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Human ATP5B Protein expressed in Wheat germ - ABIN1346052
Hansson, Korsgren, Pontén, Korsgren: Enteroviruses and the pathogenesis of type 1 diabetes revisited: cross-reactivity of enterovirus capsid protein (VP1) antibodies with human mitochondrial proteins. in The Journal of pathology 2013
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This study showed that beta-actin (show ACTB Proteins), L32 (show RPL32 Proteins) ribosomal protein, and ATP5B proteins were the most stabily expressed genes in cryopreserved horse semen.
Results show that the relationship between ATPsyn-beta and insulin (show INS Proteins) 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 (show LEPR Proteins) mice.
inhibition of calmodulin (CaM) completely abolished ATPSbeta-induced Akt (show AKT1 Proteins) 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 (show APOA1 Proteins) is a selective process that involves the ectopically expressed beta-subunit (show POLG Proteins) of ATP synthase.
Neuron-specific changes for F(1)-complex in the Ppt1 (show PPT1 Proteins)-deficient cells and give clues for a possible link between lipid metabolism and neurodegeneration in Infantile neuronal ceroid lipofuscinosis (show CLN6 Proteins).
Downregulated ATP5b also reduced ATP production in the murine macrophages infected with B. anthracis spores.
CyPD (show CYPD Proteins) association to the lateral stalk of ATP synthase modulates the activity of the complex
experiments implicate circulating NEFA (show NUCB2 Proteins) 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 (show ETFB Proteins) were associated with worsening renal injury.
In this instance, the ATP5B/CALR (show CALR Proteins)/HSP90B1 (show HSP90B1 Proteins)/HSPB1 (show HSPB1 Proteins)/HSPD1 (show HSPD1 Proteins)-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 (show RUNX1 Proteins) patients.
Hemoglobin - a novel ligand of hepatocyte ectopic F1-ATPase
PKA phosphorylates the ATPase inhibitory factor 1 (show ATPIF1 Proteins) 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.
ATP5B probably plays a key role in porcine skeletal muscle development.
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 (show POLG Proteins), 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 (show POLG Proteins) 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
Inhibition arises by IF(1 (show ATPIF1 Proteins)) imposing the structure and properties of the beta(TP)-alpha(TP) interface on the beta(DP)-alpha(DP (show SRPR Proteins)) 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