BIOMAT Database Logo BIOMAT Database Logo

Modulation of calcium binding in sarcoplasmic reticulum adenosinetriphosphatase. 1981

T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining

Related Publications

T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Binding of Ca2+ to the calcium adenosinetriphosphatase of sarcoplasmic reticulum.
November 1988, Biochemistry,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Reversible loss of cooperative calcium ion binding by sarcoplasmic reticulum calcium adenosinetriphosphatase.
August 1982, Biochemistry,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Self-association and modification of calcium binding in solubilized sarcoplasmic reticulum adenosinetriphosphatase.
February 1983, Biochemistry,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Roles of phosphorylation and nucleotide binding domains in calcium transport by sarcoplasmic reticulum adenosinetriphosphatase.
August 1988, Biochemistry,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Potassium-activated adenosinetriphosphatase and calcium uptake by sarcoplasmic reticulum.
March 1967, Life sciences,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Modulation of the binding characteristics of a fluorescent nucleotide derivative to the sarcoplasmic reticulum adenosinetriphosphatase.
February 1986, Biochemistry,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Stoichiometric and electrostatic characterization of calcium binding to native and lipid-substituted adenosinetriphosphatase of sarcoplasmic reticulum.
September 1985, Biochimica et biophysica acta,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
The binding of ATP and Mg2+ to the calcium adenosinetriphosphatase of sarcoplasmic reticulum follows a random mechanism.
July 1993, Biochemistry,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Calcium uptake, calcium release and adenosinetriphosphatase activity in sarcoplasmic reticulum fragments deposited on millipore filters.
July 1977, Biochimica et biophysica acta,
T Watanabe, and D Lewis, and R Nakamoto, and M Kurzmack, and C Fronticelli, and G Inesi
Calcium binding properties of sarcoplasmic reticulum membranes.
June 1969, Biochimica et biophysica acta,
Copied contents to your clipboard!