The pathogenic L392V mutation of presenilin 1 decreases the affinity to glycogen synthase kinase-3β

This publication has 20 references indexed in Scilit:

• Early-Onset Autosomal Dominant Alzheimer Disease: Prevalence, Genetic Heterogeneity, and Mutation Spectrum
  American Journal of Human Genetics, 1999
• The L392V mutation of presenilin 1 associated with autosomal dominant early-onset Alzheimerʼs disease alters the secondary structure of the hydrophilic loop
  NeuroReport, 1999
• Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport
  Human Molecular Genetics, 1999
• Presenilin 1 Facilitates the Constitutive Turnover of β-Catenin: Differential Activity of Alzheimer’s Disease–Linked PS1 Mutants in the β-Catenin–Signaling Pathway
  Journal of Neuroscience, 1999
• The Glu318Gly Substitution in Presenilin 1 Is Not Causally Related to Alzheimer Disease
  American Journal of Human Genetics, 1999
• The Proteolytic Fragments of the Alzheimer's Disease-associated Presenilin-1 Form Heterodimers and Occur as a 100–150-kDa Molecular Mass Complex
  Journal of Biological Chemistry, 1998
• Evidence for a Six-transmembrane Domain Structure of Presenilin 1
  Published by Elsevier ,1997
• Phosphorylation, Subcellular Localization, and Membrane Orientation of the Alzheimer's Disease-associated Presenilins
  Journal of Biological Chemistry, 1997
• Protein Topology of Presenilin 1
  Neuron, 1996
• Mutations of the presenilin I gene in families with early-onset Alzheimer's disease
  Human Molecular Genetics, 1995