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NDUFS4 encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Additionally we are shipping NADH Dehydrogenase (Ubiquinone) Fe-S Protein 4, 18kDa (NADH-Coenzyme Q Reductase) Antibodies (62) and NADH Dehydrogenase (Ubiquinone) Fe-S Protein 4, 18kDa (NADH-Coenzyme Q Reductase) Proteins (11) and many more products for this protein.
Study showed that the earliest cell loss in complex 1-deficient Ndufs4 mice retinas is retinal bipolar cells at p20 (show HSPB6 ELISA Kits), followed by Starburst Amacrine Cells at p24, that precede a rise in inflammatory molecules at p30 (show HMGB1 ELISA Kits) and retinal ganglion cell death at p42 (show EPB42 ELISA Kits); results could suggest a mechanism in which the death of bipolar and amacrine cells incite an inflammatory wave that ultimately results in retinal ganglion cell loss.
NDUFS4 deletion affected gene expression following neural differentiation and the potential of the cells to generate beating embryoid bodies.
Using the Ndufs4 knockout (Ndufs4 KO) mouse, a model of Leigh syndrome, we demonstrate for the first time that protein succination is increased in the brainstem (BS), particularly in the vestibular nucleus.
Locally insufficient respiration capacity of the nerve terminals may drive focal neurodegeneration in the Ndufs4 knockout mouse model of the Leigh syndrome.
This study demonstrated that Genetic reduction of Ndufs4 function does not lead to loss of dopamine neurons in vivo.
Mitochondrial complex I dysfunction in the retina, present in Ndufs4 KO mouse, triggers an innate immune and inflammatory response that results in loss of retinal ganglion cell function and death.
Global Ndufs4 deletion causes systemic inflammation and osteopetrosis (show CSF1 ELISA Kits).
Complex I deficiency due to selective loss of Ndufs4 in the mouse heart results in severe hypertrophic cardiomyopathy.
deletion of Ndufs4 results in a significant loss of complex I-supported respiration in the heart, which is well tolerated with no major changes of cardiac function, energetics, and longevity of the mice under unstressed conditions.
Oxidation of the reactive oxygen species sensor hydroethidium was increased and mitochondria were less branched and/or shorter in NDUFS4(-/-) fibroblasts.
The clinical presentations of five individuals of Hutterite descent with Leigh disease are described herein. An identity-by-descent mapping and candidate gene approach was used to identify a novel homozygous c.393dupA frameshift mutation in the NADH dehydrogenase (ubiquinone) Fe-S protein 4 (NDUFS4) gene.
The authors concluded that NDUFS4-related Leigh syndrome is invariably linked to an early onset severe phenotype that results in early death.
The c.462delA deletion led to a complete lack of NDUFS4 peptide in isolated mitochondria, and this deficiency caused an inefficient mitochondrial complex I assembly and Leigh syndrome symptoms.
Mutations in the NDUFS4 gene and its subunits are associated with the mitochondrial complex I deficiency. (Review)
Elevated expression of CO I and ND4 (show MT-ND4 ELISA Kits) were associated with gastric tumorigenesis and tumor dedifferentiation
Studies indicate that that the functional capacity of complex I depends on phosphorylation and import of subunit NDUFS4 protein.
In fibroblast cultures, protein kinase A-mediated phosphorylation of the NDUFS4 subunit of complex I rescues the activity of the oxidatively damaged complex.
case Report: A novel mutation in NDUFS4 causes Leigh syndrome in an Ashkenazi Jewish family.
REVIEW: Phosphorylation of the NDUFS4 protein, overall respiratory activity, and mutations sassociated with deficiency of complex I.
observations show the essential role of the 18-kDa subunit of respiratory complex I (NDUFS4) gene in the structure and function of complex I and give insight into pathogenic mechanism of NDUFS4 gene mutations in a severe defect of complex I
Two-dimensional gel electrophoresis, (32)P labelling and immunodetection show that "in vitro" PKA phosphorylates the serine in the C-terminus of the NDUFS4 subunit in isolated bovine complex I.
This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane. Complex I is composed of at least 41 subunits, of which 7 are encoded by the mitochondrial genome and the remainder by nuclear genes.
, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
, NADH-ubiquinone oxidoreductase 18 kDa subunit
, complex I-18 kDa
, complex I-AQDQ
, NADH dehydrogenase (ubiquinone) Fe-S protein 4, 18kDa (NADH-coenzyme Q reductase)
, NADH dehydrogenase (ubiquinone) iron-sulfur protein 4
, NADH-coenzyme Q reductase, 18-KD
, complex I 18kDa subunit
, mitochondrial respiratory chain complex I (18-KD subunit)
, NADH-ubiquinone oxidoreductase 18 kDa subunit, mitochondrial