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ATPase, class VI, type 11A

ATPase is
The protein encoded by this gene is an integral membrane ATPase. The encoded protein is probably phosphorylated in its intermediate state and likely drives the transport of ions such as calcium across membranes. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ATPase, CAN, V-ATPase, ACID, V1a
Papers on ATPase is
Distinct α2 Na,K-ATPase membrane pools are differently involved in early skeletal muscle remodeling during disuse.
Krivoi et al., Saint Petersburg, Russia. In J Gen Physiol, Feb 2016
UNASSIGNED: The Na,K-ATPase is essential for the contractile function of skeletal muscle, which expresses the α1 and α2 subunit isoforms of Na,K-ATPase.
Colorimetric Assays of Na,K-ATPase.
Sweadner, Boston, United States. In Methods Mol Biol, Dec 2015
The Na,K-ATPase is a plasma membrane enzyme that catalyzes active ion transport by the hydrolysis of ATP.
Isolation of H(+),K(+)-ATPase-enriched Membrane Fraction from Pig Stomachs.
Olesen et al., Nagoya, Japan. In Methods Mol Biol, Dec 2015
Gastric H(+),K(+)-ATPase is an ATP-driven proton pump responsible for the acid secretion.
Functional Studies of Na(+),K(+)-ATPase Using Transfected Cell Cultures.
Sweadner et al., Boston, United States. In Methods Mol Biol, Dec 2015
Renal Na,K-ATPase is tightly bound to a small single-span membrane protein, the γ subunit, or FXYD2.
Electrophysiological Characterization of Na,K-ATPases Expressed in Xenopus laevis Oocytes Using Two-Electrode Voltage Clamping.
Poulsen et al., Århus, Denmark. In Methods Mol Biol, Dec 2015
The transport of three Na(+) per two K(+) means that the Na,K-ATPase is electrogenic, and though the currents generated by the ion pump are small compared to ion channel currents, they can be measured using electrophysiology, both steady-state pumping and individual steps in the transport cycle.
V-type ATPase proton pump expression during enamel formation.
Paine et al., Los Angeles, United States. In Matrix Biol, Dec 2015
V-type ATPase is a multi-subunit protein complex expressed in enamel forming cells.
Plasma membrane H(+)-ATPase regulation in the center of plant physiology.
Palmgren et al., Frederiksberg, Denmark. In Mol Plant, Dec 2015
UNASSIGNED: The plasma membrane (PM) H(+)-ATPase is an important ion pump in the plant cell membrane.
Role of vacuolar-type proton ATPase in signal transduction.
Wada et al., Kyoto, Japan. In Biochim Biophys Acta, Oct 2015
The acidic pH generated by V-ATPase is important for a wide range of cellular processes as well as acidification-independent processes such as secretion and membrane fusion.
General and specific lipid-protein interactions in Na,K-ATPase.
Karlish et al., Århus, Denmark. In Biochim Biophys Acta, Sep 2015
The molecular activity of Na,K-ATPase and other P2 ATPases like Ca(2+)-ATPase is influenced by the lipid environment via both general (physical) and specific (chemical) interactions.
Circadian rhythms. Atomic-scale origins of slowness in the cyanobacterial circadian clock.
Akiyama et al., Okazaki, Japan. In Science, Aug 2015
The slow ATPase is coupled with another ATPase catalyzing autodephosphorylation in the carboxyl-terminal half of KaiC, yielding the circadian response frequency of intermolecular interactions with other clock-related proteins that influences the transcription and translation cycle.
Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase.
Rubinstein et al., Toronto, Canada. In Nature, Jun 2015
The eukaryotic V-ATPase is the most complex rotary ATPase: it has three peripheral stalks, a hetero-oligomeric proton-conducting proteolipid ring, several subunits not found in other rotary ATPases, and is regulated by reversible dissociation of its catalytic and proton-conducting regions.
Transcriptional regulators of Na,K-ATPase subunits.
Langhans et al., Wilmington, United States. In Front Cell Dev Biol, 2014
The spatial and temporal expression of Na,K-ATPase is partially regulated at the transcriptional level.
Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state.
Inesi et al., Tokyo, Japan. In Nature, 2013
In the absence of Ca(2+) and at pH 7 or higher, the ATPase is predominantly in E1, not in E2 (low affinity for Ca(2+)), and if millimolar Mg(2+) is present, one Mg(2+) is expected to occupy one of the Ca(2+)-binding sites with a millimolar dissociation constant.
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase.
Hayer-Hartl et al., Martinsried, Germany. In Nature, 2011
The CbbX ATPase is strongly stimulated by RuBP and Rubisco.
Neurological disease mutations compromise a C-terminal ion pathway in the Na(+)/K(+)-ATPase.
Nissen et al., Århus, Denmark. In Nature, 2010
This novel model for ion transport by the Na(+)/K(+)-ATPase is established by electrophysiological studies of C-terminal mutations in familial hemiplegic migraine 2 (FHM2) and is further substantiated by molecular dynamics simulations.
ATP11A is a novel predictive marker for metachronous metastasis of colorectal cancer.
Mori et al., Suita, Japan. In Oncol Rep, 2010
ATP11A is a useful predictive marker of metastasis in colorectal cancer patients.
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