The Schilling lab uses advanced mass spectrometric technology to understand molecular mechanisms that underlie aging. Analyzing samples on the molecular level provides insights into protein pathways and mechanisms of disease and aging. We collaborate with all investigators at the Buck as well as investigators from outside institutions. The Schilling lab develops and implements advanced innovative protein analytical technologies (including quantitative proteomics, posttranslational modifications, protein dynamics and biomarker discovery) to advance basic biology and biomedical research related to aging research.
The Schilling lab engages in many collaborative projects and is engaged in worldwide mass spectrometric studies, as well as software development. Many different workflows are supported at our facility or can be developed together to support biological projects with innovative technologies to gain insights into molecular details in a system-wide approach. At the same time, worldwide collaborations with other proteomics and mass spectrometry laboratories keep our cutting edge workflows and our approach at the forefront of analytical technology.
Why it matters
Understanding what happens during aging and the development of age-related disease, and what is different in a diseased organism compared with a healthy organism, are key to developing treatments, drugs and interventions. We have focused on developing assays to discover biomarkers of aging and disease from easily accessible biofluids, such as plasma or blood from human patients. Connecting these findings with fundamental mechanisms of aging in model systems available at the Buck will drive our research forward in significant ways.
Combining specialized Proteomics Technology with Aging Biology will allow us to gain deeper insights into underlying mechanisms and pathways of Aging.
Birgit Schilling, PhD
Birgit Schilling is the Director of the Mass Spectrometry Core and an Assistant Professor at The Buck Institute for Research on Aging. Dr. Schilling studied Chemistry at the University of Hamburg and received her Doctorate (PhD) from the University of Clausthal, Germany. Dr. Schilling obtained additional research training as a postdoctoral fellow at UCSF, and joined the Buck Institute in 2000. She is also Adjunct Professor at University of Southern California and is teaching at the Buck Institute as part of the joined Buck Institute/USC PhD program.
Dr. Schilling and the Mass Spectrometry Core provide expertise in mass spectrometry to efficiently analyze biological samples, for example to determine changes in protein expression or protein modifications as a result of a disease or other biological conditions. Collaborative research projects investigated at the Mass Spectrometry Core comprise projects related to neurodegenerative diseases, aging, cancer, muscle atrophy, protein posttranslational modifications, mitochondrial damage, biomarker research, and many other scientific areas. Specific areas of interest are a sarcopenia project deciphering underlying causes and biological pathways of muscle atrophy, as well as the role of sirtuins on posttranslational modifications of proteins.
Dr. Schilling is also interested in developing new Proteomics workflows and new technological approaches that will subsequently benefit biological projects. Dr. Schilling is a board member of the US HUPO, the Human Proteome Organization, which is dedicated to advance mass spectrometric technologies to study the human proteome (‘from genes to function’). Dr. Schilling has participated in large, international, mass spectrometric studies.
Dr. Schilling has experience working with biotechnology companies. Dr. Schilling collaborated with MitoSciences in the development of new antibodies. She investigated protein acetylation in collaboration with Sirtris Pharmaceuticals, and she has worked with BioMarin providing mass spectrometric expertise and sample analysis. Recently, Dr. Schilling started collaborations with Unity Biotechnology focusing on the role of cellular senescence in an ongoing research project.
Natan Basisty, PhD Postdoctoral Research Fellow
Natan Basisty is a postdoctoral fellow who joined The Buck Institute in 2015. He received his Ph.D. in Pathology and B.S. in Biochemistry from the University of Washington. He has been developing and applying mass spectrometry approaches to study the role of proteins and cellular protein quality control in health and aging for over 7 years. His current research focuses on discovering biomarkers of cellular senescence and developing translationally relevant approaches to study senescent cells.
Anja Holtz, BS Research Associate
Anja Holtz went to the University of Minnesota and graduated in 2017 with a BS in Genetics, Cell Biology and Development as well as Ecology, Evolution and Behavior. Since then she worked at the Masonic Cancer Center doing breast cancer research for a year until she joined the Buck Institute in the summer of 2018. Anja has been extremely interested in genetics ever since the Human Genome Project was first publicized.
Samah Shah Research Intern
Samah Shah graduated from the University of British Columbia with a BS in Microbiology. While there, she contributed to research on a bifunctional enzyme of F. nucleatum, and worked as a teaching assistant for a second year genetics module. She is interested in the medical and therapeutic applications of microbiology and immunology.
Xueshu Xie, PhD Postdoctoral Research Fellow
Xueshu Xie received her Ph.D. degree in Medical Science from Karolinska Institute, Sweden under the guidance of Prof. Roman Zubarev. She joined the Schilling lab at the Buck Institute as a postdoc in June 2018. Xueshu has a strong interest in applying mass spectrometry-based proteomics to solve biological questions. Her current research is focused on studying protein posttranslational modifications (acylation, phosphorylation), protein aggregation and protein-protein interactions.
J. M.Jesse Meyer, PhD Postdoctoral Research Fellow
University of Wisconsin – Madison
R. Q.Ryan Quinn
Touro Univeristy College of Osteopathic Medicine
K. P.Kevin Perrott
SENS Research Foundation
D. P.Deborah Post, PhD
L. W.Lei Wei, B.S. PhD Graduate Student
UC Davis - Microbiology PhD program
- Bullard SA, Seo S, Schilling B, Dyle MC, Dierdorff JM, Ebert SM, DeLau AD, Gibson BW, Adams, CM. Gadd45a Protein Promotes Skeletal Muscle Atrophy by Forming a Complex with the Protein Kinase MEKK4 Protein. J Biol Chem. 2016; 291(34):17496-17509.
- Mark KA, Dumas KJ, Bhaumik D, Schilling B, Davis S, Ronnen Oron T, Sorensen DJ, Lucanic M, Brem R, Melov S, Ramanathan A, Gibson BW, Lithgow GJ. Vitamin D Promotes Protein Homeostasis and Longevity via the Stress Response Pathway Genes SKN-1/Nrf2 and IRE-1/XBP-1. Cell Reports. 2016; 17:1227-1237.
- Min SW, Chen X, Tracy TE, Dongmin Sohn P, Wang C, Shirakawa K, Devidze N, Minami SS, Lee BH, Schilling B, Cong C, Ellerby L, Gibson BW, Johnson J, Krogan N, Ponnusamy R, Zhou Y, Li Y, Shamloo M, Masliah E, King R, Finley D, Verdin E, Gan L. Critical Role of Acetylation in Tau-Mediated Neurodegeneration and Cognitive Deficits: Therapeutic Implications. Nature Medicine. 2015; 21(10):1154-1162.
- Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW. Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways. Proc Natl Acad Sci U S A. 2013; 110(16):6601-6.
- Addona TA, Abbatiello SE, Schilling B, Skates SJ, Mani DR, Bunk DM, Spiegelman CH, Zimmerman LJ, Ham AJ, Keshishian H, Hall SC, Allen S, Blackman RK, Borchers CH, Buck C, Cardasis HL, Cusack MP, Dodder NG, Gibson BW, Held JM, Hiltke T, Jackson A, Johansen EB, Kinsinger CR, Li J, Mesri M, Neubert TA, Niles RK, Pulsipher TC, Ransohoff D, Rodriguez H, Rudnick PA, Smith D, Tabb DL, Tegeler TJ, Variyath AM, Vega-Montoto LJ, Wahlander A, Waldemarson S, Wang M, Whiteaker JR, Zhao L, Anderson NL, Fisher SJ, Liebler DC, Paulovich AG, Regnier FE, Tempst P, Carr SA. Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma. Nature Biotechnology. 2009; 27(7):633-41.