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Methods in Enzymology|November 20, 2025
Enzyme-free biochemical production of seamlessly N-to-C cyclized peptides from natural or recombinant proteinsAli Behboodian, Eugene SerebryanyBiorxiv : the Preprint Server for Biology|August 6, 2025
Enzyme-free biochemical production of seamlessly N-to-C cyclized peptides from natural or recombinant proteinsAli Behboodian, Eugene SerebryanyBiorxiv : the Preprint Server for Biology|January 16, 2026
Disulfide engineering reveals unexpected pro- and anti-aggregation conformers of human α-synucleinAslam Uddin, Eugene SerebryanyProgress in Biophysics and Molecular Biology|May 20, 2014
The βγ-crystallins: native state stability and pathways to aggregationEugene Serebryany, Jonathan A KingThe Journal of Biological Chemistry|March 20, 2015
Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutantEugene Serebryany, Jonathan A KingExperimental Eye Research|August 1, 2021
Redox chemistry of lens crystallins: A system of cysteinesEugene Serebryany, David C Thorn, Liliana QuintanarBiomolecules|May 24, 2024
The Functional Significance of High Cysteine Content in Eye Lens γ-CrystallinsEugene Serebryany, Rachel W Martin, Gemma R TakahashiBiophysical Journal|July 9, 2023
Co-translational formation of disulfides guides folding of the SARS-CoV-2 receptor binding domainAmir Bitran, Kibum Park, Eugene Serebryany, et al.Biochimica Et Biophysica Acta|August 20, 2011
Artificial membrane-like environments for in vitro studies of purified G-protein coupled receptorsEugene Serebryany, Gefei Alex Zhu, Elsa C Y YanBiorxiv : the Preprint Server for Biology|November 16, 2022
Cotranslational formation of disulfides guides folding of the SARS COV-2 receptor binding domainAmir Bitran, Kibum Park, Eugene Serebryany, et al.Pageof 3