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Mice were created that allotopically express either a mutant (A6M) or wildtype (A6W) mt-Atp6 transgene.
Interaction between mitochondrially encoded ATP synthase 6 (p.MT-ATP6) subunit and an environmental exposure of the ATP synthase inhibitor tributyltin chloride might contribute to the etiology of striatal necrosis syndromes.
A novel frameshift mutation in the mitochondrial ATP6 gene was identified in a 4-year-old girl with ataxia, microcephaly, developmental delay and intellectual disability.
Three mutations in the MT-ATP6 gene associated to the mitochondrial cardiomyopathy.
ATP6 genetic polymorphisms associated with breast cancer in Mizoram mongloid population.
analysis of mitochondrial deletion and double mutations in the MT-ATP6 gene in Tunisian patients
Two synonymous substitutions (mt.8614T>C and mt.8994G>A) in the mt-ATP6 gene may be associated with childhood obesity; study provides first data about mitochondrial genome variations in a Turkish obese population and also the first in obese children
This study suggests that, in part, polymorphisms in the MT-ATP6 and MT-CYB (show MT-CYB ELISA Kits) genes may contribute to the unexpected fertilization failure.
T8821G mutation of the ATPase6 is associated with Leber's hereditary optic neuropathy.
Screening of the MT-ATP6 gene in a large collection of patients suspected of suffering different mitochondrial DNA (mtDNA) disorders. Biochemical, molecular-genetics and other analyses show three new pathologic mutations.
Five mutations able to change amino acid synthesis for the ATP synthase subunit 6 were associated with acute lymphoblastic leukemia in a Saudi Arabian cohort.
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. Key component of the proton channel\; it may play a direct role in the translocation of protons across the membrane.
ATP synthase F0 subunit 6