The max of the Ca2+-ATPase of Cardiac Sarcoplasmic Reticulum (SERCA2a) Is Not Altered by Ca2+/Calmodulin-dependent Phosphorylation or by Interaction with Phospholamban
Open Access
- 1 June 1996
- journal article
- Published by Elsevier
- Vol. 271 (24) , 14206-14213
- https://doi.org/10.1074/jbc.271.24.14206
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Inactivation of calcium uptake by EGTA is due to an irreversible thermotropic conformational change in the calcium binding domain of the calcium-ATPaseBiochemistry, 1992
- Excitation-contraction coupling in vertebrate skeletal muscle: A tale of two calcium channelsCell, 1991
- Expression and characterization of the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II using the baculovirus expression systemBiochemical and Biophysical Research Communications, 1990
- Involvement of electrostatic phenomena in phospholamban‐induced stimulation of Ca uptake into cardiac sarcoplasmic reticulumFEBS Letters, 1989
- Rabbit cardiac and slow‐twitch muscle express the same phospholamban geneFEBS Letters, 1988
- [31] Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligandsPublished by Elsevier ,1988
- INTRACELLULAR CALCIUM HOMEOSTASISAnnual Review of Biochemistry, 1987
- Mechanism of the Stimulation of Cardiac Sarcoplasmic Reticulum Calcium Pump by CalmodulinMembrane Biochemistry, 1987
- Concerted phosphorylation of the 26-kilodalton phospholamban oligomer and of the low molecular weight phospholamban subunitsBiochemistry, 1986
- Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequencesCell, 1986