In:
Annual Review of Biochemistry, Annual Reviews, Vol. 88, No. 1 ( 2019-06-20), p. 383-408
Abstract:
The cellular thermal shift assay (CETSA) is a biophysical technique allowing direct studies of ligand binding to proteins in cells and tissues. The proteome-wide implementation of CETSA with mass spectrometry detection (MS-CETSA) has now been successfully applied to discover targets for orphan clinical drugs and hits from phenotypic screens, to identify off-targets, and to explain poly-pharmacology and drug toxicity. Highly sensitive multidimensional MS-CETSA implementations can now also access binding of physiological ligands to proteins, such as metabolites, nucleic acids, and other proteins. MS-CETSA can thereby provide comprehensive information on modulations of protein interaction states in cellular processes, including downstream effects of drugs and transitions between different physiological cell states. Such horizontal information on ligandmodulation in cells is largely orthogonal to vertical information on the levels of different proteins and therefore opens novel opportunities to understand operational aspects of cellular proteomes.
Type of Medium:
Online Resource
ISSN:
0066-4154
,
1545-4509
DOI:
10.1146/annurev-biochem-062917-012837
Language:
English
Publisher:
Annual Reviews
Publication Date:
2019
detail.hit.zdb_id:
1470446-8
SSG:
12