The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. [electronic resource]
Producer: 20000502Description: 329-35 p. digitalISSN:- 1072-8368
- 3' Untranslated Regions -- chemistry
- Allosteric Regulation
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Humans
- Models, Molecular
- Molecular Sequence Data
- Molecular Weight
- Nuclear Magnetic Resonance, Biomolecular
- Nucleic Acid Conformation
- Poly A -- metabolism
- Polynucleotide Adenylyltransferase -- antagonists & inhibitors
- Protein Binding
- Protein Structure, Secondary
- RNA Processing, Post-Transcriptional -- genetics
- RNA, Messenger -- chemistry
- RNA-Binding Proteins -- chemistry
- Regulatory Sequences, Nucleic Acid -- genetics
- Ribonucleoprotein, U1 Small Nuclear -- chemistry
- Structure-Activity Relationship
- Substrate Specificity
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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