{"id":27,"date":"2022-03-15T09:35:25","date_gmt":"2022-03-15T09:35:25","guid":{"rendered":"http:\/\/localhost\/BIC-NII\/?page_id=27"},"modified":"2025-06-02T11:04:20","modified_gmt":"2025-06-02T05:34:20","slug":"publications","status":"publish","type":"page","link":"http:\/\/202.54.249.134\/BIC-NII\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"\n<ul class=\"wp-block-list\">\n<li>Chaudhary, S., Sravya, M., Pahwa, F., V, Sureshkumar., Singh, P., Chaturvedi, S., <strong>Mohanty, D.<\/strong>, Dash, D., &amp; Nanda, R. K. (2025). Single-cell profiling of the lung immune cells of diabetes-tuberculosis comorbidity reveals reduced type-II interferon and elevated TH17 responses. <em>eLife<\/em>. https:\/\/doi.org\/10.7554\/elife.106025.1<\/li>\n\n\n\n<li>Ansari, A., Sachan, S., Ahuja, J., Venkadesan, S., Nikam, B., Kumar, V., &#8230;<strong>Mohanty, D.<\/strong>, &amp; Gupta, N. (2025). Distinct features of a peripheral T helper subset that drives the B cell response in dengue virus infection.\u00a0<em>Cell reports<\/em>,\u00a0<em>44<\/em>(3).<\/li>\n\n\n\n<li>Amir, S., Kumar, M., Kumar, V., &amp; <strong>Mohanty, D<\/strong>. (2025). HgutMgene-Miner: In silico genome mining tool for deciphering the drug-metabolizing potential of human gut microbiome.&nbsp;<em>Computers in Biology and Medicine<\/em>,&nbsp;<em>186<\/em>, 109679.<\/li>\n\n\n\n<li>Khanduja, A., &amp; <strong>Mohanty, D<\/strong>. (2025). SProtFP: a machine learning-based method for functional classification of small ORFs in prokaryotes.&nbsp;<em>NAR Genomics and Bioinformatics<\/em>,&nbsp;<em>7<\/em>(1), lqae186.<\/li>\n\n\n\n<li>Sarkar, B., Singh, J., Yadav, M., Sharma, P., Sharma, R. D., Singh, S., &#8230;, <strong>Mohanty, D<\/strong>., Kumar, Dhiraj., &amp; Gokhale, R. S. (2025). PPAR\u03b3 mediated enhanced lipid biogenesis fuels Mycobacterium tuberculosis growth in a drug-tolerant hepatocyte environment.&nbsp;<em>eLife<\/em>,&nbsp;<em>14<\/em>.<\/li>\n\n\n\n<li>Pal, S., Pal, A., and <strong>Mohanty, D<\/strong>. (2025). SG\u2010ML\u2010PLAP: A structure\u2010guided machine learning\u2013based scoring function for protein\u2013ligand binding affinity prediction.&nbsp;<em>Protein Science<\/em>,&nbsp;<em>34<\/em>(1), e5257. doi: <a href=\"https:\/\/doi.org\/10.1002\/pro.5257\" target=\"_blank\" rel=\"noreferrer noopener\">10.1002\/pro.5257<\/a><\/li>\n\n\n\n<li>Khanduja, A., M. Kumar, and <strong>D. Mohanty<\/strong>. 2023. &#8220;ProsmORF-pred: a machine learning-based method for the identification of small ORFs in prokaryotic genomes.&#8221; Brief Bioinform. doi: 10.1093\/bib\/bbad101.<\/li>\n\n\n\n<li>Mehdiratta, K., S. Nain, M. Sharma, S. Singh, S. Srivastava, B.D. Dhamale, <strong>D. Mohanty<\/strong>, S.S. Kamat, V.T. Natarajan, R. Sharma, and R.S. Gokhale. 2022. &#8220;Respiratory Quinone Switches from Menaquinone to Polyketide Quinone during the Development Cycle in Streptomyces sp. Strain MNU77.&#8221; Microbiol Spectr:e0259722. doi: 10.1128\/spectrum.02597-22.<\/li>\n\n\n\n<li>Gupta, P., and <strong>D. Mohanty<\/strong>. 2022. &#8220;Allosteric regulation of the inactive to active state conformational transition in CDPK1 protein of Plasmodium falciparum.&#8221; Int J Biol Macromol 215:489-500. doi: 10.1016\/j.ijbiomac.2022.06.065.<\/li>\n\n\n\n<li>Gupta, P., S. Venkadesan, and <strong>D. Mohanty<\/strong>. 2022. &#8220;Pf-Phospho: a machine learning-based phosphorylation sites prediction tool for Plasmodium proteins.&#8221; Brief Bioinform 23 (4). doi: 10.1093\/bib\/bbac249.<\/li>\n\n\n\n<li>Mehdiratta, K., S. Singh, S. Sharma, R.S. Bhosale, R. Choudhury, D.P. Masal, A. Manocha, B.D. Dhamale, N. Khan, V. Asokachandran, P. Sharma, M. Ikeh, A.C. Brown, T. Parish, A.K. Ojha, J.S. Michael, M. Faruq, G.R. Medigeshi, <strong>D. Mohanty<\/strong>, D.S. Reddy, V.T. Natarajan, S.S. Kamat, and R.S. Gokhale. 2022. &#8220;Kupyaphores are zinc homeostatic metallophores required for colonization of Mycobacterium tuberculosis.&#8221; Proc Natl Acad Sci U S A 119 (8). doi: 10.1073\/pnas.2110293119.<\/li>\n\n\n\n<li>Kumar, P., and <strong>D. Mohanty<\/strong>. 2022. &#8220;Development of a Novel Pharmacophore Model Guided by the Ensemble of Waters and Small Molecule Fragments Bound to SARS-CoV-2 Main Protease.&#8221; Mol Inform 41 (2):e2100178. doi: 10.1002\/minf.202100178.<\/li>\n\n\n\n<li>Gupta, P., and <strong>D. Mohanty<\/strong>. 2021. &#8220;SMMPPI: a machine learning-based approach for prediction of modulators of protein-protein interactions and its application for identification of novel inhibitors for RBD:hACE2 interactions in SARS-CoV-2.&#8221; Brief Bioinform 22 (5). doi: 10.1093\/bib\/bbab111.<\/li>\n\n\n\n<li>Agrawal, P., S. Amir, Deepak, D. Barua, and <strong>D. Mohanty<\/strong>. 2021. &#8220;RiPPMiner-Genome: A Web Resource for Automated Prediction of Crosslinked Chemical Structures of RiPPs by Genome Mining.&#8221; J Mol Biol 433 (11):166887. doi: 10.1016\/j.jmb.2021.166887.<\/li>\n\n\n\n<li>Agrawal, P., and <strong>D. Mohanty<\/strong>. 2021. &#8220;A machine learning-based method for prediction of macrocyclization patterns of polyketides and non-ribosomal peptides.&#8221; Bioinformatics 37 (5):603-611. doi: 10.1093\/bioinformatics\/btaa851.<\/li>\n\n\n\n<li>Kaur, P., M. Rausch, B. Malakar, U. Watson, N.P. Damle, Y. Chawla, S. Srinivasan, K. Sharma, T. Schneider, G.D. Jhingan, D. Saini, <strong>D. Mohanty<\/strong>, F. Grein, and V.K. Nandicoori. 2019. &#8220;LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation.&#8221; Nat Commun 10 (1):1231. doi: 10.1038\/s41467-019-09223-9.<\/li>\n\n\n\n<li>Kaur, H., N. Sain, <strong>D. Mohanty<\/strong>, and D.M. Salunke. 2018. &#8220;Deciphering evolution of immune recognition in antibodies.&#8221; BMC Struct Biol 18 (1):19. doi: 10.1186\/s12900-018-0096-1.<\/li>\n\n\n\n<li>Sharma, C., and <strong>D. Mohanty<\/strong>. 2018. &#8220;Sequence- and structure-based analysis of proteins involved in miRNA biogenesis.&#8221; J Biomol Struct Dyn 36 (1):139-151. doi: 10.1080\/07391102.2016.1269687.<\/li>\n\n\n\n<li>Agrawal, P., S. Khater, M. Gupta, N. Sain, and <strong>D. Mohanty<\/strong>. 2017. &#8220;RiPPMiner: a bioinformatics resource for deciphering chemical structures of RiPPs based on prediction of cleavage and cross-links.&#8221; Nucleic Acids Res 45 (W1):W80-W88. doi: 10.1093\/nar\/gkx408.<\/li>\n\n\n\n<li>Khater, S., M. Gupta, P. Agrawal, N. Sain, J. Prava, P. Gupta, M. Grover, N. Kumar, and <strong>D. Mohanty<\/strong>. 2017. &#8220;SBSPKSv2: structure-based sequence analysis of polyketide synthases and non-ribosomal peptide synthetases.&#8221; Nucleic Acids Res 45 (W1):W72-W79. doi: 10.1093\/nar\/gkx344.<\/li>\n\n\n\n<li>Sharma, C., and <strong>D. Mohanty<\/strong>. 2017. &#8220;Molecular Dynamics Simulations for Deciphering the Structural Basis of Recognition of Pre-let-7 miRNAs by LIN28.&#8221; Biochemistry 56 (5):723-735. doi: 10.1021\/acs.biochem.6b00837.<\/li>\n\n\n\n<li>Sain, N., and <strong>D. Mohanty<\/strong>. 2016. &#8220;modPDZpep: a web resource for structure based analysis of human PDZ-mediated interaction networks.&#8221; Biol Direct 11 (1):48. doi: 10.1186\/s13062-016-0151-4.<\/li>\n\n\n\n<li>Sain, N., G. Tiwari, and <strong>D. Mohanty<\/strong>. 2016. &#8220;Understanding the molecular basis of substrate binding specificity of PTB domains.&#8221; Sci Rep 6:31418. doi: 10.1038\/srep31418.<\/li>\n\n\n\n<li>Khater, S., S. Anand, and <strong>D. Mohanty<\/strong>. 2016. &#8220;In silico methods for linking genes and secondary metabolites: The way forward.&#8221; Synth Syst Biotechnol 1 (2):80-88. doi: 10.1016\/j.synbio.2016.03.001.<\/li>\n\n\n\n<li>Khater, S., and <strong>D. Mohanty<\/strong>. 2015. &#8220;Deciphering the Molecular Basis of Functional Divergence in AMPylating Enzymes by Molecular Dynamics Simulations and Structure Guided Phylogeny.&#8221; Biochemistry 54 (33):5209-5224. doi: 10.1021\/acs.biochem.5b00351.<\/li>\n\n\n\n<li>Khater, S., and <strong>D. Mohanty<\/strong>. 2015. &#8220;In silico identification of AMPylating enzymes and study of their divergent evolution.&#8221; Sci Rep 5:10804. doi: 10.1038\/srep10804.<\/li>\n\n\n\n<li>Khater, S., and <strong>D. Mohanty<\/strong>. 2015. &#8220;novPTMenzy: a database for enzymes involved in novel post-translational modifications.&#8221; Database (Oxford) 2015:bav039. doi: 10.1093\/database\/bav039.<\/li>\n\n\n\n<li>Kumar, N., N.P. Damle, and <strong>D. Mohanty<\/strong>. 2015. &#8220;Getting phosphorylated: is it necessary to be solvent accessible?&#8221; Proc Indian Natn Sci Acad.<\/li>\n\n\n\n<li>Khater, S., and <strong>D. Mohanty<\/strong>. 2014. &#8220;Genome-wide search for eliminylating domains reveals novel function for BLES03-like proteins.&#8221; Genome Biol Evol 6 (8):2017-2033. doi: 10.1093\/gbe\/evu161.<\/li>\n\n\n\n<li>Damle, N.P., and <strong>D. Mohanty<\/strong>. 2014. &#8220;Mechanism of autophosphorylation of mycobacterial PknB explored by molecular dynamics simulations.&#8221; Biochemistry 53 (28):4715-4726. doi: 10.1021\/bi500245v.<\/li>\n\n\n\n<li>Tiwari, G., and <strong>D. Mohanty<\/strong>. 2014. &#8220;Structure-based multiscale approach for identification of interaction partners of PDZ domains.&#8221; J Chem Inf Model 54 (4):1143-1156. doi: 10.1021\/ci400627y.<\/li>\n\n\n\n<li>Damle, N.P., and <strong>D. Mohanty<\/strong>. 2014. &#8220;Deciphering kinase-substrate relationships by analysis of domain-specific phosphorylation network.&#8221; Bioinformatics 30 (12):1730-1738. doi: 10.1093\/bioinformatics\/btu112.<\/li>\n\n\n\n<li>Tiwari, G., and <strong>D. Mohanty<\/strong>. 2013. &#8220;An in silico analysis of the binding modes and binding affinities of small molecule modulators of PDZ-peptide interactions.&#8221; PLoS One 8 (8):e71340. doi: 10.1371\/journal.pone.0071340.<\/li>\n\n\n\n<li>Yadav, G., S. Anand, and <strong>D. Mohanty<\/strong>. 2013. &#8220;Prediction of inter domain interactions in modular polyketide synthases by docking and correlated mutation analysis.&#8221; J Biomol Struct Dyn 31 (1):17-29. doi: 10.1080\/07391102.2012.691342.<\/li>\n\n\n\n<li>KHATER, S., and <strong>D. MOHANTY<\/strong>. 2013. &#8220;STRUCTURAL BIOINFORMATICS APPROACHES FOR DECIPHERING BIOSYNTHETIC CODE OF SECONDARY METABOLITES.&#8221; Biomolecular Forms and Functions: A Celebration of 50 Years of the Ramachandran Map:428-442.<\/li>\n\n\n\n<li>Vats, A., A.K. Singh, R. Mukherjee, T. Chopra, M.S. Ravindran, <strong>D. Mohanty<\/strong>, D. Chatterji, J.M. Reyrat, and R.S. Gokhale. 2012. &#8220;Retrobiosynthetic approach delineates the biosynthetic pathway and the structure of the acyl chain of mycobacterial glycopeptidolipids.&#8221; J Biol Chem 287 (36):30677-30687. doi: 10.1074\/jbc.M112.384966.<\/li>\n\n\n\n<li>Anand, S., and <strong>D. Mohanty<\/strong>. 2012. &#8220;Modeling holo-ACP:DH and holo-ACP:KR complexes of modular polyketide synthases: a docking and molecular dynamics study.&#8221; BMC Struct Biol 12:10. doi: 10.1186\/1472-6807-12-10.<\/li>\n\n\n\n<li>Ahmed, A., K. Gaadhe, G.P. Sharma, N. Kumar, M. Neculai, R. Hui, <strong>D. Mohanty<\/strong>, and P. Sharma. 2012. &#8220;Novel insights into the regulation of malarial calcium-dependent protein kinase 1.&#8221; FASEB J 26 (8):3212-3221. doi: 10.1096\/fj.12-203877.<\/li>\n\n\n\n<li>De, S., J. Kumari, R. Mudgal, P. Modi, S. Gupta, K. Futami, H. Goto, N.M. Lindor, Y. Furuichi, <strong>D. Mohanty<\/strong>, and S. Sengupta. 2012. &#8220;RECQL4 is essential for the transport of p53 to mitochondria in normal human cells in the absence of exogenous stress.&#8221; J Cell Sci 125 (Pt 10):2509-2522. doi: 10.1242\/jcs.101501.<\/li>\n\n\n\n<li>Anand, S., and <strong>D. Mohanty<\/strong>. 2012. &#8220;Inter-domain movements in polyketide synthases: a molecular dynamics study.&#8221; Mol Biosyst 8 (4):1157-1171. doi: 10.1039\/c2mb05425f.<\/li>\n\n\n\n<li>Kaushik, S., <strong>D. Mohanty<\/strong>, and A. Surolia. 2012. &#8220;Molecular dynamics simulations on pars intercerebralis major peptide-C (PMP-C) reveal the role of glycosylation and disulfide bonds in its enhanced structural stability and function.&#8221; J Biomol Struct Dyn 29 (5):905-920. doi: 10.1080\/073911012010525026.<\/li>\n\n\n\n<li>Nair, D.R., S. Anand, P. Verma, <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2012. &#8220;Genetic, biosynthetic and functional versatility of polyketide synthases.&#8221; Current Science:277-287.<\/li>\n\n\n\n<li>Nair, D.R., R. Ghosh, A. Manocha, <strong>D. Mohanty<\/strong>, S. Saran, and R.S. Gokhale. 2011. &#8220;Two functionally distinctive phosphopantetheinyl transferases from amoeba Dictyostelium discoideum.&#8221; PLoS One 6 (9):e24262. doi: 10.1371\/journal.pone.0024262.<\/li>\n\n\n\n<li><strong>Mohanty, D<\/strong>., R. Sankaranarayanan, and R.S. Gokhale. 2011. &#8220;Fatty acyl-AMP ligases and polyketide synthases are unique enzymes of lipid biosynthetic machinery in Mycobacterium tuberculosis.&#8221; Tuberculosis (Edinb) 91 (5):448-455. doi: 10.1016\/j.tube.2011.04.006.<\/li>\n\n\n\n<li>Kaushik, S., <strong>D. Mohanty<\/strong>, and A. Surolia. 2011. &#8220;Role of glycosylation in structure and stability of Erythrina corallodendron lectin (EcorL): a molecular dynamics study.&#8221; Protein Sci 20 (3):465-481. doi: 10.1002\/pro.578.<\/li>\n\n\n\n<li>Anand, S., and <strong>D. Mohanty<\/strong>. 2011. &#8220;Computational methods for identification of novel secondary metabolite biosynthetic pathways by genome analysis.&#8221; In Handbook of research on computational and systems biology: Interdisciplinary applications, 380-405. IGI Global.<\/li>\n\n\n\n<li>Kumar, N., and <strong>D. Mohanty<\/strong>. 2010. &#8220;Structure-based identification of MHC binding peptides: Benchmarking of prediction accuracy.&#8221; Mol Biosyst 6 (12):2508-2520. doi: 10.1039\/c0mb00013b.<\/li>\n\n\n\n<li>Kaur, S., P. Modi, V. Srivastava, R. Mudgal, S. Tikoo, P. Arora, <strong>D. Mohanty<\/strong>, and S. Sengupta. 2010. &#8220;Chk1-dependent constitutive phosphorylation of BLM helicase at serine 646 decreases after DNA damage.&#8221; Mol Cancer Res 8 (9):1234-1247. doi: 10.1158\/1541-7786.MCR-10-0233.<\/li>\n\n\n\n<li>Anand, S., M.V. Prasad, G. Yadav, N. Kumar, J. Shehara, M.Z. Ansari, and <strong>D. Mohanty<\/strong>. 2010. &#8220;SBSPKS: structure based sequence analysis of polyketide synthases.&#8221; Nucleic Acids Res 38 (Web Server issue):W487-496. doi: 10.1093\/nar\/gkq340.<\/li>\n\n\n\n<li>Khurana, P., R.S. Gokhale, and <strong>D. Mohanty<\/strong>. 2010. &#8220;Genome scale prediction of substrate specificity for acyl adenylate superfamily of enzymes based on active site residue profiles.&#8221; BMC Bioinformatics 11:57. doi: 10.1186\/1471-2105-11-57.<\/li>\n\n\n\n<li>Kumar, N., and <strong>D. Mohanty<\/strong>. 2010. &#8220;Identification of substrates for Ser\/Thr kinases using residue-based statistical pair potentials.&#8221; Bioinformatics 26 (2):189-197. doi: 10.1093\/bioinformatics\/btp633.<\/li>\n\n\n\n<li>Sharma, D., <strong>D. Mohanty<\/strong>, and A. Surolia. 2009. &#8220;RegAnalyst: a web interface for the analysis of regulatory motifs, networks and pathways.&#8221; Nucleic Acids Res 37 (Web Server issue):W193-201. doi: 10.1093\/nar\/gkp388.<\/li>\n\n\n\n<li>Yadav, G., R.S. Gokhale, and <strong>D. Mohanty<\/strong>. 2009. &#8220;Towards prediction of metabolic products of polyketide synthases: an in silico analysis.&#8221; PLoS Comput Biol 5 (4):e1000351. doi: 10.1371\/journal.pcbi.1000351.<\/li>\n\n\n\n<li>Arora, P., A. Goyal, V.T. Natarajan, E. Rajakumara, P. Verma, R. Gupta, M. Yousuf, O.A. Trivedi, <strong>D. Mohanty<\/strong>, A. Tyagi, R. Sankaranarayanan, and R.S. Gokhale. 2009. &#8220;Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis.&#8221; Nat Chem Biol 5 (3):166-173. doi: 10.1038\/nchembio.143.<\/li>\n\n\n\n<li>Kaushik, S., <strong>D. Mohanty<\/strong>, and A. Surolia. 2009. &#8220;The role of metal ions in substrate recognition and stability of concanavalin A: a molecular dynamics study.&#8221; Biophys J 96 (1):21-34. doi: 10.1529\/biophysj.108.134601.<\/li>\n\n\n\n<li>Ansari, M.Z., J. Sharma, R.S. Gokhale, and <strong>D. Mohanty<\/strong>. 2008. &#8220;In silico analysis of methyltransferase domains involved in biosynthesis of secondary metabolites.&#8221; BMC Bioinformatics 9:454. doi: 10.1186\/1471-2105-9-454.<\/li>\n\n\n\n<li>Chopra, T., S. Banerjee, S. Gupta, G. Yadav, S. Anand, A. Surolia, R.P. Roy, <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2008. &#8220;Novel intermolecular iterative mechanism for biosynthesis of mycoketide catalyzed by a bimodular polyketide synthase.&#8221; PLoS Biol 6 (7):e163. doi: 10.1371\/journal.pbio.0060163.<\/li>\n\n\n\n<li>Ghosh, R., A. Chhabra, P.A. Phatale, S.K. Samrat, J. Sharma, A. Gosain, <strong>D. Mohanty<\/strong>, S. Saran, and R.S. Gokhale. 2008. &#8220;Dissecting the functional role of polyketide synthases in Dictyostelium discoideum: biosynthesis of the differentiation regulating factor 4-methyl-5-pentylbenzene-1,3-diol.&#8221; J Biol Chem 283 (17):11348-11354. doi: 10.1074\/jbc.M709588200.<\/li>\n\n\n\n<li>Natarajan, V.T., <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2008. &#8220;Biosynthesis of mycobacterial lipids by multifunctional polyketide synthases.&#8221; The mycobacterial cell envelope:235-248.<\/li>\n\n\n\n<li>Gokhale, R.S., R. Sankaranarayanan, and <strong>D. Mohanty<\/strong>. 2007. &#8220;Versatility of polyketide synthases in generating metabolic diversity.&#8221; Curr Opin Struct Biol 17 (6):736-743. doi: 10.1016\/j.sbi.2007.08.021.<\/li>\n\n\n\n<li>Kumar, N., and <strong>D. Mohanty<\/strong>. 2007. &#8220;MODPROPEP: a program for knowledge-based modeling of protein-peptide complexes.&#8221; Nucleic Acids Res 35 (Web Server issue):W549-555. doi: 10.1093\/nar\/gkm266.<\/li>\n\n\n\n<li>Goyal, K., <strong>D. Mohanty<\/strong>, and S.C. Mande. 2007. &#8220;PAR-3D: a server to predict protein active site residues.&#8221; Nucleic Acids Res 35 (Web Server issue):W503-505. doi: 10.1093\/nar\/gkm252.<\/li>\n\n\n\n<li>Gokhale, R.S., P. Saxena, T. Chopra, and D. Mohanty. 2007. &#8220;Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids.&#8221; Nat Prod Rep 24 (2):267-277. doi: 10.1039\/b616817p.<\/li>\n\n\n\n<li>Krithika, R., U. Marathe, P. Saxena, M.Z. Ansari, <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2006. &#8220;A genetic locus required for iron acquisition in Mycobacterium tuberculosis.&#8221; Proc Natl Acad Sci U S A 103 (7):2069-2074. doi: 10.1073\/pnas.0507924103.<\/li>\n\n\n\n<li>Arora, P., A. Vats, P. Saxena, <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2005. &#8220;Promiscuous fatty acyl CoA ligases produce acyl-CoA and acyl-SNAC precursors for polyketide biosynthesis.&#8221; J Am Chem Soc 127 (26):9388-9389. doi: 10.1021\/ja052991s.<\/li>\n\n\n\n<li>Kamra, P., R.S. Gokhale, and <strong>D. Mohanty<\/strong>. 2005. &#8220;SEARCHGTr: a program for analysis of glycosyltransferases involved in glycosylation of secondary metabolites.&#8221; Nucleic Acids Res 33 (Web Server issue):W220-225. doi: 10.1093\/nar\/gki449.<\/li>\n\n\n\n<li>Trivedi, O.A., P. Arora, A. Vats, M.Z. Ansari, R. Tickoo, V. Sridharan, <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2005. &#8220;Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid.&#8221; Mol Cell 17 (5):631-643. doi: 10.1016\/j.molcel.2005.02.009.<\/li>\n\n\n\n<li>Ansari, M.Z., G. Yadav, R.S. Gokhale, and <strong>D. Mohanty<\/strong>. 2004. &#8220;NRPS-PKS: a knowledge-based resource for analysis of NRPS\/PKS megasynthases.&#8221; Nucleic Acids Res 32 (Web Server issue):W405-413. doi: 10.1093\/nar\/gkh359.<\/li>\n\n\n\n<li>Trivedi, O.A., P. Arora, V. Sridharan, R. Tickoo, <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2004. &#8220;Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria.&#8221; Nature 428 (6981):441-445. doi: 10.1038\/nature02384.<\/li>\n\n\n\n<li>Trivedi, O.A., P. Arora, V. Sridharan, R. Tickoo, <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2004. &#8220;Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria.&#8221; Nature 428 (6981):441-445. doi: 10.1038\/nature02384.<\/li>\n\n\n\n<li>Saxena, P., G. Yadav, <strong>D. Mohanty<\/strong>, and R.S. Gokhale. 2003. &#8220;A new family of type III polyketide synthases in Mycobacterium tuberculosis.&#8221; J Biol Chem 278 (45):44780-44790. doi: 10.1074\/jbc.M306714200.<\/li>\n\n\n\n<li>Yadav, G., R.S. Gokhale, and <strong>D. Mohanty<\/strong>. 2003. &#8220;SEARCHPKS: A program for detection and analysis of polyketide synthase domains.&#8221; Nucleic Acids Res 31 (13):3654-3658. doi: 10.1093\/nar\/gkg607.<\/li>\n\n\n\n<li>Yadav, G., R.S. Gokhale, and <strong>D. Mohanty<\/strong>. 2003. &#8220;Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases.&#8221; J Mol Biol 328 (2):335-363. doi: 10.1016\/s0022-2836(03)00232-8.<\/li>\n\n\n\n<li><strong>Mohanty, D.<\/strong>, R. Elber, and D. Thirumalai. 2000. &#8220;Probing the role of local propensity in peptide turn formation.&#8221; International Journal of Quantum Chemistry 80 (4\u20105):1125-1128.<\/li>\n\n\n\n<li><strong>Mohanty, D.<\/strong>, A. Kolinski, and J. Skolnick. 1999. &#8220;De novo simulations of the folding thermodynamics of the GCN4 leucine zipper.&#8221; Biophys J 77 (1):54-69. doi: 10.1016\/S0006-3495(99)76872-4.<\/li>\n\n\n\n<li><strong>Mohanty, D.<\/strong>, B.N. Dominy, A. Kolinski, C.L. Brooks III, and J. Skolnick. 1999. &#8220;Correlation between knowledge\u2010based and detailed atomic potentials: application to the unfolding of the GCN4 leucine zipper.&#8221; Proteins: Structure, Function, and Bioinformatics 35 (4):447-452.<\/li>\n\n\n\n<li>Skolnick, J., A. Kolinski, and <strong>D. Mohanty<\/strong>. 1999. &#8220;De novo predictions of the quaternary structure of leucine zippers and other coiled coils.&#8221; International Journal of Quantum Chemistry 75 (3):165-176.<\/li>\n\n\n\n<li>Elber, R., <strong>D. Mohanty<\/strong>, and C. Simmerling. 1998. &#8220;Dynamics of peptide folding.&#8221; In Classical And Quantum Dynamics In Condensed Phase Simulations, 423-444. World Scientific.<\/li>\n\n\n\n<li><strong>Mohanty, D<\/strong>., R. Elber, D. Thirumalai, D. Beglov, and B. Roux. 1997. &#8220;Kinetics of peptide folding: computer simulations of SYPFDV and peptide variants in water.&#8221; J Mol Biol 272 (3):423-442. doi: 10.1006\/jmbi.1997.1246.<\/li>\n\n\n\n<li><strong>Mohanty, D.<\/strong>, and M. Bansal. 1995. &#8220;Chain folding and A:T pairing in human telomeric DNA: a model-building and molecular dynamics study.&#8221; Biophys J 69 (3):1046-1067. doi: 10.1016\/S0006-3495(95)79979-9.<\/li>\n\n\n\n<li><strong>Mohanty, D.<\/strong>, and M. Bansal. 1994. &#8220;Conformational polymorphism in telomeric structures: loop orientation and interloop pairing in d(G4TnG4).&#8221; Biopolymers 34 (9):1187-1211. doi: 10.1002\/bip.360340908.<\/li>\n\n\n\n<li><strong>Mohanty, D.<\/strong>, and M. Bansal. 1993. &#8220;Conformational polymorphism in G-tetraplex structures: strand reversal by base flipover or sugar flipover.&#8221; Nucleic Acids Res 21 (8):1767-1774. doi: 10.1093\/nar\/21.8.1767.<\/li>\n\n\n\n<li>Balagurumoorthy, P., S.K. Brahmachari, <strong>D. Mohanty<\/strong>, M. Bansal, and V. Sasisekharan. 1992. &#8220;Hairpin and parallel quartet structures for telomeric sequences.&#8221; Nucleic Acids Res 20 (15):4061-4067. doi: 10.1093\/nar\/20.15.4061.<\/li>\n\n\n\n<li><strong>Mohanty, D.<\/strong>, and M. Bansal. 1991. &#8220;DNA polymorphism and local variation in base-pair orientation: a theoretical rationale.&#8221; J Biomol Struct Dyn 9 (1):127-142. doi: 10.1080\/07391102.1991.10507898.<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":3,"comment_status":"closed","ping_status":"closed","template":"","meta":{"neve_meta_sidebar":"","neve_meta_container":"","neve_meta_enable_content_width":"","neve_meta_content_width":0,"neve_meta_title_alignment":"","neve_meta_author_avatar":"","neve_post_elements_order":"","neve_meta_disable_header":"","neve_meta_disable_footer":"","neve_meta_disable_title":"","footnotes":""},"class_list":["post-27","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"http:\/\/202.54.249.134\/BIC-NII\/wp-json\/wp\/v2\/pages\/27","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/202.54.249.134\/BIC-NII\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/202.54.249.134\/BIC-NII\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/202.54.249.134\/BIC-NII\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/202.54.249.134\/BIC-NII\/wp-json\/wp\/v2\/comments?post=27"}],"version-history":[{"count":10,"href":"http:\/\/202.54.249.134\/BIC-NII\/wp-json\/wp\/v2\/pages\/27\/revisions"}],"predecessor-version":[{"id":752,"href":"http:\/\/202.54.249.134\/BIC-NII\/wp-json\/wp\/v2\/pages\/27\/revisions\/752"}],"wp:attachment":[{"href":"http:\/\/202.54.249.134\/BIC-NII\/wp-json\/wp\/v2\/media?parent=27"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}