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First group to discover the expression of the human CHCHD4 isoforms and first to call the human gene CHCHD4, and to clone and show the expression of its alternatively expressed CHCHD4 isoforms (CHCHD4.1 and CHCHD4.2).
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Compared to wild type control littermates, mice with a knockout of CHCHD4 exhibit reduced weight gain when fed a high-fat diet.
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Data show that the redox state of cytochrome c oxidase assembly protein 17 (Cox17), mitochondrial membrane transport protein Mia40 and superoxide dismutase 1 (SOD1) in the cytoplasm were directly observed with in-cell NMR spectroscopy.
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our findings suggest that MIA40 reduction contributes to the effects of AIF deficiency on OXPHOS, as it may impact on the correct assembly and maintenance of the respiratory subunits.
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results demonstrate an indispensable role for hMIA40 for the export of Fe-S clusters from mitochondria.
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Data indicate that poptosis-inducing factor (AIF) controls the mitochondrial import of mitochondrial membrane transport protein CHCHD4.
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In aggregate these data suggest that the Mia40/lfALR system has a broad sequence specificity and that potential substrates may be protected from adventitious oxidation by kinetic sequestration within the mitochondrial IMS.
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Import and oxidative folding of proteins are kinetically and functionally coupled and depend on the expression of Mia40, ALR, and the intracellular glutathione pool.
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Data indicate that decreased CHCHD4 expression prevents the mitochondrial translocation of p53 while augmenting its nuclear localization and activity.
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illustrate a very atypical behaviour for the Mia40 precursor compared to other substrates of the MIA pathway. By contrast, interaction with Erv1 occurs after 5 min of import and relies on a more stringent specificity
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mitochondrial localization of MIA40 requires sulfhydryl oxidase ALR in heterologous expression yeast system.
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Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR.
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biogenesis and function of MIA40 in the mitochondrial intermembrane space is dependent on redox processes involving conserved cysteine residues
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After passage across the translocase of the mitochondrial outer membrane Erv1 interacts via disulfide bonds with Mia40.
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analysis of how mitochondrial biogenesis switches the sorting pathway of the intermembrane space receptor Mia40
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Catalysis involves a flow of reducing equivalents from the reduced CxC cysteine motif of Mia40 to distal and then proximal CxxC motifs of long-form ALR to the flavin ring and, finally, to cytochrome c or molecular oxygen.
