Page last updated: 2024-09-04

ic 831423 and lysine

ic 831423 has been researched along with lysine in 4 studies

Compound Research Comparison

Studies
(ic 831423)
Trials
(ic 831423)
Recent Studies (post-2010)
(ic 831423)
Studies
(lysine)
Trials
(lysine)
Recent Studies (post-2010) (lysine)
440537,44962211,213

Protein Interaction Comparison

ProteinTaxonomyic 831423 (IC50)lysine (IC50)
Cationic amino acid transporter 3Homo sapiens (human)158

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (50.00)18.2507
2000's2 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Fan, B; Gettins, PG; Turko, IV1
Knauer, DJ; Kridel, SJ1
Arocas, V; Bjork, I; Bock, SC; Olson, ST; Raja, S1
Björk, I; Bock, SC; Desai, UR; Olson, ST; Schedin-Weiss, S1

Other Studies

4 other study(ies) available for ic 831423 and lysine

ArticleYear
Lysine-heparin interactions in antithrombin. Properties of K125M and K290M,K294M,K297M variants.
    Biochemistry, 1994, Nov-29, Volume: 33, Issue:47

    Topics: Antithrombins; Base Sequence; Binding Sites; Cell Line; Electrophoresis, Polyacrylamide Gel; Factor Xa Inhibitors; Heparin; Humans; Kinetics; Lysine; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligosaccharides; Recombinant Proteins; Structure-Activity Relationship; Thermodynamics; Thrombin

1994
Lysine residue 114 in human antithrombin III is required for heparin pentasaccharide-mediated activation.
    The Journal of biological chemistry, 1997, Mar-21, Volume: 272, Issue:12

    Topics: Antithrombin III; Heparin; Humans; Kinetics; Lysine; Mutagenesis; Oligosaccharides; Recombinant Proteins

1997
Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding.
    The Journal of biological chemistry, 2001, Nov-23, Volume: 276, Issue:47

    Topics: Antithrombins; Heparin; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Oligosaccharides; Protein Conformation

2001
Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change.
    Biochemistry, 2004, Jan-27, Volume: 43, Issue:3

    Topics: Alanine; Amino Acid Substitution; Antithrombins; Arginine; Aspartic Acid; Glutamic Acid; Heparin; Humans; Ions; Kinetics; Lysine; Oligosaccharides; Peptide Fragments; Protease Inhibitors; Protein Binding; Protein Conformation; Protein Structure, Tertiary

2004