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  • Book
    Andres Trostchansky, Homero Rubbo, editors.
    Summary: The purpose of this book is to introduce the readers on the perspective of the role that unsaturated fatty acids and complex lipids play on health and disease. Bioactive lipids can be modified affecting membrane composition, structure and fluidity in addition to changes in cell signaling associated to lipid-protein (membrane receptors) interactions, issues that are addressed by the authors. This book analyzes key topics involving bioactive lipids and their role in normal signaling and the mechanisms of disease. The book navigates from structural studies of oxidized and non-oxidized lipids to the reactions and cell signaling processes that bioactive lipids play in cardiovascular and neurodegenerative diseases. The book contains the recent advances reported in the literature about lipidomics as well as the role that lipid-derived compounds exert on unfolded protein response and lipid metabolism and disease. This book represents a state of the art introduction to lipid metabolism from a biochemical to an in vivo overview being an useful tool for students and investigators. We hope the mechanistic observations on the role of bioactive lipids in health and disease serve a perspective to improve the existing treatments or propose new lipid-based pharmacology.

    Contents:
    Intro; Preface; Contents; Part I: Structure, Characterization and Physicochemical Properties of Bioactive Lipids;
    1: Diffusion and Transport of Reactive Species Across Cell Membranes; 1.1 Cellular Membranes; 1.2 Diffusion Across Membranes; 1.3 The Permeability Coefficient; 1.4 Interactions of Reactive Species with Membranes; 1.4.1 Oxygen; 1.4.2 Singlet Oxygen; 1.4.3 Nitric Oxide; 1.4.4 Nitrogen Dioxide; 1.4.5 Hydrogen Sulfide; 1.4.6 Peroxynitrite Anion and Peroxynitrous Acid; 1.4.7 Superoxide and Hydroperoxyl Radical; 1.4.8 Hydrogen Peroxide; 1.4.9 Hydroxyl Radical 1.5 Considerations About the Permeability of Membranes to Reactive SpeciesReferences;
    2: Characterization of Hydroxy and Hydroperoxy Polyunsaturated Fatty Acids by Mass Spectrometry; 2.1 Introduction; 2.2 Fatty Acid Hydroperoxide Formation; 2.3 Hydroperoxide- and Hydroxy-Polyunsaturated Fatty Acids Analysis; 2.3.1 Characterization of Linoleic Acid Hydro(pero)xides; 2.3.2 Characterization of Arachidonic Acid Hydro(pero)xides; 2.3.3 Characterization of Eicosapentaenoic Acid Hydro(pero)xides; 2.3.4 Characterization of Docosahexaenoic Acid Hydro(pero)xides; 2.4 Conclusion; References
    4: Diminishing Inflammation by Reducing Oxidant Generation: Nitrated Fatty Acid-Mediated Inactivation of Xanthine Oxidoreductase4.1 Xanthine Oxidoreductase (XOR); 4.2 Shortcomings Associated with Allo/Oxypurinol Inhibition of XOR; 4.3 Nitrated Fatty Acids; 4.4 OA-NO2 and LNO2 Inactivate XOR; 4.5 XOR-Endothelium Interaction Does not Affect Inactivation by OA-NO2; References;
    5: Unfolded Protein Response: Cause or Consequence of Lipid and Lipoprotein Metabolism Disturbances?; 5.1 Introduction; 5.2 The Unfolded Protein Response 5.3 From the Unfolded Protein Response to Lipid Metabolism Disturbances5.4 From Lipotoxicity to Unfolded Protein Response; 5.5 Closing Remarks and Perspectives; References; Part III: Bioactive Lipids in Inflammatory and Cardiovascular Diseases;
    6: Arachidonic Acid and Nitroarachidonic: Effects on NADPH Oxidase Activity; 6.1 Introduction; 6.2 Arachidonic Acid Metabolism in Macrophage Activation; 6.3 NADPH Oxidase 2 Activation; 6.4 Activation of NOX2 by Arachidonic Acid; 6.5 Inhibition of NOX2 by Nitroarachidonic Acid; 6.6 Summary; References
    Digital Access Springer 2019
  • Article
    Kastrup RV, Schmidt PG.
    Nucleic Acids Res. 1978 Jan;5(1):257-69.
    Methyl and methylene protons of dihydrouridine 17 (hU), 6-methyladenosine 37 (M6A), 7-methylguanosine 46 (m7G), and ribothymidine 54 (rT) give clearly resolved peaks (220 MHz) for tRNA1val (coli solutions in D2O, 0.25 m NaCl, at 27 degrees C. Chemical shifts are generally consistent with a solution structure of tRNA1val similar to the crystal structure of tRNAphe (yeast). At least 3 separate transitions are observed as the temperature is raised. The earliest involves disruption of native tertiary structure and formation of intermediate structures in the m7G and rT regions. A second transition results in a change in structure of the anticodon loop, containing m6A. The final step involves unfolding of the m7G and rT intermediates and melting of the TpsiC helix. Low salt concentrations produce multiple, partially denatured conformations, rather than a unique form, for tRNA1val. Native structure is almost completely reformed by addition of Na+ but Mg2+ is required for correct conformation in the vicinity of m7G.
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