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The protein encoded by NDUFS1 belongs to the complex I 75 kDa subunit family. Additionally we are shipping NDUFS1 Antibodies (80) and NDUFS1 Kits (6) and many more products for this protein.
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lysosomal membrane permeability induced by TNFalpha (show TNF Proteins) plus cycloheximide, the release of lysosomal cathepsins and reactive oxygen species formation require the caspase-3 (show CASP3 Proteins)-mediated cleavage of the p75 (show NGFR Proteins) NDUFS1 subunit of respiratory complex I.
High NDUFS1 expression is associated with cognitive impairment in lung cancer.
Results found nominal significant associations of 2 SNPs in the NDUFS1 gene and 4 SNPs in the NDUFS2 (show NDUFS2 Proteins) gene with early onset schizophrenia (EOS (show IKZF4 Proteins)), but none of these associations survived the Bonferroni correction.
Loss of FOXRED1 (show FOXRED1 Proteins), coupled with protein, choline and/or folate-deficient diets results in the depletion of glutathione, the dysregulation of nitric oxide metabolism and the peroxynitrite-mediated inactivation of complex I.
NDUFS1 may confer susceptibility to schizophrenia in male subjects, acting as a causative factor for the severity of negative symptoms in schizophrenia.
The presented clinical courses of NDUFV1 (show NDUFV1 Proteins) and NDUFS1 mutation-based complex I deficiencies are characterized by leukoencephalopathy or early death and expand the already heterogeneous phenotypic spectrum.
Some mutations in NDUFS1 cause a milder phenotype with a more benign course despite the initial decompensation phase. Homozygosity for the c.755A > G missense mutation may correlate with the milder clinical picture in the patient.
homozygous c.1783A>G (p.Thr595Ala) mutation in NDUFS1 in two inbred siblings with isolated complex I deficiency associated to a progressive cavitating leukoencephalopathy
report 3 patients with low residual complex I activity who displayed novel mutations in the NDUFS1 gene. One mutation introduces a premature stop codon, 3 mutations cause a substitution of amino acids and another mutation a deletion of one amino acid.
A patient with Leigh syndrome had a mutation in the NDUFS1 protein of Complex I of the Respiratory Chain. Identifying nuclear mutations will help us understand how molecular defects can lead to complex I deficiency.
mutations in the NDUFS1 and NDUFS4 (show NDUFS4 Proteins) genes of complex I cause dysfunction in cellular oxidative metabolism
Data show that during NADH-ubiquinone oxidoreductase (Complex (show NDUFA2 Proteins) I) catalytic electron transfer from NADH to DBQ, the superoxide generation site was mostly shifted to the SQ.
Data suggest that Q(Nf) plays a role in a "direct" redox-driven proton pump, while Q(Ns) triggers an "indirect" conformation-driven proton pump in NADH-ubiquinone oxidoreductase (complex (show NDUFA2 Proteins) I).
Bovine heart NADH-ubiquinone oxidoreductase contains one molecule of ubiquinone with ten isoprene units as one of the cofactors
The protein encoded by this gene belongs to the complex I 75 kDa subunit family. Mammalian complex I is composed of 45 different subunits. It locates at the mitochondrial inner membrane. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This protein is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. Mutations in this gene are associated with complex I deficiency. Several transcript variants encoding different isoforms have been found for this gene.
, NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
, complex I-75kD
, NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa
, complex I 75kDa subunit
, complex I, mitochondrial respiratory chain, 75-kD subunit
, mitochondrial NADH-ubiquinone oxidoreductase 75 kDa subunit