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Results 1-10 of 14 (Search time: 0.005 seconds).

  Highly constrained cyclic (S,S) -CXaaC- peptides as inhibitors of fibrinogen binding to platelets (Journal article)

  Inhibition of platelet activation and fibrinogen binding to alpha(IIb)beta(3) using synthetic peptide-analogues derived from the beta(3) subunit: A comparative study (Journal article)

  Inhibition of platelet activation by peptide analogs of the beta(3)-intracellular domain of platelet integrin alpha(IIb)beta(3) conjugated to the cell-penetrating peptide Tat(48-60) (Journal article)

  Inhibitory Effects of Synthetic Peptide Analogues of the Human Platelet Integrin Alphaiibeta Subunit on Rabbit Platelet Aggregation (Journal article)

  Investigation of the role of adjacent amino acids to the 313-320 sequence of the alpha(IIb) subunit on platelet activation and fibrinogen binding to alpha(IIb)beta(3) (Journal article)

  Mapping the binding domains of the alpha(IIb) subunit - A study performed on the activated form of the platelet integrin alpha(IIb)beta(3) (Journal article)

  A palmitoylated peptide, derived from the acidic carboxyl-terminal segment of the integrin IIb cytoplasmic domain, inhibits platelet activation (Journal article)

  A highly constrained cyclic (S,S)-CDC- peptide is a potent inhibitor of carotid artery thrombosis in rabbits (Journal article)

  Effect of a Synthetic Peptide Corresponding to Residues 313 to 320 of the alpha(IIb) Subunit of the Human Platelet Integrin alpha(IIb)beta(3) on Carotid Artery Thrombosis in Rabbits (Journal article)

  Synthetic peptide-analogues of the GPIIb subunit inhibit fibrinogen binding to the GPIIb/IIIa receptor and platelet activation (Journal article)