A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex. [electronic resource]
Producer: 20030113Description: 8514-26 p. digitalISSN:- 0270-7306
- 14-3-3 Proteins
- 3T3 Cells
- Active Transport, Cell Nucleus -- physiology
- Amino Acid Sequence
- Animals
- Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
- Cell Nucleus -- metabolism
- Cytoplasm -- metabolism
- DNA-Binding Proteins -- genetics
- Dimerization
- Genes, Reporter
- Helix-Loop-Helix Motifs
- Humans
- Leucine Zippers
- Macromolecular Substances
- Mice
- Molecular Sequence Data
- Nuclear Localization Signals
- Nuclear Proteins -- genetics
- Protein Structure, Tertiary
- Recombinant Fusion Proteins -- genetics
- Sequence Alignment
- Transcription Factors -- genetics
- Two-Hybrid System Techniques
- Tyrosine 3-Monooxygenase -- metabolism
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
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