Author

E. Serebryany

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 4 Organism:human· 3 Assay:protein structure· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Organism:E. coli· 1

Frequent Co-Authors

E. I. Shakhnovich· 3 shared A. Bitran· 2 shared B. Budnik· 2 shared E. Shakhnovich· 2 shared K. Park· 2 shared S. A. Trauger· 2 shared A. McClelland· 1 shared C. N. Woods· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersBiophysics

E. I. Shakhnovich

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5 papers

Recent·Most cited

Cotranslational formation of disulfides guides folding of the SARS CoV-2 receptor binding domain

A. Bitran, K. Park, E. Serebryany, E. Shakhnovich

The paper investigates how disulfide bond formation during translation guides the folding of the SARS-CoV-2 RBD, showing that non-equilibrium mechanisms are required to prevent misfolding.

bioRxiv · Nov 10, 2022Biophysics

Systematic conformation-to-phenotype mapping via limited deep-sequencing of proteins

E. Serebryany, V. Y. Zhao, K. Park, A. Bitran, S. A. Trauger, B. Budnik, E. I. Shakhnovich

The paper develops a method to map protein conformations to phenotypes by systematically analyzing disulfide bonds in proteins.

bioRxiv · Apr 12, 2022Biophysics

A native chemical chaperone in the human eye lens

E. Serebryany, S. Chowdhury, C. N. Woods, D. C. Thorn, N. E. Watson, A. McClelland, R. E. Klevit, E. I. Shakhnovich

This study identifies myo-inositol as a chemical chaperone that suppresses lens crystallin aggregation, suggesting its potential as a therapeutic target for age-related cataracts.

bioRxiv · Dec 16, 2020Biophysics

Conformational catalysis of cataract-associated aggregation in a human eye lens crystallin occurs via interface stealing.

E. Serebryany, W. M. Jacobs, R. Razban, E. Shakhnovich

This study reveals that wild-type HγD accelerates aggregation of the cataract-related W42Q variant through a mechanism called interface stealing, where intermolecular domain interactions outcompete native intramolecular stabilization.

bioRxiv · Apr 29, 2019 · PreprintBiophysics

Catalysis of cataract-associated human γD crystallin aggregation via dynamic disulfide exchange

E. Serebryany, S. Yu, S. A. Trauger, B. Budnik, E. I. Shakhnovich

The paper shows wild-type human γD crystallin catalyzes aggregation of its W42Q variant through disulfide bond transfer, revealing a redox mechanism relevant to protein aggregation in oxidizing environments.

bioRxiv · Apr 12, 2018Biochemistry