Author

Brendan M. McShane

University of PittsburghORCID 0000-0002-8601-2541Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:yeast· 2 Research Focus:cell-cell communication· 1 Assay:ChIP-seq· 1 Research Focus:gene regulatory network inference· 1 Research Focus:protein design· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1

Frequent Co-Authors

Karen M. ArndtiD· 2 shared A Elizabeth HildrethiD· 1 shared Amber L. MosleyiD· 1 shared Christine E. CucinottaiD· 1 shared Donya N. ShodjaiD· 1 shared Jason D. TrueiD· 1 shared Margaret K. ShirraiD· 1 shared Nicole L. HoraniD· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 21 mutual co-author links

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2 shared papersMolecular Biology

Karen M. ArndtORCID

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2 papers

Recent·Most cited

Paf1 complex subunit Rtf1 stimulates H2B ubiquitylation by interacting with the highly conserved N-terminal helix of Rad6

Tasniem Fetian, Brendan M. McShane, Nicole L. Horan, Donya N. Shodja, Jason D. True, Amber L. Mosley, Karen M. Arndt

The paper identifies how the Paf1 complex subunit Rtf1 interacts with Rad6 to stimulate H2B ubiquitylation, revealing a conserved interface that guides substrate specificity during transcription.

Proceedings of the National Academy of Sciences · May 22, 2023Peer-reviewedMolecular Biology

The nucleosome acidic patch directly interacts with subunits of the Paf1 and FACT complexes and controls chromatin architecture in vivo

Christine E. Cucinotta, A Elizabeth Hildreth, Brendan M. McShane, Margaret K. Shirra, Karen M. Arndt

The paper identifies direct interactions between the nucleosome acidic patch and Paf1 and FACT complex subunits, showing their role in chromatin architecture and transcription elongation.

Nucleic Acids Research · Jun 11, 2019Peer-reviewedMolecular Biology