Ontology highlight
ABSTRACT:
SUBMITTER: Linthwaite VL
PROVIDER: S-EPMC8462908 | biostudies-literature | 2021 Sep
REPOSITORIES: biostudies-literature
Linthwaite Victoria L VL Pawloski Wes W Pegg Hamish B HB Townsend Philip D PD Thomas Michael J MJ So Victor K H VKH Brown Adrian P AP Hodgson David R W DRW Lorimer George H GH Fushman David D Cann Martin J MJ
Science advances 20210924 39
The identification of CO<sub>2</sub>-binding proteins is crucial to understanding CO<sub>2</sub>-regulated molecular processes. CO<sub>2</sub> can form a reversible posttranslational modification through carbamylation of neutral N-terminal α-amino or lysine ε-amino groups. We have previously developed triethyloxonium (TEO) ion as a chemical proteomics tool for covalent trapping of carbamates, and here, we deploy TEO to identify ubiquitin as a mammalian CO<sub>2</sub>-binding protein. We use <sup ...[more]