Author

L. Dillard

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell type annotation· 3 Assay:cryo-EM· 2 Research Focus:protein folding & dynamics· 2 Organism:C. elegans· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Assay:electronic health records· 1

Frequent Co-Authors

M. J. Borgnia· 4 shared A. Hojjatian· 2 shared K. A. Taylor· 2 shared K. H. Lim· 2 shared R. Kayed· 2 shared U. Sengupta· 2 shared A. Dasari· 1 shared A. K. R. Dasari· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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4 shared papersBiochemistry

M. J. Borgnia

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Author profile →

4 papers

Recent·Most cited

A higher order PUF complex is central to regulation of C. elegans germline stem cells

C. Qiu, S. L. Crittenden, B. Carrick, L. Dillard, S. Costa dos Santos, V. Dandey, R. Dutcher, E. Viverette, R. Wine, J. Woodworth, Z. Campbell, M. Wickens, M. J. Borgnia, J. Kimble, T. Hall

The paper identifies a ternary PUF complex in C. elegans that regulates germline stem cells by repressing and activating gld-1 mRNA through adjacent FBEs.

bioRxiv · Jun 14, 2024 · PreprintBiochemistry

Untwisted α-synuclein Filaments formed in the Presence of Lipid Vesicles

A. K. R. Dasari, L. Dillard, A. Hojjatian, U. Sengupta, R. Kayed, K. A. Taylor, M. J. Borgnia, K. H. Lim

This study investigates the structure of α-synuclein filaments formed in the presence of lipid vesicles, revealing untwisted structures not previously observed in vitro.

bioRxiv · Oct 19, 2021Biochemistry

Distinct cryo-EM Structure of α-synuclein Filaments derived by Tau

A. Hojjatian, A. Dasari, U. Sengupta, D. Taylor, N. Daneshparvar, F. A. Yeganeh, L. Dillard, B. Michael, R. G. Griffin, M. J. Borgnia, R. Kayed, K. A. Taylor, K. H. Lim

This study reports a cryo-EM structure of α-synuclein filaments promoted by tau, revealing distinct conformations compared to in vitro filaments.

bioRxiv · Dec 31, 2020 · PreprintBiochemistry

Cryo-EM Structures of the SARS-CoV-2 Endoribonuclease Nsp15

M. C. Pillon, M. N. Frazier, L. Dillard, J. G. Williams, S. Kocaman, J. M. Krahn, L. Perera, C. K. Hayne, J. Gordon, Z. D. Stewart, M. Sobhany, L. J. Deterding, A. L. Hsu, V. P. Dandey, M. J. Borgnia, R. E. Stanley

This study determines the cryo-EM structures of SARS-CoV-2 Nsp15, revealing its active site interactions with uridine and conformational changes, which inform potential therapeutic targets.

bioRxiv · Aug 11, 2020 · PreprintBiochemistry