Aberrant Amyloid Precursor Protein (APP) Processing in Hereditary Forms of Alzheimer Disease Caused by APP Familial Alzheimer Disease Mutations Can Be Rescued by Mutations in the APP GxxxG Motif

This publication has 46 references indexed in Scilit:

• Neuroprotective Secreted Amyloid Precursor Protein Acts by Disrupting Amyloid Precursor Protein Dimers
  Published by Elsevier ,2009
• Mutational Analysis in Early-Onset Familial Dementia in the Japanese Population
  Dementia and Geriatric Cognitive Disorders, 2008
• Substrate-targeting γ-secretase modulators
  Nature, 2008
• Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants
  BMC Neuroscience, 2008
• Aβ42 Overproduction Associated with Structural Changes in the Catalytic Pore of γ-Secretase
  Published by Elsevier ,2007
• GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42
  The EMBO Journal, 2007
• Loss‐of‐function presenilin mutations in Alzheimer disease
  EMBO Reports, 2007
• Homo- and heterodimerization of APP family members promotes intercellular adhesion
  The EMBO Journal, 2005
• Nonfibrillar diffuse amyloid deposition due to a gamma42-secretase site mutation points to an essential role for N-truncated Abeta42 in Alzheimer's disease
  Human Molecular Genetics, 2000
• Membrane inserted APP fragments containing the βA4 sequence of Alzheimer's disease do not aggregate
  FEBS Letters, 1992