Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid beta-peptides.

Nakaya, Yoshifumi

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