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Data show that ATP synthase 8, mouse (mtATP8) nt7778 G/T polymorphism correlated with reduced hemoglobin content of erythrocytes.
the mtAtp8 polymorphism alters mitochondrial performance, increasing H(2)O(2) production and affecting mitochondrial structure.
ATP8 genetic polymorphisms associated with breast cancer in Mizoram mongloid population.
polymorphisms in MT-ATP8 may have an impact on the pathogenesis of BP in the German population.
identified 8 changes in ATP6 (zeige MT-ATP6 Proteine) gene in 36/50 examined breast cancer cell samples and 5 changes in ATP8 gene (10/50); most were homoplasmic changes of missense type; 4 changes (A8439C, G8858C, C9130G and T9119G) had not been described in the literature before
Mutations in ATP synthase F0 subunit 8 is associated with peripheral neuropathy of diabetes.
Three mutations were significantly related to the presence of epilepsy. These mutations were found at the 8502, 11994, and 13,231 bp of mtDNA, which resulted in amino acid changes at the MT-ATP-8, MT-ND4 (zeige MT-ND4 Proteine) and MT-ND5 (zeige MT-ND5 Proteine) genes.
Case Report: absence of mtDNA-encoded ATPase6 (zeige MT-ATP6 Proteine) and ATPase8 genes in progressive external ophthalmoplegia patient clearly resulted in aberrant synthesis of ATP synthase.
Patients with irritable bowel syndrome with diarrhea have a higher incidence of MT-ATP 6 (zeige MT-ATP6 Proteine) and 8 polymorphisms than healthy subjects, implying that the mtDNA polymorphism may play a role in irritable bowel syndrome with diarrhea.
Mutations in mitochondrial DNA MT-ATP6/8 genes may be responsible for acute episodes of limb weakness.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
ATP synthase F0 subunit 8