Satellite-based delivery of educational content to geographically isolated communities: A service based approach

Enabling learning for members of geographically isolated communities presents benefits in terms of promoting regional development and cost savings for governments and companies. However, notwithstanding recent advances in e-Learning, from both technological and pedagogical perspectives, there are very few, if any, recognised methodologies for user-led design of satellite-based e-learning infrastructures. In this paper, we present a methodology for designing a satellite and wireless based network infrastructure and learning services to support distance learning for such isolated communities. This methodology entails (a) the involvement of community members in the development of targeted learning services from an early stage, and (b) a service-oriented approach to learning solution deployment. Results show, that, while the technological premises of distance learning can be accommodated by hybrid satellite/wireless infrastructures,this has to be complemented with (a) high-quality audio–visual educational material, and (b) the opportunity for community members to interact with other community members either as groups (common-room oriented scenarios) or individuals (home-based scenarios), thus providing an impetus for learner engagement in both formal and informal activities

Simple and monolithic picosecond pulse shaper based on fiber Bragg gratings

In this contribution we present a simple and robust pulse shaping device based on coherent pulse stacking. The device is based on fiber Bragg gratings written in a polarisation maintaining step index fiber and a fiber optical circulator. Up to four pulse replicas are reflected by fiber Bragg gratings and interfere at the output of the device. Temperature control allows tuning of the relative pulse amplitudes and phases of the pulse replicas. We experimentally demonstrated 235 ps and 416 ps long flattop pulses with rising and falling edges shorter than 100 ps. In contrast to other pulse shaping techniques the presented setup is robust, alignment free, provides excellent beam quality and is also suitable for pulse durations up to several nanoseconds

Structural basis for recognition of phosphodiester-containing lysosomal enzymes by the cation-independent mannose 6-phosphate receptor

Mannose 6-phosphate (Man-6-P)-dependent trafficking is vital for normal development. The biogenesis of lysosomes, a major cellular site of protein, carbohydrate, and lipid catabolism, depends on the 300-kDa cation-independent Man-6-P receptor (CI-MPR) that transports newly synthesized acid hydrolases from the Golgi. The CI-MPR recognizes lysosomal enzymes bearing the Man-6-P modification, which arises by the addition of GlcNAc-1-phosphate to mannose residues and subsequent removal of GlcNAc by the uncovering enzyme (UCE). The CI-MPR also recognizes lysosomal enzymes that elude UCE maturation and instead display the Man-P-GlcNAc phosphodiester. This ability of the CI-MPR to target phosphodiester-containing enzymes ensures lysosomal delivery when UCE activity is deficient. The extracellular region of the CI-MPR is comprised of 15 repetitive domains and contains three distinct Man-6-P binding sites located in domains 3, 5, and 9, with only domain 5 exhibiting a marked preference for phosphodiester-containing lysosomal enzymes. To determine how the CI-MPR recognizes phosphodiesters, the structure of domain 5 was determined by NMR spectroscopy. Although domain 5 contains only three of the four disulfide bonds found in the other seven domains whose structures have been determined to date, it adopts the same fold consisting of a flattened β-barrel. Structure determination of domain 5 bound to N-acetylglucosaminyl 6-phosphomethylmannoside, along with mutagenesis studies, revealed the residues involved in diester recognition, including Y679. These results show the mechanism by which the CI-MPR recognizes Man-P-GlcNAc-containing ligands and provides new avenues to investigate the role of phosphodiester-containing lysosomal enzymes in the biogenesis of lysosomes