High sensibility to reactivation by acidic lipids of the recombinant human plasma membrane Ca2+-ATPase isoform 4xb purified from Saccharomyces cerevisiae

Author:

Cura Carolina I.,Corradi Gerardo R.,Rinaldi Débora E.,Adamo Hugo P.

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference49 articles.

1. Evolution of P-type ATPases;Palmgren;Biochim. Biophys. Acta,1998

2. A highly active 120-kDa truncated mutant of the plasma membrane Ca2+ pump;Enyedi;J. Biol. Chem.,1993

3. Purified (Ca2+-Mg2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids;Niggli;J. Biol. Chem.,1981

4. Protein kinase C activates the plasma membrane Ca2+ pump isoform 4b by phosphorylation of an inhibitory region downstream of the calmodulin-binding domain;Enyedi;J. Biol. Chem.,1996

5. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps;Strehler;Phys. Rev.,2001

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