Projects per year
Personal profile
Research interests
Investigating how RNA binding proteins recognise and chaperone RNA in health and disease. From mRNA that encodes protein to catalytic RNA at the heart of machines such as the ribosome, the single stranded nature of RNA is fundamental to its versatility. However, this also renders RNA susceptible to misfolding. We use nuclear magnetic resonance and other biophysical techniques to study the detailed mechanisms by which proteins bind and guide RNA structures. Understanding these fundamental properties can lead to new insights into how aberrant RNA-protein interactions contribute to neurodegenerative diseases such as Amyotrophic lateral sclerosis.
Biography
Fionna Loughlin is a research associate in the Wilce laboratory at Monash University. She obtained her PhD from the University of Sydney following and was awarded an ETH fellowship to undertake postdoctoral research at ETH Zurich, Switzerland. Her work probes the biomolecular mechanisms of RNA binding proteins within the life cycle of RNA during development and disease including cancer and neurodegeneration. Biochemistry and NMR spectroscopy are her main tools, and her work has been published in PNAS, NSMB and Mol Cell.
Expertise related to UN Sustainable Development Goals
In 2015, UN member states agreed to 17 global Sustainable Development Goals (SDGs) to end poverty, protect the planet and ensure prosperity for all. This person’s work contributes towards the following SDG(s):
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Projects
- 1 Active
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Novel enzymes to transform the manufacturing of RNA in Victoria
Knott, G., Loughlin, F., Burgio, G. & Fox, A.
24/10/22 → 20/01/26
Project: Research
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Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1
Loughlin, F. E., West, D. L., Gunzburg, M. J., Waris, S., Crawford, S. A., Wilce, M. C. J. & Wilce, J. A., 18 Mar 2021, In: Nucleic Acids Research. 49, 5, p. 2403-2417 15 p.Research output: Contribution to journal › Article › Research › peer-review
Open Access16 Citations (Scopus) -
The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity
Loughlin, F. E., Lukavsky, P. J., Kazeeva, T., Reber, S., Hock, E. M., Colombo, M., Von Schroetter, C., Pauli, P., Cléry, A., Mühlemann, O., Polymenidou, M., Ruepp, M. D. & Allain, F. H. T., 7 Feb 2019, In: Molecular Cell. 73, 3, p. 490-504 15 p.Research output: Contribution to journal › Article › Research › peer-review
83 Citations (Scopus) -
Aberrant interaction of FUS with the U1 snRNA provides a molecular mechanism of FUS induced amyotrophic lateral sclerosis
Jutzi, D., Campagne, S., Schmidt, R., Reber, S., Mechtersheimer, J., Gypas, F., Schweingruber, C., Colombo, M., von Schroetter, C., Loughlin, F. E., Devoy, A., Hedlund, E., Zavolan, M., Allain, F. H. T. & Ruepp, M. D., 11 Dec 2020, In: Nature Communications. 11, 1, 14 p., 6341.Research output: Contribution to journal › Article › Research › peer-review
Open Access26 Citations (Scopus) -
TDP-43 and FUS–structural insights into RNA recognition and self-association
Loughlin, F. E. & Wilce, J. A., 1 Dec 2019, In: Current Opinion in Structural Biology. 59, p. 134-142 9 p.Research output: Contribution to journal › Review Article › Research › peer-review
26 Citations (Scopus) -
Regulation of TIA-1 Condensates: Zn2+ and RGG Motifs Promote Nucleic Acid Driven LLPS and Inhibit Irreversible Aggregation
West, D. L., Loughlin, F. E. & Wilce, J. A., 14 Jul 2022, In: Frontiers in Molecular Biosciences. 9, 14 p., 960806.Research output: Contribution to journal › Article › Research › peer-review
Open Access