A urokinase-type plasminogen activator-inhibiting cyclic peptide with an unusual P2 residue and an extended protease binding surface demonstrates new modalities for enzyme inhibition. [electronic resource]
Producer: 20060110Description: 38424-37 p. digitalISSN:- 0021-9258
- 4-Aminobenzoic Acid -- chemistry
- Alanine -- chemistry
- Amino Acid Sequence
- Binding Sites
- Binding, Competitive
- Capsid Proteins
- Catalysis
- Cell Line
- DNA -- chemistry
- DNA-Binding Proteins -- chemistry
- Disulfides -- chemistry
- Dose-Response Relationship, Drug
- Electrophoresis, Polyacrylamide Gel
- Enzyme Inhibitors -- pharmacology
- Enzyme-Linked Immunosorbent Assay
- Factor Xa -- chemistry
- Humans
- Hydrogen-Ion Concentration
- Inhibitory Concentration 50
- Kinetics
- Models, Chemical
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Peptide Hydrolases -- chemistry
- Peptide Library
- Peptides -- chemistry
- Peptides, Cyclic -- chemistry
- Plasminogen -- chemistry
- Protease Inhibitors -- pharmacology
- Protein Binding
- Protein C -- chemistry
- Protein Conformation
- Protein Structure, Tertiary
- Recombinant Proteins -- chemistry
- Substrate Specificity
- Temperature
- Thermodynamics
- Time Factors
- Trypsin -- chemistry
- U937 Cells
- Urokinase-Type Plasminogen Activator -- chemistry
- Viral Fusion Proteins -- chemistry
No physical items for this record
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
There are no comments on this title.
Log in to your account to post a comment.