder, Judy Jackson, Ritchie Patterson, and William Trischuk

Effect of antiserum to luteinizing hormone (LHAS) on the physiology of the epididymis and accessory glands in the albino rat

Rabbit antiserum specific to ovine luteinizing hormone free of contaminating antibodies to nonspecific proteins and FSH was administered to adult, intact rats at a dose of 0.1 and 0.2 ml/day for five days. LHAS had no effect on the weights of the epididymis but decreased their secretory activity to castrate level. Administration of 0.2 ml of LHAS or castration resulted in a marked and comparable reduction in the weights and secretory activity of the accessory glands. LHAS, even at a lower dose (0.1 ml/day), caused a significant reduction in the content of sialic acid in the vas deferons and Cowper's glands. These results are discussed in relation to the factors that regulate the functions of the epididymis and accessory glands

Crystal structure of the serine protease domain of Sesbania mosaic virus polyprotein and mutational analysis of residues forming the S1-binding pocket

Sesbania mosaic virus (SeMV) polyprotein is processed by its N-terminal serine protease domain. The crystal structure of the protease domain was determined to a resolution of 2.4 Å using multiple isomorphous replacement and anomalous scattering. The SeMV protease domain exhibited the characteristic trypsin fold and was found to be closer to cellular serine proteases than to other viral proteases. The residues of the S1-binding pocket, H298, T279 and N308 were mutated to alanine in the ΔN70-Protease–VPg polyprotein, and the cis-cleavage activity was examined. The H298A and T279A mutants were inactive, while the N308A mutant was partially active, suggesting that the interactions of H298 and T279 with P1-glutamate are crucial for the E–T/S cleavage. A region of exposed aromatic amino acids, probably essential for interaction with VPg, was identified on the protease domain, and this interaction could play a major role in modulating the function of the protease