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humans of hupo

Each month we will highlight a member of HUPO. A diverse group of researchers representing different career stages, disciplines, geographical locations, and ethnicities will be invited to submit a profile for the monthly highlight. This initiative will improve visibility of HUPO members, advertise research and enhance the HUPO community.


Marlene Oeffinger, Canada

Website: oeffingerlab.org

What is your current position and location?

I am an Associated Research Professor at the Institut de recherches cliniques Montréal (IRCM) and Professeure-chercheure agrégée at the département de biochimie et médecine moléculaire, Université de Montréal.

How did you get started in the field of proteomics?

I first attempted proteomics during my PhD in David Tollervey’s lab in Edinburgh. Our initial goal was to characterize pre-ribosomal complexes from yeast by mass spectrometry. But  we weren’t very successful at it back then and the MS facility still in their optimization process. Needless to say, I changed my project. But I picked up those threads again as a post-doc in Mike Rout’s lab at Rockefeller, who had been successful at doing proteomics on the yeast nuclear pore complex. So I joined his lab to adopt and optimize his approaches to RNA-protein complexes, learning hands-on proteomics in Brian Chait’s lab.

What does being a member of HUPO mean to you?

To me, it means being part of a lively community that shares a common interest and excitement about pushing the technology and methods, both experimental and computational. But it also means being part of a community that values diversity, collaboration, and training – all of which, at least for me, are important components of a scientific community that is creative and progressive, on a scientific level and beyond.

What makes your research program exciting and unique?

I don’t know if it is unique, but in the lab, we definitely think it’s exciting.

Our research program is focused on understanding the plasticity and disease etiology of RNA-protein complexes. We are using proteomics to define their heterogenous compositions under ‘normal conditions’ and altered ones in response to external and internal changes or stress. But many of the changes and interactions are extremely dynamic, so we are developing and refining techniques such as crosslinking or differential affinity purification MS approaches to capture subtle changes but also wider interaction networks of cellular crosstalk.

What are your interests outside of the lab?

Reading, cooking, and yoga – in that order. Food and the arts have been important parts of my life, always. I love nothing more than a good book on philosophy, poetry or fiction to relax, or cooking a nice meal with my partner after a busy day. And for over two decades now, yoga has provided me with a great place to rebalance during stressful times. I wouldn’t want to miss it.

Where do you envision the field of proteomics in the next 10 years?

That is a hard question to answer. Within the proteomics community, I think – and hope – there will be more user-friendly computational analysis tools, better ways of data validation the community agrees on as a whole, and, most likely, there will be even more approaches and increasingly sensitive instruments, for better and worse. Within the wider scientific community, I would hope that proteomics loses the labels it has acquired in the past decade, of being risky, too broad, or just the thing core facilities do.






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