Author

V. F. Thompson

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:chromatin & epigenetic regulation· 2 Organism:bacteria (other)· 1 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Organism:human· 1 Approach:statistical model· 1

Frequent Co-Authors

J. C. Schwartz· 3 shared M. A. Lay· 3 shared D. R. Wieland· 2 shared L. M. Harrell· 2 shared A. D. Adelakun· 1 shared C. R. Millan· 1 shared H. I. Janis· 1 shared M. Francis· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiochemistry

J. C. Schwartz

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Ewing Sarcoma Related protein 1 recognizes R-loops by binding DNA forks

M. A. Lay, V. F. Thompson, A. D. Adelakun, J. C. Schwartz

This study identifies how EWSR1 recognizes R-loops by binding DNA forks, revealing the role of its ZnF and RRM domains in specificity.

bioRxiv · Jan 20, 2024Biochemistry

FUS binding to RNA prevents R-loops

V. F. Thompson, D. R. Wieland, V. Mendoza-Leon, H. I. Janis, M. A. Lay, L. M. Harrell, J. C. Schwartz

This study shows FUS binds nascent transcripts to prevent R-loop formation, reducing their impact on transcription and RNA metabolism.

bioRxiv · Aug 11, 2022 · PreprintBiochemistry

Fusion protein EWS-FLI1 is incorporated into a protein granule in cells

N. S. Ahmed, L. M. Harrell, D. R. Wieland, M. A. Lay, V. F. Thompson, J. C. Schwartz

The paper investigates how EWS-FLI1 forms protein assemblies and its role in gene regulation in Ewing sarcoma cells.

bioRxiv · May 31, 2020 · PreprintBiochemistry

The peptide sensor motif stabilizes the outward-facing conformation of TmrAB

C. R. Millan, M. Francis, V. F. Thompson, T. M. Thaker, T. M. Tomasiak

This study investigates how the peptide sensor motif in TmrAB coordinates conformational changes during ATP-dependent transport, showing it stabilizes the outward-facing state.

bioRxiv · Jan 12, 2020 · PreprintBiochemistry