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The human NDUFA1 gene codes for an essential component of complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. Additionally we are shipping NDUFA1 Proteins (7) and many more products for this protein.
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In an X-chromosome linked model for partial Complex I deficiency, Ndufa1 mutant males displayed reduced respiratory exchange and produced less body heat.
Species-specific and mutant MWFE proteins effect on the assembly of a functional mammalian mitochondrial complex I.
The gene signature of OPA1 (show OPA1 Antibodies), CTSA (show CTSA Antibodies), NDUFA1, STK10 and PRDX1 (show PRDX1 Antibodies) was able to identify patients post-implant with a sensitivity of 91% and a specificity of 86% in discrimination between post-implant group and healthy controls.
Fanconi anemia complementation group A (show FANCA Antibodies) mutants show defective respiration through Complex I, diminished ATP production and metabolic sufferance with an increased AMP (show APRT Antibodies)/ATP ratio.
Heterozygous mutation in the X chromosomal NDUFA1 gene in a girl with complex I deficiency
Mutations in the NDUFA1 gene is linked to a delayed mitochondrial network recovery in OXPHOS disorders.
A family-based association study finds that the NDUFA1 gene is unlikely to harbor a major visual loss susceptibility locus for Leber hereditary optic neuropathy.
Suppression of NDUFA1 expression could represent a key pathogenic mechanism in the development of basal cell carcinoma
Two novel p.Gly8Arg and p.Arg37Ser hemizygous mutations in NDUFA1 were identified in two unrelated male patients presenting with Leigh's syndrome and with myoclonic epilepsy and developmental delay.
hypothesize that the novel G32R mutation in NDUFA1 is causing complex I deficiency either by itself or in synergy with additional mtDNA variants
subunit MWFE is required for assembly into complex I of seven hydrophobic subunits encoded in the mitochondrial genome
The human NDUFA1 gene codes for an essential component of complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha-helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and might act as an anchor for the NADH:ubiquinone oxidoreductase complex at the inner mitochondrial membrane. However, the NDUFA1 peptide is one of about 31 components of the 'hydrophobic protein' (HP) fraction of complex I which is involved in proton translocation. Thus the NDUFA1 peptide may also participate in that function.
, NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 1 (7.5kD, MWFE)
, NADH dehydrogenase 1 alpha subcomplex, 1
, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
, NADH ubiquinone oxidoreductase subunit MWFE
, NADH-ubiquinone oxidoreductase MWFE subunit
, complex I-MWFE
, Complex I-MWFE
, NADH ubiquinone oxidoreductase NDUFA1
, NADH oxidoreductase subunit MWFE
, NADH:ubiquinone oxidoreductase (complex 1)
, complex I MWFE subunit
, type I dehydrogenase