@article{10902/38194,
year = {2020},
url = {https://hdl.handle.net/10902/38194},
abstract = {The haemathrins are tick-derived thrombin-inhibiting proteins predicted to be post-translationally sulfated. This study reports the ligation-based assembly of eight homogeneously sulfated variants of haemathrin-1 and haemathrin-2. Functional assays revealed a two orders-of-magnitude enhancement in thrombin-inhibitory potency by tyrosine sulfation, thus reinforcing the crucial role of this post-translational modification for the activity of anticoagulant proteins.},
publisher = {Royal Society of Chemistry},
publisher = {RSC Chemical Biology, 2020, 1, 379},
title = {Chemical synthesis of a haemathrin sulfoprotein library reveals enhanced thrombin inhibition following tyrosine sulfation},
author = {Clayton, Daniel and Kulkarni, Sameer S. and Sayers, Jessica and Dowman, Luke J. and Ripoll Rozada, Jorge and Barbosa Pereira, Pedro José and Payne, Richard J.},
}