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Natan BASISTY

Nathan Basisty, Ph.D., Tenure-Track Investigator
Title: Tenure-Track Investigator
Office(s): Translational Geroproteomics Unit (TGU)
Email Address: nathan.basisty@nih.gov

Biography

Dr. Nathan Basisty is currently an Investigator at the NIA and head of the Translational Geroproteomics Unit (TGU). He received his Ph.D. in Pathology and B.S. in Biochemistry from the University of Washington, where he investigated the role of protein turnover in mammalian aging and longevity using novel combinations of metabolic labeling, LC-MS/MS, and software tools. In 2015, he joined The Buck Institute for Research on Aging, where he did his postdoctoral fellowship in the labs of Dr. Birgit Schilling and Dr. Judith Campisi. There he developed novel and specialized proteomic approaches to understand aging processes and age-related diseases, including the application of data-independent acquisition (DIA) or SWATH workflows to identify and quantify PTMs and secretomes. Dr. Basisty’s awards include two “Aging Cell Best Paper Prizes”, in 2014 and 2017 and the Joseph A. Pignolo, Sr. Award in Aging Research 2016, and the prestigious K99/R00 Pathway to Independence Award in 2020.

Selected Publications

  1. Tanaka T, Basisty N, Fantoni G, Candia J, Moore AZ, Biancotto A, Schilling B, Bandinelli S, Ferrucci L.  Plasma proteomic biomarker signature of age predicts health and life span. eLife. Nov 19, 2020.
  2. Moaddel R, Ubaida-Mohien C, Tanaka T, Lyashkov A, Basisty N, Schilling B, Semba RD,  Franceschi C, Gorospe M, Ferrucci L. Proteomics in aging research: a roadmap to clinical, translational research. Aging Cell. 2021.
  3. Basisty N, Kale A, Jeon OH, et al. A Proteomic Atlas of Senescence-Associated Secretomes for Aging Biomarker Development. PLoS Biol. 2020;18(1):e3000599. Published 2020 Jan 16. doi:10.1371/journal.pbio.3000599
  4. Basisty N, Kale A, Patel S, Campisi J, Schilling B. The Power of Proteomics to Monitor Senescence- Associated Secretory Phenotypes and Beyond: Toward Clinical Applications. Expert Rev Proteomics. 2020;17(4):297-308. doi:10.1080/14789450.2020.1766976
  5. Basisty N, Meyer JG, Wei L, Schilling B. Simultaneous Quantification of the Acetylome and Succinylome by 'One-Pot' Affinity Enrichment. Proteomics. 2018;18(17):e1800123. doi:10.1002/pmic.201800123
  6. Basisty N, Meyer JG, Schilling B. Protein Turnover in Aging and Longevity. Proteomics. 2018;18(5-6):e1700108. doi:10.1002/pmic.201700108
  7. Basisty NB, Liu Y, Reynolds J, et al. Stable Isotope Labeling Reveals Novel Insights Into Ubiquitin-Mediated Protein Aggregation With Age, Calorie Restriction, and Rapamycin Treatment. J Gerontol A Biol Sci Med Sci. 2018;73(5):561-570. doi:10.1093/gerona/glx047
  8. Basisty N, Dai DF, Gagnidze A, Gitari L, Fredrickson J, Maina Y, Beyer RP, Emond MJ, Hsieh EJ, MacCoss MJ, Martin GM, Rabinovitch PS. Mitochondrial-targeted catalase is good for the old mouse proteome, but not for the young: 'reverse' antagonistic pleiotropy? Aging Cell. 2016 Aug;15(4):634-45. doi:10.1111/acel.12472.

 

Related Scientific Focus Areas

  • Aging biomarkers and therapeutic targets
  • Classifying, quantifying, and targeting senescent cells
  • Proteostasis and protein turnover in aging
  • Post-translational modifications
  • Mass spectrometry method development

Research Interests/Portfolio

The Translational Geroproteomics Unit (TGU) studies the molecular underpinnings of aging at the proteomic and multi-omic levels to guide the development of clinically relevant biomarkers and therapeutic targets for the pathologies of aging. We leverage modern mass spectrometry based proteomic technologies and computational tools in preclinical aging models and human cohorts such as the Baltimore Longitudinal Study of Aging (BLSA) with the ultimate goals of discovering protein- and PTM-based biomarkers of aging, enabling the development of senotherapeutics, improving healthspan, and understanding mechanisms of aging at the cellular and molecular levels. The TGU focuses on three hallmarks of aging: cellular senescence, altered protein turnover, and accumulation of post-translational modifications. .