Year |
Citation |
Score |
2024 |
Davis RB, Supakar A, Ranganath AK, Moosa MM, Banerjee PR. Heterotypic interactions can drive selective co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex. Nature Communications. 15: 1168. PMID 38326345 DOI: 10.1038/s41467-024-44945-5 |
0.338 |
|
2023 |
Davis RB, Ranganath AK, Moosa MM, Banerjee PR. Heterotypic interactions in the dilute phase can drive co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex. Biorxiv : the Preprint Server For Biology. PMID 37090622 DOI: 10.1101/2023.04.12.536623 |
0.342 |
|
2022 |
Davis RB, Moosa MM, Banerjee PR. Ectopic biomolecular phase transitions: fusion proteins in cancer pathologies. Trends in Cell Biology. PMID 35484036 DOI: 10.1016/j.tcb.2022.03.005 |
0.34 |
|
2020 |
Alshareedah I, Moosa MM, Raju M, Potoyan DA, Banerjee PR. Phase transition of RNA-protein complexes into ordered hollow condensates. Proceedings of the National Academy of Sciences of the United States of America. PMID 32571937 DOI: 10.1073/pnas.1922365117 |
0.327 |
|
2019 |
Onuchic PL, Milin AN, Alshareedah I, Deniz AA, Banerjee PR. Divalent cations can control a switch-like behavior in heterotypic and homotypic RNA coacervates. Scientific Reports. 9: 12161. PMID 31434954 DOI: 10.1038/s41598-019-48457-x |
0.566 |
|
2019 |
Kaur T, Alshareedah I, Wang W, Ngo J, Moosa MM, Banerjee PR. Molecular Crowding Tunes Material States of Ribonucleoprotein Condensates. Biomolecules. 9. PMID 30791483 DOI: 10.3390/biom9020071 |
0.302 |
|
2019 |
Kriwacki R, Mitrea D, Ferrolino M, Gibbs E, Phillips AH, Tolbert M, Stanley CB, Nourse A, Onuchic PL, Banerjee PR, Deniz AA. The Ins and Outs of Phase Separation in Nucleolar Biology Biophysical Journal. 116: 454a. DOI: 10.1016/J.Bpj.2018.11.2448 |
0.557 |
|
2018 |
Mitrea DM, Cika JA, Stanley CB, Nourse A, Onuchic PL, Banerjee PR, Phillips AH, Park CG, Deniz AA, Kriwacki RW. Self-interaction of NPM1 modulates multiple mechanisms of liquid-liquid phase separation. Nature Communications. 9: 842. PMID 29483575 DOI: 10.1038/S41467-018-03255-3 |
0.637 |
|
2017 |
Banerjee PR, Milin AN, Moosa MM, Onuchic PL, Deniz A. Reentrant phase transition drives dynamic substructure formation in ribonucleoprotein droplets. Angewandte Chemie (International Ed. in English). PMID 28556382 DOI: 10.1002/anie.201703191 |
0.6 |
|
2017 |
Banerjee PR, Moosa M, Deniz A. Single-Molecule Spectroscopy Reveals the Role of Two-Dimensional Crowding in Disordered Protein Folding Biophysical Journal. 112: 480a. DOI: 10.1016/J.Bpj.2016.11.2598 |
0.602 |
|
2017 |
Banerjee PR, Milin AN, Moosa MM, Onuchic PL, Deniz AA. Frontispiece: Reentrant Phase Transition Drives Dynamic Substructure Formation in Ribonucleoprotein Droplets Angewandte Chemie International Edition. 56. DOI: 10.1002/ANIE.201783861 |
0.571 |
|
2016 |
Banerjee PR, Moosa MM, Deniz AA. Two-Dimensional Crowding Uncovers a Hidden Conformation of α-Synuclein. Angewandte Chemie (International Ed. in English). PMID 27612332 DOI: 10.1002/anie.201606963 |
0.599 |
|
2016 |
Mitrea DM, Cika JA, Guy CS, Ban D, Banerjee PR, Stanley CB, Nourse A, Deniz AA, Kriwacki RW. Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA. Elife. 5. PMID 26836305 DOI: 10.7554/Elife.13571 |
0.629 |
|
2016 |
Banerjee PR, Mitrea DM, Kriwacki RW, Deniz A. Conformational Polymorphism in Conditionally Disordered Nucleophosmin: From Single-Molecules to Liquid Droplets Biophysical Journal. 110: 402a. DOI: 10.1016/J.Bpj.2015.11.2171 |
0.648 |
|
2015 |
Banerjee PR, Mitrea DM, Kriwacki RW, Deniz AA. Asymmetric Modulation of Protein Order-Disorder Transitions by Phosphorylation and Partner Binding. Angewandte Chemie (International Ed. in English). PMID 26679013 DOI: 10.1002/Anie.201507728 |
0.624 |
|
2015 |
Banerjee PR, Pande A, Shekhtman A, Pande J. Molecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin. Biochemistry. 54: 505-15. PMID 25478825 DOI: 10.1021/Bi5014479 |
0.542 |
|
2015 |
Banerjee PR, Deniz A. Keeping it Disordered: A New Mechanism of Protein Quality Control? Biophysical Journal. 108: 496a. DOI: 10.1016/J.Bpj.2014.11.2713 |
0.639 |
|
2014 |
Polinkovsky ME, Gambin Y, Banerjee PR, Erickstad MJ, Groisman A, Deniz AA. Ultrafast cooling reveals microsecond-scale biomolecular dynamics. Nature Communications. 5: 5737. PMID 25517430 DOI: 10.1038/Ncomms6737 |
0.526 |
|
2014 |
Banerjee PR, Deniz AA. Shedding light on protein folding landscapes by single-molecule fluorescence. Chemical Society Reviews. 43: 1172-88. PMID 24336839 DOI: 10.1039/c3cs60311c |
0.615 |
|
2013 |
Banerjee PR, Mitrea DM, Kriwacki RW, Deniz AA. Single-Molecule and Ensemble Fluorescence Study of Cryptic Disorder and Oligomerization in Nucleophosmin Biophysical Journal. 104: 190a. DOI: 10.1016/J.Bpj.2012.11.1071 |
0.612 |
|
2011 |
Banerjee PR, Puttamadappa SS, Pande A, Shekhtman A, Pande J. Increased hydrophobicity and decreased backbone flexibility explain the lower solubility of a cataract-linked mutant of γD-crystallin. Journal of Molecular Biology. 412: 647-59. PMID 21827768 DOI: 10.1016/J.Jmb.2011.07.058 |
0.566 |
|
2011 |
Banerjee PR, Pande A, Patrosz J, Thurston GM, Pande J. Cataract-associated mutant E107A of human gammaD-crystallin shows increased attraction to alpha-crystallin and enhanced light scattering. Proceedings of the National Academy of Sciences of the United States of America. 108: 574-9. PMID 21173272 DOI: 10.1073/Pnas.1014653107 |
0.546 |
|
2011 |
Banerjee PR, Puttamadappa S, Pande A, Shekhtman A, Pande J. Structure, Dynamics and Surface Hydrophobicity of the Cataract-Associated Mutant, Pro23Thr of Human Gamma D-crystallin: Molecular Basis of Cataract Formation Biophysical Journal. 100: 539a. DOI: 10.1016/J.Bpj.2010.12.3144 |
0.541 |
|
2010 |
Pande A, Ghosh KS, Banerjee PR, Pande J. Increase in surface hydrophobicity of the cataract-associated P23T mutant of human gammaD-crystallin is responsible for its dramatically lower, retrograde solubility. Biochemistry. 49: 6122-9. PMID 20553008 DOI: 10.1021/Bi100664S |
0.569 |
|
2010 |
Banerjee PR, Pande A, Thurston G, Pande J. Thermodynamic Studies on the Cataract-Associated Mutant, E107a, of Human Gamma-D Crystallin: Molecular Basis for Cataract Formation Biophysical Journal. 98: 44a. DOI: 10.1016/J.Bpj.2009.12.254 |
0.527 |
|
2009 |
Pande A, Zhang J, Banerjee PR, Puttamadappa SS, Shekhtman A, Pande J. NMR study of the cataract-linked P23T mutant of human gammaD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility. Biochemical and Biophysical Research Communications. 382: 196-9. PMID 19275895 DOI: 10.1016/J.Bbrc.2009.03.007 |
0.535 |
|
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