tryptophan has been researched along with hirudin in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (60.00) | 18.2507 |
2000's | 2 (40.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Altichieri, L; De Filippis, V; Fontana, A; Vindigni, A | 1 |
Altichieri, L; De Antoni, F; De Filippis, V; Fontana, A; Polverino de Laureto, P; Vindigni, A | 1 |
Broersma, RJ; Burkhart, JP; Kutcher, LW; Malikayil, JA; Mehdi, S; Neises, B; Peet, NP; Schatzman, GL; Schreuder, HA; Tardif, C | 1 |
Jacques, SL; Kuliopulos, A | 1 |
Dalzoppo, D; De Boni, S; De Dea, E; De Filippis, V; Fontana, A; Grandi, C | 1 |
5 other study(ies) available for tryptophan and hirudin
Article | Year |
---|---|
Core domain of hirudin from the leech Hirudinaria manillensis: chemical synthesis, purification, and characterization of a Trp3 analog of fragment 1-47.
Topics: Amino Acid Sequence; Animals; Chromatography, High Pressure Liquid; Circular Dichroism; Hirudins; Leeches; Models, Structural; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments; Protein Denaturation; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Thermodynamics; Tryptophan | 1995 |
The core domain of hirudin from the leech Hirudinaria manillensis. Chemical modification of a tryptophan-containing synthetic peptide analog.
Topics: Amino Acid Sequence; Animals; Chromatography, High Pressure Liquid; Hirudins; Indicators and Reagents; Leeches; Molecular Sequence Data; Nitrobenzenes; Peptide Fragments; Peptides; Protein Structure, Secondary; Skatole; Tryptophan | 1996 |
Molecular design and characterization of an alpha-thrombin inhibitor containing a novel P1 moiety.
Topics: Alanine; Animals; Binding Sites; Crystallography, X-Ray; Drug Design; Hirudins; Models, Molecular; Oligopeptides; Partial Thromboplastin Time; Peptide Fragments; Protein Conformation; Rats; Serine Proteinase Inhibitors; Software; Thrombin; Trypsin; Trypsin Inhibitors; Tryptophan | 1997 |
Protease-activated receptor-4 uses dual prolines and an anionic retention motif for thrombin recognition and cleavage.
Topics: Allosteric Regulation; Amino Acid Motifs; Amino Acid Sequence; Animals; Anions; Binding Sites; COS Cells; Hirudins; Kinetics; Molecular Sequence Data; Proline; Protein Structure, Tertiary; Receptor, PAR-1; Receptors, Thrombin; Sequence Alignment; Thrombin; Tryptophan | 2003 |
Incorporation of the fluorescent amino acid 7-azatryptophan into the core domain 1-47 of hirudin as a probe of hirudin folding and thrombin recognition.
Topics: Amino Acid Sequence; Animals; Chromatography, High Pressure Liquid; Hirudins; Leeches; Models, Molecular; Molecular Probes; Molecular Sequence Data; Protein Binding; Protein Folding; Spectrometry, Fluorescence; Thermodynamics; Thrombin; Tryptophan | 2004 |