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anti-Mouse (Murine) ATP5A1 Antibodies:
anti-Human ATP5A1 Antibodies:
anti-Rat (Rattus) ATP5A1 Antibodies:
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Human Polyclonal ATP5A1 Primary Antibody for IF, IHC - ABIN6676951
Zhou, Du, Liu, Zhao, Yuan, Li, Chen, Lu, Cheng, Liu: Polyacetylene glycoside attenuates ischemic kidney injury by co-inhibiting inflammation, mitochondria dysfunction and lipotoxicity. in Life sciences 2018
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Human Polyclonal ATP5A1 Primary Antibody for IF, IHC - ABIN6137324
Wang, Li, Liu, Liao, Li, Chen, Cheng, Lu, Liu: GLP-1 receptor agonist ameliorates obesity-induced chronic kidney injury via restoring renal metabolism homeostasis. in PLoS ONE 2018
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Upregulation of ATP5A1 increased ATP5A1 and ATP synthase activity, prevented mitochondrial ROS generation and oxidative damage, and reduced cardiomyopathic changes in diabetic mice.
ATP5alpha1 is an interacting subunit of the ATP synthase complex localized to the mitochondria with aryl hydrocarbon receptor in the absence of ligand.
Tumor analyses reveals a novel mechanism of polyp suppression by Mom2R (duplication of four nucleotides within exon 3).
The study demonstrates a novel role of FANCD2 in governing cellular ATP production via ATP5A, and advances the understanding of how defective Fanconi anemia signaling contributes to aging and cancer at the energy metabolism level.
17% of prostate carcinomas and 18% of benign prostate tissues showed isolated or combined deficiency of oxidative phosphorylation complexes. ATP5F1A, a complex V protein, was the most frequently affected subunit
Using systems biology techniques to study gene coexpression network, ATP5A1 was identified and found highly expressed in normal kidney than clear cell renal cell carcinoma (ccRCC) tissues of each grade. Functional and pathway enrichment analysis demonstrated that ATP5A1 is overrepresented in pathway of oxidative phosphorylation, which associated with tumorigenesis and tumor progression.
This cohort study showed that the ATP5A1 gene was down regulation between patients with idiopathic Parkinson disease and controls
these data highlight a key role of the P2Y1/PI3Kbeta axis in endothelial cell proliferation downstream of ecto-F1-ATPase activation by apoA-I. Pharmacological targeting of this pathway could represent a promising approach to enhance vascular endothelial protection.
These findings, together with the previously reported inhibition of respiratory complex I, show that depression of the activity of oxidative phosphorylation enzymes is involved in the cell growth inhibitory action of ATRA.
High mRNA levels of ATP5A1 are associated with glioblastoma.
Hemoglobin - a novel ligand of hepatocyte ectopic F1-ATPase
Here, we found that ATP synthase subunit alpha (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model
Mitochondrial calpain-1 disrupts ATP synthase, leading to mitochondrial reactive oxygen species generation, which promotes proinflammatory response and myocardial dysfunction during endotoxemia.
Studies indicate that the F-ATP synthase can reversibly undergo a Ca(2+)-dependent transition to form a channel that mediates the permeability transition.
A mutation in ATP5A1 causes a fatal neonatal mitochondrial encephalopathy.
Studies indicate that F1-ATPase (F1) is a rotary motor protein driven by ATP hydrolysis and the minimum complex of F1 for function as a rotary motor is the alpha3beta3gamma subcomplex.
Homozygous mutations in this gene are the likely cause of mitochondrial disease in two sisters, with support from a yeast model.
F1-ATPase at the cell surface of colonic epithelial cells has a role in mediating cell proliferation
An interactive proteomics study was done to examine proteins that bind heterocomplexes with ABCC1 using coimmunoprecipitation and MS/MS analyses. We found that ATP synthase alpha binds to ABCC1 in plasma membranes with a ratio of 2:1.
Antibodies to the beta- and gamma-subunits of F(1)-ATPase are further antimitochondrial antibodies in primary biliary cirrhosis.
A selective Cys in ATP synthase alpha subunit is targeted by multiple oxidative posttranslational modifications suggesting that this Cys residue may act as a redox sensor modulating ATP synthase function.
Data suggest that F1-ATPase catalytic site show the correlation between the phosphate binding and the tightening of the alphabeta-interface.
This protein has been found differentially expressed in the anterior cingulate cortex in men patients with schizophrenia.
Combining cryoelectron microscopy data with bioinformatic analysis allowed the authors to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits.
The beneficial effects of dietary resveratrol may derive in part by preventing mitochondrial ATP synthesis in tumor cells, thereby inducing apoptosis.
Nuclear magnetic resonance characterization of the interaction between OSCP-N terminal and a peptide corresponding to residues 1-25 of the alpha-subunit of bovine F(1)-ATPase is presented.
This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, using an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the alpha subunit of the catalytic core. Alternatively spliced transcript variants encoding the different isoforms have been identified. Pseudogenes of this gene are located on chromosomes 9, 2, and 16.
ATP synthase subunit alpha, mitochondrial
, mitochondrial H+ transporting ATP synthase F1
, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle
, ATP synthase H+ transporting mitochondrial F1 complex alpha subunit 1
, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit-like
, ATP synthase subunit alpha, mitochondrial-like
, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit
, modifier of Min 2
, ATP synthase alpha chain, mitochondrial
, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 1, cardiac muscle
, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 2, non-cardiac muscle-like 2
, ATP sythase (F1-ATPase) alpha subunit
, mitochondrial ATP synthetase, oligomycin-resistant
, mitochondrial H+-ATP synthase alpha subunit
, mitochondrial ATP synthase alpha subunit
, ATP synthase alpha subunit
, cardiac muscle ATP synthase H+ transporting mitochondrial F1 complex alpha subunit 1