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CSB Alumni Spotlight: Paul Barrett, PhD

Posted by on Friday, January 14, 2022 in News.

Paul Barrett, PhD, and family

Paul Barrett, PhD, completed his doctoral work in 2013. He’s always had an avid interest in science and wanted to combine that love with helping others. He developed an interest in studying neurodegeneration in Alzheimer’s and Parkinson’s diseases while working in the lab of Chuck Sanders. Paul received the Karpay Award in 2013 and presented Where’s my doughnut? A link between cholesterol and Alzheimer’s Disease at the award seminar.

What is your current job title and responsibilities? Currently I am a Program Director at the National Institute on Aging at the NIH. I manage a portfolio of grants that focus on how changes to cellular homeostasis, proteostasis, mitochondrial function and metabolism impact brain health in aging and in Alzheimer’s disease and related dementias. I speak with scientists around the world about their grants and scientific ideas and monitor their progress over the lifetime of a grant. I also help develop future funding initiatives by identifying scientific gaps in the field and developing ideas of how researchers could help fill that gap. It’s a very rewarding job. I interact with brilliant scientists to discuss emerging ideas as well as work with more junior researchers to provide advice on grant writing and career development strategies.

What was your path to your current job? My research career started at Vanderbilt in 2008. After completing my dissertation in 2013, my wife (also a Vanderbilt PhD graduate) and I were interested in building a research lab, so we took post-doctoral positions at the University of Pittsburgh. I was very excited to start my post-doc, as I was entering a new field of science. My mentor, Dr. Chuck Sanders, gave me some excellent advice when looking for a post-doctoral position: to either become an expert in my current field or take an orthogonal approach and find a position in a new field but that can be complimented by your current expertise. I chose the latter and moved to animal model work focused on Parkinson’s disease. I developed a project that integrated structural biology components and experiments with in vivo animal work. I eventually realized that running my own lab was not my ultimate career choice. I enjoyed scientific communication and grant writing, initiative development and evaluation, so I was fortunate to find a position at the NIH Common Fund where I was able to do all of those tasks and more. I stayed in that position for several years but wanted to move into a role that allowed for more interaction with the researchers, which led me to my current program director position.

What is something you learned in grad school at Vanderbilt that has helped you in your career? This is a great question. When thinking about it, two things come to mind. The first is to make sure you find a research group, company, etc., where you enjoy interacting with the people you work with. Every research lab in the country is doing amazing, interesting, cutting edge biological research, and as you progress through your career you will always be able to find interesting projects. What can be more difficult to find is a team that you mesh well with. Make sure you find a place where you can be yourself. The second thing I learned is to be a good communicator. It will make everything much easier and everyone more successful if you are able to be open and honest and not afraid to speak up to propose new ideas or answer tough questions.

Do you use structural biology in your present job? How has knowledge of structural biology helped you in your career? Yes and no. While I am no longer conducting experiments, I constantly use my structural biology background when thinking about all aspects of science. Whenever I think of a new funding initiative, read a paper or discuss a grant with an applicant, my first thoughts always go back to protein structure and how this drives how the protein functions. Mutations, post-translational modifications, protein/ligand interactions and many other scientific concepts can be influenced by protein structure or can influence how a protein changes structure. Without training in structural biology, the impact of how a protein folds/looks in 3D space can go overlooked. Having that training helped me understand a wide variety of biological activities and functions well beyond my graduate and post-doctoral training. It also allows me to discuss interesting avenues for new research often unnoticed by PIs, which is an important part of my current position.

What advice would you give to young trainees? Find something you are passionate about and make it your own, whether it’s science or life in general. When you join a new lab, take the project or concept you’re given and you make it your own. Do background reading in fields that interest you and then begin to connect the dots between your current project and unknown areas of research that your project is related to. My graduate project started off determining the structure of a protein, but by the end of my dissertation, I was establishing collaborations to do cellular biology and confocal microscopy experiments. Microscopy was always an interest of mine, so I was passionate about finding new ways to connect it to the basis of my structural biology project.

Is there anything in the structural bio world (structure, technique, etc.) that you think is especially cool right now? The amazing resolution that can be obtained using cryo-EM methods. When I was in graduate school, cryo-EM was used to get low resolution globular structures of large protein complexes. Now cryo-EM can obtain high resolution structural data which allows for great advancements in structural biology in the future.

Is there any other info, thoughts, etc., that you’d like to include? Don’t be afraid to step out of your comfort zone or to look for exciting new opportunities. There is so much you can do with the training you are receiving. Find what you are passionate about and use that training to find an exciting career.

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