Michael J. Welsh
University of Iowa
Jesús González
formerly at Vertex Pharmaceuticals
Paul A. Negulescu
Vertex Pharmaceuticals
For their key roles in developing a novel treatment for cystic fibrosis—a triple-drug combination that saves the lives of people with this lethal genetic disease
The 2025 Lasker~DeBakey Clinical Medical Research Award honors three scientists for their roles in developing a novel, life-saving treatment for cystic fibrosis (CF). Michael J. Welsh (University of Iowa) illuminated how the protein that underlies this lethal genetic disease normally works and what goes wrong in people with the illness. These discoveries broke open the possibility of finding small molecules that could correct the misbehaving protein. Jesús (Tito) González (formerly at Vertex Pharmaceuticals) pioneered a system used to screen chemical libraries for promising compounds, and Paul A. Negulescu (Vertex Pharmaceuticals) led and championed the CF project, which culminated in a triple-drug combination that has transformed CF into a manageable condition.
While conducting autopsies in the 1930s, pathologist Dorothy Andersen noticed that the pancreases of some children diagnosed with celiac disease contained fluid-filled cysts. She realized that she was looking at a distinct malady and, in 1938, named it “cystic fibrosis of the pancreas.” Cystic fibrosis, as it is now called, progressively damages multiple organs, including the lung, liver, and intestines. It interferes with nutrient absorption and cultivates thick mucus buildup that provides a breeding ground for harmful bacteria, which often spawn life-threatening lung infections. In Andersen’s time, most people with CF did not survive early childhood. Since then, symptomatic treatments have improved prognoses, but in 2010, about half of affected individuals were expected to die before age 40. Despite this progress, living with the illness meant a persistent cough, wheezing, exercise intolerance, disruptive regimens aimed at clearing the lungs, and long hospital stays.
In the mid 1980s, researchers showed that epithelial cells in sweat glands, nasal passages, and trachea of people with CF transport chloride ions poorly. These observations reflected the excessively salty sweat that researchers had turned into a diagnostic “sweat test” decades earlier—and they suggested a unified explanation for the disease’s effects on varied organs. By that time, scientists had recognized CF as an autosomal recessive condition: sick children inherit a corrupt version of the gene from both parents. In 1989, Lap-Chee Tsui (Hospital for Sick Children, Toronto), Francis Collins (University of Michigan), and colleagues identified and sequenced this gene, which they called cystic fibrosis transmembrane conductance regulator (CFTR). They also defined the most common genetic error—a missing phenylalanine at position 508, ΔF508 for short—which is carried by almost 90% of people with CF.
Cooling down, igniting progress
Welsh, in collaboration with Alan Smith (Genzyme) put the CFTR gene into airway epithelial cells from people with CF; it restored the flow of chloride ions, whereas ΔF508 CFTR did not. These observations, reported in 1990, unambiguously connected the protein with the ailment’s epithelial-cell hallmarks.
Amid lively speculation about how CFTR works, Welsh proposed the simplest idea—that it serves as an ion channel. If so, altering amino acids in its predicted membrane-spanning region would change its relative ability to allow different ions to move. In 1991, he deployed this experimental tactic and demonstrated channel activity.
FIGURE 1: Pharmaceutical synergy
In a healthy cell that lines the airway (top), CFTR is processed correctly in the endoplasmic reticulum (ER) and the Golgi (not shown). From there, it travels to the cell surface, where it allows chloride ion (Cl-) to flow across the membrane. This process leads to a proper salt/water balance that cultivates normal mucus. Potential pathogens are subject to attack by the body’s antimicrobial agents and clearance by the combined activities of the mucus and nearby ciliated cells that brush the interlopers out of the airway. In an epithelial cell with the common ΔF508 flaw in CFTR (bottom-left), defective CFTR cannot fold properly; consequently, it gets stuck in the ER and is sent to the cell’s quality-control incinerator for destruction (red X on arrow). The absence of chloride ion flow through CFTR disrupts the salt/water balance and the resulting thick and sticky mucus captures rather than clears pathogens. Loss of CFTR activity also leads to impairment of the body’s antimicrobial agents. These conditions foster chronic bacterial infections that elicit profuse inflammation. In the presence of the triple-combination drug Trikafta® (bottom-right), the correctors elexacaftor and tezacaftor help ΔF508 CFTR fold normally. The protein reaches the cell’s surface, where the potentiator ivacaftor reverses ΔF508 CFTR’s gating deficiency: It opens the channel sufficiently for chloride ions to flow and thus restores the salt/water balance that supports normal mucociliary clearance and antibacterial functions.
Illustration: Michael J. Welsh
Welsh seized on a curious observation: ΔF508 CFTR in frog eggs and insect cells retains some function. Those cells are grown at lower temperatures than are mammalian cells, and Welsh wondered whether cool conditions might allow ΔF508 CFTR to reach the surface of human cells. To probe this possibility, he tracked the protein as it travels, using the handy sugar tags from the endoplasmic reticulum and the Golgi, both of which enlarge CFTR in defined ways.
Cooling down cells allowed ΔF508 CFTR to escape the endoplasmic reticulum and complete its processing. When Welsh measured chloride ion flow at the surface of these cells, he found that the channels opened, albeit inefficiently. These results, reported in 1992, were inspiring: ΔF508 CFTR was not completely broken. Maybe it could be prodded to work better.
Opening a channel to new medicines
After scientists found the gene, they envisioned replacing flawed versions of it with operational ones to correct the disease at its root, but a decade later, that endeavor was floundering. Robert Beall, the mover-and-shaker president of the Cystic Fibrosis Foundation, was getting impatient. A different strategy seemed imperative.
Emerging technologies promised to revolutionize drug discovery. The 1980’s cloning bonanza had produced a long list of targets; combinatorial chemistry could synthesize large numbers of compounds cheaply and quickly; and advances in robotics enabled rapid, automated screening.
The biotech company Aurora Biosciences spearheaded this enterprise. The late Roger Tsien (University of California, San Diego; 2008 Nobel Prize in Chemistry) had co-founded Aurora to develop high-throughput assays that would identify small molecules that adjust protein behavior, which pharmaceutical companies would then turn into medicines.
In 1998, Beall contacted Negulescu, then Aurora’s Director of Cell Biology, and they discussed the possibility of harnessing Aurora’s approach for CF. Their goal: a pill that would restore CFTR function, body-wide, in people with the most common mutation, fixing both of ΔF508’s defects. They imagined “correctors” of protein processing that would help trapped CFTR reach the cell surface and “potentiators” of channel activity that would enhance chloride-ion migration through membrane-dwelling CFTR. The Foundation funded Aurora to explore this vision.
Exciting fluorophores, emitting hope
To screen for such compounds, they needed a fast assay that would gauge CFTR activity in a biologically meaningful context and lend itself to miniaturization so that thousands of compounds could be tested in a day. A novel way to measure ion flow lay at the heart of their system. As a postdoctoral fellow in Tsien’s lab, González had invented perfectly suited sensors for the job, which work in pairs to survey voltage changes across membranes. He brought these fluorescent dyes and his expertise about how to use them to Aurora, parlaying them from a basic-research tool into a powerful engine for drug discovery. González loaded two sensors onto the outer edge of the cell membrane. When zapped with light, one of these—the donor—absorbs energy and transfers it to its partner that lies nearby. Thus excited, this “acceptor” molecule emits light of a particular wavelength—in this case, orange. If chloride ions flow out of the cell, as occurs in healthy lung epithelial cells, the inside of the cell becomes more positive. Because the acceptor carries a negative charge, it scurries to the inner edge of the membrane. Now it is no longer close enough to capture energy discharged by the donor, which instead emits its own characteristic wavelength of light—in this case, blue. This scenario unfolds when a cell bearing faulty CFTR comes under the influence of a chemical that reverses the glitch. A detector registers the fluorescence and, when integrated into a sophisticated scanning device, can pinpoint even slight color shifts toward blue. The technology, an application of Fluorescence Resonance Energy Transfer (known as FRET), provides a sensitive and robust way to measure channel activity inside cells in real time. González and his team optimized the methodology for use in CF studies—and then he collaborated with Aurora engineers to incorporate the features that would allow them to screen thousands of compounds a day. To assess chemicals for CFTR-modulating effects, the investigators needed cells that would replicate all steps of CFTR production, including membrane delivery, when the protein was rescued. Welsh supplied cells that possess these features and that harbor ΔF508.
FIGURE 2: Capturing the caftors
Negulescu, González, and colleagues screened more than a million small molecules with the FRET-based assay to find compounds that boost channel activity in the CFTR ΔF508 mutant. The fewer than 100 confirmed active compounds that passed this hurdle were subjected to secondary tests, a subset of which are listed above. After hits passed through these additional filters, only 15 or so compounds remained. Medicinal chemists then synthesized thousands of compounds through iterative cycles to determine which structural features improved the functional properties. This process eventually produced drug candidates in each class (correctors, which help defective CFTR mature properly and get to the cell surface; and potentiators, which open the CFTR channel once it has arrived at its destination) that led to the FDA-approved drugs ivacaftor, lumacaftor, and tezacaftor. This new class of CFTR modulator medicines was named CaFToR. The final combination, Trikafta®, is comprised of ivacaftor, tezacaftor, and a different corrector—elexacaftor—that emerged from a separate screen and optimization, with about 10,000 molecules as the starting point, that aimed to identify a drug that augmented CFTR function in the presence of ivacaftor and tezacaftor.
Illustration: Cassio Lynm / © Amino Creative
Negulescu’s team devised two strategies, each of which pointed at a particular type of drug. For “potentiators,” which rouse channel activity, they exploited Welsh’s finding that cool conditions allow some ΔF508 CFTR to reach the surface and conduct chloride ions. They incubated cells at a temperature that would promote CFTR trafficking and then screened for chemicals that boost ion flow. To find “correctors,” which help ΔF508 get to the cell surface, they incubated at higher, body temperature to accumulate CFTR that got stuck in the ER unless it received assistance. They screened more than a million compounds in two years. Encouraging results spurred the Cystic Fibrosis Foundation to supply another bolus of financial support to fuel the venture. At around the same time, in 2001, Vertex Pharmaceuticals acquired Aurora and continued the quest, adding key capabilities in drug development. As González churned through chemicals and generated initial hits, Frederick Van Goor and his biology group ran them through secondary tests that assessed, for example, efficacy and potency, and they checked whether the agents acted directly on CFTR (Figure 2). Van Goor developed and refined additional experimental systems, such as monolayers of cells collected from CF patients during lung transplants that simulate crucial aspects of the human airway; this tool fulfilled a critical need, as animal models of CF did not exist. Vertex chemists, led by Sabine Hadida, worked in concert with the biologists to convert compounds into drugs, tweaking structures and iteratively improving them while scrutinizing attributes that would render them suitable or unsuitable for pursuit.
Bull’s eye for targeted therapies
In 2009, Negulescu and colleagues reported that compound VX-770 fostered channel opening from cells that carry a very rare CFTR mutation called G551D. Unfortunately, cells containing the most frequent—ΔF508—mutation did not respond to this potentiator, presumably because of their trafficking problem. Although the researchers prioritized ΔF508, they weren’t going to snub a potential CF drug. Clinical studies showed that VX-770 rapidly improved lung function in people with G551D. For the first time, an agent that aimed at the underlying cause of CF had benefited humans. Negulescu and colleagues dubbed this new class of drugs “CaFToRs.” In 2012, the U.S. Food and Drug Administration (FDA) approved this first member of the family, which they named ivacaftor. In the meantime, the investigators persevered on their corrector crusade. Eventually they produced lumacaftor, which enhances processing of ΔF508 CFTR and its movement to the cell surface. Addition of ivacaftor to lumacaftor-treated cells strengthens ion transport. Clinical studies showed that the pair performed better than did either one alone. In 2015, the FDA approved this medicine, Orkambi®, the first drug that directly ameliorates the ΔF508 defect. Unfortunately, lumacaftor induces an enzyme that breaks down ivacaftor, so the team replaced lumacaftor with its relative tezacaftor, which provided similar benefits, but left its pharmacological mate intact. The ivacaftor/tezacaftor combination, Symdeko®, gained FDA approval in 2018. Negulescu’s team cheered the triumph: The scientists had created a drug for the approximately 50% of people with CF who possess two copies of ΔF508. But they weren’t done. Neither of the correctors worked as well for people with ΔF508 as did ivacaftor for G551D. The gap beckoned. They synthesized thousands more molecules to unearth a new class of corrector that dramatically augments the effects of ivacaftor and tezacaftor. One of these new-generation correctors, elexacaftor, hit the mark; when added to the ivacaftor/texacaftor mixture, it tripled chloride transport (Figure 1). In individuals with two copies of ΔF508 or one copy of ΔF508 and a second, different CFTR mutation, the triple combination demonstrated numerous benefits, including lung function improvement and weight gain, and was generally well tolerated. The FDA approved this three-drug combination, Trikafta®, in 2019. Since then, Negulescu and colleagues have extended its use to the hundreds of people in the world who carry ultra rare CFTR mutations that respond to Trikafta®. This blockbuster drug, given orally, twice daily, is delivering profound impacts. For example, it has slashed the number of lung transplants and infection-related hospital visits, and it has uplifted quality of life; no longer are people with CF exhausted and spending hours each day trying to shake loose the gunk in their lungs. Furthermore, people who begin the therapy as children or adolescents are expected to have near-normal lifespans. Until 2012, not a single person with CF was receiving therapy that targets its molecular cause. Now, greater than 90% of the 40,000 people with the disease in the United States and at least 100,000 worldwide are eligible for such treatments; about 75,000 individuals are already taking them. Welsh, González, and Negulescu’s achievements are affording people with CF the chance to thrive now and to plan vibrant futures.
by Evelyn Strauss
Selected Publications – Michael J. Welsh
Rich DP, Anderson MP, Gregory RJ, Cheng SH, Paul S, Jefferson DM, McCann JD, Klinger KW, Smith AE, and Welsh MJ. (1990). Expression of cystic fibrosis transmembrane conductance regulator corrects defective chloride channel regulation in cystic fibrosis airway epithelial cells. Nature. 347, 358-363.
Anderson MP, Gregory RJ, Thompson S, Souza DW, Paul S, Mulligan RC, Smith AE, and Welsh MJ. (1991). Demonstration that CFTR is a chloride channel by alteration of its anion selectivity. Science. 253, 202-205.
Anderson MP, Berger HA, Rich DP, Gregory RJ, Smith AE, and Welsh MJ. (1991) Nucleoside triphosphates are required to open the CFTR chloride channel. Cell. 67, 775-784.
Anderson MP and Welsh MJ. (1992). Regulation by ATP and ADP of CFTR chloride channels that contain mutant nucleotide-binding domains. Science. 257, 1701-1704.
Denning GM, Anderson MP, Amara JF, Marshall J, Smith AE, and Welsh MJ. (1992) Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature. 358, 761-764.
Welsh MJ and Smith AE. (1993). Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell. 73, 1251-1254.
Selected Publications – Jesús E. (Tito) González
González JE and Tsien RY. (1995). Voltage-sensing by fluorescence resonance energy transfer in single cells. Biophys. J. 69, 1272-1280.
González JE and Tsien RY. (1997). Improved indicators of cell membrane potential that use fluorescence resonance energy transfer. Chem. & Biol. 4, 269-277.
González JE, Oades K, Leychkis Y, Harootunian A, and Negulescu PA. (1999). Cell-based assays and instrumentation for screening ion-channel targets. Drug Discov. Today, 4, 431-439.
González JE and Maher MP. (2002). Cellular fluorescent indicators and voltage/ion probe reader (VIPR TM): Tools for ion channel and receptor drug discovery. Recept. Channels. 8, 283-295.
Huang C-J, Harootunian A, Maher MP, Quan C, Raj CD, McCormack K, Numann R, Negulescu PA, and González JE. (2006). Characterization of voltage-gated sodium-channel blockers by electrical stimulation and fluorescence detection of membrane potential. Nat. Biotechnol. 24, 439-446.
González JE, Worley J, and Van Goor F. Expression and analysis of recombinant ion channels: From structural studies to pharmacological screening. Chapter 8. In: Ion channel assays based on ion and voltage-sensitive fluorescent probes. Edited by J.J. Clare, and D.J. Trezise. 2006. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany. pp 187-211.
Selected Publications – Paul A. Negulescu
González JE and Negulescu PA. (1998). Intracellular detection assays for high-throughput screening. Curr. Opin. Biotechnology. 9, 624-631.
González JE, Oades K, Leychkis Y, Harootunian A, and Negulescu PA. (1999). Cell-based assays and instrumentation for screening ion-channel targets. Drug Discov. Today, 4, 431-439.
Huang C-J, Harootunian A, Maher MP, Quan C, Raj CD, McCormack K, Numann R, Negulescu PA, and González JE. (2006). Characterization of voltage-gated sodium-channel blockers by electrical stimulation and fluorescence detection of membrane potential. Nat. Biotechnol. 24, 439-446.
Van Goor F, Straley KS, Cao D, González J, Hadida S, Hazlewood A, Joubran J, Knapp T, Makings LR, Miller M, Neuberger T, Olson E, Panchenko V, Rader J, Singh A, Stack JH, Tung R, Grootenhuis PDJ, and Negulescu P. (2006). Rescue of ΔF508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules. Am. J. Physiol. Lung Cell Mol. Physiol. 290, L1117-L1130.
Van Goor F, Hadida S, Grootenhuis PDJ, Burton B, Cao D, Neuberger T, Turnbull A, Singh A, Joubran J, Hazlewood A, Zhou J, McCartney J, Arumugam V, Decker C, Yang J, Young C, Olson ER, Wine JJ, Frizzell RA, Ashlock M, and Negulescu P. (2009). Rescue of CF airway epithelial cell function in vitro by a CFTR potentiator, VX-770. Proc. Natl. Acad. Sci. USA. 106, 18825-18830.
Van Goor F, Hadida S, Grootenhuis PDJ, Burton B, Stack JH, Straley KS, Decker CJ, Miller M, McCartney J, Olson ER, Wine JJ, Frizzell RA, Ashlock M, and Negulescu PA. (2011). Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809. Proc. Natl. Acad. Sci. USA. 108, 18843-18848.
Award Presentation: Richard Lifton
Five to 10% of people are born with genetic diseases, resulting in substantial morbidity and early death. Mutations that cause thousands of these diseases have been identified. Treating or curing them, however, remains a major challenge. Gene therapy, once expected to solve this problem, has proved far more challenging than hoped, with only a few successes. How else can you overcome the consequences of a broken gene?
The Lasker-Debakey Clinical Research Award recognizes one the most audacious of these efforts – developing oral drugs that reconstruct the defective protein that causes cystic fibrosis. The incredible success of this effort has transformed and extended the lives of 10’s of thousands of people to date. Today we recognize Michael Welsh, Jesus (Tito) Gonzalez and Paul Negulescu for their seminal contributions to this effort. This remarkable achievement puts on full display the incredible power of biomedical science.
Cystic fibrosis affects 40,000 people in the US and 70,000 people abroad. It was described in 1935 by Dorothy Anderson, here in New York City. Features included severe malnutrition, with cysts and scarring of the pancreas, and lung disease featuring recurrent pneumonias with sticky infected mucus blocking the airways. She and Paul di Sant’ Agnese showed that CF is a recessive genetic disease, and that pancreatic enzyme replacement and IV antibiotics improved nutrition and survival in these patients. Arduous daily clapping on the chest and back to dislodge mucus also helped. Nonetheless, by 1980 life expectancy was only 18 years. They also discovered that patients had uniquely salty sweat, providing a non-invasive diagnostic test, and studies by Knowles and Quinton identified impaired efflux of chloride from lung epithelium and its influx into sweat glands, but the cause of these defects remained elusive.
Acceptance remarks
Acceptance Remarks: Michael Welsh
I feel tremendously honored to accept this award. On reading the list of previous recipients, I also feel deeply humbled, for it includes so many people that I have long admired.
I grew up in the rolling hills of rural Iowa. My father dropped out of 10th grade to serve in the Marines, fought in World War II, returned wounded, and worked in a foundry during the day and a bakery at night. My mother raised four children, tended a large garden, canned vegetables, and made many of our clothes. Saying that someone was a “hard worker” was high praise, and I followed my parent’s example, from milking the cow to raising runt pigs that farmers gave me.
My mother taught me empathy, so many times asking me, “How would you feel if …,” and then giving an example.
My education included an elementary school that had two classrooms – each had four grades. My class was the largest – it had 5 students. I entered college with no plan but loved humanities and science.
Although I had no knowledge of medicine or research, I applied to medical school at the University of Iowa. Why did I choose the physician path? The reason was simple – I thought it must be a job worth doing. In this decision, I was profoundly influenced by President John F. Kennedy. I remember sitting on the floor in front of the television inspired by his exhortation to go beyond oneself and contribute to society.
During medical school and residency, I was impressed by physician-scientists for their clinical skills and their discussion of research advances. I did a clinical pulmonary fellowship at UCSF. After working hard for a year in the lab, I realized that I had no original thoughts. I considered quitting the lab and just doing clinical medicine because I liked it, it was a worthwhile challenge, and I thought I was good at it.
Instead, I moved to UT Houston and studied intestine to learn more advanced physiology. During the day, I worked on intestine. Then, when animal labs were finishing experiments for the day, I collected the lungs to study the trachea. One night, I saw a surprising electrophysiological response. I went home at 3 or 4 AM, couldn’t sleep, and over the next 2-3 months, I became completely obsessed with trying to understand what I had seen. I thought about my experiments while I was at the grocery store, while I was at a movie, all the time. When I discovered the answer, I was overwhelmed by an incredible sense of peace.
I knew then, that both a physician and a scientist would be my life’s work.
Acceptance Remarks: Jesús (Tito) González
I’m deeply honored to be included in this award for pivotal contributions to the discovery of life-changing CF drugs. Discovering, developing, and making available these drugs is an amazing achievement. It required basic science, therapeutic discovery, pharmaceutical, and clinical advances that spanned decades. This would not have been possible without the important contributions and sacrifices of countless scientists, colleagues, drug developers, clinicians, and patients.
Translating basic research into promising innovative drug candidates is challenging, risky and not well-defined. In this case, it required fundamental biological insight, enabling technology and an environment to rapidly generate pharmacological proof-of-concept. This bridging data is critical to garner the interest of pharmaceutical companies with the resources and expertise to take on the long and difficult next steps. It is important to support the science, people, and mechanisms that are essential for this intermediate step; so that more transformative medicines can be realized.
In discussions with people about scientific research, I’ve learned to recognize phrases or statements that are inadvertent indications that some work has been very successful. They may say something like it is so clear, or logical, or even straightforward. When I hear these types of comments, I always smile inside.
In hindsight, scientific progress appears logical, advancing monotonically, and in some ways straightforward. While this may be the way it is written in textbooks, I can attest that this was not the case for the discovery of these CFTR modulators. In the beginning, the idea of screening small molecule libraries to identify drug leads for different mutations was not widely accepted as a promising or even feasible approach. Out of a combination of inspired optimism and naivete, we pursued this new approach.
I’m truly grateful to have helped pioneer this CF discovery path with my talented and passionate colleagues. To up-and-coming scientists working on big challenges today, I encourage you to follow your instincts and seek fundamentally new approaches that can make the needle jump. There will be many obstacles and failures, this is normal. Explore, collaborate, and apply your discoveries to better the lives of those around you.
Acceptance Remarks: Paul Negulescu
I am honored to receive the Lasker-DeBakey Clinical Medical Research Award with Mike Welsh and Tito Gonzelez for contributions to the discovery of CFTR modulators to treat cystic fibrosis. I’m also honored to represent decades of work by my colleagues at Vertex to discover, develop and bring these medicines to patients.
I did not always intend to be a scientist. But as a history major, I took a physiology class from future Nobel Laureate Roger Tsien. I was fascinated by his lectures on the kidney and how it regulated sodium and chloride in our blood. I never looked at salt the same way after that.
I became interested in research and was a graduate student when the CFTR gene was discovered in 1989. I remember thinking “wow”, now someone can find a therapy to treat this disease. I had no idea that I might someday be involved.
My chance to be part of the CF story came a decade later. Initial gene therapy efforts were stalled, and we had an opportunity to try a different approach. Rather than replace the gene, the idea was to repair the defective CFTR protein with a drug. This had never been done and most people thought it was impossible. But we saw the situation differently. Mike Welsh’s work showed that CFTR was a chloride channel that was faulty in people with CF, so we knew what needed to be fixed. And new technologies such as the dyes Tito had invented allowed us to screen for compounds to restore CFTR function. I thought we should try.
Over the next twenty-five years, I discovered a passion for the collective effort required to discover and develop medicines, and dedicated myself to it. I’m grateful for the support of the CF community, including the many people with CF who participated in our clinical trials. It is thrilling and rewarding that our work may benefit about 90% of people with CF, and it inspires us to work toward effective therapy for all.
My path was influenced by inspiring teachers and the ripples from important discoveries like the CF gene and the invention of technologies. I’ve come to think about science as a flowing river. We can observe it from the bank, jump in and be carried along, and if we’re lucky and persistent, we have a chance to guide where the river goes.
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