C.J. de Haas
Department of Inflammation
Eijkman Winkler Institute
University Utrecht
Netherlands
Name/email consistency: high
- Serum amyloid P component bound to gram-negative bacteria prevents lipopolysaccharide-mediated classical pathway complement activation. de Haas, C.J., van Leeuwen, E.M., van Bommel, T., Verhoef, J., van Kessel, K.P., van Strijp, J.A. Infect. Immun. (2000)
- Serum amyloid P component prevents high-density lipoprotein-mediated neutralization of lipopolysaccharide. de Haas, C.J., Poppelier, M.J., van Kessel, K.P., van Strijp, J.A. Infect. Immun. (2000)
- Analysis of lipopolysaccharide (LPS)-binding characteristics of serum components using gel filtration of FITC-labeled LPS. de Haas, C.J., van Leeuwen, H.J., Verhoef, J., van Kessel, K.P., van Strijp, J.A. J. Immunol. Methods (2000)
- Lipopolysaccharide (LPS)-binding synthetic peptides derived from serum amyloid P component neutralize LPS. de Haas, C.J., van der Zee, R., Benaissa-Trouw, B., van Kessel, K.P., Verhoef, J., van Strijp, J.A. Infect. Immun. (1999)
- A synthetic lipopolysaccharide-binding peptide based on amino acids 27-39 of serum amyloid P component inhibits lipopolysaccharide-induced responses in human blood. de Haas, C.J., van der Tol, M.E., Van Kessel, K.P., Verhoef, J., Van Strijp, J.A. J. Immunol. (1998)
- Affinities of different proteins and peptides for lipopolysaccharide as determined by biosensor technology. de Haas, C.J., Haas, P.J., van Kessel, K.P., van Strijp, J.A. Biochem. Biophys. Res. Commun. (1998)
