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Correction to "ACLY regulates autolysosome acidification through tubulin acetylation-mediated assembly of V-ATPase subunits in Alzheimer's disease model mice". [PDF]
Alzheimers Dementeuropepmc +1 more source
Functional 14-3-3 Proteins: Master Regulators in Plant Responses to Salt Stress. [PDF]
Plants (Basel)Tang D +6 more
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In vivo antioxidant and anti-inflammatory effects of Myrtus communis against ionizing radiation-induced gastrointestinal injury: TROD-GROG-002 study. [PDF]
North Clin IstanbKilic MB +10 more
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Governor vessel acupuncture therapy in experimental ischemic stroke: A systematic review and meta-analysis. [PDF]
Medicine (Baltimore)Wang J +8 more
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Structural modeling and biochemical characterization of MSMEG_0748, a MoxR ATPase from <i>Mycobacterium smegmatis</i>. [PDF]
Comput Struct Biotechnol JLee JE +6 more
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Annual Review of Biophysics, 2011
P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by
Palmgren, Michael G., Nissen, Poul
openaire +4 more sources
P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by
Palmgren, Michael G., Nissen, Poul
openaire +4 more sources
Molecular and Cellular Biochemistry, 1981
An ecto-adenosine triphosphatase (E.C. 3.6.1.4 ATP-phosphohydrolase) is shown to be localized on the outer surface of varieties of cell membrane. The enzyme is different from the ATPase involved in biological energy transduction and ion transport mechanism.
openaire +2 more sources
An ecto-adenosine triphosphatase (E.C. 3.6.1.4 ATP-phosphohydrolase) is shown to be localized on the outer surface of varieties of cell membrane. The enzyme is different from the ATPase involved in biological energy transduction and ion transport mechanism.
openaire +2 more sources