Author

B. M. Bowman

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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Cell Biology· 3

Signature Assays, Organisms & Methods

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Organism:human· 3 Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Assay:bulk RNA-seq· 1 Research Focus:cancer & tumor microenvironment· 1 Assay:ChIP-seq· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

M. B. Major· 3 shared D. Goldfarb· 2 shared K. M. LaPak· 2 shared M. J. Agajanian· 2 shared A. D. Axtman· 1 shared A. E. Hale· 1 shared A. Khan· 1 shared A. L. Brademeyer· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersCell Biology

M. B. Major

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Author profile →

3 papers

Recent·Most cited

SETD2 maintains nuclear lamina stability to safeguard the genome

A. Khan, J. M. Metts, L. C. Collins, C. A. Mills, K. Li, A. L. Brademeyer, B. M. Bowman, M. B. Major, J. Aube, L. E. Herring, I. J. Davis, B. D. Strahl

This study identifies a non-catalytic function of SETD2 in maintaining nuclear lamina stability and genome integrity through its N-terminus interactions.

bioRxiv · Sep 28, 2023Cell Biology

Protein proximity networks and functional evaluation of the Casein Kinase 1 γ family reveals unique roles for CK1γ3 in WNT signaling

M. J. Agajanian, F. M. Potjewyd, B. M. Bowman, S. Solomon, K. M. LaPak, D. P. Bhatt, J. L. Smith, D. Goldfarb, A. D. Axtman, M. B. Major

This study identifies unique roles for CK1γ3 in WNT signaling through proximity biotinylation, functional assays, and inhibitor testing, showing its distinct activation of β-catenin and Notch pathways.

bioRxiv · Nov 30, 2021Cell Biology

Gain-of-function genetic screen of the kinome reveals BRSK2 as an inhibitor of the NRF2 transcription factor

T. Y. Tamir, B. M. Bowman, M. J. Agajanian, D. Goldfarb, T. P. Schrank, T. Stohrer, A. E. Hale, P. F. Siesser, S. J. Weir, R. M. Murphy, K. M. LaPak, B. E. Weissman, N. J. Moorman, M. B. Major

The paper identifies BRSK2 as a negative regulator of NRF2 by inhibiting protein synthesis through mTOR downregulation, suggesting it as a potential therapeutic target for NRF2-related diseases.

bioRxiv · Nov 5, 2019Cell Biology