Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif. [electronic resource]
Producer: 20060110Description: 38211-8 p. digitalISSN:- 0021-9258
- Alternative Splicing
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- COS Cells
- Calcium Channels -- chemistry
- Cattle
- Cell Line
- Chlorocebus aethiops
- Cloning, Molecular
- Cyclic GMP-Dependent Protein Kinases -- metabolism
- DNA -- chemistry
- Dimerization
- Electrophoresis, Polyacrylamide Gel
- Glutathione Transferase -- metabolism
- Humans
- Immunoblotting
- Inositol 1,4,5-Trisphosphate Receptors
- Leucine -- chemistry
- Membrane Proteins
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Phosphoproteins -- metabolism
- Protein Binding
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Receptors, Cytoplasmic and Nuclear -- chemistry
- Signal Transduction
- Static Electricity
- Transcription Factors, TFII -- metabolism
- Transcription, Genetic
- Transfection
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Publication Type: Journal Article; Research Support, N.I.H., Extramural
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