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  • Book
    edited by Eric Marsault, University of Sherbrooke, Quebec, Canada, Mark L. Peterson, Quebec, Canada.
    Contents:
    1. Contemporary macrocyclization technologies
    2. A practical guide to structural aspects of macrocyles (NMR, X-Ray and Modeling)
    3. Designing orally bioavailable peptide and peptoid macrocycles
    4. Natural and nature-inspired macrocycles: a chemoinformatic overview and relevant examples
    5. Bioactive and membrane-permeable cyclic peptide natural products
    6. Chemical approaches to macrocycle libraries
    7. Biological and hybrid biological/chemical strategies in diversity generation of peptidic macrocycles
    8. Macrocycles for protein-protein interactions
    9. Synthetic strategies for macrocyclic peptides
    10. Ring-closing metathesis-based methods in chemical biology: building a natural product-inspired macrocyclic toolbox to tackle protein-protein interactions
    11. the synthesis of peptide-based macrocycles by Huisgen Cycloaddition
    12. Palladium-catalyzed synthesis of macrocycles
    13. Alternative strategies for the construction of macrocycles
    14. Macrocycles from multicomponent reactions
    15.Synthetic approaches used in the scale-up of macrocyclic clinical candidates
    16. Overview of macrocycles in cllinical development and clinically used
    17. The discovery of macrocyclic IAP inhibitors for the treatment of cancer
    18. Discovery and pharmacokietic-pharmacodynamic evaluation of an orally available novel macrocyclic inhibitor of anaplastic lymphoma kinase and c-Ros oncogene 1
    19. Optimization of macrocyclic ghrelin receptor agonist (Part II): development of TZP-102
    20. Solithromycin: fourth generation macrolide antibiotic
    Index.
    Digital Access Wiley 2017
  • Article
    Gupta RS, Kasai T, Schlessinger D.
    J Biol Chem. 1977 Dec 25;252(24):8945-9.
    RNase II of Escherichia coli (EC 3.1.4.23) has been purified to apparent homogeneity. The K+-activated diesterase activity against poly(U), which defines RNase II, cochromatographs with activity against T4 mRNA or pulse-labeled E. coli RNA successively on DEAE-cellulose, hydroxyapatite or phosphocellulose, and Sephadex G-150 columns. Activities with both substrates are selectively reduced to less than 2% of the wild type level in a newly isolated mutant strain, S296, or after thermal inactivation in a mutant strain with temperature-sensitive RNase II. RNase II releases 5'-XMP without a lag as its only detectable alcohol-soluble produce from all substrates and has an apparent molecular weight of 80,000 to 90,000 in both nondissociating and sodium dodecyl sulfate-polyacrylamide gels. The pure enzyme shows the standard K+ activation against poly(A), poly(U), or poly(C), but only a slight preference for K+ over Na+ ions with T4 mRNA or pulse labeled E. coli RNA as substrate. Uniformly labeled E. coli rRNA or tRNA is degraded little if at all.
    Digital Access Access Options