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  Dr. SHARMISTHA MITRA  
 
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Title : Dr.
First Name : SHARMISTHA
Last Name : MITRA
University/Institution : UTSouthwestern Medical Center, Dallas
Email ID : dmitra.sharmi04@gmail.com
City : Dalla
Country : United States
State : Texas
Zipcode : 75390
Company Name :
Area of Research
Pediatrics Neurology
Area of Expertise
Biochemistry and Molecular Biology
Brief Description of Research Interest :
I am interested in post-translational modification of proteins by ubiquitylation and its impact on human diseases. I have worked with mono-ubiquitination of proteins related to cardio-vascular diseases and innate immune signaling pathways. Currently I am working on ubiquitin ligases and their contributions to certain rare neurological disorders. I am also interested in deciphering the function of soluble and membrane embedded proteins/enzymes in glycogen metabolism and its impact on human diseases. My diverse training includes protein biochemistry (protein purification- both soluble and membrane bound, NMR for protein-lipid and protein-protein interaction, X ray crystallography), enzyme based assays, kinetic studies for protein-ligand interaction (such as SPR) as well as recent cell biology training (in vivo cell culture based assays and mice study) that I am getting at UT Southwestern. 
Representative Publications :
  1. Kim K *., Mitra S *., Wu G *., Berka V., Song J., Yu Y., Poget S., Wang D., Tsai A., and Zhou M. “Six-Transmembrane Epithelial Antigen of Prostate 1 (STEAP1) Has a Single b Heme and Is Capable of Reducing Metal Ion Complexes and Oxygen” Biochemistry55:48: 6673–6684, 2016 *Equal contribution
  2. McCoy J. G., Ren Z., Stanevich V., Lee J., Mitra S., Levin E.L., Poget S., Quick M., Im W.,  and Zhou M. “The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport”  Structure24: 6: 956–964, 2016
  3. Mitra S., Traughber C.A., Brannon M.K., Gomez S., and Capelluto D.G.S. “Ubiquitin interacts with the Tollip C2 and CUE domains and inhibits binding of Tollip to phosphoinositides” J Biol Chem288:25780-91, 2013
  4. Ankem G. *, Mitra S. *, Sun F., Moreno A.C., Chutvirasakul B., Azurmendi H.F., Li L. and Capelluto D.G.S. “The C2 domain of Tollip, a Toll-like receptor signaling regulator, exhibits broad preference for phosphoinositides.” Biochem. J.435: 597-608, 2011. *Equal contribution (The article was selected as ‘Spotlight Research’ by Biochem. J. Structure section)
  5. Azurmendi HF., Mitra S., Ayala I., Li L., Finkielstein C. V., and Capelluto D.G. S.  “1H, 15N, and 13C resonance assignments and secondary structure of the Tollip CUE domain.” Mol Cells 30: 581-585, 2010.
 
     
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