1. S. Sulthana, T. Banerjee, J. Kallu, SR. Vuppala, B. Heckert, S. Naz, T. Shelby, O. Yambem, Santra, S. “Combination Therapy of NSCLC Using Hsp90 Inhibitor and Doxorubicin Carrying Functional Nanoceria". Molecular Pharmaceutics 2017, in press.

  2. S. Naz, J. Beach, B. Heckert, T. Tummala, O. Pashchenko, T. Banerjee, Santra, S. “Cerium Oxide Nanoparticles: A "Radical" Approach to Neurodegenerative Disease Treatment". Nanomedicine 2017, in press.

  3. T. Shelby, T. Banerjee, Santra, S. “How nanosensors may detect pathogen contamination before it ever reaches the dinner table". Future Microbiology 2017, in press.

  4. T. Shelby, T. Banerjee, J. Kallu, S. Sulthana, I. Zegar, Santra, S. “Novel Magnetic Relaxation Nanosensors: An Unparalleled “Spin” on Influenza Diagnosis”. Nanoscale 2016, DOI: 10.1039 / C6NR05889B.

  5. T. Banerjee, S. Sulthana, T. Shelby, B. Heckert, J. Jewell, K. Woody, V. Karimnia, J. McAfee, Santra, S. "Multiparametric Magneto-fluorescent Nanosensors for the Ultrasensitive Detection of Escherichia coli O157:H721". ACS Infectious Diseases 2016, 2, 667–673.

  6. H Burress, M. Taylor, T. Banerjee, S. A. Tatulian, K. Teter. "Co- and Post-Translocation Roles for Hsp90 in Cholera Intoxication".
    J. Biol.Chem, 2014, 289(48):33644-54.

  7. T. Banerjee, M. Taylor, A. Serrano, S. A. Tatulian, K. Teter. "ADP-Ribosylation Factor 6 acts as an allosteric activator for the folded but not disordered Cholera Toxin A1 Polypeptide". Molecular Microbiology, 2014 94(4):898-912.

  8. M. Taylor, H Burress, T. Banerjee, S. Ray, D. Curtis, SA. Tatulian, K. Teter. "Substrate-induced unfolding of protein disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin". PLoS Pathogens 2014, 10(2), e1003925.

  9. S. Ray, M. Taylor, T. Banerjee, S. A. Tatulian, K. Teter. “Lipid rafts alter the stability and activity of the cholera toxin A1 subunit”.
    J. Biol.Chem, 287, (2012)
    30395-30405.

  10. N. Salim, R. Lamichhane, R. Zhao, T. Banerjee, J. Phillip, D. Rueda, A. L. Feig. “Thermodynamic and Kinetic Analysis of an RNA Kissing Interaction and Its Resolution into an Extended Duplex”. Biophys. J, 102, (2012) 1097-1107.

  11. M. Taylor,T. Banerjee, N. VanBennekom, K. Teter. “Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance”. J. Vis. Exp. (JOVE) 59 (2012) 3686, doi: 10.3791/3686. (PubMed-indexed video journal) .

  12. M. Taylor, T. Banerjee, S. Ray, S. A. Tatulian, K. Teter. “Protein disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit”.J. Biol.Chem 286 (2011) 22090-22100.

  13. M. Taylor, *T. Banerjee* F. Navarro-Garcia, J. Huerta, S. Massey, M. Burlingame, A. H. Pande, SA Tatulian, K Teter. “A therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunit”. PLoS One 6 (2011) 18825-18834. * Contributed equally.

  14. C. Kaittanis T. Banerjee, S. Santra, O. J. Santiesteban, K. Teter, J. M. Perez. “Identification of Molecular-Mimicry-Based Ligands for Cholera Diagnostics using Magnetic Relaxation”. Bioconjugate Chemistry 16 (2011) 307-314.

  15. T. Banerjee, A. H. Pande, M. G. Jobling, M. Taylor, S. Massey, R. K. Holmes, S. A. Tatulian, K. Teter. “Contribution of subdomain structure to the thermal stability of the cholera toxin A1 subunit”. Biochemistry 49 (2010) 8839.

  16. S. Massey, T. Banerjee, A. H. Pande, M. Taylor, S. A. Tatulian, K. Teter. “Stabilization of the tertiary structure of the cholera toxin A1 subunit inhibits toxin dislocation and cellular intoxication”. J. Mol. Biol. 393 (2009) 1083.

  17. T. Banerjeeand N. Kishore. “Insights into the Energetics and Mechanism Underlying the Interaction of Tetraethyl ammonium bromide with Proteins”. J. Chem. Thermodyn. 40 (2007) 483-491.

  18. *T. Banerjee*S. K. Singh and N. Kishore. “Binding of Naproxen and Amitriltyline to Bovine Serum Albumin: Biophysical Aspects”. J. Phys. Chem. B. 110 (2006) 24147-24156.

  19. T. Banerjee, and N. Kishore. “Binding of 8-anilinonaphthalene sulfonate to dimeric and tetrameric concanavalin A: Energetics and its implications on saccharide binding studied by isothermal titration calorimetry”. J. Phys. Chem. B 110 (2006) 7022-7028.

  20. T. Banerjee, and N. Kishore. “Interactions of peptides and lysozyme with aqueous tetraethylammonium bromide at 298.15 K”. J. Solution Chem. 35 (2006) 1389-1399.

  21. T. Banerjee, and N. Kishore. “2,2,2-Trifluoroethanol induced molten globule state of concanavalin A and energetics of ANS binding: Calorimetric and spectroscopic investigation”. J. Phys. Chem. B 47 (2005) 22655-22662.

  22. T. Banerjee, and N. Kishore. “Does the anesthetic 2,2,2-trifluoroethanol interact with bovine serum albumin by direct binding or solvent mediated effects? A calorimetric and spectroscopic investigation”. Biopolymers 78 (2005) 78-86.

  23. T. Banerjee, and N. Kishore. “Interactions of Some Amino Acids with Aqueous Tetraethyl ammonium bromide at T = 298.15 K: A Volumetric Approach”. J. Solution chem. 34 (2005) 137-153.

  24. T. Banerjee, and N. Kishore. “A Differential Scanning Calorimetric Study on the Irreversible Thermal Unfolding of Concanavalin A”. Thermochimica Acta 411 (2004) 109-230.


  25. NOTE: The PDF files provided are for academic purposes only.