Author

S. L. Currie

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· 2 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 4 Approach:experimental assay· 4 Organism:human· 3 Assay:ChIP-seq· 2 Research Focus:chromatin & epigenetic regulation· 2 Assay:DNA methylation· 2 Research Focus:gene regulatory network inference· 2 Assay:proteomics· 2

Frequent Co-Authors

B. J. Graves· 2 shared B. J. Madison· 2 shared K. A. Clark· 2 shared M. K. Rosen· 2 shared N. Bhachech· 2 shared A. Kumar· 1 shared C. J. Decker· 1 shared C. Xing· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiochemistry

B. J. Graves

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Author profile →

4 papers

Recent·Most cited

Molecular features driving condensate formation and gene expression by the BRD4-NUT fusion oncoprotein are overlapping but distinct

M. Kosno, S. L. Currie, A. Kumar, C. Xing, M. K. Rosen

This study identifies molecular features of BRD4-NUT and its interaction with p300 that drive condensate formation and gene expression, showing overlapping yet distinct roles of p300 domains.

bioRxiv · May 11, 2023Cell Biology

Quantitative reconstitution of yeast RNA processing bodies

S. L. Currie, W. Xing, D. Muhlrad, C. J. Decker, R. Parker, M. K. Rosen

This study reconstitutes yeast RNA processing bodies from purified components, showing that their composition and dynamics can be recapitulated quantitatively.

bioRxiv · Aug 13, 2022 · PreprintBiophysics

Electrostatic repulsion causes anticooperative DNA binding between tumor suppressor ETS transcription factors and JUN-FOS at composite DNA sites

B. J. Madison, K. A. Clark, N. Bhachech, P. C. Hollenhorst, B. J. Graves, S. L. Currie

The paper shows that electrostatic repulsion between ETS and JUN-FOS proteins causes anticooperative DNA binding at ETS-AP1 sites, influencing their roles in prostate cancer.

bioRxiv · May 9, 2018Biochemistry

ETV4 And AP1 Transcription Factors Form Multivalent Interactions With Three Sites On The MED25 Activator-Interacting Domain

S. L. Currie, J. J. Doane, K. S. Evans, N. Bhachech, B. J. Madison, D. K. W. Lau, L. P. McIntosh, J. J. Skalicky, K. A. Clark, B. J. Graves

This study identifies multivalent interactions between ETV4, AP1 factors, and MED25, showing how these interactions enhance transcriptional regulation and are relevant in prostate cancer.

bioRxiv · Apr 11, 2017Biochemistry