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Results 1-10 of 16 (Search time: 0.003 seconds).

  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)

  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)

  A three-residue cyclic scaffold of non-RGD containing peptide analogues as platelet aggregation inhibitors: design, synthesis, and structure-function relationships (Journal article)

  A three-residue cyclic scaffold of non-RGD containing peptide analogues as platelet aggregation inhibitors: Design, synthesis, and structure-function relationships (Journal article)

  The Relative Orientation of the Arg and Asp Side Chains in Rgd Peptides: A Key Criterion for Evaluation the Structure-Activity Relationship (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)

  Further insight into the fibrinogen binding domains of platelet alpha(IIB) subunit: Structural and functional studies of the antiplatelet peptide analogue 313-320 of alpha(IIB) (Journal article)

  Peptide analogues derived from the cytoplasmic domain of alpha IIB beta 3 integrin receptor inhibit platelet aggregation (Journal article)

  Peptides Derived from Cytoplasmic Region of the Integrin Platelet Receptor as Anti-Aggregatory Agients (Journal article)

  Mapping the Fibrinogen Binding Sites of the Platelet Receptor Using Synthetic Peptides Derived from the Beta 3 Subunit (Journal article)