Hansen, Martin

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