Banerjee Lab

University at Buffalo, State University of New York


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Sequence-encoded and Composition-dependent Protein-RNA Interactions Control Multiphasic Condensate Topologies. Kaur, T., Raju, M., Alshareedah, I., Davis, R. B., Potoyan, D. A., Banerjee, P. R. bioRxiv. 2020.08.30.273748. Link to the preprint.

Methods for Characterizing the Material Properties of Biomolecular Condensates. Alshareedah, I., Kaur, T., Banerjee, P. R. 2020. Methods in Enzymology. In Press.

Subversion of Host Stress Granules by Coronaviruses: Potential Roles of π-rich Disordered Domains of Viral Nucleocapsids. Moosa, M. M., Banerjee, P. R. 2020. J Med Virol. 10.1002/jmv.26195. DOI: 10.1002/jmv.26195. Link to the paper.

Phase Transition of RNA-protein Complexes into Ordered Hollow Condensates. Alshareedah, I., Moosa, M. M., Raju, M., Potoyan, D. A., Banerjee, P. R. 2020. Proceedings of the National Academy of Sciences. DOI: 10.1073/pnas.1922365117. Link to the paper.


Interplay Between Short-range Attraction and Long-range Repulsion Controls Reentrant Liquid Condensation of Ribonucleoprotein-RNA Complexes. Alshareedah, I., Kaur, T., Ngo, J., Seppala, H., Djomnang Kounatse, L.-A., Wang, W., Moosa, M. M., Banerjee, P. R. 2019. J. Am. Chem. Soc. 141, 37, 14593-14602. Link:

Molecular Crowding Tunes Material States of Ribonucleoprotein Condensates. Kaur, T., Alshareedah, I., Wang, W., Ngo, J., Moosa, M. M., Banerjee, P. R. 2019. Biomolecules, 9(2), 71; Link:

Phase Separation of Ligand-Activated Enhancers Licenses Cooperative Chromosomal Enhancer Assembly. Nair, S. J., Yang, L., Meluzzi, D., Oh, S., Yang, F., Friedman, M., Wang, S., Suter, T., Alshareedah, I., Gamliel, A., Ma, Q., Zhang, J., Hu, Y., Tan, Y., Ohgi, K., Jayani, R., Banerjee, P. R., Aggarwal, A. K., Rosenfeld, M. G. 2019. Nature Structural & Molecular Biology. 26, 193–203; Link:

Divalent cations can control a   switch-like   behavior   in   heterotypic    and    homotypic    RNA    coacervates. Onuchic, P. L., Milin, A. N., Alshareedah, A., Deniz, A. A., Banerjee,P.R. 2018. Scientific Reports, Vol 9, Article number: 12161. Link:


Self-interaction of NPM1 modulates multiple mechanisms of liquid- liquid phase separation. Mitrea, D. M., Cika, J. A., Stanley, C. B., Nourse, A., Onuchic, P. L., Banerjee,P.R., Phillips, A. H., Park, C. G., Deniz, A. A., Kriwacki, R. W. 2018. , Nature Communications. 2018 Feb 26;9(1):842. Link to the paper.

2012-2017: Postdoctoral Work

Reentrant phase transition drives dynamic substructure formation in ribonucleoprotein droplets. Banerjee, P. R.*, Milin, A. N., Moosa M. M., Onuchic, P. L., Deniz, A. A.* 2017. Angew Chem Int Ed Engl. 2017 Sep 11;56(38):11354-11359. PMCID: PMC5647147 (*Corresponding Authors). Link to the paper.

  • Highlighted as a Very Important Paper by Angew Chem Int Ed Engl
  • Featured in TSRI News & Views, June 2017
  • Featured in The Scientist Magazine, June 2017

NPM1 integrates into the nucleolar fraction through multi-modal interactions with R- rich linear motifs and ribosomal RNA. Mitrea, D. M., Cika, J. A., Guy, C. S., Ban, D., Banerjee, P. R., Stanley, C. B., Nourse, A., Deniz, A. A., Kriwacki, R. W. 2016. eLife;10.7554/eLife.13571. Link to the paper

Two-dimensional crowding uncovers a hidden conformation of α-synuclein. Banerjee, P. R.*, Moosa M. M., Deniz, A. A.* 2016. Angew Chem Int Ed Engl. 55(41):12789-92. (*Corresponding Authors). Link to the paper.

Asymmetric Modulation of Protein Order-Disorder Transitions by Phosphorylation and Partner Binding. Banerjee, P. R., Mitrea, D. M., Kriwacki, R. W.,Deniz, A. A., 2015. Angew Chem Int Ed Engl. 55(5):1675-9. Link to the paper.

Shedding light on protein folding landscapes by single-molecule fluorescence. Banerjee, P. R., Deniz, A. A. 2014. Chem. Soc. Rev. 43, 1172-1188. Link to the paper.

Ultrafast cooling reveals microsecond-scale biomolecular dynamics. Polinkovsky, M. E.*, Gambin, Y.*, Banerjee, P. R.*, Erickstad, M. J., Groisman, A., Deniz, A. A. 2014. Nat Commun. 2014 Dec 17; 5:5737 (*Equal contributions first authors). Link to the paper.

Doctoral Work

Cataract-associated mutant E107A of human gamma D-crystallin shows increased attraction to alpha-crystallin and enhanced light scattering. Banerjee, P. R., Pande, A., Patrosz, J., Thruston, G. M., Pande, J. 2011. Proc. Natl. Acad. Sci. (U.S.A) 108, 574-579. Link to the paper.

  • Commentary published in PNAS (Link)

Increase in surface hydrophobicity of the cataract-associated P23T mutant of human γD-crystallin is responsible for its dramatically lower, retrograde solubility A Pande, K S Ghosh, P R Banerjee, J Pande. Biochemistry 49 (29), 6122-6129352010. Link to the paper.

NMR study of the cataract-linked P23T mutant of human γD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility. A Pande, J Zhang, P R Banerjee, S S Puttamadappa, A Shekhtman, J Pande. Biochemical and biophysical research communications 382 (1), 196-199242009. Link to the paper.

Molecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin. P R Banerjee, A Pande, A Shekhtman, J Pande. Biochemistry 54 (2), 505-515152014. Link to the paper.

Increased hydrophobicity and decreased backbone flexibility explain the lower solubility of a cataract-linked mutant of γD-crystallin. P R Banerjee, S S Puttamadappa, A Pande, A Shekhtman, J Pande. Journal of molecular biology 412 (4), 647-659152011. Link to the paper.

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