Amyloid beta A4 precursor protein-binding family B member 2 and Amyloid beta A4 protein

Chemical shift reference of 1H was based on the proton of water (4.784ppm at
298K) and then those of 15N and 13C were calculated based on their gyromagnetic
ratios.

Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode.

Solution Structure Of The C-Terminal Phosphotyrosine Interaction Domain Of Apbb2 From Mouse

Structure Of The C-Terminal Pid Domain Of Fe65l1 Complexed With The Cytoplasmic Tail Of App Reveals A Novel Peptide Binding Mod

Solution Structure Of The Chimera Of The C-Terminal Pid Domain Of Fe65l And The C-Terminal Tail Peptide Of App

amyloid beta (A4) precursor protein-binding, family B, member 2, isoform CRA_a [Mus musculus]

similar to amyloid beta (A4) precursor protein-binding, family B, member 2 (predicted) [Rattus norvegicus]

Amyloid beta A4 precursor protein-binding family B member 2, partial [Cricetulus griseus]

amyloid beta A4 precursor protein-binding family B member 2 [Cricetulus griseus]

amyloid beta A4 precursor protein-binding family B member 2 isoform 2 [Mus musculus]

amyloid beta A4 precursor protein-binding family B member 2 isoform 3 [Mus musculus]

amyloid beta A4 precursor protein-binding family B member 2 isoform 4 [Mus musculus]

amyloid beta A4 precursor protein-binding family B member 2 isoform 5 [Mus musculus]

amyloid beta A4 precursor protein-binding family B member 2 isoform 6 [Mus musculus]

RecName: Full=Amyloid beta A4 precursor protein-binding family B member 2

Solution structure of the chimera of the C-terminal PID domain of Fe65L and the
C-terminal tail peptide of APP

Protein Research Group, RIKEN Genomic Sciences Center
Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax