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Editorial: Focus on Top-Down Proteomics: Technology Advances and Biomedical Applications, Honoring Dr. Ying Ge, Recipient of the 2020 ASMS Biemann Medal
Journal of the American Society for Mass Spectrometry ( IF 3.2 ) Pub Date : 2021-08-23 , DOI: 10.1021/jasms.1c00209
Jenny Brodbelt 1 , Lingjun Li 2
Affiliation  

The 2020 Biemann Medal was awarded to Professor Ying Ge at the 68th Annual ASMS Conference for her outstanding research contributions to high-resolution mass spectrometry-based top-down proteomics and its applications to understanding cardiac diseases. Ying is well-recognized for her development of new methods using Fourier transform ion cyclotron resonance mass spectrometry and electron capture dissociation for pinpointing post-translational modifications of proteins (Figure 1), and she has isotopically resolved large proteins with high mass accuracy, allowing the characterization of very large proteins directly from human heart tissues. Moreover, she has pioneered a suite of strategies to address the challenges in top-down proteomics which have shown versatility and broad applicability for characterizing proteins in various tissue and cell systems. Figure 1. Ying Ge standing in front of an FTICR mass spectrometer. Ying is currently Professor of Cell and Regenerative Biology and Chemistry at the University of Wisconsin─Madison. She earned her B.S. degree in Chemistry at Peking University prior to pursuing a Ph.D. in Chemistry at Cornell University under the mentorship of Profs. Fred McLafferty and Tadhg Begley. She pursued a career in industry for several years prior to becoming the Director of Mass Spectrometry of the Human Proteomics Program in the School of Medicine and Public Health (SMPH) at the University of Wisconsin─Madison. She became an Assistant Professor in the Department of Cell and Regenerative Biology in the SMPH and Department of Chemistry in 2012 and was ultimately promoted to her current position of Professor in 2019. In addition to her tremendous research success and dedication to mentoring students, Ying has also served as the Treasurer of ASMS (2016–2018) and has served on the Board of Directors for the Top-Down Proteomics Consortium since 2015. Ying has graciously agreed to share some personal insight about her life in science: When did you become excited about mass spectrometry and realize it was going to be your career passion? I became excited about mass spectrometry during my first year in graduate school. It was unexpected yet interesting story. I was admitted to Cornell as an organic chemistry student with the plan to join an organic chemistry lab. Then I had the opportunity to meet Prof. Fred McLafferty and became very interested in mass spectrometry. Later, I was fortunate to become a joint student under the supervision of Prof. Fred McLafferty and Prof. Tadhg Begley. Fred’s passion for mass spectrometry had a profound influence on me. I felt more and more excited about the power of mass spectrometry to address biological questions. I also learned so much from others during ASMS conferences and was amazed by the remarkable capabilities of mass spectrometry. I got to know many friends through ASMS, and now each event is like a big family reunion (Figure 2). Essentially, I knew that mass spectrometry was going to be my career passion after attending my first ASMS conference, and I wanted to devote my career to promote the development and application of mass spectrometry to biomedical research. How do you train your group members to be innovative? Given the trans-disciplinary nature of our research projects, I provide each student a comprehensive training. I put a strong emphasis on creativity and innovation which are critical to complete these multidisciplinary projects. I often challenge students with bold ideas and ask them to think “outside of the box”, fostering a “can-do” attitude to push the boundaries of what may be possible. In my lab, each group member is in charge of a major multidisciplinary research project which constantly demands new lab skills and requires novel solutions. Meanwhile, I strongly encourage a culture of teamwork and collaborations within the group. I have a rather diverse team including trainees from chemistry, biology, and the medical sciences programs. No one in our group has an identical set of lab skills. Usually, one group member takes his/her lead in the project and gets the help needed to push a project to completion. Our trainees certainly have fun learning and teaching each other. My philosophy is that the best way to learn is by both learning from each other and teaching learned skills to others. As a mentor, I typically establish a training plan that is uniquely suited to each of my trainees to accommodate their specific background and career aspirations. What are the biggest changes in mass spectrometry in the last 10 years that have changed your own research program? In the past 10 years, there were major innovations in the development of high-resolution mass spectrometers, which are much more user-friendly and widely available than before. My research program significantly benefited from these high-resolution mass spectrometers for top-down proteomics. In addition, there were tremendous achievements in the software development for top-down proteomics. Overall, the innovations in both hardware and software have positioned top-down proteomics in the fast lane and certainly sped up the progress of my own research program. For new people entering the field of mass spectrometry, what words of advice can you provide to help them be better scientists? (like tips for success) Mass spectrometry is truly an enabling technology, and it will continue to demonstrate its power in many areas especially in biomedical research. The mass spectrometry field is moving very fast, and there are many new opportunities. It is critically important to keep up with the new developments and identify the remaining challenges, as mass spectrometry will continue playing critical roles in both academia and industry. Young scientists can develop creative mass spectrometry technologies to uncover fascinating insights in biology, understand the underlying mechanism in diseases, and invent new diagnostic assays. Self-motivation and passion are most important. Follow your passion and persevere through the challenges; you can then accomplish something amazing using mass spectrometry. You lead a large group with many projects and many people. How do you maintain a work–life balance? How do you manage stress? It is a constant challenge to maintain a work–life balance as a scientist and a mother. I am just trying my best to balance my work and family life. Overall, I think good time management to use time efficiently is key to maintain a work–life balance. It is important to develop the ability to multitask and make creative use of all the fragmented time throughout the day. Plan well, rank priorities, and set deadlines for each task. I often find myself working much more efficiently and productively when there is a deadline coming. Typically, after I complete a stressful task (e.g., a major grant), I will give myself a couple days to relax and spend more time with my family. For my hobbies, I enjoy gardening and cooking. I also like Yoga and relaxing music, which are very effective to destress. Recently, I have been fascinated with the “Liziqi” YouTube channel; I watch it every night, which helps me relax and get good sleep. In your group, does mass spectrometry drive the biology, or does biology drive the mass spectrometry? Actually, both! Newly developed technology in mass spectrometry certainly helps drive the biology, and likewise, our biological problems also motivate us to develop new methods. In my lab, mass spectrometry plays an integral role in bridging the silos between chemistry, biology, and medicine. What aspect of the analytical workflow has the most room for improvement? (i.e., sample preparation, separations, MS/MS methods, ionization methods, data processing and informatics) I would say nearly all aspects of the analytical workflow have room for improvement in top-down proteomics. Sample preparation and intact protein separation probably have the most room for improvement. My lab has spent a significant amount of effort in developing novel strategies to improve sample preparation, including the identification of a photocleavable MS compatible surfactant, Azo, for top-down proteomics, and developing new methods for chromatographic separation of intact proteins (in collaboration with Dr. Andy Alpert, from PolyLC). However, most of the methods are developed for denatured top-down proteomics; thus, there remains an urgent need to streamline sample preparation and separation for native top-down proteomics. There is also room to improve the ionization and fragmentation efficiency. Additionally, there are significant challenges in identifying large proteoforms (>50 kDa) due to the difficulty in achieving sufficient sequence coverage, so “new”, improved MS/MS methods that can offer more sequencing coverage are urgently needed. Finally, it is critical to further develop the data processing and informatics software for large proteoform identification and characterization. What special advice do you have for new assistant professors in the field of mass spectrometry? It is important to carve a niche based on your unique expertise and develop a plan for both short-term and long-term projects. Stay focused─focus is critical, particularly in the early years when you have just started your own lab. Focus is what enables you to become a leader. Focus on your strengths, not your weaknesses. When I started my own independent research program, I tried to avoid the areas which were already superhot since I knew speed is not my strength; instead, I chose to tackle more challenging problems with relatively lower competition so that I could have sufficient time to develop my program. Currently, there are lots of opportunities in the interdisciplinary research, and mass spectrometry is playing such an important role in biomedical research. Do not be afraid in getting to know the biology communities since many of them welcome new technologies to address their challenging problems to help move the field forward. It is also extremely important to seek out mentors and establish networks. Do not hesitate to ask for help and take advantage of any of the resources you can find. I had numerous mentors in the mass spectrometry society who provided tremendous help in establishing my independent career. I often heard great advice from them during ASMS and other meetings. ASMS is like a big family and enthusiastically supports young people. As a female scientist in the mass spectrometry field, what are the current opportunities and remaining challenges for women scientists in this field? There are more and more opportunities for women scientists in the mass spectrometry field in both industry and academia now. But gender disparity remains a major problem in academia. Many talented female scientists do not choose academic careers because of the family obligations. Instead, they would prefer to take industry or non-tenure-track positions with less demanding hours, or they may opt to leave the workforce entirely. As we all know, childbearing and caring truly consumes a humongous amount of work. Generally, women are taking more of the work of childcare and household management than do male partners─even after the early, physically intensive months of childbirth and childrearing. This may result in lower productivity at work, and those female scientists with children really face significant challenges especially during the COVID-19 pandemic. Like Marie Curie said, “I have frequently been questioned, especially by women, of how I could reconcile family life with a scientific career. Well, it has not been easy.” Indeed, it is not easy to reconcile family life with a scientific career. Women scientists will need the support from family and society to have a productive career. Personally, I decided to take on an industry position after my Ph.D., and I would not have taken an academic career without the tremendous support from my family and society. To address the gender disparity, institutions and society should recognize the tremendous childbearing/caring burden women scientists face. Thus, it is essential to offer women scientists the support and flexibility to allow them taking on academic career paths at a later stage after they fulfill family obligations. It is also critically important for women scientists to have the support from their family in sharing the childcare responsibilities. Figure 2. Enjoying good time together with ASMS friends and colleagues. On behalf of the ASMS community, the JASMS editors, and her many colleagues and friends, we congratulate Ying on her outstanding accomplishments and wish her continued success and many more years of exciting discoveries in top-down proteomics and related mass spectrometry advancements. This article has not yet been cited by other publications. Figure 1. Ying Ge standing in front of an FTICR mass spectrometer. Figure 2. Enjoying good time together with ASMS friends and colleagues.
更新日期:2021-08-23
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