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.

Publication

Alterations in the brain interactome of the intrinsically disordered N-terminal domain of the cellular prion protein (PrPC) in Alzheimer's disease.

Ulbrich S, Janning P, Seidel R, Matschke J, Gonsberg A, Jung S, Glatzel M, Engelhard M, Winklhofer KF, Tatzelt J

The cellular prion protein (PrPC) is implicated in neuroprotective signaling and neurotoxic pathways in both prion diseases and Alzheimer's disease (AD). Specifically, the intrinsically disordered N-terminal domain (N-PrP) has been shown to interact with neurotoxic ligands, such as A? and Scrapie prion protein (PrPSc), and to be crucial for the neuroprotective activity of PrPC. To gain further insight into cellular ... [more]

PLoS One May. 24, 2018; 13(5);e0197659 [Pubmed: 29791485]

Throughput

  • High Throughput

Additional Notes

  • interaction identified using tandem mass spectrometry in Alzheimer's disease (AD) brain tissue but not in non-AD brain tissue

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
NCAM1 PRNP
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
-
PRNP NCAM1
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
-
NCAM1 PRNP
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID