1 citations · 1 across the 4 of their papers we have counts for
4 papers
Systematic conformation-to-phenotype mapping via limited deep-sequencing of proteins
Eugene Serebryany, Victor Y. Zhao, Kibum Park +4
Non-native conformations drive protein misfolding diseases, complicate bioengineering efforts, and fuel molecular evolution. No current experimental technique is well-suited for el…
A native chemical chaperone in the human eye lens
Eugene Serebryany, Sourav Chowdhury, Nicki E. Watson +2
Cataract is one of the most prevalent protein aggregation disorders and still the biggest cause of vision loss worldwide. The human lens, in its core region, lacks turnover of any…
Conformational catalysis of cataract-associated aggregation by interacting intermediates in a human eye lens crystallin
Eugene Serebryany, Rostam Razban, Eugene I Shakhnovich
Most known proteins in nature consist of multiple domains. Interactions between domains may lead to unexpected folding and misfolding phenomena. This study of human γD-crystallin,…
An internal disulfide locks a misfolded aggregation-prone intermediate in cataract-linked mutants of human γD-crystallin
Eugene Serebryany, Jaie C. Woodard, Bharat V. Adkar +3
Considerable mechanistic insight has been gained into amyloid aggregation; however, a large class of non-amyloid protein aggregates are considered 'amorphous,' and in most cases li…