▪ Abstract Most transport proteins in plant cells are energized by electrochemical gradients of
protons across the plasma membrane. The formation of these gradients is due to the action …

▪ Abstract The cell membrane Na, K-ATPase is a member of the P-type family of active cation
transport proteins. Recently the molecular structure of the related sarcoplasmic reticulum Ca …

The Na+, K+-ATPase belongs to the P-ATPase family, whose characteristic property is the
formation of a phosphorylated intermediate. The enzyme is also a defined target for …

The crystal structure of SERCA1a (skeletal-muscle sarcoplasmic-reticulum/endoplasmic-
reticulum Ca2+-ATPase) has recently been determined at 2.6 Å (note 1 Å= 0.1 nm) …

The focus of this article is on progress in establishing structure–function relationships
through site-directed mutagenesis and direct binding assay of Tl+, Rb+, K+, Na+, Mg2+ or …

CopA, a thermophilic membrane ATPase from Archaeoglobus fulgidus, drives the outward
movement of Cu+ or Ag+ [Mandal et al.(2002) J. Biol. Chem. 277, 7201− 7208]. This, as …

The K+ and Na+ concentrations in living cells are strictly regulated at almost constant
concentrations, high for K+ and low for Na+. Because these concentrations correspond to …

Biological rafts were identified and isolated at 37° C and neutral pH. The strategy for
isolating rafts utilized membrane tension to generate large domains. For lipid compositions …

▪ Abstract Active transport of cations is achieved by a large family of ATP-dependent ion
pumps, known as P-type ATPases. Various members of this family have been targets of …

The copper-transporting ATPase ATP7B is essential for normal distribution of copper in
human cells. Mutations inATP7B lead to Wilson's disease, a severe disorder with …