Phosphorylation of p40AUF1 regulates binding to A + U-rich mRNA-destabilizing elements and protein-induced changes in ribonucleoprotein structure. [electronic resource]
Producer: 20031002Description: 33039-48 p. digitalISSN:- 0021-9258
- Amino Acid Sequence
- Anisotropy
- Cyclic AMP-Dependent Protein Kinases -- metabolism
- Dimerization
- Fluorescence Resonance Energy Transfer
- Glycogen Synthase Kinase 3 -- metabolism
- Glycogen Synthase Kinase 3 beta
- Heterogeneous Nuclear Ribonucleoprotein D0
- Heterogeneous-Nuclear Ribonucleoprotein D -- chemistry
- Histidine -- chemistry
- Humans
- Kinetics
- Models, Chemical
- Models, Statistical
- Molecular Sequence Data
- Nucleic Acid Conformation
- Oligonucleotides -- chemistry
- Phosphorylation
- Protein Binding
- Protein Conformation
- Protein Processing, Post-Translational
- Protein Structure, Tertiary
- RNA -- metabolism
- RNA, Messenger -- metabolism
- Recombinant Proteins -- chemistry
- Ribonucleoproteins -- chemistry
- Serine -- chemistry
- Signal Transduction
- Spectrometry, Fluorescence
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Thermodynamics
- Time Factors
- Tumor Cells, Cultured
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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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