Kelly Nguyen’s journey into this problem began far from the world’s major research centres. She grew up in Quang Ngai, a rural province in Vietnam, where a career in structural molecular biology was by no means the obvious path. Her interest and ability in science carried her first to New Zealand, then Australia, Cambridge, and California, and finally back to Cambridge.

Kelly’s trajectory reflects an achievement in itself: her hard work which led to the recognition of her talent, and her grit to make a success of the opportunity to work at the frontiers of knowledge. Kelly is now a Principal Investigator leading a successful and dedicated group at the MRC Laboratory of Molecular Biology, focused on understanding how chromosome ends are maintained, division after division.

For years, telomerase posed a puzzle. Researchers knew what it did, but not how it worked. Without knowing the structure, it was difficult to explain how disease-linked mutations disrupted its function, or how its activity might be tuned for therapy. In 1987, Elizabeth Blackburn and Carol Greider discovered telomerase. Progress was steady, careful, but slow. 26 years later, in 2013, the first structure of telomerase was proposed by Rhodes, Lingner and team. Then, a turning point came with the maturation of cryo-electron microscopy (cryo-EM).
The combination of Nobel Prize-recognised cryo-EM methods with powerful statistical image processing finally made it possible to visualize large, flexible molecular assemblies at near-atomic resolution.

Finally, the veil was pulled back and the structure and function of telomerase became discernable. Through dedicated work, Kelly’s team were able to decipher the mutation sites in telomerase which explain several pathologies in patients. Much to their surprise, in 2025 they discovered that telomerase can form dimers – pairs of enzyme complexes – leading to an explanation of molecular pathologies that could not be explained by the monomer alone.

The work raised new questions. Since their discovery that telomerase forms dimers, the biological significance of this arrangement is beginning to be understood. Mutations found at dimer interface hint at mechanisms linking structure directly to aging phenotypes. Histones, best known for packaging DNA, are emerging as active players in telomerase, influencing regulation. Another open question is whether telomerase can be stabilized and delivered as a medicine, rather than merely inhibited. Underpinning all of this is the Hayflick limit: the observation that cells tend to stop dividing when telomeres shorten to around two kilobases. Why that threshold exists, and how cells sense it, remains a central mystery of telomere biology.

Telomerase is essential to all life on our planet. As telomerase activity fades, all living things die. When telomerase is too active, cancers can develop. Knowledge of how telomerase works is essential for understanding how we might fight premature aging as well as mankind’s eternal nemesis, cancer.

And the first signs of progress in telomere-based therapeutics
are now appearing. In June 2024, the very first telomerase inhibitor, Imetelstat, an oligonucleotide drug indicated for adult patients with low- to intermediate-1 risk myelodysplastic syndromes (MDS) was approved by the FDA.

By resolving the structure of one of biology’s most elusive enzymes, Kelly Nguyen has shifted telomerase research onto firm ground. The insights from her work now inform efforts in both cancer biology and aging research, guiding strategies that aim to restore balance to our cells. Her story, like telomerase itself, shows how dedication and precision at the smallest scales can shape outcomes that affect the entire human condition.