The max of the Ca2+-ATPase of Cardiac Sarcoplasmic Reticulum (SERCA2a) Is Not Altered by Ca2+/Calmodulin-dependent Phosphorylation or by Interaction with Phospholamban-Reference-Cited by-同舟云学术

The max of the Ca2+-ATPase of Cardiac Sarcoplasmic Reticulum (SERCA2a) Is Not Altered by Ca2+/Calmodulin-dependent Phosphorylation or by Interaction with Phospholamban

Published:1996-06 Issue:24 Volume:271 Page:14206-14213
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Odermatt Alex,Kurzydlowski Kazimierz,MacLennan David H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference52 articles.

1. Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences

2. Expression and characterization of the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II using the baculovirus expression system

3. Phospholamban expressed in slow-twitch and chronically stimulated fast-twitch muscles minimally affects calcium affinity of sarcoplasmic reticulum Ca(2+)-ATPase.

4. cDNA Cloning, functional expression, and mRNA Tissue Distribution of a Third Organellar Ca2+ Pump

5. Comparative studies of cardiac and skeletal sarcoplasmic reticulum ATPases. Effect of a phospholamban antibody on enzyme activation by Ca2+

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