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]
- The Journal of biological chemistry Nov 2005
- 38424-37 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.M505933200 doi
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