1 |
ATP antagonizes the crowding-induced destabilization of the human eye-lens protein gamma S-crystallin He Y, Kang J, Song JX Biochemical and Biophysical Research Communications, 526(4), 1112, 2020 |
2 |
The cataract-related S39C variant increases gamma S-crystallin sensitivity to environmental stress by destroying the intermolecular disulfide cross-links Yang XX, Xu JJ, Fu CX, Jia ZK, Yao K, Chen XJ Biochemical and Biophysical Research Communications, 526(2), 459, 2020 |
3 |
ATP differentially antagonizes the crowding-induced destabilization of human gamma S-crystallin and its four cataract-causing mutants He Y, Kang J, Song JX Biochemical and Biophysical Research Communications, 533(4), 913, 2020 |
4 |
Cataract-causing G18V eliminates the antagonization by ATP against the crowding-induced destabilization of human gamma S-crystallin He Y, Kang J, Song JX Biochemical and Biophysical Research Communications, 530(3), 554, 2020 |
5 |
Enhanced H/D exchange unravels sequential structural excursions in G57W variant of human gamma S-crystallin with pro-cataractogenic conformations Bari KJ, Sharma S, Chary KVR Biochemical and Biophysical Research Communications, 514(3), 901, 2019 |
6 |
Hemin as a generic and potent protein misfolding inhibitor Liu Y, Carver JA, Ho LH, Elias AK, Musgrave IF, Pukala TL Biochemical and Biophysical Research Communications, 454(2), 295, 2014 |