Endogenous Phosphorylation of Distinct γ-Aminobutyric Acid Type A Receptor Polypeptides by Ser/Thr and Tyr Kinase Activities Associated with the Purified Receptor
Open Access
- 1 November 1995
- journal article
- Published by Elsevier
- Vol. 270 (44) , 26482-26487
- https://doi.org/10.1074/jbc.270.44.26482
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Protein kinase C enhances recombinant bovine α1β1γ2L GABAA receptor whole-cell currents expressed in L929 fibroblastsNeuron, 1994
- Differential phosphorylation of intracellular domains of gamma-aminobutyric acid type A receptor subunits by calcium/calmodulin type 2-dependent protein kinase and cGMP-dependent protein kinase.Published by Elsevier ,1994
- Regulation of GABAA receptor function by protein kinase C phosphorylationNeuron, 1994
- GABAA Receptor ChannelsAnnual Review of Neuroscience, 1994
- GABAA Receptor Subtypes: Ligand Binding Heterogeneity Demonstrated by Photoaffinity Labeling and AutoradiographyJournal of Neurochemistry, 1993
- Functional Modulation of GABA A Receptors by cAMP-Dependent Protein PhosphorylationScience, 1992
- GABA A receptor subtypes: from pharmacology to molecular biologyThe FASEB Journal, 1991
- Cyclic AMP-dependent protein kinase decreases GABAA receptor current in mouse spinal neuronsNeuron, 1990
- Protein kinase C and cAMP-dependent protein kinase phosphorylate the beta subunit of the purified gamma-aminobutyric acid A receptor.Proceedings of the National Academy of Sciences, 1990
- Sequence and functional expression of the GABAA receptor shows a ligand-gated receptor super-familyNature, 1987