Author

Eugene I. Shakhnovich

Primary ORCID profile (0000-0002-4769-2265 · 25 papers)Unclaimed ORCID profile · follow to get notified of new preprints

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Eugene I. ShakhnovichiD25 papers · Harvard University

Biology Disciplines

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Approach:statistical model· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:DNA methylation· 1 Organism:E. coli· 1 Assay:protein structure· 1 Assay:proteomics· 1 Research Focus:variant effect prediction· 1

Frequent Co-Authors

Eugene Serebryany· 2 shared William M. Jacobs· 2 shared Bharat V. Adkar· 1 shared Jaie C. Woodard· 1 shared Jonathan A. King· 1 shared Mohammed Shabab· 1 shared Rostam M. Razban· 1 shared

Activity by Year

2016-2019 · peak 1/yr

Co-Author Collaboration Network

7 top collaborators · 13 mutual co-author links

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2 shared papersBiophysics

Eugene Serebryany

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3 papers

Recent·Most cited

BiophysicsbioRxivPreprintApr 29, 2019

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

Eugene Serebryany, William M. Jacobs, Rostam M. Razban, Eugene I. 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.

DOI 10.1101/601708

humanprotein structure

𝕏 PostBluesky

BiophysicsbioRxivPreprintOct 23, 2017

Evidence of evolutionary selection for co-translational folding

William M. Jacobs, Eugene I. Shakhnovich

The paper identifies evolutionary selection for co-translational folding by analyzing synonymous substitutions in E. coli genes.

DOI 10.1101/121871

E. coliDNA methylation

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BiophysicsJournal of Biological ChemistryPeer-reviewedSep 1, 2016

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…·Eugene I. Shakhnovich

The paper investigates how an internal disulfide bond stabilizes a misfolded intermediate in cataract-linked γD-crystallin mutants, leading to amorphous aggregation.

DOI 10.1074/jbc.m116.735977

humanproteomics

𝕏 PostBluesky