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Bioscience Reports|October 1, 1995
The mechanism of coupling chemical and physical reactions by the calcium ATPase of sarcoplasmic reticulum and other coupled vectorial systemsW P JencksProceedings of the National Academy of Sciences of the United States of America|July 1, 1981
On the attribution and additivity of binding energiesW P JencksAnnual Review of Biochemistry|January 1, 1997
From chemistry to biochemistry to catalysis to movementW P JencksThe Journal of Biological Chemistry|September 25, 1990
Lanthanum inhibits steady-state turnover of the sarcoplasmic reticulum calcium ATPase by replacing magnesium as the catalytic ionT Fujimori, W P JencksBiochemistry|December 1, 1987
Reactions of the sarcoplasmic reticulum calcium adenosinetriphosphatase with adenosine 5'-triphosphate and Ca2+ that are not satisfactorily described by an E1-E2 modelN Stahl, W P JencksBiochemistry|November 6, 1984
Adenosine 5'-triphosphate at the active site accelerates binding of calcium to calcium adenosinetriphosphataseN Stahl, W P JencksBiochemistry|July 26, 1994
Lumenal and cytoplasmic binding sites for calcium on the calcium ATPase of sarcoplasmic reticulum are different and independentJ Myung, W P JencksThe Journal of Biological Chemistry|March 25, 1976
Mechanism and specificity of succinyl-CoA:3-ketoacid coenzyme A transferaseH White, W P JencksBiochemistry|April 19, 1988
Two-step internalization of Ca2+ from a single E approximately P.Ca2 species by the Ca2+-ATPaseD Khananshvili, W P JencksArchives of Biochemistry and Biophysics|August 15, 1994
Substrate specificity for catalysis of phosphoryl transfer by the calcium ATPase of sarcoplasmic reticulumJ Myung, W P JencksPageof 176