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Literature summary for 1.8.1.4 extracted from

  • Way, L.; Faktor, J.; Dvorakova, P.; Nicholson, J.; Vojtesek, B.; Graham, D.; Ball, K.L.; Hupp, T.
    Rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein-protein interactions by the MDM2 ligand nutlin-3 (2016), Proteomics, 16, 2327-2344 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.1.4

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli strain BL21(DE3) Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information Nutlin-3 inhibits mitochondrial activity Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P09622
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
HCT-116 cell immunochemical analysis of dihydrolipoamide dehydrogenase protein levels Homo sapiens
-

Synonyms

Synonyms Comment Organism
dihydrolipoamide dehydrogenase
-
 Homo sapiens
E3
-
 Homo sapiens

Expression

Organism Comment Expression
Homo sapiens the full-length isoform of dihydrolipoamide dehydrogenase is induced by Nutin-3, while the shorter isoform of dihydrolipoamide dehydrogenase is downregulated by Nutlin-3, immunochemical analysis of dihydrolipoamide dehydrogenase protein levels after MDM2 perturbation, verview down
Homo sapiens the full-length isoform of dihydrolipoamide dehydrogenase is induced by Nutin-3, while the shorter isoform of dihydrolipoamide dehydrogenase is downregulated by Nutlin-3, immunochemical analysis of dihydrolipoamide dehydrogenase protein levels after MDM2 perturbation, overview. Depletion of MDM2 using siRNA elevates dihydrolipoamide dehydrogenase in Nutlin-3-treated cells. An increase in MDM2/dihydrolipoamide dehydrogenase complexes in the nucleus is further enhanced by the nuclear export inhibitor Leptomycin B up

General Information

General Information Comment Organism
physiological function dihydrolipoamide dehydrogenase is the E3 subunit of the mitochondrial pyruvate dehydrogenase complex, rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein-protein interactions by the MDM2 ligand nutlin-3 Homo sapiens