Author

Matthew R. McFarland

University of AberdeenORCID 0009-0004-4308-7545Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Cell Biology· 1 Systems Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:Drosophila· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1 Organism:yeast· 1

Frequent Co-Authors

Adélaïde RaguiniD· 1 shared Andrew D. RenaultiD· 1 shared Brandon M. ChildersiD· 1 shared Corina D Keller· 1 shared Holly Corrigall· 1 shared Ian StansfieldiD· 1 shared Jennifer K Bergman· 1 shared Lee A. ArmstrongiD· 1 shared

Activity by Year

2020-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperSystems Biology

Adélaïde RaguinORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

A ribosome exit tunnel component is required for robust expression of the Drosophila hox gene, abdominal A

Matthew R. McFarland, Ratna Tripathy, Jennifer K Bergman, Michael L. Wood, Andrew D. Renault

This study shows that a mutation in the Drosophila ribosomal protein RpL39 causes embryonic patterning defects by impairing hox gene expression.

bioRxiv · Oct 26, 2026 · PreprintCell Biology

The EF-hand domain of MINDY3 is a Ubiquitin and RAD23 UBL-binding domain

Lee A. Armstrong, Matthew R. McFarland, Rachel O’Dea, Rościsław Krutyhołowa, Magdalena Górka, Thomas D. Carroll, Sebastian Glatt, Yogesh Kulathu

This paper identifies the EF-hand domain of MINDY3 as a ubiquitin and RAD23 UBL-binding domain, revealing its role in DNA damage response regulation.

EMBO Reports · Jun 9, 2026Peer-reviewedBiochemistry

The molecular aetiology of tRNA synthetase depletion: induction of a GCN4 amino acid starvation response despite homeostatic maintenance of charged tRNA levels

Matthew R. McFarland, Corina D Keller, Brandon M. Childers, Stephen A. Adeniyi, Holly Corrigall, Adélaïde Raguin, Maria Carmen Romano, Ian Stansfield

The paper investigates how depletion of the glutamine tRNA synthetase (Gln4p) in yeast triggers a GCN4 amino acid starvation response despite maintaining charged tRNA levels.

Nucleic Acids Research · Jan 18, 2020Peer-reviewedSystems Biology