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This book addresses main issues concerned with the future learning, learning and academic analytics, virtual world and smart user interface, and mobile learning. This book gathers the newest research results of smart learning environments from the aspects of learning, pedagogies, and technologies in learning. It examines the advances in technology development and changes in the field of education that has been affecting and reshaping the learning environment. Then, it proposes that under the changed technological situations, smart learning systems, no matter what platforms (i.e., personal computers, smart phones, and tablets) they are running at, should be aware of the preferences and needs that their users (i.e., the learners and teachers) have, be capable of providing their users with the most appropriate services, helps to enhance the users' learning experiences, and to make the learning efficient.

Education. --- Educational Technology. --- Education --- Artificial intelligence -- Educational applications. --- Computer-assisted instruction. --- Educational innovations. --- Educational technology. --- Social Sciences --- Education, Special Topics --- Artificial intelligence --- Educational applications. --- Instructional technology --- Technology in education --- Innovations, Educational --- Technological change in education --- Innovations --- Technological innovations --- Technology --- Educational innovations --- Instructional systems --- Teaching --- Children --- Education, Primitive --- Education of children --- Human resource development --- Instruction --- Pedagogy --- Schooling --- Students --- Youth --- Civilization --- Learning and scholarship --- Mental discipline --- Schools --- Training --- Aids and devices --- Educational planning --- Educational change --- Educational technology --- Experimental methods --- Data processing

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Lasso peptides form a growing family of fascinating ribosomally-synthesized and post-translationally modified peptides produced by bacteria. They contain 15 to 24 residues and share a unique interlocked topology that involves an N-terminal 7 to 9-residue macrolactam ring where the C-terminal tail is threaded and irreversibly trapped. The ring results from the condensation of the N-terminal amino group with a side-chain carboxylate of a glutamate at position 8 or 9, or an aspartate at position 7, 8 or 9. The trapping of the tail involves bulky amino acids located in the tail below and above the ring and/or disulfide bridges connecting the ring and the tail. Lasso peptides are subdivided into three subtypes depending on the absence (class II) or presence of one (class III) or two (class I) disulfide bridges. The lasso topology results in highly compact structures that give to lasso peptides an extraordinary stability towards both protease degradation and denaturing conditions. Lasso peptides are generally receptor antagonists, enzyme inhibitors and/or antibacterial or antiviral (anti-HIV) agents. The lasso scaffold and the associated biological activities shown by lasso peptides on different key targets make them promising molecules with high therapeutic potential. Their application in drug design has been exemplified by the development of an integrin antagonist based on a lasso peptide scaffold. The biosynthesis machinery of lasso peptides is therefore of high biotechnological interest, especially since such highly compact and stable structures have to date revealed inaccessible by peptide synthesis. Lasso peptides are produced from a linear precursor LasA, which undergoes a maturation process involving several steps, in particular cleavage of the leader peptide and cyclization. The post-translational modifications are ensured by a dedicated enzymatic machinery, which is composed of an ATP-dependent cysteine protease (LasB) and a lactam synthetase (LasC) that form an enzymatic complex called lasso synthetase. Microcin J25, produced by Escherichia coli AY25, is the archetype of lasso peptides and the most extensively studied. To date only around forty lasso peptides have been isolated, but genome mining approaches have revealed that they are widely distributed among Proteobacteria and Actinobacteria, particularly in Streptomyces, making available a rich resource of novel lasso peptides and enzyme machineries towards lasso topologies.

Biomedicine. --- Medical Microbiology. --- Immunology. --- Vaccine. --- Medicine. --- Microbiology. --- Vaccines. --- Médecine --- Immunologie --- Microbiologie --- Vaccins --- Peptides --- Bacteria --- Protein Modification, Translational --- Complex Mixtures --- Proteins --- Biological Science Disciplines --- Amino Acids, Peptides, and Proteins --- Protein Biosynthesis --- Chemicals and Drugs --- Natural Science Disciplines --- Peptide Biosynthesis --- Disciplines and Occupations --- Biochemical Processes --- Biochemical Phenomena --- Chemical Phenomena --- Phenomena and Processes --- Bacterial Proteins --- Physiology --- Biological Products --- Protein Processing, Post-Translational --- Biology --- Health & Biological Sciences --- Microbiology & Immunology --- Structure --- Synthesis --- Physiological effect --- Peptide antibiotics. --- Antimicrobial peptides --- Medical microbiology. --- Antibiotics --- Biologicals --- Immunobiology --- Life sciences --- Serology --- Microbial biology --- Microorganisms