Page last updated: 2024-08-17

lysine and fibrinopeptide a

lysine has been researched along with fibrinopeptide a in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19902 (40.00)18.7374
1990's1 (20.00)18.2507
2000's2 (40.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Holmquist, R1
Osbahr, AJ1
Furlan, M; Heinemann, G; Jungo, M; Lämmle, B; Reber, P; Steinmann, C; Wermuth, B1
De Cristofaro, R; Landolfi, R1
Akhavan, S; Altomare, C; Carotti, A; De Cristofaro, R; Mannucci, PM; Peyvandi, F1

Other Studies

5 other study(ies) available for lysine and fibrinopeptide a

ArticleYear
Deviations from compositional randomness in eukaryotic and prokaryotic proteins: the hypothesis of selective-stochastic stability and a principle of charge conservation.
    Journal of molecular evolution, 1975, Mar-24, Volume: 4, Issue:4

    Topics: Amino Acids; Animals; Arginine; Aspartic Acid; Bacillus; Bacterial Proteins; Biological Evolution; Cattle; Cytochrome c Group; Deoxyribonucleases; Fibrinopeptide A; Glutamate Dehydrogenase; Glutamates; Guinea Pigs; Humans; Insulin; Lysine; Probability; Proteins; Rabbits; Snakes; Species Specificity; Statistics as Topic; Stochastic Processes; Triose-Phosphate Isomerase; Viral Proteins

1975
The action of thrombin on modified fibrinogen.
    Thrombosis and haemostasis, 1983, Jun-28, Volume: 49, Issue:3

    Topics: Amino Acids; Animals; Chemical Phenomena; Chemistry; Citraconic Anhydrides; Dogs; Fibrinogen; Fibrinopeptide A; Furans; Kinetics; Lysine; Macromolecular Substances; Thrombin

1983
Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization.
    Blood, 1993, Oct-01, Volume: 82, Issue:7

    Topics: Adult; Aged; Amino Acid Sequence; Asparagine; Base Sequence; DNA; DNA Primers; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Female; Fibrin; Fibrinogen; Fibrinogens, Abnormal; Fibrinopeptide A; Fibrinopeptide B; Genetic Variation; Humans; Kinetics; Lysine; Male; Molecular Sequence Data; Nuclear Family; Oligonucleotides, Antisense; Point Mutation; Polymerase Chain Reaction

1993
Oxidation of human alpha-thrombin by the myeloperoxidase-H2O2-chloride system: structural and functional effects.
    Thrombosis and haemostasis, 2000, Volume: 83, Issue:2

    Topics: Amino Acid Sequence; Antithrombin III; Blood Platelets; Chlorides; Chromatography, High Pressure Liquid; Fibrinopeptide A; Fibrinopeptide B; Hemostatics; Heparin; Humans; Hydrogen Peroxide; Hydrolysis; Hypochlorous Acid; Kinetics; Lysine; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peptides; Peroxidase; Platelet Activation; Protein C; Pyridoxal Phosphate; Structure-Activity Relationship; Substrate Specificity; Thrombin; Thrombomodulin

2000
A natural prothrombin mutant reveals an unexpected influence of A-chain structure on the activity of human alpha-thrombin.
    The Journal of biological chemistry, 2004, Mar-26, Volume: 279, Issue:13

    Topics: Animals; Arginine; Blood Platelets; Catalytic Domain; Cell Membrane; Chromatography, High Pressure Liquid; COS Cells; DNA; Fibrinogen; Fibrinopeptide A; Gene Deletion; Humans; Hydrolysis; Hypoprothrombinemias; Ions; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Binding; Protein C; Protein Conformation; Protein Structure, Secondary; Prothrombin; Sodium; Sodium Chloride; Thrombin; Time Factors; Transfection

2004