Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid beta-peptides. [electronic resource]
Producer: 20050712Description: 19070-7 p. digitalISSN:- 0021-9258
- 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
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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.
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