Craig Crews is a renowned American biochemist and the Lewis B. Cullman Professor of Molecular, Cellular, and Developmental Biology at Yale University. He has made significant contributions to the field of biochemistry, particularly in the area of proteolysis and the development of novel therapeutic strategies. Crews' research focuses on the discovery of small molecules that can selectively inhibit specific protein-degradation pathways, which has led to the development of new treatments for various diseases, including cancer and neurodegenerative disorders.
Early Life and Education
Craig Crews was born in 1957 in the United States. He developed an interest in science at an early age and pursued his undergraduate degree in chemistry from the University of Virginia, graduating in 1979. Crews then moved to the University of Georgia, where he earned his Ph.D. in organic chemistry in 1984 under the supervision of Dr. Charles L. Liotta. During his graduate studies, Crews gained expertise in organic synthesis and medicinal chemistry, which laid the foundation for his future research endeavors.
Academic Career
After completing his Ph.D., Crews joined the laboratory of Dr. Sidney Hecht at the University of Virginia as a postdoctoral researcher. In 1986, he moved to Yale University, where he began his independent research career as an assistant professor in the Department of Molecular, Cellular, and Developmental Biology. Crews’ research group at Yale focuses on the discovery and development of small molecules that can modulate protein function, with a particular emphasis on the ubiquitin-proteasome pathway. Over the years, Crews has risen through the academic ranks, becoming a full professor in 2000 and being appointed as the Lewis B. Cullman Professor of Molecular, Cellular, and Developmental Biology in 2006.
| Year | Position | Institution |
|---|---|---|
| 1984-1986 | Postdoctoral Researcher | University of Virginia |
| 1986-1993 | Assistant Professor | Yale University |
| 1993-2000 | Associate Professor | Yale University |
| 2000-present | Professor | Yale University |
Research Contributions
Crews’ research has made significant contributions to our understanding of the ubiquitin-proteasome pathway and its role in disease. His laboratory has developed novel small molecules that can selectively inhibit specific protein-degradation pathways, which has led to the discovery of new therapeutic targets for various diseases. One of the key areas of focus for Crews’ research group is the development of proteolysis-targeting chimera (PROTAC) technology, which allows for the selective degradation of specific proteins. This technology has shown promise in the treatment of various diseases, including cancer, neurodegenerative disorders, and infectious diseases.
PROTAC Technology
PROTAC technology is a novel approach to targeted protein degradation, which involves the use of small molecules that can recruit an ubiquitin ligase to a specific protein, leading to its degradation. Crews’ laboratory has developed a range of PROTAC molecules that can target various proteins, including androgen receptor, estrogen receptor, and BCL-2. These molecules have shown promise in preclinical studies, demonstrating their potential as therapeutic agents for the treatment of various diseases.
- PROTAC molecules can selectively target specific proteins for degradation
- PROTAC technology has shown promise in the treatment of various diseases, including cancer and neurodegenerative disorders
- Crews' laboratory has developed a range of PROTAC molecules that can target various proteins
What is the ubiquitin-proteasome pathway?
+The ubiquitin-proteasome pathway is a cellular process that involves the degradation of proteins by the proteasome, a large protein complex. The pathway is initiated by the attachment of a ubiquitin molecule to the target protein, which serves as a signal for its degradation.
What is PROTAC technology?
+PROTAC technology is a novel approach to targeted protein degradation, which involves the use of small molecules that can recruit an ubiquitin ligase to a specific protein, leading to its degradation.
