A latent form of protein phosphatase 1 α associated with bovine heart myofibrils
- 21 September 1994
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1208 (1) , 45-54
- https://doi.org/10.1016/0167-4838(94)90158-9
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The control of protein phosphatase‐1 by targetting subunitsEuropean Journal of Biochemistry, 1992
- A myofibrillar protein phosphatase from rabbit skeletal muscle contains the β isoform of protein phosphatase‐1 complexed to a regulatory subunit which greatly enhances the dephosphorylation of myosinEuropean Journal of Biochemistry, 1992
- The Structure, Role, and Regulation of Type 1 Protein PhosphatasesCritical Reviews in Biochemistry and Molecular Biology, 1992
- THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASESAnnual Review of Biochemistry, 1989
- The glycogen‐binding subunit of protein phosphatase‐1g from rabbit skeletal muscleEuropean Journal of Biochemistry, 1989
- Identification of a third form of protein phosphatase 1 in rabbit skeletal muscle that is associated with myosinBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1988
- Purification, subunit composition and regulatory properties of the ATP · Mg2+‐dependent form of type I phosphoprotein phosphatase from bovine heartEuropean Journal of Biochemistry, 1986
- The protein phosphatases involved in cellular regulationEuropean Journal of Biochemistry, 1986
- The protein phosphatases involved in cellular regulation. Comparison of native and reconstituted Mg-ATP-dependent protein phosphatases from rabbit skeletal muscleEuropean Journal of Biochemistry, 1984
- Subunit structure and activation of inactive phosphorylase phosphataseBiochemistry, 1983