ArticleMolecular and cellular biochemistry2000
Hexokinase 'binding sites' of normal and tumoral human brain mitochondria.
Article in Molecular and cellular biochemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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
5 citing papers in PubMed, 9 citations in OpenAlex.
- The structural and functional coordination of glycolytic enzymes in muscle: evidence of a metabolon?Biology · 2014Review
- Mitochondrial metabolism inhibitors for cancer therapy.Pharmaceutical research · 2011Review
- Glucose phosphorylation and mitochondrial binding are required for the protective effects of hexokinases I and II.Molecular and cellular biology · 2008Article
- A study on the two binding sites of hexokinase on brain mitochondria.BMC biochemistry · 2007Article
- Interaction of hexokinase with the outer mitochondrial membrane and a hydrophobic matrix.Molecular and cellular biochemistry · 2001Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interaction of type I hexokinase (HK-I) with the mitochondria obtained from the biopsy specimens of normal and tumoral human brain tissues was studied in the present investigation. This effort was undertaken with the aim of exploring possible differences in the mode of association of the enzyme with the outer mitochondrial membrane in the described sources. Results indicate that the two 'sites' for binding of HK-I suggested in the literature, based on extensive studies carried out on rat brain mitochondria, are similarly present in the human brain mitochondria. Differences in the microenvironments of HK binding, as reflected by the presented data, are suggested to be of importance in regulation of the catalytic potential of the bound enzyme. The real metabolic significance of this association in relation to cancer and its practical importance would need further investigation.
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