Author

Quyen V. Vu

Pennsylvania State UniversityORCID 0000-0002-9863-0486Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Bioinformatics· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:statistical model· 3 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:differential expression· 1 Organism:E. coli· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Assay:protein structure· 1

Frequent Co-Authors

Edward P. O’BrieniD· 3 shared Ian M. SitarikiD· 3 shared Hyebin SongiD· 2 shared Daniel Allen NissleyiD· 1 shared James D. StephensoniD· 1 shared Justin Petucci· 1 shared Maria F Anglero Mendez· 1 shared Pilar FrutosiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

9 top collaborators · 24 mutual co-author links

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3 shared papersBioinformatics

Edward P. O’BrienORCID

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3 papers

Recent·Most cited

Natively entangled proteins are linked to human disease and pathogenic mutations likely due to a greater misfolding propensity

Maria F Anglero Mendez, Ian M. Sitarik, Quyen V. Vu, Prabhat Totoo, James D. Stephenson, Hyebin Song, Edward P. O’Brien

The paper investigates whether proteins with native entanglements are more prone to misfolding and associated with disease, finding significant statistical associations.

bioRxiv · Apr 20, 2026 · PreprintBioinformatics

Native entanglement misfolding contributes to age-associated structural changes across the Saccharomyces cerevisiae proteome

Quyen V. Vu, Ian M. Sitarik, Daniel Allen Nissley, Edward P. O’Brien

The paper examines age-related structural changes in yeast proteins using mass spectrometry and simulations, finding that entanglement misfolding contributes to proteome aging.

bioRxiv · Apr 17, 2026 · PreprintBiochemistry

A widespread protein misfolding mechanism is differentially rescued by chaperones based on gene essentiality

Ian M. Sitarik, Quyen V. Vu, Justin Petucci, Pilar Frutos, Hyebin Song, Edward P. O’Brien

The paper identifies a widespread protein misfolding mechanism involving non-covalent lasso entanglement (NCLE) and shows that chaperones rescue it more effectively for essential proteins.

bioRxiv · Sep 18, 2025 · PreprintBiophysics