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adenosine diphosphate and glycyl-arginyl-glycyl-aspartyl-serine

adenosine diphosphate has been researched along with glycyl-arginyl-glycyl-aspartyl-serine in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19901 (25.00)18.7374
1990's2 (50.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Adelman, B; Gennings, C; Hanners, E; Strony, J1
Adelman, B; Hanners, E; Rizk, A1
Eldor, A; Gorecki, M; Guy, R; Legrand, C; Levanon, A; Nimrod, A; Panet, A; Vogel, T; Werber, MM1
Chaulet, H; Desgranges, C; Dupuch, F; Ezan, G; Gadeau, AP; Loirand, G; Pacaud, P; Peiretti, F; Renault, MA1

Other Studies

4 other study(ies) available for adenosine diphosphate and glycyl-arginyl-glycyl-aspartyl-serine

ArticleYear
Synergistic inhibition of platelet aggregation by fibrinogen-related peptides.
    Circulation research, 1990, Volume: 67, Issue:4

    Topics: Adenosine Diphosphate; Amino Acid Sequence; Drug Synergism; Fibrinogen; Humans; Molecular Sequence Data; Oligopeptides; Peptide Fragments; Peptides; Platelet Aggregation; Platelet Aggregation Inhibitors

1990
Plasminogen interactions with platelets in plasma.
    Blood, 1988, Volume: 72, Issue:5

    Topics: Adenosine Diphosphate; Aminocaproates; Binding Sites; Blood Platelets; Cell Adhesion; Fibrinogen; Flow Cytometry; Humans; In Vitro Techniques; Oligopeptides; Plasminogen; Platelet Aggregation; Protein Binding

1988
Studies on fibronectin and its domains. I. Novel recombinant cell-binding domain of fibronectin--a modulator of human platelet functions.
    Archives of biochemistry and biophysics, 1993, Volume: 300, Issue:1

    Topics: 3T3 Cells; Adenosine Diphosphate; Animals; Base Sequence; Binding Sites; Blood Platelets; Calcimycin; Cell Adhesion; Cloning, Molecular; Codon; Collagen; Epinephrine; Escherichia coli; Fibronectins; Gene Library; Humans; Mice; Oligopeptides; Plasmids; Platelet Aggregation; Protein Biosynthesis; Protein Folding; Recombinant Proteins; Restriction Mapping

1993
Extracellular nucleotides induce arterial smooth muscle cell migration via osteopontin.
    Circulation research, 2001, Oct-26, Volume: 89, Issue:9

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Aorta; Calcium; Cell Movement; Cells, Cultured; Chemotaxis; Diffusion Chambers, Culture; Dose-Response Relationship, Drug; Enzyme Inhibitors; Extracellular Space; Intracellular Signaling Peptides and Proteins; Mitogen-Activated Protein Kinases; Muscle, Smooth, Vascular; Nucleotides; Oligopeptides; Osteopontin; Phosphorylation; Protein Serine-Threonine Kinases; Rats; Rats, Wistar; rho-Associated Kinases; rhoA GTP-Binding Protein; Sialoglycoproteins; Uridine Diphosphate; Uridine Triphosphate

2001