Purification, characterization, and molecular cloning of a 60-kDa phosphoprotein in rabbit skeletal sarcoplasmic reticulum which is an isoform of phosphoglucomutase.-Reference-Cited by-同舟云学术

Purification, characterization, and molecular cloning of a 60-kDa phosphoprotein in rabbit skeletal sarcoplasmic reticulum which is an isoform of phosphoglucomutase.

Published:1992-10 Issue:29 Volume:267 Page:21080-21088
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Lee Y.S.,Marks A.R.,Gureckas N,Lacro R,Nadal-Ginard B,Kim D.H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference43 articles.

1. Deduced primary structure of the beta subunit of brain type II Ca2+/calmodulin-dependent protein kinase determined by molecular cloning.

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

3. Molecular interactions of the junctional foot protein and dihydropyridine receptor in skeletal muscle triads

4. A calmodulin-dependent protein kinase system from skeletal muscle sarcoplasmic reticulum. Phosphorylation of a 60,000-dalton protein.

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