ArticleThe Biochemical journal1994
Regulation of oxidative degradation of L-lysine in rat liver mitochondria.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 26 citations in OpenAlex.
- Gestational age and models for predicting gestational diabetes mellitus.Metabolomics : Official journal of the Metabolomic Society · 2025Observational
- A Systematic Review of Oxidative Stress Markers and Risk of Coronary Artery Calcification.The journal of Tehran Heart Center · 2024Review
- Advanced Glycation End Products, Oxidation Products, and the Extent of Atherosclerosis During the VA Diabetes Trial and Follow-up Study.Diabetes care · 2017Article
- Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn.Protein science : a publication of the Protein Society · 2009Article
- Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse.The Biochemical journal · 1999Article
- Purification and Characterization of the Bifunctional Enzyme Lysine-Ketoglutarate Reductase-Saccharopine Dehydrogenase from Maize.Plant physiology · 1996Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The generation of 14CO2 from [1-14C]lysine by hepatic mitochondria through the saccharopine pathway is controlled by intramitochondrial concentrations of lysine, 2-oxoglutarate and NADPH. Mitochondria, isolated from rats pre-treated with glucagon, exhibited higher activities of L-lysine: 2-oxoglutarate reductase, saccharopine dehydrogenase and 2-aminoadipate aminotransferase. The flux through this pathway is stimulated in liver mitochondria after glucagon treatment. Multiple regulation of lysine oxidation in liver mitochondria confirms a complex mechanism of 'mitochondrial activation' by glucagon.
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Registered trials
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