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 non Alzheimer's disease (non-AD) brain tissue but not in AD brain tissue

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PRNP SYNPO
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
-

Curated By

  • BioGRID