Chook honored with Protein Society’s Daly Award
Award recognizes scientist’s work that led to a first-in-class drug for cancer

Yuh Min Chook, Ph.D., Professor of Pharmacology and Biophysics, has been selected to receive The Protein Society’s 2025 Marie Maynard Daly Award in honor of research that led to the development and eventual Food and Drug Administration approval of a first-in-class drug for cancer. Dr. Chook’s studies relate to the fundamental biophysics and biochemistry of nucleocytoplasmic transport.
Named in honor of the first Black woman in the U.S. to receive a Ph.D. in chemistry, the Daly Award recognizes groundbreaking research at the interface between protein science and human health.
“I am deeply honored and humbled to be selected by The Protein Society to receive the third-ever Marie Maynard Daly Award,” Dr. Chook said. “I am very inspired to learn about Dr. Daly’s life as a scientist and how we have so much in common – both first-generation university graduates from all-women colleges, studies of enzymes during our Ph.D.s, training at the Rockefeller University, and her focus on basic science to answer questions in cancer research.
“That last bit is important to me because I’m fundamentally a basic scientist, but when I have the opportunity to apply basic research to the study of disease, I feel not only deeply fortunate but also a sense of responsibility to do my best to make a direct impact on human health.”
The Daly Award includes a $3,000 prize and one-year membership in The Protein Society. Dr. Chook will also present “The Logic of Nuclear Export: Proteins, Mechanisms, Medicines” at The Protein Society Annual Symposium June 26-29 in San Francisco.
The Chook Lab explores how biological molecules like proteins are transported in and out of the cell’s nucleus. Specifically, the team studies how certain transport receptors – importins, exportins, and biportins – recognize the correct cargoes and drop them off at the right place and time in healthy cells.
“In disease, things go wrong and cargoes often end up in the wrong place at the wrong time. For example, in cancer, many cargoes that live in the nucleus, and function to sense the state of genetic materials, mistakenly end up outside the nucleus where they cannot do their work,” Dr. Chook explained.
This mislocalization happens because of an exportin named XPO1 that is produced in unusually high levels in cancer cells.
“The removal of certain proteins from the nucleus by XPO1 inadvertently allows cancer cells to avoid cell death and survive. Our lab was the first to show how XPO1 recognizes the export signals that cargoes carry,” she said.
Producing a 3D structure of XPO1 bound to a cargo, the lab showed that the spot where XPO1 reads signals is also where many XPO1-blocking chemicals attach. That revelation in 2009, using X-ray crystallography, led to the development of anti-XPO1 drugs by Karyopharm Therapeutics.
The lab and pharmaceutical company also collaborated to study how drug candidates are different from older XPO1 blockers produced by bacteria. (Dr. Chook was a nuclear-cytoplasmic transport consultant to Karyopharm.) That work contributed to FDA approval of the drug selinexor in 2019 to treat multiple myeloma and in 2020 to treat diffuse large B-cell lymphoma.
“Most recently, we discovered how selinexor doesn’t just block or inhibit XPO1 but also causes XPO1 to be destroyed in a process known as protein degradation. This work suggests that we can tune XPO1 inhibition versus degradation to treat different cancers and for optimal drug effectiveness and safety,” Dr. Chook said.
In addition to continued studies with XPO1, the Chook Lab is also expanding its focus.
“It took us more than 20 years of foundational work to get to the point where we can start work to decode an export signal that is recognized by another exportin named Msn5,” Dr. Chook said. “This new class of signal is totally different from the one recognized by XPO1. We are excited to figure out what the common features are that unite the export signals of many different Msn5 cargoes.”
She added: “Many of our projects are difficult and often take more than one generation of trainees to complete. I am most proud of the curiosity, persistence, hard work, and generosity of the trainees who did the work.”