isoleucyl-prolyl-arginine-4-nitroanilide has been researched along with fibrinogen in 5 studies
| Studies (isoleucyl-prolyl-arginine-4-nitroanilide) | Trials (isoleucyl-prolyl-arginine-4-nitroanilide) | Recent Studies (post-2010) (isoleucyl-prolyl-arginine-4-nitroanilide) | Studies (fibrinogen) | Trials (fibrinogen) | Recent Studies (post-2010) (fibrinogen) |
|---|---|---|---|---|---|
| 23 | 0 | 0 | 34,477 | 1,707 | 7,083 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (40.00) | 18.7374 |
| 1990's | 3 (60.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Botstein, D; Brady, K; Johnson, AC; Kerr, EM; Nguyen, HV; Paoni, NF; Peña, LC; Refino, CJ; van Reis, R; Wurm, FM | 1 |
| Collen, D; Li, XK; Lijnen, HR; Nelles, L; Stassen, JM; Van Hoef, B | 1 |
| Hogg, PJ; Jackson, CM | 1 |
| Castellino, FJ; deSerrano, VS; Urano, S; Urano, T | 1 |
| Chmielewska, J; Rånby, M; Wiman, B | 1 |
5 other study(ies) available for isoleucyl-prolyl-arginine-4-nitroanilide and fibrinogen
| Article | Year |
|---|---|
Involvement of residues 296-299 in the enzymatic activity of tissue-type plasminogen activator.
Topics: Alanine; Amino Acid Sequence; Fibrin; Fibrinogen; Fibrinolysis; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligopeptides; Plasma; Plasminogen; Protein Engineering; Tissue Plasminogen Activator | 1992 |
Biochemical and biologic properties of rt-PA del (K296-G302), a recombinant human tissue-type plasminogen activator deletion mutant resistant to plasminogen activator inhibitor-1.
Topics: Amino Acid Sequence; Animals; Chemical Phenomena; Chemistry, Physical; Chromogenic Compounds; Cricetinae; DNA; Fibrin; Fibrinogen; Fibrinolysis; Gene Expression; Humans; Hydrolysis; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligopeptides; Plasminogen; Plasminogen Inactivators; Pulmonary Embolism; Recombinant Proteins; Tissue Plasminogen Activator | 1992 |
Formation of a ternary complex between thrombin, fibrin monomer, and heparin influences the action of thrombin on its substrates.
Topics: Amino Acid Sequence; Chromogenic Compounds; Fibrin Fibrinogen Degradation Products; Fibrinogen; Fibrinopeptide A; Fibrinopeptide B; Heparin; Humans; Hydrogen-Ion Concentration; Hydrolysis; Macromolecular Substances; Molecular Sequence Data; Oligopeptides; Prothrombin; Substrate Specificity; Thrombin | 1990 |
Stimulation by fibrinogen of the amidolytic activity of single-chain tissue plasminogen activator.
Topics: Amides; Dose-Response Relationship, Drug; Enzyme Activation; Fibrin; Fibrinogen; Kinetics; Oligopeptides; Recombinant Proteins; Tissue Plasminogen Activator | 1989 |
Kinetics of the inhibition of plasminogen activators by the plasminogen-activator inhibitor. Evidence for 'second-site' interactions.
Topics: Binding Sites; Fibrin; Fibrinogen; Glycoproteins; Humans; Isoflurophate; Kinetics; Ligands; Oligopeptides; Plasminogen Activators; Plasminogen Inactivators | 1988 |