Results 341 to 350 of about 619,710 (391)
Energy-Dependent Phosphate and Acid Transport for Bone Formation and Resorption. [PDF]
J Cell BiochemTourkova IL +3 more
europepmc +1 more source
Conduction pathway for potassium through the E. coli pump KdpFABC
Hussein A +3 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Analytical Biochemistry, 1988
A newly developed microtechnique for quantitating activity of myosin ATPase (EC 3.6.1.32) is more sensitive and less time-consuming than existing spectrophotometric methods. Measurement of ATPase activity using the new method can be accomplished in a final volume of 0.25 ml, allowing the assay to be conducted in individual wells of 96-well microplates ...
Richard A. Walsh +3 more
openaire +3 more sources
A newly developed microtechnique for quantitating activity of myosin ATPase (EC 3.6.1.32) is more sensitive and less time-consuming than existing spectrophotometric methods. Measurement of ATPase activity using the new method can be accomplished in a final volume of 0.25 ml, allowing the assay to be conducted in individual wells of 96-well microplates ...
Richard A. Walsh +3 more
openaire +3 more sources
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 +5 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 +5 more sources
Journal of Bioenergetics and Biomembranes, 1992
The energy dependent exchange of cytoplasmic Na+ for extracellular K+ in mammalian cells is due to a membrane bound enzyme system, the Na,K-ATPase. The exchange sustains a gradient for Na+ into and for K+ out of the cell, and this is used as an energy source for creation of the membrane potential, for its de- and repolarisation, for regulation of ...
Skou, J C, Esmann, Mikael
openaire +4 more sources
The energy dependent exchange of cytoplasmic Na+ for extracellular K+ in mammalian cells is due to a membrane bound enzyme system, the Na,K-ATPase. The exchange sustains a gradient for Na+ into and for K+ out of the cell, and this is used as an energy source for creation of the membrane potential, for its de- and repolarisation, for regulation of ...
Skou, J C, Esmann, Mikael
openaire +4 more sources
Regulation of Ca2+-ATPases,V-ATPases and F-ATPases
2016The biological membranes of cellular organization enfold an important group of membrane proteins called the ATPases, which are not only versatile in maintaining chemical gradient and electrical potential across the membrane but also bring metabolites necessary for cell metabolism and drive out toxins, waste products and solutes that otherwise can curb ...
Sajal Chakraborti, Naranjan S. Dhalla
openaire +2 more sources
1995
Publisher Summary This chapter discusses the role of Ca2+-ATPases in maintaining Ca2+ homeostasis in the cell. The chapter focuses on sarcoplasmic reticular (SR) Ca2+-ATPase(s), which is the primary regulator of the Ca2+ levels and thus, contractility in muscle.
István Édes, Evangelia G. Kranias
openaire +2 more sources
Publisher Summary This chapter discusses the role of Ca2+-ATPases in maintaining Ca2+ homeostasis in the cell. The chapter focuses on sarcoplasmic reticular (SR) Ca2+-ATPase(s), which is the primary regulator of the Ca2+ levels and thus, contractility in muscle.
István Édes, Evangelia G. Kranias
openaire +2 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 +3 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 +3 more sources
Regulatory proteins of F1F0-ATPase: Role of ATPase inhibitor
Journal of Bioenergetics and Biomembranes, 1990An intrinsic ATPase inhibitor inhibits the ATP-hydrolyzing activity of mitochondrial F1F0-ATPase and is released from its binding site on the enzyme upon energization of mitochondrial membranes to allow phosphorylation of ADP. The mitochondrial activity to synthesize ATP is not influenced by the absence of the inhibitor protein.
Tadao Hashimoto +2 more
openaire +3 more sources