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anti-Mouse (Murine) ATP5B Antibodies:
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Human Polyclonal ATP5B Primary Antibody for IF (p), IHC (p) - ABIN1387611
Zhao, Zhang, Liu, Zhang, Hao, Li, Chen, Shen, Tang, Min, Meng, Wang, Yi, Zhang: Hydrogen Sulfide and/or Ammonia Reduces Spermatozoa Motility through AMPK/AKT Related Pathways. in Scientific reports 2016
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Cow (Bovine) Polyclonal ATP5B Primary Antibody for IP, IHC - ABIN2783269
Vantourout, Martinez, Fabre, Collet, Champagne: Ecto-F1-ATPase and MHC-class I close association on cell membranes. in Molecular immunology 2007
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Cow (Bovine) Polyclonal ATP5B Primary Antibody for IHC, WB - ABIN2783268
Li, Bates, An, Terry, Wang: Up-regulation of key microRNAs, and inverse down-regulation of their predicted oxidative phosphorylation target genes, during aging in mouse brain. in Neurobiology of aging 2011
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Human Polyclonal ATP5B Primary Antibody for IF, IHC - ABIN6676953
Qi, Han: Microbial Siderophore Enterobactin Promotes Mitochondrial Iron Uptake and Development of the Host via Interaction with ATP Synthase. in Cell 2018
This study showed that beta-actin, L32 ribosomal protein, and ATP5B proteins were the most stabily expressed genes in cryopreserved horse semen.
The results of this study found that the expression levels of Cd68 and Atp5b were significantly correlated with the neurofibrillary tangle burden in the Alzheimer's Disease brain and with their cognition.
Results show that the relationship between ATPsyn-beta and insulin secretion deficiency suggests that ATPsyn-beta potentially could serve as a marker for type 2 diabetes mellitus disease risk in women with polycystic ovary syndrome.
Data show that overexpressed ATP synthase subunit-beta (ATP5b) was significantly located on renal proximal tubules in db/db mice.
Aging altered the expression of ATP synthase subunit beta.
inhibition of calmodulin (CaM) completely abolished ATPSbeta-induced Akt activation in liver cells
association of calcium channel alpha2/delta subunit 1 and ATP5b occurs in intracellular membranes and at the plasma membrane of developing muscle cells, where they form a signaling complex capable of accelerating the rate of decline of calcium transients
Adipocyte recycling of apoA-I is a selective process that involves the ectopically expressed beta-subunit of ATP synthase.
Disturbed flow and hypercholesterolemia synergistically promote gamma/delta T-lymphocyte activation by the membrane translocation of ATPSbeta in endothelial cells.
Neuron-specific changes for F(1)-complex in the Ppt1-deficient cells and give clues for a possible link between lipid metabolism and neurodegeneration in Infantile neuronal ceroid lipofuscinosis.
Downregulated ATP5b also reduced ATP production in the murine macrophages infected with B. anthracis spores.
CyPD association to the lateral stalk of ATP synthase modulates the activity of the complex
ATP5B reduction would be at least in part due to neuronal loss.
The results revealed that ATP5B expression is associated with the process of keratinocyte differentiation which may be related to intracellular ATP synthesis.
findings show the T163S mutation affects the catalytic activity with a decrease in Ca2+-dependent and an increase in Mg2+-dependent ATP hydrolysis and desensitizes the permeability transition pore to Ca2+, resulting in increased resistance to Ca2+-dependent mitochondrial depolarization and to cell death
experiments implicate circulating NEFA in obesity in suppressing muscle protein metabolism, and establish impaired beta-F1-ATPase translation as an important consequence of obesity
ATP5B, as a binding partner of a metastasis-related short peptide (B04) on prostate cancer cells, is involved in promoting prostate cancer metastasis.
These results suggested that increasing levels of ATP5B and ETFB were associated with worsening renal injury.
In this instance, the ATP5B/CALR/HSP90B1/HSPB1/HSPD1-signaling network was revealed as the predominant target which was associated with the majority of the observed protein-protein interactions. As a result, the identified targets may be useful in explaining the anticancer mechanisms of ursolic acid and as potential targets for colorectal cancer therapy.
High mRNA levels of ATP5B are associated with glioblastoma.
Hypermethylation of ATPsyn-beta gene promoter is associated with a down-regulated mRNA expression and chemoresistance in AML patients.
Hemoglobin - a novel ligand of hepatocyte ectopic F1-ATPase
PKA phosphorylates the ATPase inhibitory factor 1 and inactivates its capacity to bind and inhibit the mitochondrial H(+)-ATP synthase.
Our study suggested that positive beta2M expression or loss of ATP5B expression in tumor tissues is closely related to the metastasis, invasion, and poor-prognosis of gallbladder cancer.
Mitochondrial ATPsyn-beta expression and ATP synthase activity in relapsed/refractory acute myeloid leukemia patients were downregulated. This downregulated expression exhibited a positive correlation with the response to adriamycin of primary cells.
ATP5B gene expressions were detected significantly higher in colorectal cancer samples.
H2O2 may induce melanogenesis via the upregulation of PAH and activation of cAMP/p-CREB/MITF signaling by increasing intracellular cAMP levels through the induction of ATP5B.
Identification of ATP synthase as a lipid peroxide protein adduct in pancreatic islets from humans with and without type 2 diabetes mellitus.
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.
miR-127-5p targets the 3'UTR of beta-F1-ATPase mRNA (beta-mRNA) significantly reducing its translational efficiency.
ATP5B probably plays a key role in porcine skeletal muscle development.
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.
These data indicate that interaction with the alpha-phosphate is not crucial for efficient catalysis, but likely contributes to avoid formation of ADP-inhibited intermediates.
Molecular dynamics simulations show that the nucleotide-free beta subunit, initially in the open, low-affinity state, undergoes a spontaneous closing transition to the half-open state in response to the gamma rotation in the synthesis direction.
analysis of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria
Molecular dynamics simulations of F1-ATPase suggest that the equilibrium conformation of a nucleotide-free beta-subunit is the open conformation and that the transition from the closed to the open conformation can occur in a few tens of nanoseconds.
molecular dynamic analysis of interaction between the gamma-subunit and a C-terminal fragment of the beta-subunit of F1-ATPase
The beneficial effects of dietary resveratrol may derive in part by preventing mitochondrial ATP synthesis in tumor cells, thereby inducing apoptosis
Inhibition arises by IF(1) imposing the structure and properties of the beta(TP)-alpha(TP) interface on the beta(DP)-alpha(DP) interface, thereby preventing it from hydrolyzing the bound ATP.
The catalytic sites of beef heart mitochondrial F1-ATPase were studied by electron spin echo envelope modulation (ESEEM) spectroscopy, using Mn(II) as a paramagnetic probe
This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing 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 beta subunit of the catalytic core.
mitochondrial ATP synthase, H+ transporting F1 complex beta subunit
, mitochondrial ATP synthase beta subunit
, H+ transporting, mitochondrial F1 complex, beta polypeptide
, ATP synthase, H+ transporting, mitochondrial F1 complex, beta subunit
, ATP synthase subunit beta, mitochondrial
, ATP synthase-beta
, OXPHOS complex V beta chain
, ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide
, ATP synthase beta subunit
, ATP synthase subunit beta, mitochondrial-like
, ATP synthase, H+ transporting mitochondrial F1 complex, alpha subunit
, mitochondrial ATP synthetase, beta subunit
, F1-ATPase beta-subunit
, f1-ATPase beta
, ATP synthase, H+ transporting mitochondrial F1 complex, beta subunit