Bhupesh Taneja studies proteins from pathogenic organisms-M. tuberculosis and B. anthracis - and their interactions with other biomolecules using structural biology. His earlier work has been on the correlation between structure and mechanism of action of topoisomerase V which addresses fundamental issues of DNA structure and architecture during the catalytic cycle of DNA modulating enzymes.
His major interests are:
Structural insights into nucleotide modifying and regulatory proteins of M. tuberculosis
Understanding the interaction of dermatophytes with skin through structural, molecular and cellular approaches
- Structural and Functional Characterization of Rv2966c Protein Reveals an RsmD-like Methyltransferase from Mycobacterium tuberculosis and the Role of Its N-terminal Domain in Target Recognition. Kumar, A., Saigal, K., Malhotra, K., Sinha, K.M., Taneja, B. 2011. J Biol Chem. 286:19652-61
- Integration host factor of Mycobacterium tuberculosis, mIHF, compacts DNA by a bending mechanism. Mishra A, Vij M, Kumar D, Taneja V, Mondal AK, Bothra A, Rao V, Ganguli M, Taneja B. 2013 PLoS One. 8(7):e69985.
- Identification of one of the apurinic/apyrimidinic lyase active sites of topoisomerase V by structural and functional studies. Rajan R, Prasad R, Taneja B, Wilson SH, Mondragón A. 2013 Nucleic Acids Res. 41(1):657-66.
- An Indian effort towards affordable drugs: "generic to designer drugs". Taneja, B., Yadav, J., Chakraborty, T. K., and Brahmachari, S. K. Biotechnol.J. 2009. 4, 348-360.
- Topoisomerase V relaxes supercoiled DNA by a constrained swiveling mechanism. Taneja B., Schnurr B., Slesarev A., Marko J.F. and Mondragon A. Proc Natl Acad Sci, U S A. (2007) 104:14670-14675.