Benjamin Cravatt III
|Benjamin F Cravatt|
The Scripps Research Institute|
|Doctoral advisors||Dale L. Boger, Richard Lerner|
Benjamin Franklin Cravatt III is a professor in and chair of the Department of Chemical Physiology at The Scripps Research Institute in La Jolla, California. Considered a co-inventor of activity based proteomics and a substantial contributor to research on the endocannabinoid system, he is a prominent figure in the nascent field of chemical biology. Cravatt was elected to the National Academy of Sciences in 2014, and the American Academy of Arts and Sciences in 2016. He is also a Cope Scholar and a Searle Scholar.
Cravatt entered Stanford University in 1988, graduating in 1992 with a BS in the Biological Sciences and a BA in History. He then received a PhD in Macromolecular and Cellular Structure and Chemistry from The Scripps Research Institute in 1996, where he worked under the joint supervision of Dale L. Boger and Richard Lerner. His early contributions to the cannabinoid field include identification and characterization of the endocannabinoid-terminating enzyme fatty acid amide hydrolase (FAAH), as well as the isolation of the novel soporific compound oleamide from cerebrospinal fluid.
Cravatt and colleagues pioneered the activity based protein profiling (ABPP) chemical proteomic technology, which they used in 2010 to elucidate certain global proteomic features of cysteines. Cravatt's lab has since combined the ABPP technology with metabolomics.
Among the awards that Cravatt has received are the TR100 Award in 2002, the Eli Lilly Award in Biological Chemistry in 2004, the ASBMB-Merck Award in 2014 and the Sato Memorial Award in 2015. Cravatt also received an NCI MERIT grant in 2009.
Cravatt is a co-founder of Vividion Therapeutics, Abide Therapeutics and ActivX Biosciences. He currently serves as an Associate Editor for the Journal of the American Chemical Society, and previously served in the same capacity for Chemical Science.
PROTOMAP is a recently developed proteomic technology for identifying changes to proteins that manifest in altered migration by one-dimensional SDS-PAGE. It is similar, conceptually, to two-dimensional gel electrophoresis and difference gel electrophoresis in that it enables global identification of proteins that undergo altered electrophoretic migration resulting from, for example, proteolysis or post-translational modification. However, it is unique in that all proteins are sequenced using mass spectrometry which provides information on the sequence coverage detected in each isoform of each protein thereby facilitating interpretation of proteolytic events.
PROTOMAP is performed by resolving control and experimental samples in separate lanes of a 1D SDS-PAGE gel. Each lane is cut into evenly spaced bands (usually 15-30 bands) and proteins in these bands are sequenced using shotgun proteomics. Sequence information from all of these bands are bioinformatically integrated into a visual format called a peptograph which plots gel-migration in the vertical dimension (high- to low-molecular weight, top to bottom) and sequence coverage in the horizontal dimension (N- to C-terminus, left to right). A peptograph is generated for each protein the sample (thousands of peptographs are generated from a single experiment) and this data format enables rapid identification of proteins undergoing proteolytic cleavage by making evident changes in gel-migration that are accompanied by altered topography.
- Viegas, Jennifer (2 February 2016). "Profile of Benjamin Cravatt". Proceedings of the National Academy of Sciences of the United States of America. 113: 1109–11. doi:10.1073/pnas.1525099113. PMC . PMID 26811454.
- "National Academy of Sciences Members and Foreign Associates Elected" (Press release). United States: National Academy of Sciences. 29 April 2014. Archived from the original on 18 August 2015. Retrieved 2016-12-31.
Cravatt, Benjamin F.; professor and chair, department of chemical physiology, The Scripps Research Institute, La Jolla, Calif.
- Bogyo, Matthew; Cravatt, Benjamin F. (February 2007). "Genomics and proteomics: From genes to function: advances in applications of chemical and systems biology". Current Opinion in Chemical Biology (Editorial Overview). 11: 1–3. doi:10.1016/j.cbpa.2006.12.029 – via ScienceDirect. (Subscription required (. ))
- Cravatt, B.F.; Giang, D.K.; Mayfield, S.P.; Boger, D.L.; Lerner, R.A. (7 November 1996). "Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides". Nature. 384 (6604): 83–7. doi:10.1038/384083a0. PMID 8900284. (Subscription required (. ))
- Cravatt, BF; Prospero-Garcia, O; Siuzdak, G; Gilula, NB; Henriksen, SJ; Boger, DL; Lerner, RA (9 June 1995). "Chemical characterization of a family of brain lipids that induce sleep". Science. 268 (5216): 1506–9. doi:10.1126/science.7770779. PMID 7770779. (Subscription required (. ))
- Johnson CE, Kornbluth S (September 2008). "Caspase cleavage is not for everyone". Cell. 134 (5): 720–1. doi:10.1016/j.cell.2008.08.019. PMID 18775303.
- Dix MM, Simon GM, Cravatt BF (August 2008). "Global mapping of the topography and magnitude of proteolytic events in apoptosis". Cell. 134 (4): 679–91. doi:10.1016/j.cell.2008.06.038. PMC . PMID 18724940.