Mechanism of inhibition of protein phosphatase 1 by DARPP-32: studies with recombinant DARPP-32 and synthetic peptides.

Desdouits, F; Cheetham, J J; Huang, H B; Kwon, Y G; da Cruz e Silva, E F; Denefle, P; Ehrlich, M E; Nairn, A C; Greengard, P; Girault, J A

Desdouits, F; Cheetham, J J; Huang, H B; Kwon, Y G; da Cruz e Silva, E F; Denefle, P; Ehrlich, M E; Nairn, A C; Greengard, P; Girault, J A.

Affiliation

Desdouits F; INSERM U114, Collège de France, Paris.

Biochem Biophys Res Commun ; 206(2): 652-8, 1995 Jan 17.

Article in En | MEDLINE | ID: mdl-7826384

Subject(s)

Nerve Tissue Proteins/pharmacology; Peptide Fragments/pharmacology; Phosphopeptides/pharmacology; Phosphoprotein Phosphatases/antagonists & inhibitors; Amino Acid Sequence; Animals; Base Sequence; Cattle; Cell Line; Cyclic AMP-Dependent Protein Kinases/metabolism; Dopamine and cAMP-Regulated Phosphoprotein 32; Escherichia coli; Kinetics; Molecular Sequence Data; Muscle, Skeletal/enzymology; Mutagenesis, Site-Directed; Myocardium/enzymology; Oligodeoxyribonucleotides; Peptide Fragments/chemical synthesis; Phosphopeptides/chemical synthesis; Phosphoproteins/pharmacology; Phosphorylation; Protein Binding; Protein Phosphatase 1; Rabbits; Recombinant Proteins/pharmacology; Spodoptera

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Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Phosphopeptides / Phosphoprotein Phosphatases / Nerve Tissue Proteins Limits: Animals Language: En Journal: Biochem Biophys Res Commun Year: 1995 Document type: Article

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