Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

"Every second throughout life, billions of sodium-potassium pumps enable the human muscle cells to function. The pump is an enzyme found in the plasma membrane of all animal cells and is an important example of active transport. The Na⁺, K⁺-pumps keep us going by pumping sodium out of cells while pumping potassium into cells and without them, we would not survive. Addressed to scientists in the field of biomedicine, the author presents a thorough overview of his scientific results over more than 40 years. The book is richly illustrated and seeks to explain how a single molecule creates the required conditions for our muscles to work."

Sodium/potassium ATPase. --- Sodium --- Potassium --- Physiological transport.

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Carrier proteins. --- Ion channels. --- Ion pumps. --- Sodium/potassium ATPase. --- Biological Transport --- Carrier Proteins --- Membrane Proteins --- Protein Binding --- Physiology. --- Metabolism. --- Metabolism. --- Physiology.

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Enzymology --- General biophysics --- Molecular biology --- Sodium-Potassium Pump --- Sodium/potassium ATPase --- Congresses --- Biological Transport, Active. --- Sodium-Potassium-Exchanging ATPase --- Active Biological Transport --- Biologic Transport, Active --- Transport, Active Biological --- Active Transport --- Uphill Transport --- Active Biologic Transport --- Transport, Active --- Transport, Active Biologic --- Transport, Uphill --- chemistry. --- ultrastructure. --- physiology. --- ADENOSINE TRIPHOSPHATASE, SODIUM, POTASSIUM, chemistry --- ADENOSINE TRIPHOSPHATASE, SODIUM, POTASSIUM, ultrastructure --- BIOLOGICAL TRANSPORT, ACTIVE --- SODIUM-POTASSIUM PUMP, physiology --- Congresses. --- Adenosine triphosphatase, sodium, potassium, chemistry --- Adenosine triphosphatase, sodium, potassium, ultrastructure --- Biological transport, active --- Sodium-potassium pump, physiology --- Sodium/potassium atpase --- Biological Transport, Active --- Pump, Sodium (Physiology) --- Sodium-potassium pump (Physiology) --- Sodium pump (Physiology) --- Adenosine triphosphatase --- Sodium cotransport systems --- chemistry --- physiology --- ultrastructure --- Sodium/potassium ATPase - Congresses

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Na+-K+ ATPase or Na-pump ATPase, a member of “P”-type ATPase superfamily, is characterized by association of multiple isoforms mainly of it’s α- and β- subunits. At present four different α- (α-1,α-2,α-3 and α-4) and three β- (β-1, β-2, and β-3) isoforms have been identified in mammalian cells and their differential expressions are tissue specific. Regulation of Na+-K+ ATPase activity is an important but a complex process, which involves short-term and long-term mechanisms. Short-term regulation of Na+-K+ ATPase is either mediated by changes in intracellular Na+ concentrations that directly affect the Na+-pump activity or by phosphorylation/dephosphorylation-mediated by some stimulants leading to changes in its expression and transport properties. On the other hand, long-term regulation of Na+-K+ ATPase is mediated by hormones, such as mineralocorticoids and thyroid hormones, which cause changes in the transcription of genes of α- and β- subunits leading to an increased expression in the level of Na+-pump. Several studies have revealed a relatively new type of regulation that involves the association of small, single span membrane proteins with this enzyme. These proteins belong to the FXYD family, the members of which share a common signature sequence encompassing the transmembrane domain adjacent to the isoform(s) of α-β subunits of Na+-K+ ATPase. Considering the extraordinary importance of Na+-K+ ATPase in cellular function, several internationally established investigators have contributed their articles in the monograph entitled “Regulation of Membrane Na+-K+ ATPase” for inspiring young scientists and graduate students to enrich their knowledge on the enzyme, and we are sure that this book will soon be considered as a comprehensive scientific literature in the area of Na+-K+ ATPase regulation in health and disease.

Biochemistry --- Chemistry --- Physical Sciences & Mathematics --- Sodium/potassium ATPase. --- Membranes (Biology) --- Biological membranes --- Biomembranes --- Pump, Sodium (Physiology) --- Sodium-potassium pump (Physiology) --- Sodium pump (Physiology) --- Biological interfaces --- Protoplasm --- Adenosine triphosphatase --- Sodium cotransport systems --- Biochemistry. --- Cell membranes. --- Medicine. --- Protein Structure. --- Membrane Biology. --- Protein Science. --- Atomic/Molecular Structure and Spectra. --- Molecular Medicine. --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Cell surfaces --- Cytoplasmic membranes --- Plasma membranes --- Plasmalemma --- Glycocalyces --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Composition --- Health Workforce --- Proteins . --- Cell membranes . --- Atomic structure  . --- Molecular structure . --- Molecular biology. --- Molecular biochemistry --- Molecular biophysics --- Biophysics --- Biomolecules --- Systems biology --- Structure, Molecular --- Chemical structure --- Structural bioinformatics --- Structure, Atomic --- Atomic theory --- Proteids --- Polypeptides --- Proteomics --- Proteins. --- Biological transport. --- Atomic structure . --- Molecular structure. --- Medicine --- Membrane Trafficking. --- Protein Biochemistry. --- Atomic and Molecular Structure and Properties. --- Biomedical Research. --- Research. --- Biological research --- Biomedical research --- Membrane transport --- Passive transport, Biological --- Physiological transport --- Transport, Biological --- Diffusion --- Osmosis