A Consensus Tetrapeptide Selected by Phage Display Adopts the Conformation of a Dominant Discontinuous Epitope of a Monoclonal Anti-VWF Antibody That Inhibits the von Willebrand Factor-Collagen Interaction
Open Access
- 1 September 2003
- journal article
- Published by Elsevier BV
- Vol. 278 (39), 37815-37821
- https://doi.org/10.1074/jbc.m304289200
Abstract
No abstract availableThis publication has 52 references indexed in Scilit:
- Collagen-binding mode of vWF-A3 domain determined by a transferred cross-saturation experimentNature Structural & Molecular Biology, 2002
- Low Molecular Weight Peptides Restore the Procoagulant Activity of Factor VIII in the Presence of the Potent Inhibitor Antibody ESH8Published by Elsevier BV ,2002
- The use of phage‐peptide libraries to define the epitope specificity of a mouse monoclonal anti‐Der p 1 antibody representative of a major component of the human immunoglobulin E anti‐Der p 1 responseClinical and Experimental Allergy, 1999
- Phage DisplayChemical Reviews, 1997
- Characterization of the Unique Mechanism Mediating the Shear-dependent Binding of Soluble von Willebrand Factor to PlateletsPublished by Elsevier BV ,1995
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Synthetic peptides inhibit the interaction of von Willebrand factor-platelet membrane glycoproteinsPeptides, 1993
- Effect of deletion of the A1 domain of von Willebrand factor on its binding to heparin, collagen and platelets in the presence of ristocetinJBIC Journal of Biological Inorganic Chemistry, 1991
- Searching for Peptide Ligands with an Epitope LibraryScience, 1990
- The BRUGEL package: toward computer-aided design of macromoleculesJournal of Molecular Graphics, 1988