Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide. [electronic resource]
Producer: 20030107Description: 44754-9 p. digitalISSN:- 0021-9258
- Alzheimer Disease -- metabolism
- Amino Acid Sequence
- Amyloid Precursor Protein Secretases
- Amyloid beta-Peptides -- metabolism
- Amyloid beta-Protein Precursor -- genetics
- Animals
- Aspartic Acid Endopeptidases -- metabolism
- Carbamates -- pharmacology
- Cell Line
- Cell Membrane -- metabolism
- Dipeptides -- pharmacology
- Endopeptidases -- metabolism
- Enzyme Inhibitors -- pharmacology
- Fibroblasts -- cytology
- Humans
- Hyaluronan Receptors -- genetics
- Membrane Proteins -- genetics
- Mice
- Mice, Knockout
- Molecular Sequence Data
- Peptides -- genetics
- Presenilin-1
- Presenilin-2
- Protein Structure, Tertiary
- Sequence Alignment
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Triglycerides -- pharmacology
- gamma-Aminobutyric Acid -- analogs & derivatives
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
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