Author

Dylan E. Ramage

University of CambridgeORCID 0009-0004-4596-9509Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Organism:human· 3 Approach:experimental assay· 2 Approach:statistical model· 2 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Assay:proteomics· 1

Frequent Co-Authors

Drew W. GrantiD· 3 shared Richard T. TimmsiD· 3 shared Iva A. TchasovnikarovaiD· 2 shared Michael P. WeekesiD· 2 shared Alan John WarreniD· 1 shared Alessio CiulliiD· 1 shared Charlotte CroweiD· 1 shared Jens Bager ChristenseniD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 40 mutual co-author links

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3 shared papersMolecular Biology

Drew W. GrantORCID

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Author profile →

3 papers

Recent·Most cited

LRRC58 defines an E3 ubiquitin ligase complex sensitive to cysteine abundance

Dylan E. Ramage, Lianne H. E. Wieske, Charlotte Crowe, Jens Bager Christensen, Theo A. von Wilmowski, Zoe Bannister, Drew W. Grant, Mark A. Nakasone, Kevin Haubrich, Mark Dorward, Iva A. Tchasovnikarova, Michael P. Weekes, Nicholas J. Matheson, N. Sumru Bayin, Alessio Ciulli, Richard T. Timms

The paper identifies LRRC58 as a substrate adaptor in a Cul2 E3 ligase complex that regulates CDO1 degradation in response to cysteine availability, preventing ferroptosis and neurodevelopmental defects.

Molecular Cell · Jun 19, 2026Peer-reviewedMolecular Biology

Proteome-wide C-degron activity profiling connects conditional regulation of the CTLH E3 ligase complex to ribosome biogenesis

Drew W. Grant, Shengjiang Tan, Dylan E. Ramage, Mamie Z. Li, Ying Di, Iva A. Tchasovnikarova, Michael P. Weekes, Stephen Joseph Elledge, Alan John Warren, Richard T. Timms

The paper identifies C-terminal degron substrates of the CTLH E3 ligase complex and links their regulation to ribosome biogenesis through the chaperone activity of AAMP.

bioRxiv · Jan 14, 2026 · PreprintMolecular Biology

Loss-of-function mutations in the dystonia gene THAP1 impair proteasome function by inhibiting PSMB5 expression

Dylan E. Ramage, Drew W. Grant, Richard T. Timms

This study identifies THAP1 as a regulator of PSMB5 expression, showing that its loss impairs proteasome function and contributes to dystonia.

Nature Communications · Feb 10, 2025Peer-reviewedGenetics