Regular ArticleKinetic Analysis of Antibody–Antigen Interactions at a Supported Lipid Monolayer
References (27)
- et al.
Methods: Companion Methods Enzymol.
(1994) - et al.
J. Biol. Chem.
(1996) - et al.
Anal. Biochem.
(1998) - et al.
Anal. Biochem.
(1991) - et al.
Mol. Immunol.
(1993) - et al.
Biochem. J.
(1992) - et al.
Anal. Biochem.
(1995) - et al.
Biochim. Biophys. Acta
(1998) Anal. Biochem.
(1976)- et al.
Biochim. Biophys. Acta
(1986)
Biochim. Biophys. Acta
(1991)
J. Immunol. Methods
(1995)
J. Colloid Interface Sci.
(1991)
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