Dr. John 'Jay' Schneekloth

Dr. John 'Jay' Schneekloth
Chemical Genetics
301-228-4620

Research Summary

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.

Publications

1 - 5 of 15 results

1 2 3

1) Kim YS, Nagy K, Keyser S, Schneekloth JS.
An electrophoretic mobility shift assay identifies a mechanistically unique inhibitor of protein sumoylation.
Chem. Biol. 20: 604-13, 2013. [Journal]

2) Kim J, Schneekloth J, Sorensen E.
A chemical synthesis of 11-methoxy mitragynine pseudoindoxy featuring the interrupted Ugi reaction.
Chem. Sci. 3: 2849-52, 2012. [Journal]

3) Noblin DJ, Page CM, Tae HS, Gareiss PC, Schneekloth JS, Crews CM.
A HaloTag-based Small Molecule Microarray Screening Methodology with Increased Sensitivity and Multiplex Capabilities.
ACS Chem. Biol. 7: 2055-63, 2012. [Journal]

4) Schneekloth JS, Crews CM.
Natural Product Inhibitors of the Ubiquitin-Proteasome Pathway.
Curr. Drug Targets. 12: 1581-94, 2011. [Journal]

5) Schneekloth JS, Kim J, Sorensen EJ.
An interrupted Ugi reaction enables the preparation of substituted indoxyls and aminoindoles.
Tetrahedron. 65: 3096-3101, 2009. [Journal]

A service of the National Cancer Institute

Dr. John 'Jay' Schneekloth

Research Summary

Small Molecule Probes of Ubiquitin-like Signaling

Inhibiting Protein-Protein Interactions With Oligomeric Molecules