tryptophan and hirudin

tryptophan has been researched along with hirudin in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (60.00)18.2507
2000's2 (40.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Altichieri, L; De Filippis, V; Fontana, A; Vindigni, A1
Altichieri, L; De Antoni, F; De Filippis, V; Fontana, A; Polverino de Laureto, P; Vindigni, A1
Broersma, RJ; Burkhart, JP; Kutcher, LW; Malikayil, JA; Mehdi, S; Neises, B; Peet, NP; Schatzman, GL; Schreuder, HA; Tardif, C1
Jacques, SL; Kuliopulos, A1
Dalzoppo, D; De Boni, S; De Dea, E; De Filippis, V; Fontana, A; Grandi, C1

Other Studies

5 other study(ies) available for tryptophan and hirudin

ArticleYear
Core domain of hirudin from the leech Hirudinaria manillensis: chemical synthesis, purification, and characterization of a Trp3 analog of fragment 1-47.
    Biochemistry, 1995, Jul-25, Volume: 34, Issue:29

    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.
    Advances in experimental medicine and biology, 1996, Volume: 398

    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.
    Biochemistry, 1997, Feb-04, Volume: 36, Issue:5

    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.
    The Biochemical journal, 2003, Dec-15, Volume: 376, Issue:Pt 3

    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.
    Protein science : a publication of the Protein Society, 2004, Volume: 13, Issue:6

    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