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
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space.
MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria.
Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import.
Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells.
Mitochondrial disulfide relay mediates translocation of p53 and partitions its subcellular activity.
Interaction between AIF and CHCHD4 Regulates Respiratory Chain Biogenesis.
The Ca(2+)-Dependent Release of the Mia40-Induced MICU1-MICU2 Dimer from MCU Regulates Mitochondrial Ca(2+) Uptake.
Mutations in the accessory subunit NDUFB10 result in isolated complex I deficiency and illustrate the critical role of intermembrane space import for complex I holoenzyme assembly.
Inhibition of proteasome rescues a pathogenic variant of respiratory chain assembly factor COA7.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
A two-step mitochondrial import pathway couples the disulfide relay with matrix complex I biogenesis.
Falcon deep research report for CHCHD4
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Falcon research supports CHCHD4/MIA40 as the central mitochondrial intermembrane-space oxidoreductase/import receptor for the MIA disulfide relay.
"CHCHD4 is defined as the IMS-localized oxidoreductase/import receptor that recognizes IMS-targeting signals in substrates, forms a transient intermolecular disulfide with substrates via its CPC motif, and catalyzes formation of intramolecular disulfides."