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Philip To

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Nature Communications|June 2, 2022

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functionalDaniel A Nissley, Yang Jiang, Fabio Trovato, et al.

Nature Chemistry|December 5, 2022

How synonymous mutations alter enzyme structure and function over long timescalesYang Jiang, Syam Sundar Neti, Ian Sitarik, et al.

Journal of Molecular Biology|February 10, 2024

Synonymous Mutations Can Alter Protein Dimerization Through Localized Interface Misfolding Involving Self-entanglementsPham Dang Lan, Daniel Allen Nissley, Ian Sitarik, et al.

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Search research articles

Showing results (11-20 of 13) with videos related to

Sort By:

Pageof 2

You have reached the last page of results.This site can display upto 13 results.

Nature Communications|June 2, 2022

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functionalDaniel A Nissley, Yang Jiang, Fabio Trovato, et al.

Nature Chemistry|December 5, 2022

How synonymous mutations alter enzyme structure and function over long timescalesYang Jiang, Syam Sundar Neti, Ian Sitarik, et al.

Journal of Molecular Biology|February 10, 2024

Synonymous Mutations Can Alter Protein Dimerization Through Localized Interface Misfolding Involving Self-entanglementsPham Dang Lan, Daniel Allen Nissley, Ian Sitarik, et al.

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