Prior to their work, it was thought that proteins, which at "birth" resemble a line of beads on a string, spontaneously fold themselves into their final, three-dimensional structures. Drs. Hartl and Horwich discovered that inside cells, proteins need assistance from other proteins, known as chaperones, to guide the process and ensure they fold into the proper shape. In independent and often complementary work, they also established the pathway and molecular mechanisms involved in this process.
The work of Drs. Hartl and Horwich demonstrated that when the protein folding pathway is imperfect, protein can accumulate in cells, leading to disease. Protein misfolding has been associated with approximately 20 diseases, including Alzheimer's, Huntington's and cystic fibrosis. Targeting the activity of the chaperones to correct misfolded proteins is a therapeutic goal currently under development.
"The selection of Arthur Horwich and Ulrich Hartl for this year's Horwitz Prize recognizes their scientific contribution began in part by Rosalind Franklin on the role of shape in human biology; and as the pathway has been replicated in bacteria, fungi, plants, animals and humans, their work has been seminal in understanding the protein folding as vital to biological function," said Andrew R. Marks, M.D., chair of the Horwitz Prize Committee at Columbia University. Dr. Marks is the Clyde and Helen Wu Professor of Molecular Cardiology and chairman of the Department of Physiology and Cellular Biophysics at Columbia University College of Physicians and Surgeons.
"We are delighted to highlight the contributions of women in science by honoring the work of Rosalind Franklin," added Dr. Marks. "It is particularly important that her key role in unraveling the structure of DNA is widely recognized so that she can serve as a role model for young women in science and for al
|Contact: Elizabeth Streich|
Columbia University Medical Center