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John 'Jay' Schneekloth Jr., Ph.D.

Portait Photo of John Schneekloth
Chemical Biology Laboratory
Head, Chemical Genetics Section
Investigator
Center for Cancer Research
National Cancer Institute
Building 376, Room 225C
P.O. Box B
Frederick, MD 21702-1201
Phone:  
301-228-4620
Fax:  
301-846-6033
E-Mail:  
schneeklothjs@mail.nih.gov

Biography

Dr. Schneekloth received his undergraduate degree from Dartmouth College in 2001, where he wrote his honors thesis with Prof. Gordon Gribble. He then moved to Yale University and obtained a Ph.D. from the chemistry department with Prof. Craig Crews in 2006. As a graduate student he studied natural product total synthesis and chemical biology relating to the ubiquitin-proteasome pathway. He then pursued an NIH postdoctoral fellowship with Prof. Erik Sorensen at Princeton University, where he worked on the development of a new multicomponent reaction and the application of this reaction to the synthesis of analgesic natural products. He returned to Yale in 2009 where he worked as a medicinal chemist at the Yale Small Molecule Discovery Center. In 2011, Dr. Schneekloth joined NCI where his research involves using synthetic chemistry and screening techniques to develop small molecule probes of signal transduction pathways. Specific areas of interest include the identification of small molecule inhibitors of ubiquitin-like signaling pathways and the study of oligomeric small molecules that disrupt protein-protein interactions relevant to cancer, HIV and Alzheimer's disease.

Research

Small Molecule Probes of Ubiquitin-like Signaling
The dynamic modulation of protein posttranslational modifications is a major regulatory mechanism in cellular homeostasis. Greater than 90% of the proteome is regulated by modification with small protein tags such as ubiquitin or ubiquitin-like molecules. The posttranslational ligation or cleavage of these tags affects critical events such as gene transcription, subcellular localization, protein degradation, and many others. It is not surprising to note that disruption of these pathways is associated with a large number of disease states, including a many cancers. A major goal of the lab is to utilize synthetic chemistry to generate new small molecule probes of specific enzymes within ubiquitin-like signaling pathways, including druglike enzyme inhibitors as well as activity based probes.

Inhibiting Protein-Protein Interactions With Oligomeric Molecules
A major area of interest in medicinal chemistry is the inhibition of protein-protein interactions with small synthetic molecules. Many protein-protein interactions are of high therapeutic interest, but are classically considered 'undruggable'. Strategies to disrupt these interactions (for example, receptor-ligand interactions on cell surfaces) will provide new opportunities for the treatment of cancer, HIV/AIDS, and many other diseases. This area of the lab focuses on developing new oligomeric small molecules that perturb disease-relevant protein-protein interactions, and understanding how the structure of these molecules allows them to interact with protein surfaces.

This page was last updated on 6/7/2013.