[HTML][HTML] The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
G Carmel, EM Mager, LI Binder, J Kuret - Journal of Biological Chemistry, 1996 - ASBMB
The epitope on tau protein recognized by the monoclonal antibody Alz50 was defined
through internal deletion mutagenesis and quantified by affinity measurements. The epitope
is discontinuous and requires both a previously identified N-terminal segment and the
microtubule binding region for efficient binding of Alz50. The interaction between these
regions is consistent with an intramolecular reaction mechanism, suggesting that Alz50
binding depends on the conformation of individual tau monomers. The results suggest that …
through internal deletion mutagenesis and quantified by affinity measurements. The epitope
is discontinuous and requires both a previously identified N-terminal segment and the
microtubule binding region for efficient binding of Alz50. The interaction between these
regions is consistent with an intramolecular reaction mechanism, suggesting that Alz50
binding depends on the conformation of individual tau monomers. The results suggest that …