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  • Book
    Hongzhi Sun, Xiangdong Wang, editors.
    Contents:
    1. How far can mitochondrial DNA drive the disease?
    2. Mitochondrial DNA in lung cancer
    3. Approach, application, and bioethics of mtDNA sequencing in cancer
    4. Roles of mitochondrial DNA signaling in immune responses
    5. Mitochondrial DNA in telocytes
    6. Roles of mitochondrial DNA in energy metabolism
    7. The role of DNA repair in maintaining mitochondrial DNA stability
    8. Is mitochondrial cell fragility a cell weakness?
    9. Mitochondrial DNA methylation and related disease
    10. Beyond deubiquitylation: USP30-mediated regulation of mitochondrial homeostasis
    11. Metabolic regulation in mitochondria and drug resistance
    12. Mitochondrial lon protease and cancer
    13. Regulatory roles of mitochondrial ribosome in lung diseases and single cell biology
    14. Epithelial mitochondrial dysfunction in lung disease
    15. Significance of mitochondria DNA mutations in diseases.
    Digital Access Springer 2017
  • Article
    Suter P, Rosenbusch JP.
    J Biol Chem. 1977 Nov 25;252(22):8136-41.
    The allosteric effectors of aspartate transcarbamoylase from Escherichia coli, CTP and ATP, associate with both the regulatory and the catalytic moieties of the enzyme. Studies with isolated, active subunits yield one binding site per regulatory dimer and one per catalytic trimer. Investigations of effector association with hybrid enzymes, containing either the three regulatory dimers or the two catalytic trimers in inactivated forms, indicate that the data obtained with isolated subunits can be used to analyze the binding patterns of these ligands to the native hexamer. Thus, the nonlinear Scatchard plots, characteristic of the binding of CTP and ATP to the native enzyme, can be interpreted in terms of three effector molecules associating with the regulatory subunits, and two binding to the catalytic moiety of the enzyme. Results with native protein in the presence of saturating concentrations of active site ligands support these assignments. The differences between the binding isotherms of CTP and ATP to the enzyme are due to their different affinities to the two types of subunits. The apparent half-of-the-site saturation of the regulatory moiety of aspartate transcarbamoylase supports the concept that this protein has a tendency to exist in an asymmetric state.
    Digital Access Access Options