Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. [electronic resource]
Producer: 19970728Description: 875-86 p. digitalISSN:- 0092-8674
- Amino Acid Isomerases -- chemistry
- Binding Sites -- physiology
- Carrier Proteins -- chemistry
- Cell Cycle -- physiology
- Crystallography
- DNA-Binding Proteins -- chemistry
- Endodeoxyribonucleases -- chemistry
- Heat-Shock Proteins -- chemistry
- Humans
- Mitosis -- physiology
- Molecular Sequence Data
- NIMA-Interacting Peptidylprolyl Isomerase
- Peptidylprolyl Isomerase
- Phosphorylation
- Protein Conformation
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Sequence Homology, Amino Acid
- Substrate Specificity
- Tacrolimus Binding Proteins
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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