Ontology highlight
ABSTRACT:
SUBMITTER: Hauser A
PROVIDER: S-EPMC7898648 | biostudies-literature | 2021 Feb
REPOSITORIES: biostudies-literature
Hauser Anett A Poulou Eleftheria E Müller Fabian F Schmieder Peter P Hackenberger Christian P R CPR
Chemistry (Weinheim an der Bergstrasse, Germany) 20201207 7
The intrinsic lability of the phosphoramidate P-N bond in phosphorylated histidine (pHis), arginine (pHis) and lysine (pLys) residues is a significant challenge for the investigation of these post-translational modifications (PTMs), which gained attention rather recently. While stable mimics of pHis and pArg have contributed to study protein substrate interactions or to generate antibodies for enrichment as well as detection, no such analogue has been reported yet for pLys. This work reports the ...[more]