his intern and residency. In 1979, he moved to the U.S. National Institutes of Health as a research fellow under Thomas A. Waldmann. Collaborating with Philip Leder's group, Korsmeyer defined the chromosomal translocation that underlay most follicular lymphoma, naming the affected gene Bcl-2. Academic career In 1982, Korsmeyer was promoted to senior investigator at the National Cancer Institute. A few years later in 1986, he moved his laboratory to Washington University School of Medicine's Department of Medicine, eventually becoming professor of medicine, director of the Division of Medical Oncology, and a Howard Hughes Investigator. There his group continued to work on B-cell lymphomas, showing that mice overexpressing Bcl-2 in their B cells developed long-lived B cells that would accumulate other mutations, leading eventually to cancer. This was the first example establishing dysregulated cell death as a path to oncogenesis, rather than just dysregulated cell proliferation. Korsmeyer's group went on to define the role of Bcl-2 in normal B- and T-cell physiology, and showed that many types of cells require Bcl-2 for their normal development. In 1990, Korsmeyer's group found that Bcl-2 typically resides in mitochondria, sparking further research into how mitochondrial proteins regulate cell death. They went on to define the mechanism by which mitochondria influence apoptosis – via Bcl-2 and a family of related proteins including BID, BAD, and BAX. Korsmeyer synthesized this work into a "rheostat model" of cell death regulation, whereby cell death is governed by the balance of pro- and anti-cell death proteins. Demonstrating this theory, his group showed that cancer cells can be killed either by blocking the anti-death protein Bcl-2, or by activating the pro-death protein BAX. In 1998, Korsmeyer was recruited to Harvard Medical School to serve as the Sydney Farber Professor of Pathology and Medicine as well as Director of the Dana–Farber Cancer Institute's Program in Molecular Oncology. There his group continued their research into mitochondrial regulators of apoptosis, defining the mechanism by which Bcl-2 and the related Bcl-xL sequester pro-death regulators. Without Bcl-2 suppression, BID and other pro-death regulators oligomerize BAX and BAK, initiating the cell death pathway. This work on apoptosis regulators also revealed roles for these proteins outside of apoptosis. Korsmeyer's group described a role for BAX and BAK maintaining calcium levels in the cell's endoplasmic reticulum, for BAD in regulating glycolysis via glucokinase, and for another anti-apoptotic protein MCL1 in blood cell development. Over his career in science,