Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
YeastPathways to GO-CAM conversion
Subunit interactions of yeast NAD+-specific isocitrate dehydrogenase.
Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.
Kinetic and physiological effects of alterations in homologous isocitrate-binding sites of yeast NAD(+)-specific isocitrate dehydrogenase.
Subcellular localization of the yeast proteome.
The proteome of Saccharomyces cerevisiae mitochondria.
Proteome survey reveals modularity of the yeast cell machinery.
Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.
Novel allosteric properties produced by residue substitutions in the subunit interface of yeast NAD+-specific isocitrate dehydrogenase.
Allosteric motions in structures of yeast NAD+-specific isocitrate dehydrogenase.
Micropreparative fractionation of the complexome by blue native continuous elution electrophoresis.
Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae.
Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae.
The social and structural architecture of the yeast protein interactome.
Molecular genetics of yeast TCA cycle isozymes.
Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RNA-binding protein.
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The mitochondrial mRNA 5'-leader binding protein p40 is NAD-IDH, and RNA binding needs both Idh1 and Idh2.
"Both enzyme and RNA-binding activities are specifically lost in cells containing disruptions in either IDH1 or IDH2"
Allosteric inhibition of NAD+-specific isocitrate dehydrogenase by a mitochondrial mRNA.
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Mitochondrial mRNA 5'-UTR transcripts inhibit IDH activity, and AMP relieves the inhibition.
"These results suggest that inhibition of activity is relatively specific for the 5'-untranslated regions of mitochondrial mRNAs."
Analysis of interactions with mitochondrial mRNA using mutant forms of yeast NAD(+)-specific isocitrate dehydrogenase.
SGD gene description for IDH2 (yeast)