BAIT
PRDX1
MSP23, NKEF-A, NKEFA, PAG, PAGA, PAGB, PRX1, PRXI, TDPX2, RP11-291L19.4
peroxiredoxin 1
GO Process (3)
GO Function (4)
GO Component (5)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
CKB
Ckbb, Ckbr
creatine kinase, brain
GO Process (4)
GO Function (2)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Rattus norvegicus
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
Structural and biochemical analyses reveal ubiquitin C-terminal hydrolase-L1 as a specific client of the peroxiredoxin II chaperone.
Peroxiredoxins (Prxs) play dual roles as both thiol-peroxidases and molecular chaperones. Peroxidase activity enables various intracellular functions, however, the physiological roles of Prxs as chaperones are not well established. To study the chaperoning function of Prx, we previously sought to identify heat-induced Prx-binding proteins as the clients of a Prx chaperone. By using His-tagged Prx I as a bait, we ... [more]
Arch. Biochem. Biophys. Dec. 15, 2017; 640();61-74 [Pubmed: 29339092]
Throughput
- High Throughput
Curated By
- BioGRID