2019 Dr. Paul Janssen Award winners, Drs. Hartl and Horwich were celebrated at events in Beerse – the home of Dr. Paul, and New York City. Following are remarks from Chair of the Selection Committee, David Julius, Ph.D. Dr. Julius is professor and chair of the Department of Physiology at the University of California, San Francisco, and was a winner of the Dr. Paul Janssen Award in 2013.
Good evening everyone. As outgoing Chair of the Paul Janssen Award Selection Committee, I am pleased to have a chance to congratulate this year’s awardees.
Let me begin by saying a few words about what the selection committee looks for when we choose laureates. First, and foremost, we look for those who have opened or transformed a field though a bold and seminal discovery. Second we ask if that advance or discovery is likely to have a broad impact on our understanding of biology, physiology and/or medicine. And third we ask if the individual or individuals has been an intellectual leader who has brought positive energy to their field to inspire growth and development. Indeed, these criteria in many ways reflect the legacy of Dr. Paul Janssen.
This year’s laureates fulfill these criteria in spades and their discoveries detailing the machinery and mechanisms of protein folding is remarkable on a number of fronts. First, their work overturned long-standing dogma about how proteins fold in cells, challenging the idea that the linear sequence of a polypeptide is, in and of itself, sufficient to dictate proper protein folding in the cell. Instead, they found that protein machines known as a chaperonins perform this vital task. Second their work has broad implications for all of biology because chaperonins are found throughout living organisms ranging from microbes to man, and in multiple cellular compartments including the cytoplasm and mitochondria. Third, problems in protein folding are associated with a variety of diseases - most notably neurodegenerative disorders such as Alzheimer’s and ALS - and thus the discoveries of our laureates have tremendous potential to yield transformative insights into mechanisms underlying debilitating human disease.
From a basic science perspective, and especially for those of us who are excited by biochemistry and biophysics, chaperonins are just beautiful things to behold. Often described as a capsule or can with a lid that sequesters unfolded proteins until they attain their proper shape, chaperonins are perhaps the loveliest example of how evolution has solved a fundamental problem in a way that is so elegantly revealed by the structure and lifecycle of this magnificent biological machine.
On behalf of the selection committee, I am pleased to congratulate Drs. Hartl and Horwich for their profound and beautiful scientific discoveries and achievements, which are recognized by this year’s Dr. Paul Janssen Award in Biomedical Research.
Good evening everyone. As outgoing Chair of the Paul Janssen Award Selection Committee, I am pleased to have a chance to congratulate this year’s awardees.
Let me begin by saying a few words about what the selection committee looks for when we choose laureates. First, and foremost, we look for those who have opened or transformed a field though a bold and seminal discovery. Second we ask if that advance or discovery is likely to have a broad impact on our understanding of biology, physiology and/or medicine. And third we ask if the individual or individuals has been an intellectual leader who has brought positive energy to their field to inspire growth and development. Indeed, these criteria in many ways reflect the legacy of Dr. Paul Janssen.
This year’s laureates fulfill these criteria in spades and their discoveries detailing the machinery and mechanisms of protein folding is remarkable on a number of fronts. First, their work overturned long-standing dogma about how proteins fold in cells, challenging the idea that the linear sequence of a polypeptide is, in and of itself, sufficient to dictate proper protein folding in the cell. Instead, they found that protein machines known as a chaperonins perform this vital task. Second their work has broad implications for all of biology because chaperonins are found throughout living organisms ranging from microbes to man, and in multiple cellular compartments including the cytoplasm and mitochondria. Third, problems in protein folding are associated with a variety of diseases - most notably neurodegenerative disorders such as Alzheimer’s and ALS - and thus the discoveries of our laureates have tremendous potential to yield transformative insights into mechanisms underlying debilitating human disease.
From a basic science perspective, and especially for those of us who are excited by biochemistry and biophysics, chaperonins are just beautiful things to behold. Often described as a capsule or can with a lid that sequesters unfolded proteins until they attain their proper shape, chaperonins are perhaps the loveliest example of how evolution has solved a fundamental problem in a way that is so elegantly revealed by the structure and lifecycle of this magnificent biological machine.
On behalf of the selection committee, I am pleased to congratulate Drs. Hartl and Horwich for their profound and beautiful scientific discoveries and achievements, which are recognized by this year’s Dr. Paul Janssen Award in Biomedical Research.