PREY

APP

AAA, ABETA, ABPP, AD1, APPI, CTFgamma, CVAP, PN-II, PN2
amyloid beta (A4) precursor protein
GO Process (29)
GO Function (8)
GO Component (21)
Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones.

Narayan P, Meehan S, Carver JA, Wilson MR, Dobson CM, Klenerman D

The aberrant aggregation of the amyloid-β peptide into β-sheet rich, fibrillar structures proceeds via a heterogeneous ensemble of oligomeric intermediates that have been associated with neurotoxicity in Alzheimer's disease (AD). Of particular interest in this context are the mechanisms by which molecular chaperones, part of the primary biological defenses against protein misfolding, influence Aβ aggregation. We have used single-molecule fluorescence ... [more]

Biochemistry Nov. 20, 2012; 51(46);9270-6 [Pubmed: 23106396]

Throughput

  • Low Throughput

Additional Notes

  • binds APP aggregates

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
APP CRYAB
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Low-BioGRID
-
APP CRYAB
Affinity Capture-Western
Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
CRYAB APP
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
1528517
CRYAB APP
Protein-peptide
Protein-peptide

An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.

Low-BioGRID
728540
APP CRYAB
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
CRYAB APP
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID