Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1

Nat Cell Biol. 2000 Jul;2(7):463-5. doi: 10.1038/35017108.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amyloid Precursor Protein Secretases
  • Amyloid beta-Peptides / chemistry
  • Amyloid beta-Peptides / metabolism
  • Amyloid beta-Protein Precursor / chemistry
  • Amyloid beta-Protein Precursor / genetics
  • Amyloid beta-Protein Precursor / metabolism*
  • Animals
  • Aspartic Acid Endopeptidases
  • Cells, Cultured
  • Endopeptidases / metabolism*
  • Gene Deletion
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Knockout
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Presenilin-1
  • Presenilin-2
  • Protein Processing, Post-Translational*
  • Protein Structure, Tertiary
  • Receptor, Notch1
  • Receptors, Cell Surface*
  • Transcription Factors*
  • Transfection

Substances

  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Membrane Proteins
  • Notch1 protein, mouse
  • Peptide Fragments
  • Presenilin-1
  • Presenilin-2
  • Receptor, Notch1
  • Receptors, Cell Surface
  • Transcription Factors
  • Amyloid Precursor Protein Secretases
  • Endopeptidases
  • Aspartic Acid Endopeptidases
  • Bace1 protein, mouse