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Search: L773:1567 7249

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  • Bentinger, M, et al. (author)
  • The antioxidant role of coenzyme Q
  • 2007
  • In: Mitochondrion. - : Elsevier BV. - 1567-7249. ; 7, s. Suppl:S41-50
  • Journal article (peer-reviewed)
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  • Björkman, Kristoffer, et al. (author)
  • Broad phenotypic variability in patients with complex I deficiency due to mutations in NDUFS1 and NDUFV1.
  • 2015
  • In: Mitochondrion. - : Elsevier BV. - 1872-8278 .- 1567-7249. ; 21, s. 33-40
  • Journal article (peer-reviewed)abstract
    • We report clinical, metabolic, genetic and neuroradiological findings in five patients from three different families with isolated complex I deficiency. Genetic analysis revealed mutations in NDUFS1 in three patients and in NDUFV1 in two patients. Four of the mutations are novel and affect amino acid residues that either are invariant among species or conserved in their properties. The presented clinical courses are characterized by leukoencephalopathy or early death and expand the already heterogeneous phenotypic spectrum. A literature review was performed, showing that patients with mutations in NDUFS1 in general have a worse prognosis than patients with mutations in NDUFV1.
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  • Bykova, Natalia V., et al. (author)
  • The function of glycine decarboxylase complex is optimized to maintain high photorespiratory flux via buffering of its reaction products
  • 2014
  • In: Mitochondrion (Amsterdam. Print). - : Elsevier BV. - 1567-7249 .- 1872-8278. ; 19, s. 357-364
  • Journal article (peer-reviewed)abstract
    • Oxidation of glycine in photorespiratory pathway is the major flux through mitochondria of C3 plants in the light. It sustains increased intramitochondrial concentrations of NADH and NADPH, which are required to engage the internal rotenone-insensitive NAD(P)H dehydrogenases and the alternative oxidase. We discuss here possible mechanisms of high photorespiratory flux maintenance in mitochondria and suggest that it is fulfilled under conditions where the concentrations of glycine decarboxylase reaction products NADH and CO2 achieve an equilibrium provided by malate dehydrogenase and carbonic anhydrase, respectively. This results in the removal of these products from the glycine decarboxylase multienzyme active sites and in the maintenance of their concentrations at levels sufficiently low to prevent substrate inhibition of the reaction. 
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  • Cochemé, Helena M, et al. (author)
  • Mitochondrial targeting of quinones: therapeutic implications.
  • 2007
  • In: Mitochondrion. - : Elsevier BV. - 1567-7249. ; 7 Suppl
  • Research review (peer-reviewed)abstract
    • Mitochondrial oxidative damage contributes to a range of degenerative diseases. Ubiquinones have been shown to protect mitochondria from oxidative damage, but only a small proportion of externally administered ubiquinone is taken up by mitochondria. Conjugation of the lipophilic triphenylphosphonium cation to a ubiquinone moiety has produced a compound, MitoQ, which accumulates selectively into mitochondria. MitoQ passes easily through all biological membranes and, because of its positive charge, is accumulated several hundred-fold within mitochondria driven by the mitochondrial membrane potential. MitoQ protects mitochondria against oxidative damage in vitro and following oral delivery, and may therefore form the basis for mitochondria-protective therapies.
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