Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid beta-peptides. [electronic resource]
- The Journal of biological chemistry May 2005
- 19070-7 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0021-9258
10.1074/jbc.M501130200 doi
Allosteric Site Amyloid beta-Peptides--chemistry Amyloid beta-Protein Precursor--chemistry Animals Binding Sites Blotting, Western Cell Line Cell Membrane--metabolism Centrifugation, Density Gradient DNA, Complementary--metabolism Dose-Response Relationship, Drug Enzyme-Linked Immunosorbent Assay Fibroblasts--metabolism Glycerol--pharmacology Humans Immunoblotting Immunohistochemistry Immunoprecipitation Mass Spectrometry Membrane Proteins--genetics Mice Mutagenesis Mutation Mutation, Missense Presenilin-1 Protein Isoforms Protein Structure, Tertiary Proteins--chemistry Receptors, Notch Retroviridae--genetics Subcellular Fractions--metabolism Sulindac--analogs & derivatives Transfection Up-Regulation