Author

Tobias Schmidt

Cancer Research UK Scotland InstituteORCID 0000-0001-7230-1214Unclaimed ORCID profile · follow to get notified of new preprints

Additional preprints under this name without ORCID

Tobias Schmidt5 papers · GlaxoSmithKline (United Kingdom)

Biology Disciplines

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Molecular Biology· 2 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell-cell communication· 2 Research Focus:differential expression· 2 Research Focus:gene regulatory network inference· 2 Assay:proteomics· 2 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

Martin BushelliD· 4 shared Adrianna DąbrowskaiD· 2 shared Danny T. C. HuangiD· 2 shared Joseph A. WaldroniD· 2 shared June Munro· 2 shared Kelly Hodge· 2 shared Sara R. ZanivaniD· 2 shared A.P. TurnbulliD· 1 shared

Activity by Year

2022-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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4 shared papersMolecular Biology

Martin BushellORCID

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4 papers

Recent·Most cited

Molecular BiologyNucleic Acids ResearchPeer-reviewedFeb 19, 2026

The yeast phosphofructokinase β-subunit has ATP-dependent RNA unwinding activity and modulates cell cycle progression

Waleed S. Albihlal, Ana M. Matia‐González, Tobias Schmidt…·André P. Gerber

This study identifies Pfk2p as an ATP-dependent RNA unwinding enzyme that modulates cell cycle progression by promoting translation of mitotic genes.

1 citation

yeastmetagenomics

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Cell BiologybioRxivPreprintMar 24, 2025

The differential mechanisms of eIF4A1-mediated translational activation instructed by distinct RNA features

Tobias Schmidt, A.P. Turnbull, Amit Gupta…·Martin Bushell

This study identifies how eIF4A1 differentially activates translation based on mRNA features, revealing distinct mechanisms for mRNA selection and inhibition by eFT226 and hippuristanol.

DOI 10.1101/2025.03.24.644895

proteomicsmachine learning (classical)

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BiochemistryeLifePeer-reviewedJul 8, 2024

DTX3L ubiquitin ligase ubiquitinates single-stranded nucleic acids

Emily L Dearlove, Chatrin Chatrin, Lori Buetow…·Danny T. C. Huang

This study shows that DTX3L ubiquitinates single-stranded DNA and RNA, expanding the known substrates of ubiquitination beyond proteins.

31 citations

DNA methylationproteomics

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Molecular BiologybioRxivPreprintAug 8, 2022

Purine-rich RNA sequences in the 5'UTR site-specifically regulate eIF4A1-unwinding through eIF4A1-multimerisation to facilitate translation

Tobias Schmidt, Adrianna Dąbrowska, Joseph A. Waldron…·Martin Bushell

The paper identifies AG-rich RNA sequences in 5'UTRs that regulate eIF4A1 multimerisation to enhance translation of oncogenic mRNAs.

1 citation

humanbulk RNA-seq

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