Author

L. L. David

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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Biochemistry· 1 Biophysics· 1 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

C. J. Vetter· 2 shared B. X. Li· 1 shared C. Mundorff· 1 shared D. Thorn· 1 shared E. J. Barbar· 1 shared H. M. Forsythe· 1 shared J. A. Carver· 1 shared K. Halverson-Kolkind· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

C. J. Vetter

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Author profile →

3 papers

Recent·Most cited

PRMT5 as a Novel Druggable Vulnerability for EWSR1-ATF1-driven Clear Cell Sarcoma

B. X. Li, X. Xiao, L. L. David, L. E. Davis

This study identifies PRMT5 as a druggable target for EWSR1-ATF1-driven clear cell sarcoma, showing that its inhibition reduces tumor cell growth.

bioRxiv · Mar 23, 2022 · PreprintCancer Biology

Accumulative deamidation of human lens protein γS-crystallin leads to partially unfolded intermediates with enhanced aggregation propensity

C. J. Vetter, D. Thorn, S. G. Wheeler, C. Mundorff, K. Halverson-Kolkind, J. A. Carver, L. L. David, K. J. Lampi

This study shows that deamidation of γS-crystallin at specific sites leads to protein destabilization, increased unfolding, and enhanced aggregation in cataractous lenses.

bioRxiv · Feb 21, 2020 · PreprintBiochemistry

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