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anti-Mouse (Murine) Antibodies:
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We report biallelic mutations in ATP6V1E1 and ATP6V1A (show ATP6V1A Antibodies), respectively encoding the E1 and A subunits of the V1 domain of V-ATPase (show ATP6V1H Antibodies), as a cause of distinct metabolic and multisystemic cutis laxa entities.
Low-grade PanIN lesions with typical columnar morphology displayed diffuse labeling of the V1E subunit. In advanced lesions it was (show ATP6V1H Antibodies) found along t (show WNT2 Antibodies)he basolatera (show CTNNB1 Antibodies)l membranes.
The genes CECR2, SLC25A18 and ATP6V1E1, mapping within the critical region for cat eye syndrome (CES), may be responsible for anorectal, renal and preauricular anomalies in patients with CES.
Data demonstrate the physiological significance of the interaction between the E and H subunits of V-ATPase (show ATP6V1H Antibodies) and extend previous studies on the arrangement of subunits on the peripheral stalk of V-ATPase (show ATP6V1H Antibodies).
HuR (show ELAVL1 Antibodies) shows increased binding to some V-ATPase (show ATP6V1H Antibodies) mRNAs during ATP depletion; siRNA-mediated knockdown of HuR (show ELAVL1 Antibodies) results in diminished V-ATPase (show ATP6V1H Antibodies) expression
Rat vacuolar H(+)ATPase (show ATP6V1B2 Antibodies) associates with NHE-RF (Na(+)/H(+) exchanger regulatory factor); the E subunit was co-immunoprecipitated from rat kidney cytosol with NHE-RF antibodies.
The mouse V-ATPase E may participate in the regulation of the mSos1-dependent Rac1 signaling pathway involved in growth factor receptor (show RYK Antibodies)-mediated cell growth control.
In pancreatic intraepithelial lesions, V1E subunits localized to the basolateral domain in specific regions. Blocking the v-ATPase (show ATP6V1H Antibodies) disrupted Wnt (show WNT2 Antibodies)/beta-catenin (show CTNNB1 Antibodies) signaling in primary PanIN cells.
These results suggest that the B1 vacuolar H(+)-ATPase (show ATP6V1B2 Antibodies) subunit (show ATP6AP1 Antibodies) is necessary for the furosemide-induced acute urinary acidification.
These results suggest that subunit E, especially its amino-terminal domain, plays a pertinent role in the assembly of V-ATPase (show ATP6V1H Antibodies) subunits in vacuolar membranes from mice and yeast.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different V1 domain E subunit isoforms. Pseudogenes for this gene have been found in the genome.
H(+)-transporting two-sector ATPase, 31kDa subunit
, H+-transporting ATP synthase chain E, vacuolar
, V-ATPase 31 kDa subunit
, V-ATPase subunit E 1
, V-ATPase, subunit E
, V-type proton ATPase subunit E 1
, vacuolar proton pump subunit E 1
, ATPase, H+ transporting lysosomal (vacuolar proton pump), 32 kDa
, ATPase, H+ transporting, V1 subunit E
, ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E
, H(+)-ATPase E-like protein
, H+ ATPase subunit E
, VATPase, H+ transporting, lysosomal V1 subunit E1
, lysosomal 31kDa
, vacuolar H+ ATPase E1
, vacuolar H(+)-ATPase, E subunit
, ATPase, H+ transporting, vacuolar, V1 subunit E
, v-type proton ATPase subunit e 1