Postdoctoral Associates

Kate is currently researching PRMT1-catalyzed methylation of arginine residues in kinase consensus sequences.  She is also investigating crosstalk between these two posttranslational modifications as a potential regulatory mechanism for cell signaling and transcription.

Santanu is currently working on the design, synthesis and biological evaluation of inhibitors targeting the PAD family of enzymes. His work also focuses on the development of isozyme-selective inhibitors and probes for the PADs.

Mitesh’s research is focused on identifying “Readers” of citrullination as well as a putative decitrullinase.  This effort uses a combination of chemical biology tools and proteomics to identify these interpreters of citrullination.

Venky’s research is focused on using proteomic approaches to uncover the targets and off targets of our PAD selective inhibitors as well as using proteomic methods to identify the citrullinated biomarkers associated with rheumatoid arthritis, lupus and breast cancer. 

Son is currently focused on identifying citrullinated biomarkers associated with Rheumatoid Arthritis and lupus.  In addition, Son is adapting a quantitative proteomics platform for use with our glyoxals based probes.

Ari is currently focused on using chemoproteomic methods to identify citrullinated proteins and disease associated biomarkers.  This work is being performed jointly with the Weerapana group at Boston College.
In 2018 Ari has been awarded a Ruth L. Kirschtein fellowship by the NIH and the award was given to Ari for his proposal to develop enhanced methods for identifying the sites of citrullnation in proteins.

Ronak is currently focused on identifying citrullinated biomarkers associated with Rheumatoid Arthritis and breast cancer.  In addition, Ronak is studying the functional impact of these citrullination events on protein function, enzymatic activity and the generation of antibodies targeting citrullinated proteins.

Min's research is focused on the kinetic and catalytic mechanism study of Protein Arginine Methyltransferase5.  These works may provide guidance for the development for PRMT5 inhibitors for cancer therapy.  He is also interested in the interaction between PRMT5 and it's binding partners MEP50 and the effect of binding MEP50 on the function of PRMT5.

Li’s research is focused on identifying the factors that modulate the calcium dependence of the PADs using a combination of chemical proteomics to identify candidate interacting proteins mutagenesis of known post-translational modifications sites.