SiO in G34.26: Outflows and shocks in a high mass star forming region

We have looked for SiO emission as evidence of shocks in the high mass star formation region G34.26+0.15. JCMT, VLA and FCRAO observations show that SiO emission is widespread across the region. The SiO emission highlights a massive, collimated out ow and other regions where stellar winds are interacting with molecular clumps. As in other star forming regions, there is also SiO at ambient velocities which is related to the out ow activity. No strong SiO abundance enhancement was measured in either the out ow or the low velocity gas, though abundances up to 10(-8) are possible if the SiO is locally enhanced in clumps and optically thick. SiO emission is not detected from the hot core itself, indicating either that SiO is not strongly enhanced in the hot core or that column densities in the region where grain mantle evaporation has taken place are low. In line of sight spiral arm clouds, we measure a SiO abundance of 0.4-2 x 10(-10), consistent with previous estimates for quiescent clouds.

The role of the supply chain in developing a 'lagging' region's manufacturing industry. How important are links with suppliers and customers?

This paper investigates the use of supply chains as a source of knowledge transfer to manufacturing businesses in South Yorkshire and the effect this can have on improving economic performance. It also looks at where assistance originates from, what factors influence who gets the assistance, and what the benefits are.

Identification of Determinants of Glucose-Dependent Insulinotropic Polypeptide Receptor That Interact with N-Terminal Biologically Active Region of the Natural Ligand

Glucose-dependent insulinotropic polypeptide receptor (GIPR), a member of family B of the G-protein coupled receptors, is a potential therapeutic target for which discovery of nonpeptide ligands is highly desirable. Structure-activity relationship studies indicated that the N-terminal part of glucose-dependent insulinotropic polypeptide (GIP) is crucial for biological activity. Here, we aimed at identification of residues in the GIPR involved in functional interaction with N-terminal moiety of GIP. A homology model of the transmembrane core of GIPR was constructed, whereas a three-dimensional model of the complex formed between GIP and the N-terminal extracellular domain of GIPR was taken from the crystal structure. The latter complex was docked to the transmembrane domains of GIPR, allowing in silico identification of putative residues of the agonist binding/activation site. All mutants were expressed at the surface of human embryonic kidney 293 cells as indicated by flow cytometry and confocal microscopy analysis of fluorescent GIP binding. Mutation of residues Arg183, Arg190, Arg300, and Phe357 caused shifts of 76-, 71-, 42-, and 16-fold in the potency to induce cAMP formation, respectively. Further characterization of these mutants, including tests with alanine-substituted GIP analogs, were in agreement with interaction of Glu3 in GIP with Arg183 in GIPR. Furthermore, they strongly supported a binding mode of GIP to GIPR in which the N-terminal moiety of GIP was sited within transmembrane helices (TMH) 2, 3, 5, and 6 with biologically crucial Tyr1 interacting with Gln224 (TMH3), Arg300 (TMH5), and Phe357 (TMH6). These data represent an important step toward understanding activation of GIPR by GIP, which should facilitate the rational design of therapeutic agents.