Characterization of a novel protein-binding module—the WW domain

M Sudol, HI Chen, C Bougeret, A Einbond, P Bork - FEBS letters, 1995 - Elsevier
We have identified, characterized and cloned human, mouse and chicken cDNA of a novel
protein that binds to the Src homology domain 3 (SH3) of the Yes proto-oncogene product …

Structure and function of the WW domain

M Sudol - Progress in biophysics and molecular biology, 1996 - Elsevier
Although intuitively clear, the concept of the protein domain eludes strict and universally
accepted definition. At the recent Meeting on Perspectives of Protein Engineering (held from …

A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60

X Cao, TC Sudhof - Science, 2001 - science.org
Amyloid-β precursor protein (APP), a widely expressed cell-surface protein, is cleaved in the
transmembrane region by γ-secretase. γ-Cleavage of APP produces the extracellular …

Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions

PJ Cook, BG Ju, F Telese, X Wang, CK Glass… - Nature, 2009 - nature.com
Life and death fate decisions allow cells to avoid massive apoptotic death in response to
genotoxic stress. Although the regulatory mechanisms and signalling pathways controlling …

The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner

WT Kimberly, JB Zheng, SY Guénette… - Journal of Biological …, 2001 - ASBMB
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 domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein

JP Borg, J Ooi, E Levy, B Margolis - Molecular and cellular biology, 1996 - Am Soc Microbiol
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 APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor

RC Von Rotz, BM Kohli, J Bosset… - Journal of cell …, 2004 - journals.biologists.com
The physiological functions of the beta-amyloid precursor protein (APP) may include nuclear
signaling. To characterize the role of the APP adaptor proteins Fe65, Jip1b, X11α (MINT1) …

Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein

M Trommsdorff, JP Borg, B Margolis, J Herz - Journal of Biological …, 1998 - ASBMB
Apolipoprotein E, α 2-macroglobulin, and amyloid precursor protein (APP) are involved in
the development of Alzheimer's disease. All three proteins are ligands for the low density …

Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain

P May, YK Reddy, J Herz - Journal of Biological Chemistry, 2002 - ASBMB
The low density lipoprotein (LDL) receptor-related protein (LRP) is a multifunctional cell
surface receptor that interacts through its cytoplasmic tail with adaptor and scaffold proteins …

The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the …

F Fiore, N Zambrano, G Minopoli, V Donini… - Journal of Biological …, 1995 - ASBMB
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 …