Page last updated: 2024-08-23

1-carboxyglutamic acid and phosphatidylcholines

1-carboxyglutamic acid has been researched along with phosphatidylcholines in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19901 (14.29)18.7374
1990's3 (42.86)18.2507
2000's2 (28.57)29.6817
2010's1 (14.29)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Rosing, J; Speijer, H; Tans, G; Zwaal, RF1
Govers-Riemslag, JW; Janssen, MP; Rosing, J; Zwaal, RF1
Morrissey, JH; Neuenschwander, PF1
Castellino, FJ; Chan, JC; Christiansen, WT; Jalbert, LR1
Falls, LA; Furie, B; Furie, BC; Jacobs, M; Rigby, AC1
Manithody, C; Qureshi, SH; Rezaie, AR; Yang, L1
Houston, DF; Timson, DJ1

Other Studies

7 other study(ies) available for 1-carboxyglutamic acid and phosphatidylcholines

ArticleYear
Calcium-independent activation of prothrombin on membranes with positively charged lipids.
    Biochemistry, 1988, Dec-13, Volume: 27, Issue:25

    Topics: 1-Carboxyglutamic Acid; Amines; Animals; Calcium; Cattle; Cetrimonium; Cetrimonium Compounds; Electrochemistry; Factor V; Factor X; Factor Xa; Liposomes; Membrane Lipids; Phosphatidylcholines; Prothrombin; Serine Endopeptidases; Sphingosine

1988
Prothrombin activation on dioleoylphosphatidylcholine membranes.
    European journal of biochemistry, 1994, Feb-15, Volume: 220, Issue:1

    Topics: 1-Carboxyglutamic Acid; Animals; Calcium; Cattle; Electrochemistry; Factor Xa; In Vitro Techniques; Kinetics; Lipid Bilayers; Membranes, Artificial; Osmolar Concentration; Phosphatidylcholines; Phosphatidylglycerols; Phosphatidylserines; Prothrombin

1994
Roles of the membrane-interactive regions of factor VIIa and tissue factor. The factor VIIa Gla domain is dispensable for binding to tissue factor but important for activation of factor X.
    The Journal of biological chemistry, 1994, Mar-18, Volume: 269, Issue:11

    Topics: 1-Carboxyglutamic Acid; Binding Sites; Brain; Calcium; Factor IX; Factor VIIa; Humans; Kinetics; Liposomes; Mathematics; Models, Theoretical; Phosphatidylcholines; Phosphatidylserines; Thromboplastin

1994
The hydrophobic nature of residue-5 of human protein C is a major determinant of its functional interactions with acidic phospholipid vesicles.
    Biochemistry, 1996, Jun-04, Volume: 35, Issue:22

    Topics: 1-Carboxyglutamic Acid; Amino Acid Sequence; Antibodies, Monoclonal; Anticoagulants; Base Sequence; Calcium; DNA, Complementary; Factor V; Factor VIII; Fluorescence; Humans; Liposomes; Molecular Sequence Data; Mutagenesis, Site-Directed; Partial Thromboplastin Time; Phosphatidylcholines; Protein Binding; Protein C; Protein Conformation; Recombinant Proteins

1996
The omega-loop region of the human prothrombin gamma-carboxyglutamic acid domain penetrates anionic phospholipid membranes.
    The Journal of biological chemistry, 2001, Jun-29, Volume: 276, Issue:26

    Topics: 1-Carboxyglutamic Acid; Fluorescent Dyes; Humans; Models, Biological; Peptide Fragments; Phosphatidylcholines; Phosphatidylserines; Phospholipids; Potassium Iodide; Protein Binding; Protein Structure, Tertiary; Prothrombin; Spectrometry, Fluorescence

2001
Membrane-dependent interaction of factor Xa and prothrombin with factor Va in the prothrombinase complex.
    Biochemistry, 2009, Jun-09, Volume: 48, Issue:22

    Topics: 1-Carboxyglutamic Acid; Binding, Competitive; Cell Line; Epidermal Growth Factor; Factor V; Factor Va; Factor Xa; Humans; Phosphatidylcholines; Phosphatidylserines; Phospholipids; Protein Binding; Protein Structure, Tertiary; Prothrombin; Sequence Deletion; Static Electricity; Substrate Specificity; Thromboplastin

2009
Interaction of prothrombin with a phospholipid surface: evidence for a membrane-induced conformational change.
    Molecular and cellular biochemistry, 2011, Volume: 348, Issue:1-2

    Topics: 1-Carboxyglutamic Acid; Calcium; Cathepsin G; Humans; Kinetics; Lipid Bilayers; Models, Biological; Molecular Conformation; Phosphatidylcholines; Phosphatidylserines; Protein Binding; Protein Conformation; Protein Interaction Domains and Motifs; Protein Processing, Post-Translational; Prothrombin; Surface Plasmon Resonance; Thrombin

2011