000 01806 a2200469 4500
005 20250513091815.0
264 0 _c19960820
008 199608s 0 0 eng d
022 _a0021-9258
024 7 _a10.1074/jbc.271.24.14206
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aOdermatt, A
245 0 0 _aThe vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholamban.
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cJun 1996
300 _a14206-13 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
650 0 4 _aAnimals
650 0 4 _aBiological Transport
650 0 4 _aCalcium
_xmetabolism
650 0 4 _aCalcium-Binding Proteins
_xmetabolism
650 0 4 _aCalcium-Calmodulin-Dependent Protein Kinases
_xmetabolism
650 0 4 _aCalcium-Transporting ATPases
_xmetabolism
650 0 4 _aCalmodulin
_xpharmacology
650 0 4 _aCell Line
650 0 4 _aCyclic AMP-Dependent Protein Kinases
_xmetabolism
650 0 4 _aEgtazic Acid
_xpharmacology
650 0 4 _aHeart Ventricles
650 0 4 _aHumans
650 0 4 _aKinetics
650 0 4 _aMicrosomes
_xenzymology
650 0 4 _aMyocardium
_xenzymology
650 0 4 _aPhosphorylation
650 0 4 _aPolymerase Chain Reaction
650 0 4 _aRabbits
650 0 4 _aRecombinant Proteins
_xmetabolism
650 0 4 _aSarcoplasmic Reticulum
_xenzymology
650 0 4 _aTransfection
700 1 _aKurzydlowski, K
700 1 _aMacLennan, D H
773 0 _tThe Journal of biological chemistry
_gvol. 271
_gno. 24
_gp. 14206-13
856 4 0 _uhttps://doi.org/10.1074/jbc.271.24.14206
_zAvailable from publisher's website
999 _c8661605
_d8661605