Research groups
Martina Hallegger
Deregulated RNA metabolism in ALS/Motor Neurone Disease (MND)
Martina Hallegger is leading the research program on how deregulated RNA metabolism contributes to the earliest events in the molecular pathogenesis of motor neurone disease (MND), and how we can modulate this for therapeutic interventions. By applying high-throughput methods like iCLIP (cross-linking Immuno-precipitation), RNAseq and proteomics, she studies the central role of RNA-protein condensates in MND.
Martina investigates how concentrating biopolymers via condensation is fundamental to cellular organisation and physiology, and she uniquely focuses on its effect on RNA regulation. She is particularly interested in how the altered condensation properties of the RNA-binding protein TDP-43, which is central to MND pathology, contribute to altered RNA metabolism in neurons and in vitro.
Most recently Martina held an MND Association Lady Edith Wolfson Senior Non-Clinical Fellow at the Institute of Neurology, UCL, and later on at the UK DRI at King’s and the Francis Crick Institute, where she is a Visiting Research Fellow.
She began her scientific career during her postgraduate work at the University of Vienna, and subsequently during a Postdoctoral position in the Department of Biochemistry at the University of Cambridge with the main objective of uncovering how the genetic information in our cells is amplified by combinatorial mechanisms called ‘alternative splicing’ and ‘RNA editing’. As an OPDC fellow at the University of Oxford, she laid the foundation for working in RNomics in neurodegeneration by investigating how non-coding RNAs shape cell function, particularly in neurons affected in Parkinson’s disease.
If you are interested in her approaches, would like to collaborate or join her team, then please get in touch with her.
Hiring now: Apply before the 2nd of December for two post-doc positions available on how altered condensation of TDP-43 changes RNA metabolism. Biophysics of protein-RNA condensates and neuronal transcriptomics:
https://my.corehr.com/pls/uoxrecruit/erq_jobspec_version_4.display_form?p_company=10&p_internal_external=I&p_display_in_irish=N&p_process_type=&p_applicant_no=&p_form_profile_detail=&p_display_apply_ind=Y&p_refresh_search=Y&p_recruitment_id=176286
https://my.corehr.com/pls/uoxrecruit/erq_jobspec_version_4.display_form?p_company=10&p_internal_external=I&p_display_in_irish=N&p_process_type=&p_applicant_no=&p_form_profile_detail=&p_display_apply_ind=Y&p_refresh_search=Y&p_recruitment_id=176287
Recent publications
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Author Correction: TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of UNC13A.
Journal article
Brown A-L. et al, (2024), Nature, 631
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Mis-spliced transcripts generate de novo proteins in TDP-43-related ALS/FTD.
Journal article
Seddighi S. et al, (2024), Science translational medicine, 16
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Transcriptome-wide RNA binding analysis of C9orf72 poly(PR) dipeptides.
Journal article
Balendra R. et al, (2023), Life science alliance, 6
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TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of UNC13A.
Journal article
Brown A-L. et al, (2022), Nature, 603, 131 - 137
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Genome-wide RNA binding analysis ofC9orf72poly(PR) dipeptides
Preprint
Balendra R. et al, (2022)
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TDP-43 condensation properties specify its RNA-binding and regulatory repertoire.
Journal article
Hallegger M. et al, (2021), Cell, 184, 4680 - 4696.e22
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psiCLIP reveals dynamic RNA binding by DEAH-box helicases before and after exon ligation.
Journal article
Strittmatter LM. et al, (2021), Nature communications, 12
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PsiCLIP reveals dynamic RNA binding by DEAH-box helicases before and after exon ligation
Preprint
Strittmatter L. et al, (2020)
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Mice with endogenous TDP-43 mutations exhibit gain of splicing function and characteristics of amyotrophic lateral sclerosis.
Journal article
Fratta P. et al, (2018), The EMBO journal, 37