2021
Singh, P., Chaudhuri, A, Banerjea, M., Marathe, N., and Das, B. (2021) Nrd1p identifies aberrant and natural exosomal target messages during the nuclear mRNA surveillance in Saccharomyces cerevisiae. Nucleic Acids Research, 49, 11512-11536, DOI: https://doi.org/10.1093/nar/gkab930.
2020
Chaudhuri, A., Das, S., and Das, B. (2020) The Role RNA cis-Elements in the intracellular trafficking,
transport, and localization  of messenger RNAs in Saccharomyces cerevisiae  WIREs RNA e1591, 1-37,  DOI: https://doi.org/10.1002/wrna.1591
2019
Das, S., Biswas, S., Chaudhuri, S., Bhattacharya, A. and Das, B. (2019) A nuclear zip code in SKS1 mRNA promotes its slow export, nuclear retention and degradation by the Nuclear exosome/DRN in Saccharomyces cerevisiae. J. Mol. Biol., 431, 3626-3646, DOI: 10.1016/j.jmb.2019.07.005.I:   
2018
Maity, J., Das, B., Bohr, V., and Karmakar, P. (2018) Acidic domain of WRNp is critical for autophagy and
up-regulates age associated proteins. DNA Repair, 68, 1-11, DOI: https://doi.org/10.1016/ j.dnarep.2018.05.003.

Singh, P., Saha, U., Paira, S. and Das, B. (2018) Nuclear mRNA Surveillance mechanisms: Function and links to human diseases. J. Mol. Biol, 430, 1993-2013, doi:10.1016/j.jmb.2018.05.009
Sarkar, D. Paira, S. and Das, B. (2018) Nuclear mRNA degradation tunes the gain of the unfolded protein response in Saccharomyces cerevisiae. Nucleic Acids Res., 46, 1139-1156, doi: 10.1093/nar/gkx1160
2016-17
2014-15
Kabir, M. A. and Das, B. (2014) Fred Sherman (1932-2013). Current Science, 107, 704.
2009-2014
2000-2009
Das, B., Guo, Z., Russo, P., Chartrand, P., and Sherman, F (2000). The Role of Nuclear Cap Binding   Protein Cbc1p of Yeast in mRNA Termination and Degradation. Mol. Cell Biol., 20,. 2827-2838.
Polevoda, B., Martzen, M., Das, B., Phizicky, E.M., and Sherman, F. (2000) Cytochrome c methyl- transferase, Ctm1p of yeast. J. Biol. Chem., 275, 20508-20513.
1990-200
Pearce, D.A., Carr, C. J., Das, B. and Sherman, F. (1999). Phenotypic reversal of btn1 defects in yeast by chloroquine : A yeast model for batten disease. Proc. Natl. Acad. Sci. USA , 96, 11341-11345 .
Chakrabarti, A., Bera, A.K., Das, B., Chattopadhyay, C., Sarkar, D. and DasGupta, C. (1999)Binding and conformation of denatured horseradish peroxidase during E. coli ribosome mediated folding.Curr. Sci., 76, 1235-1238.
Pearce, D.A., Ferea, T., Nosel, S. A., Das, B. and Sherman, F (1999) DNA microarray analysis of strains lacking BTN1, the yeast. ortholog of the human Batten disease gene. Nature Genet., 23, 73-73.
Pearce, D.A., Ferea, T., Nosel, S. A., Das, B. and Sherman, F (1999) Action of BTN1, the yeast orthologue of  the gene mutated in Batten disease. Nature Genet., 22, 55-58.
Chattopadhyay, S., Das, B., and DasGupta, C. (1996) Reactivation of denatured proteins by 23S ribosomal RNA: Role of domain V. Proc. Natl. Acad. Sci. USA, 93, 8284-8287.
Das, B., Chattopadhyay, S., Bera, A.K. and DasGupta, C. (1996). In vitro protein folding by ribosomes from  Escherichia coli, wheat germ and rat liver: The role of 50S subunit and its 23S rRNA. Eur. J. Biochem., 235,613-62 1.
Bera A. K., Das, B., Chattopadhyay, S. and DasGupta, C. (1994). Refolding of denatured restriction  endonucleases with ribosomal preparations from Methanosarcina barkeri. Biochem. Mol. Biol. International., 32, 315-323.
Chattopadhyay, S., Das, B., Bera, A. K. and DasGupta, C. (1994) Refolding of denatured lactate dehydrogenase by E. coli ribosome. Biochem. J. (London), 300, 717-721.
Bera, A. K., Das, B., Chattopadhyay, S. and DasGupta, C. (1994) Protein folding by ribosome and its RNA. Curr. Sci., 66, 230-232.
Das, B. and DasGupta, C. (1992) Reconstitution of denatured alkaline phosphatase with E. coli ribosome.   Ind. J. Biochem. Biophys., 29, 512-515.
Das, B., Chattopadhyay, S. and DasGupta, C. (1992) Reactivation of denatured fungal glucose 6-phosphate   dehydrogenase and E. coli alkaline phosphatase with E. coli ribosome. Biochem. Biophys. Res. Commun., 183, 774-780.
Maity, S., Das, B. and Mandal, N.C. (1991) Isolation and preliminary characterization of mutants of Escherichia coli resistant to lethal action of bacteriophage lambda P gene. Virology, 182, 351-352 .
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