Utilization of Stability-based Proteomics for the Investigation of Structured RNA-protein Interactions
Ontology highlight
ABSTRACT: The stability of proteins from rates of oxidation (SPROX), thermal protein profiling (TPP) methods as well as triple helix pulldowns with LC-MS/MS readouts are used to identify the protein targets of three RNA ligands, the MALAT1 triple helix (TH), a viral stem loop (SL), and an unstructured RNA (PolyU) in LNCaP nuclear lysate. This work establishes a novel platform for the global discovery and interrogation of RNA-protein interactions that is generalizable to numerous biological contexts and RNA targets.
INSTRUMENT(S): Orbitrap Exploris 480
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Lncap Cell, Cell Culture
DISEASE(S): Prostate Adenocarcinoma
SUBMITTER: Morgan Bailey
LAB HEAD: Dr. Michael C. Fitzgerald
PROVIDER: PXD043878 | Pride | 2024-01-31
REPOSITORIES: Pride
ACCESS DATA