Phosphoserine as a recognition determinant for glycogen synthase kinase-3: Phosphorylation of a synthetic peptide based on the G-component of protein phosphatase-1-Reference-Cited by-同舟云学术

Phosphoserine as a recognition determinant for glycogen synthase kinase-3: Phosphorylation of a synthetic peptide based on the G-component of protein phosphatase-1

Published:1988-12 Issue:2 Volume:267 Page:797-802
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Fiol Carol J.,Haseman Joseph H.,Wang Yuhuan,Roach Peter J.,Roeske Roger W.,Kowalczuk Maria,DePaoli-Roach Anna A.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference14 articles.

1. Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3.

2. Amino acid sequence of a region on the glycogen-binding subunit of protein phosphatase-1 phosphorylated by cyclic AMP-dependent protein kinase

3. Peptides: Structure and Biological Function;Gesellchen,1979

4. Multiple phosphorylation of rabbit skeletal muscle glycogen synthase. Evidence for interactions among phosphorylation sites and the resolution of electrophoretically distinct forms of the subunit.

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