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- Bookedited 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 - ArticleGupta 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.