Ian M. Sitarik

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional

Daniel A. Nissley, E. O’Brien, S. Fried, 2022, Nature communications.

A New Class of Protein Misfolding is Observed in All-atom Folding Simulations

E. O’Brien, M. Li, Quyen V. Vu, 2022, bioRxiv.

How synonymous mutations alter enzyme structure and function over long timescales

E. O’Brien, S. Fried, S. Booker, 2021, bioRxiv.

A Newly Identified Class of Protein Misfolding in All-atom Folding Simulations Consistent with Limited Proteolysis Mass Spectrometry

E. O’Brien, M. Li, S. Fried, 2022, bioRxiv.

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional

Daniel A. Nissley, E. O’Brien, S. Fried, 2021, Nature Communications.

Subpopulations of soluble, misfolded proteins commonly bypass chaperones: How it happens at the molecular level

Daniel A. Nissley, E. O’Brien, Ritaban Halder, 2021, bioRxiv.

How soluble misfolded proteins bypass chaperones at the molecular level

Daniel A. Nissley, J. Pritchard, E. O’Brien, 2023, Nature communications.