Christ\u27s Teaching On Prayer

https://digitalcommons.acu.edu/crs_books/1574/thumbnail.jp

The Old Paths

https://digitalcommons.acu.edu/crs_books/1385/thumbnail.jp

Services surround you:physical-virtual linkage with contextual bookmarks

Our daily life is pervaded by digital information and devices, not least the common mobile phone. However, a seamless connection between our physical world, such as a movie trailer on a screen in the main rail station and its digital counterparts, such as an online ticket service, remains difficult. In this paper, we present contextual bookmarks that enable users to capture information of interest with a mobile camera phone. Depending on the user’s context, the snapshot is mapped to a digital service such as ordering tickets for a movie theater close by or a link to the upcoming movie’s Web page

Reversible inhibition of cathepsin L-like proteases by 4-mer pseudopeptides

AbstractA library of 121 pseudopeptides was designed to develop reversible inhibitors of trypanosomal enzymes (cruzain from Trypanosoma cruzi and congopain from Trypanosoma congolense). The peptides share the framework: Cha-X1-X2-Pro (Cha=cyclohexyl-alanine, X1 and X2 were phenylalanyl analogs), based on a previous report [Lecaille, F., Authié, E., Moreau, T., Serveau, C., Gauthier, F. and Lalmanach, G. (2001) Eur. J. Biochem. 268, 2733–2741]. Five peptides containing a nitro-substituted aromatic residue (Tyr/Phe) and one a 4-chloro-phenylalanine at the X1 position, and 3-(2-naphthyl)-alanine, homocyclohexylalanine or 3-nitro-tyrosine (3-NO2-Tyr) at the X2 position, were selected. They inhibited congopain more effectively than cruzain, except Cha-4-NO2-Phe-3-NO2-Tyr-Pro which bound the two parasitic enzymes similarly. Among this series, Cha-3-NO2-Tyr-HoCha-Pro and Cha-4-NO2-Phe-3-NO2-Tyr-Pro are the most selective for congopain relative to host cathepsins. No hydrolysis occurred upon prolonged incubation time with purified enzymes. In addition introduction of non-proteogenic residues in the peptidyl backbone greatly enhanced resistance to proteolysis by mammalian sera