A distinctive tract of all the forms of Alzheimer's disease is the extracellular deposition of a 40–
42/43 amino acid-long peptide derived from the so-called β-amyloid precursor protein …

The β-amyloid precursor protein (APP) is a ubiquitous receptor-like molecule without a
known function. However, the recent recognition that APP and Notch undergo highly similar …

The phosphotyrosine interaction (PI) domains (also known as the PTB, or phosphotyrosine
binding, domains) of Shc and IRS-1 are recently described domains that bind peptides …

The AICD (amyloid precursor protein [APP] intracellular domain) and C31, the caspase‐
cleaved C‐terminal fragment of APP, have been found in the brains of patients with …

The neural protein FE65 contains two types of protein-protein interaction modules: one WW
binding domain and two phosphotyrosine binding domains. The carboxyl-terminal …

Fe65 is a protein mainly expressed in several districts of the mammalian nervous system.
The search of protein sequence data banks revealed that Fe65 contains two …

The neural protein Fe65 possesses three putative protein-protein interaction domains: one
WW domain and two phosphotyrosine interaction/phosphotyrosine binding domains (PID1 …

In this study we addressed the question of the intracellular localization of Fe65, an adaptor
protein interacting with the β-amyloid precursor protein (APP) and with the transcription …

The two tandem phosphotyrosine interaction/phosphotyrosine binding (PID/PTB) domains of
the Fe65 protein interact with the intracellular region of the Alzheimer's β-amyloid precursor …

Mutations in the amyloid precursor proteingene (APP) coding for the β-amyloid precursor
protein (βPP) have been identified in autosomal dominant forms of familial Alzheimer's …