Author

J. Workman

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· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:cell signaling & trafficking· 3 Research Focus:chromatin & epigenetic regulation· 3 Organism:human· 3 Assay:ChIP-seq· 2 Assay:proteomics· 2 Approach:statistical model· 2 Research Focus:transcription & RNA processing· 2

Frequent Co-Authors

S. Bhattacharya· 5 shared H. Li· 3 shared L. Florens· 3 shared M. Washburn· 3 shared N. Zhang· 3 shared Y. Zhang· 2 shared B. Slaughter· 1 shared C. Banks· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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5 shared papersBiochemistry

S. Bhattacharya

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5 papers

Recent·Most cited

Serial Capture Affinity Purification and Integrated Structural Modeling of the H3K4me3 Binding and DNA Damage Related WDR76:SPIN1 Complex

X. Liu, Y. Zhang, Z. Wen, Y. Hao, C. Banks, J. J. Lange, J. Cesare, S. Bhattacharya, B. Slaughter, J. Unruh, L. Florens, J. Workman, M. Washburn

The paper uses SCAP to isolate the WDR76:SPIN1 complex, identifies H3K4me3 binding, and shows its role in DNA damage response through structural modeling and interaction network analysis.

bioRxiv · Jan 31, 2023Biochemistry

Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing

S. Bhattacharya, S. Wang, D. Reddy, S. Shen, Y. Zhang, N. Zhang, H. Li, M. Washburn, L. Florens, Y. Shi, F. Li, J. Workman

This study reveals the structural basis of SETD2 methyltransferase interaction with hnRNP L paralogs, showing how a leucine pair in SETD2 interacts with hnRNP L RRM2 and affects splicing regulation.

bioRxiv · May 22, 2021Biochemistry

The histone methyltransferase SETD2 couples transcription and splicing by engaging pre-mRNA processing factors through its SHI domain

S. Bhattacharya, M. J. Levy, N. Zhang, H. Li, L. Florens, M. Washburn, J. Workman

This study identifies SETD2 as a factor that interacts with hnRNP L to regulate alternative splicing by linking transcription and splicing through its SHI domain.

bioRxiv · Jun 6, 2020Biochemistry

The disordered regions of SETD2 govern H3K36me3 deposition by regulating its proteasome-mediated decay

S. Bhattacharya, N. Zhang, H. Li, J. Workman

This study shows that the disordered N-terminal region of SETD2 regulates its proteasome-mediated decay, affecting H3K36me3 deposition and transcriptional fidelity.

bioRxiv · Jun 5, 2020 · PreprintBiochemistry

Regulation of SETD2 stability is important for the fidelity of H3K36me3 deposition

S. Bhattacharya, J. Workman

This study identifies the N-terminal region of SETD2 as critical for its proteasomal degradation and shows that its removal increases H3K36me3 levels independently of Pol II.

bioRxiv · May 21, 2020Biochemistry