Author

H. M. Forsythe

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· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1 Organism:virus· 1

Frequent Co-Authors

E. J. Barbar· 2 shared P. N. Reardon· 2 shared A. B. Estelle· 1 shared B. Lasher· 1 shared C. J. Vetter· 1 shared D. A. Hendrix· 1 shared K. Hughes· 1 shared K. J. Jara· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersBiophysics

E. J. Barbar

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2 papers

Recent·Most cited

RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid

A. B. Estelle, H. M. Forsythe, Z. Yu, K. Hughes, B. Lasher, P. Allen, P. N. Reardon, D. A. Hendrix, E. J. Barbar

This study identifies RNA structures and N domains responsible for specific interactions and phase separation in SARS-CoV-2 nucleocapsid, showing that multiple weak interactions drive phase separation while strong interactions are specific.

bioRxiv · Jul 2, 2023Biophysics

Cataract-associated deamidations on the surface of γS-crystallin increase protein unfolding and flexibility at distant regions

H. M. Forsythe, C. J. Vetter, K. J. Jara, P. N. Reardon, L. L. David, E. J. Barbar, K. Lampi

This study identifies deamidation sites in γS-crystallin that increase protein dynamics and flexibility in distant regions, contributing to cataract formation.

bioRxiv · May 22, 2019 · PreprintBiophysics