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  • Book
    Paulo J. Oliveira, editor.
    Summary: This book addresses the therapeutic strategies to target mitochondrial metabolism in diseases where the function of that organelle is compromised, and it discusses the effective strategies used to create mitochondrial-targeted agents that can become commercially available drug delivery platforms. The consistent growth of research focused in understanding the multifaceted role of mitochondria in cellular metabolism, controlling pathways related with cell death, and ionic/redox regulation has extended the research of mitochondrial chemical-biological interactions to include various pharmacological and toxicological applications. Not only does the book extensively cover basic mitochondrial physiology, but it also links the molecular interactions within these pathways to a variety of diseases. It is one of the first books to combine state-of-the-art reviews regarding basic mitochondrial biology, the role of mitochondrial alterations in different diseases, and the importance of that organelle as a target for pharmacological and non-pharmacological interventions to improve human health. The different chapters highlight the chemical-biological linkages of the mitochondria in context with drug development and clinical applications.

    Contents:
    Intro; Foreword; Contents; Part I: Mitochondrial Biology; Introduction: Mitochondria, the Cell Furnaces; References; Mitochondria: Where Are They Coming From?; 1 Introduction; 2 Problems and Controversies Regarding the Precise Bacterial Origin of Mitochondria; 3 Integrated Approaches to Identify Possible Relatives of Proto-mitochondria; 4 Conclusion; References; Mitochondrial Dynamics: A Journey from Mitochondrial Morphology to Mitochondrial Function and Quality; 1 Mitochondrial Fusion and Fission: Shaping the Mitochondrial Network; 1.1 Mitochondrial Fusion. 1.1.1 Mitochondrial Fusion Proteins1.1.2 Regulation of Mitochondrial Fusion; 1.2 Mitochondrial Fission; 1.2.1 Mitochondrial Fission Proteins; 1.2.2 Regulation of Mitochondrial Fission; 2 Mitochondrial Dynamics Regulates Mitochondrial Function and Quality; 2.1 Regulation of Mitochondrial Function by Mitochondrial Dynamics; 2.2 Regulation of Mitochondrial Quality by Mitochondrial Dynamics; References; Mitochondria and Ageing; 1 The Free Radical Theory of Ageing. The Mitochondrial Free Radical Theory of Ageing as Proposed by Miquel; 2 Mitochondrial Disruption of Cell Signalling in Ageing. 2 Mitochondria Contribute to the Progression of Liver Disease3 Mitochondria Changes in Liver Diseases; 3.1 Non-alcoholic Fatty Liver Disease (NAFLD); 3.2 Alcoholic Liver Disease (ALD); 3.3 Hepatitis C Virus (HCV) Infection; 3.4 Hemochromatosis; 3.5 Wilson's Disease; 3.6 Chronic Cholestatic Disorders; 4 Assessment of Liver Mitochondrial Function In Vivo; 4.1 Respiratory Chain Activity; 4.2 Alpha-Ketoacid Dehydrogenase; 4.3 Octanoic Acid; 4.4 Benzoic Acid; 4.5 Urea Production; 4.6 [31P] Nuclear Magnetic Resonance Spectroscopy; 5 Conclusions; References. 3 Mitochondrial DNA Is More Susceptible to Damage than Nuclear DNA4 Mitochondria Are Damaged Inside Cells; 5 Sex Differences in Free Radical Production and Its Relationship with Longevity; 6 Mitochondrial Diseases; 7 Toxicological Aspects: The Treatment of AIDS with Zidovudine Causes Mitochondrial Pathology that Explains Muscle Damage Associated with AIDS Treatment; 8 Alzheimer's Disease; References; The Mitochondrial Permeability Transition Pore; 1 Mitochondrial Permeability Transition; 2 Mitochondrial Permeability Transition Pore Complex: Molecular Structure; 2.1 Regulatory Components. 3 Pathological Relevance3.1 Ischemia/Reperfusion Injury; 3.2 Cancer; 3.3 Neurodegenerative Diseases; 4 Conclusions; References; Mitochondrial Regulation of Cell Death; 1 Introduction; 2 Mitochondrial Reactive Oxygen Species and Mitochondrial Dysfunction; 3 Mitochondrial Calcium as a Trigger of Cell Death; 4 BCL-2 Family Members; 5 Mitochondrial Intermembrane Space Proteins; 6 Mitophagy; 6.1 Molecular Mechanisms; 6.2 Mitophagy, Cell Death or Cytoprotection; 7 Conclusion and Perspectives; References; Mitochondria in Liver Diseases; 1 Introduction.
    Digital Access Springer 2018
  • Article
    Schottel JL.
    J Biol Chem. 1978 Jun 25;253(12):4341-9.
    Two separate enzymes, which determine resistance to inorganic mercury and organomercurials, have been purified from the plasmid-bearing Escherichia coli strain J53-1(R831). The mercuric reductase that reduces Hg2+ to volatile Hg0 was purified about 240-fold from the 160,000 X g supernatant of French press disrupted cells. This enzyme contains bound FAD, requires NADPH as an electron donor, and requires the presence of a sulfhydryl compound for activity. The reductase has a Km of 13 micron HgCl2, a pH optimum of 7.5 in 50 mM sodium phosphate buffer, an isoelectric point of 5.3, a Stokes radius of 50 A, and a molecular weight of about 180,000. The subunit molecular weight, determined by gel electrophoresis in the presence of sodium dodecyl sulfate, is about 63,000 +/- 2,000. These results suggest that the native enzyme is composed of three identical subunits. The organomercurial hydrolase, which breaks the mercury-carbon bond in compounds such as methylmercuric chloride, phenylmercuric acetate, and ethylmercuric chloride, was purified about 38-fold over the starting material. This enzyme has a Km of 0.56 micron for ethylmercuric chloride, a Km of 7.7 micron for methylmercuric chloride, and two Km values of 0.24 micron and over 200 micron for phenylmercuric acetate. The hydrolase has an isoelectric point of 5.5, requires the presence of EDTA and a sulfhydryl compound for activity, has a Stokes radius of 24 A, and has a molecular weight of about 43,000 +/- 4,000.
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