Author

Michael E. Bekier

University of MichiganORCID 0000-0002-0886-3105Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Neuroscience· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Assay:bulk RNA-seq· 1 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1 Research Focus:gene regulatory network inference· 1 Approach:statistical model· 1

Frequent Co-Authors

Elizabeth M.H. TankiD· 3 shared Sami J. BarmadaiD· 3 shared Xingli LiiD· 3 shared Emile S. PinarbasiiD· 2 shared Jacob Waksmacki· 2 shared Nicolás GómeziD· 2 shared Aditya V. Suryakumar· 1 shared Allison G. Snyder· 1 shared

Activity by Year

2023-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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3 shared papersNeuroscience

Elizabeth M.H. TankORCID

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Author profile →

3 papers

Recent·Most cited

Nemo-like kinase disrupts nuclear import and drives TDP43 mislocalization in ALS

Michael E. Bekier, Emile S. Pinarbasi, Gopinath Krishnan, Jack J. Mesojedec, Madelaine Hurley, Harisankar Harikumar Sheela, Catherine A. Collins, Layla Ghaffari, Martina de Majo, Erik M. Ullian, Mark Koontz, Sarah Coleman, Xingli Li, Elizabeth M.H. Tank, Jacob Waksmacki, , Sami J. Barmada

This study shows NLK disrupts nuclear import, causing TDP43 mislocalization in ALS, and suggests NLK as a therapeutic target.

Journal of Clinical Investigation · Jun 24, 2025Peer-reviewedNeuroscience

TDP43 autoregulation gives rise to shortened isoforms that are tightly controlled by both transcriptional and post-translational mechanisms

Megan M. Dykstra, Kaitlin Weskamp, Nicolás Gómez, Jacob Waksmacki, Elizabeth M.H. Tank, M. Rebecca Glineburg, Allison G. Snyder, Emile S. Pinarbasi, Michael E. Bekier, Xingli Li, Jen Bai, Shameena Shahzad, Juno Nedumaran, Clare M. Wieland, Corey Stewart, , Sami J. Barmada

This study identifies TDP43 autoregulation as a source of shortened isoforms, showing they are regulated by NMD and post-translational degradation, and their dysregulation leads to neurodegeneration.

bioRxiv · Jul 2, 2024 · PreprintNeuroscience

RNA methylation influences TDP43 binding and disease pathogenesis in models of amyotrophic lateral sclerosis and frontotemporal dementia

Michael McMillan, Nicolás Gómez, Caroline Hsieh, Michael E. Bekier, Xingli Li, Roberto Miguez, Elizabeth M.H. Tank, Sami J. Barmada

This study shows that RNA methylation influences TDP43 binding and contributes to neurodegeneration in ALS by modulating RNA stability and TDP43 function.

Molecular Cell · Jan 1, 2023Peer-reviewedNeuroscience