AbstractThe three-dimensional structure of Na,K-ATPase was determined by electron microscopy and image processing. Tilt series of negatively stained membrane crystals were recorded. The projections were analyzed by Fourier methods and the data combined to a 3-D model. The unit cell contains two rod-shaped stain-deficient regions interpreted as αβ-protomers of Na,K-ATPase. The rods are related by dyad axes oriented perpendicular to the membrane. Outside the lipid bilayer the rods contact different protein units on the two sides of the membrane
The membrane protein Na,K-ATPase is well known for its critical function of transporting sodium out ...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
AbstractRaman spectra of active Na+,K+-ATPase from pig kidney and membrane-bound products of its two...
AbstractThe three-dimensional structure of Na,K-ATPase was determined by electron microscopy and ima...
The molecular structure of Na,K-ATPase was determined by electron crystallography from two-dimension...
AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2...
AbstractIon channels and pumps in cell membranes consist of multiple transmembrane segments that are...
AbstractTwo-dimensional membrane crystals of renal Na,K-ATPase were analyzed by electron microscopy ...
AbstractFor topological analysis of integral membrane protein in situ, we used a novel immunoelectro...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...
The isolated membrane-bound enzyme retains its ouabain-sensitive ATP hydrolysis activity, and produc...
Na$^+$,K$^+$-ATPase is responsible for the transport of Na$^+$ and K$^+$ across the plasma membrane ...
AbstractNa+,K+-ATPase is a heterodimer of α and β subunits and a member of the P-type ATPase family ...
BackgroundSodium-potassium-adenosinetriphosphatase (Na,K-ATPase) is the primary membrane enzyme resp...
AbstractUsing four oligopeptide-specific polyclonal antibodies, we mapped the α subunit ofNa,K-ATPas...
The membrane protein Na,K-ATPase is well known for its critical function of transporting sodium out ...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
AbstractRaman spectra of active Na+,K+-ATPase from pig kidney and membrane-bound products of its two...
AbstractThe three-dimensional structure of Na,K-ATPase was determined by electron microscopy and ima...
The molecular structure of Na,K-ATPase was determined by electron crystallography from two-dimension...
AbstractProlonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2...
AbstractIon channels and pumps in cell membranes consist of multiple transmembrane segments that are...
AbstractTwo-dimensional membrane crystals of renal Na,K-ATPase were analyzed by electron microscopy ...
AbstractFor topological analysis of integral membrane protein in situ, we used a novel immunoelectro...
Electron microscopy and two-dimensional crystallography have been used to study the molecular struct...
The isolated membrane-bound enzyme retains its ouabain-sensitive ATP hydrolysis activity, and produc...
Na$^+$,K$^+$-ATPase is responsible for the transport of Na$^+$ and K$^+$ across the plasma membrane ...
AbstractNa+,K+-ATPase is a heterodimer of α and β subunits and a member of the P-type ATPase family ...
BackgroundSodium-potassium-adenosinetriphosphatase (Na,K-ATPase) is the primary membrane enzyme resp...
AbstractUsing four oligopeptide-specific polyclonal antibodies, we mapped the α subunit ofNa,K-ATPas...
The membrane protein Na,K-ATPase is well known for its critical function of transporting sodium out ...
AbstractTreatment of purified preparations of porcine Na+,K+-ATPase with phospholipase A2, MgCl2 and...
AbstractRaman spectra of active Na+,K+-ATPase from pig kidney and membrane-bound products of its two...