Year |
Citation |
Score |
2020 |
Majumdar A, Das D, Madhu P, Avni A, Mukhopadhyay S. Excitation Energy Migration Unveils Fuzzy Interfaces within the Amyloid Architecture. Biophysical Journal. PMID 32402242 DOI: 10.1016/J.Bpj.2020.04.015 |
0.461 |
|
2020 |
Bhasne K, Jain N, Karnawat R, Arya S, Majumdar A, Singh A, Mukhopadhyay S. Discerning Dynamic Signatures of Membrane-Bound α-Synuclein Using Site-Specific Fluorescence Depolarization Kinetics. The Journal of Physical Chemistry. B. PMID 31917569 DOI: 10.1021/Acs.Jpcb.9B09118 |
0.776 |
|
2020 |
Mukhopadhyay S, Majumdar A, Dogra P, Maity S, Joshi A. The Dynamism of Intrinsically Disordered Proteins in Liquid-Liquid Phase Separation Biophysical Journal. 118: 60a. DOI: 10.1016/J.Bpj.2019.11.503 |
0.322 |
|
2020 |
Bhattacharya M, Giri A, Kaur J, Dogra P, Mukhopadhyay S. Unraveling the Mechanism of Functional and Pathological Amyloid Formation from Intrinsically Disordered Proteins Biophysical Journal. 118: 59a. DOI: 10.1016/J.Bpj.2019.11.499 |
0.459 |
|
2019 |
Madhu P, Mukhopadhyay S. Preferential Recruitment of Conformationally Distinct Amyloid-β Oligomers by the Intrinsically Disordered Region of the Human Prion Protein. Acs Chemical Neuroscience. PMID 31808343 DOI: 10.1021/Acschemneuro.9B00646 |
0.451 |
|
2019 |
Dogra P, Joshi A, Majumdar A, Mukhopadhyay S. Intermolecular charge-transfer modulates liquid-liquid phase separation and liquid-to-solid maturation of an intrinsically disordered pH-responsive domain. Journal of the American Chemical Society. PMID 31783713 DOI: 10.1021/Jacs.9B10892 |
0.354 |
|
2019 |
Agarwal A, Das D, Banerjee T, Mukhopadhyay S. Energy migration captures membrane-induced oligomerization of the prion protein. Biochimica Et Biophysica Acta. Proteins and Proteomics. 140324. PMID 31740413 DOI: 10.1016/J.Bbapap.2019.140324 |
0.452 |
|
2019 |
Avni A, Swasthi HM, Majumdar A, Mukhopadhyay S. Intrinsically disordered proteins in the formation of functional amyloids from bacteria to humans. Progress in Molecular Biology and Translational Science. 166: 109-143. PMID 31521230 DOI: 10.1016/Bs.Pmbts.2019.05.005 |
0.807 |
|
2019 |
Majumdar A, Dogra P, Maity S, Mukhopadhyay S. Liquid-Liquid Phase Separation Is Driven by Large-Scale Conformational Unwinding and Fluctuations of Intrinsically Disordered Protein Molecules. The Journal of Physical Chemistry Letters. 3929-3936. PMID 31260322 DOI: 10.1021/Acs.Jpclett.9B01731 |
0.424 |
|
2019 |
Mukhopadhyay S. Editorial on intrinsically disordered proteins: Amyloid formation and phase separation. Biochimica Et Biophysica Acta. Proteins and Proteomics. PMID 31247343 DOI: 10.1016/J.Bbapap.2019.06.011 |
0.428 |
|
2019 |
Pani I, Swasthi HM, Mukhopadhyay S, Pal SK. Correction to “Design of Aqueous-Liquid Crystal Interfaces To Monitor Protein Aggregation at Nanomolar Concentrations” The Journal of Physical Chemistry C. 123: 19254-19254. DOI: 10.1021/Acs.Jpcc.9B06613 |
0.775 |
|
2019 |
Majumdar A, Das D, Dogra P, Maity S, Mukhopadhyay S. Proximity Rulers in Amyloids and Liquid Droplets of Intrinsically Disordered Proteins Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.190 |
0.419 |
|
2018 |
Majumdar A, Mukhopadhyay S. Fluorescence Depolarization Kinetics to Study the Conformational Preference, Structural Plasticity, Binding, and Assembly of Intrinsically Disordered Proteins. Methods in Enzymology. 611: 347-381. PMID 30471693 DOI: 10.1016/Bs.Mie.2018.09.031 |
0.418 |
|
2018 |
Swasthi HM, Bhasne K, Mahapatra S, Mukhopadhyay S. Human Fibrinogen Inhibits Amyloid Assembly of Biofilm-Forming CsgA. Biochemistry. PMID 30338995 DOI: 10.1021/Acs.Biochem.8B00841 |
0.803 |
|
2018 |
Bhasne K, Mukhopadhyay S. Formation of Heterotypic Amyloids: α-Synuclein in Co-Aggregation. Proteomics. e1800059. PMID 30216674 DOI: 10.1002/pmic.201800059 |
0.428 |
|
2018 |
DAS D, Mukhopadhyay S. Studying backbone torsional dynamics of intrinsically disordered proteins using fluorescence depolarization kinetics. Journal of Biosciences. 43: 455-462. PMID 30002265 DOI: 10.1007/S12038-018-9766-1 |
0.463 |
|
2018 |
Arya S, Singh AK, Bhasne K, Dogra P, Datta A, Das P, Mukhopadhyay S. Femtosecond Hydration Map of Intrinsically Disordered α-Synuclein. Biophysical Journal. 114: 2540-2551. PMID 29874605 DOI: 10.1016/J.Bpj.2018.04.028 |
0.762 |
|
2018 |
Bhasne K, Sebastian S, Jain N, Mukhopadhyay S. Synergistic Amyloid Switch Triggered by Early Heterotypic Oligomerization of Intrinsically Disordered α-Synuclein and Tau. Journal of Molecular Biology. PMID 29704492 DOI: 10.1016/J.Jmb.2018.04.020 |
0.624 |
|
2018 |
Pani I, Swasthi HM, Mukhopadhyay S, Pal SK. Design of Aqueous-Liquid Crystal Interfaces To Monitor Protein Aggregation at Nanomolar Concentrations The Journal of Physical Chemistry C. 123: 1305-1312. DOI: 10.1021/Acs.Jpcc.8B10863 |
0.808 |
|
2018 |
Dogra P, Singha Roy S, Bhattacharya M, Prabhu SS, Mukhopadhyay S. Proton-Induced Switching of an Intrinsically Disordered Domain of a Melanosomal Protein into a Polymorphic Functional Amyloid Biophysical Journal. 114: 590a. DOI: 10.1016/J.Bpj.2017.11.3228 |
0.395 |
|
2018 |
Mukhopadhyay S, Arya S, Bhasne K, Dogra P, Singh AK, Khan T, Datta A, Das P. Prying into Hydration Water in Amyloidogenic Intrinsically Disordered Proteins Biophysical Journal. 114: 586a. DOI: 10.1016/J.Bpj.2017.11.3209 |
0.745 |
|
2017 |
Swasthi HM, Mukhopadhyay S. Electrostatic lipid-protein interactions sequester the curli amyloid fold on the lipopolysaccharide membrane surface. The Journal of Biological Chemistry. PMID 29021250 DOI: 10.1074/Jbc.M117.815522 |
0.804 |
|
2017 |
Narang D, Swasthi HM, Mahapatra S, Mukhopadhyay S. Site-Specific Fluorescence Depolarization Kinetics Distinguishes the Amyloid Folds Responsible for Distinct Yeast Prion Strains. The Journal of Physical Chemistry. B. PMID 28840728 DOI: 10.1021/Acs.Jpcb.7B05550 |
0.799 |
|
2017 |
Bhasne K, Sebastian S, Mukhopadhyay S. A Tale of Two Amyloidogenic Intrinsically Disordered Proteins: Interplay of Tau and α-Synuclein Biophysical Journal. 112: 480a. DOI: 10.1016/J.Bpj.2016.11.2599 |
0.4 |
|
2017 |
Arya S, Dogra P, Jain N, Mukhopadhyay S. Detergent-induced aggregation of an amyloidogenic intrinsically disordered protein Journal of Chemical Sciences. 129: 1817-1827. DOI: 10.1007/S12039-017-1386-Z |
0.82 |
|
2016 |
Dogra P, Bhattacharya M, Mukhopadhyay S. A pH-Responsive Mechanistic Switch Regulates the Formation of Dendritic and Fibrillar Nanostructures of a Functional Amyloid. The Journal of Physical Chemistry. B. PMID 28005369 DOI: 10.1021/Acs.Jpcb.6B11281 |
0.45 |
|
2016 |
Arya S, Singh AK, Khan T, Bhattacharya M, Datta A, Mukhopadhyay S. Water Rearrangements upon Disorder-to-Order Amyloid Transition. The Journal of Physical Chemistry Letters. PMID 27689394 DOI: 10.1021/Acs.Jpclett.6B02088 |
0.785 |
|
2016 |
Jain N, Narang D, Bhasne K, Dalal V, Arya S, Bhattacharya M, Mukhopadhyay S. Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins. Biophysical Journal. 111: 768-74. PMID 27558720 DOI: 10.1016/J.Bpj.2016.07.023 |
0.804 |
|
2016 |
Narang D, Singh A, Swasthi HM, Mukhopadhyay S. Characterization of Salt-Induced Oligomerization of Human β2-Microglobulin at Low pH. The Journal of Physical Chemistry. B. PMID 27467899 DOI: 10.1021/Acs.Jpcb.6B05619 |
0.815 |
|
2016 |
Dalal V, Arya S, Mukhopadhyay S. Confined Water in Amyloid-Competent Oligomers of the Prion Protein. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 27253720 DOI: 10.1002/Cphc.201600440 |
0.77 |
|
2016 |
Narang D, Singh A, Mukhopadhyay S. Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH. European Biophysics Journal : Ebj. PMID 27225299 DOI: 10.1007/S00249-016-1138-X |
0.447 |
|
2016 |
Arya S, Mukhopadhyay S. Water in Amyloidogenic Intrinsically Disordered Proteins: Interplay of Conformational Preference and Amyloid Aggregation Biophysical Journal. 110: 398a. DOI: 10.1016/J.Bpj.2015.11.2150 |
0.783 |
|
2015 |
Dalal V, Arya S, Bhattacharya M, Mukhopadhyay S. Conformational Switching and Nanoscale Assembly of Human Prion Protein into Polymorphic Amyloids via Structurally-Labile Oligomers. Biochemistry. PMID 26645611 DOI: 10.1021/Acs.Biochem.5B01110 |
0.796 |
|
2015 |
Arya S, Kumari A, Dalal V, Bhattacharya M, Mukhopadhyay S. Appearance of annular ring-like intermediates during amyloid fibril formation from human serum albumin. Physical Chemistry Chemical Physics : Pccp. 17: 22862-71. PMID 26264974 DOI: 10.1039/C5Cp03782D |
0.801 |
|
2015 |
Narang D, Srivastava AK, Mukhopadhyay S. The Role of Structural Dynamics in Determining the Prion Strain Diversity Biophysical Journal. 108: 386a. DOI: 10.1016/J.Bpj.2014.11.2116 |
0.401 |
|
2014 |
Arya S, Mukhopadhyay S. Ordered water within the collapsed globules of an amyloidogenic intrinsically disordered protein. The Journal of Physical Chemistry. B. 118: 9191-8. PMID 25035108 DOI: 10.1021/Jp504076A |
0.776 |
|
2014 |
Bhattacharya M, Mukhopadhyay S. Nanophotonics of protein amyloids Nanophotonics. 3: 51-59. DOI: 10.1515/Nanoph-2013-0045 |
0.456 |
|
2014 |
Bhattacharya M, Jain N, Dogra P, Dalal V, Narang D, Sharma PK, Samai S, Mukhopadhyay S. Nanoscale Assembly of Proteins into Amyloid Oligomers, Pores and Fibrils Biophysical Journal. 106. DOI: 10.1016/J.Bpj.2013.11.3781 |
0.652 |
|
2014 |
Mukhopadhyay S, Jain N, Bhasne K, Hemaswasthi M. Site-Specific Hydration Dynamics Illuminates the Key Structural Features of Membrane-Bound α-Synuclein Biophysical Journal. 106: 268a. DOI: 10.1016/J.Bpj.2013.11.1569 |
0.603 |
|
2013 |
Bhattacharya M, Jain N, Dogra P, Samai S, Mukhopadhyay S. Nanoscopic Amyloid Pores Formed via Stepwise Protein Assembly. The Journal of Physical Chemistry Letters. 4: 480-5. PMID 26281744 DOI: 10.1021/Jz3019786 |
0.68 |
|
2013 |
Jain N, Bhasne K, Hemaswasthi M, Mukhopadhyay S. Structural and dynamical insights into the membrane-bound α-synuclein. Plos One. 8: e83752. PMID 24376740 DOI: 10.1371/Journal.Pone.0083752 |
0.616 |
|
2013 |
Narang D, Sharma PK, Mukhopadhyay S. Dynamics and dimension of an amyloidogenic disordered state of human β(2)-microglobulin. European Biophysics Journal : Ebj. 42: 767-76. PMID 23974249 DOI: 10.1007/S00249-013-0923-Z |
0.433 |
|
2012 |
Dalal V, Bhattacharya M, Narang D, Sharma PK, Mukhopadhyay S. Nanoscale Fluorescence Imaging of Single Amyloid Fibrils. The Journal of Physical Chemistry Letters. 3: 1783-7. PMID 26291859 DOI: 10.1021/Jz300687F |
0.464 |
|
2012 |
Krishnan R, Goodman JL, Mukhopadhyay S, Pacheco CD, Lemke EA, Deniz AA, Lindquist S. Conserved features of intermediates in amyloid assembly determine their benign or toxic states. Proceedings of the National Academy of Sciences of the United States of America. 109: 11172-7. PMID 22745165 DOI: 10.1073/Pnas.1209527109 |
0.679 |
|
2012 |
Bhattacharya M, Mukhopadhyay S. Structural and dynamical insights into the molten-globule form of ovalbumin. The Journal of Physical Chemistry. B. 116: 520-31. PMID 22097968 DOI: 10.1021/Jp208416D |
0.399 |
|
2012 |
Mukhopadhyay S, Jain N, Bhattacharya M. Polypeptide Chain Collapse of Amyloidogenic Intrinsically Disordered Proteins Biophysical Journal. 102: 6-9. DOI: 10.1016/J.Bpj.2011.11.3428 |
0.619 |
|
2012 |
Bhattacharya M, Jain N, Dogra P, Samai S, Patil S, Mukhopadhyay S. Biophysical Studies on Protein Aggregation and Amyloid Fibril Formation Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.2425 |
0.697 |
|
2011 |
Jain N, Bhattacharya M, Mukhopadhyay S. Chain collapse of an amyloidogenic intrinsically disordered protein. Biophysical Journal. 101: 1720-9. PMID 21961598 DOI: 10.1016/J.Bpj.2011.08.024 |
0.669 |
|
2011 |
Bhattacharya M, Jain N, Mukhopadhyay S. Insights into the mechanism of aggregation and fibril formation from bovine serum albumin. The Journal of Physical Chemistry. B. 115: 4195-205. PMID 21417250 DOI: 10.1021/Jp111528C |
0.664 |
|
2011 |
Bhattacharya M, Jain N, Bhasne K, Kumari V, Mukhopadhyay S. pH-Induced conformational isomerization of bovine serum albumin studied by extrinsic and intrinsic protein fluorescence. Journal of Fluorescence. 21: 1083-90. PMID 21128099 DOI: 10.1007/S10895-010-0781-3 |
0.583 |
|
2011 |
Jain N, Bhattacharya M, Mukhopadhyay S. Kinetics of surfactant-induced aggregation of lysozyme studied by fluorescence spectroscopy. Journal of Fluorescence. 21: 615-25. PMID 20953821 DOI: 10.1007/S10895-010-0749-3 |
0.658 |
|
2008 |
Wang H, Duennwald ML, Roberts BE, Rozeboom LM, Zhang YL, Steele AD, Krishnan R, Su LJ, Griffin D, Mukhopadhyay S, Hennessy EJ, Weigele P, Blanchard BJ, King J, Deniz AA, et al. Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs. Proceedings of the National Academy of Sciences of the United States of America. 105: 7159-64. PMID 18480256 DOI: 10.1073/Pnas.0801934105 |
0.7 |
|
2008 |
Deniz AA, Mukhopadhyay S, Lemke EA. Single-molecule biophysics: at the interface of biology, physics and chemistry. Journal of the Royal Society, Interface / the Royal Society. 5: 15-45. PMID 17519204 DOI: 10.1098/Rsif.2007.1021 |
0.616 |
|
2007 |
Mukhopadhyay S, Deniz AA. Fluorescence from diffusing single molecules illuminates biomolecular structure and dynamics. Journal of Fluorescence. 17: 775-83. PMID 17641956 DOI: 10.1007/S10895-007-0214-0 |
0.631 |
|
2007 |
Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S, Deniz AA. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proceedings of the National Academy of Sciences of the United States of America. 104: 2649-54. PMID 17299036 DOI: 10.1073/Pnas.0611503104 |
0.694 |
|
2006 |
Mukhopadhyay S, Nayak PK, Udgaonkar JB, Krishnamoorthy G. Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics. Journal of Molecular Biology. 358: 935-42. PMID 16546212 DOI: 10.1016/J.Jmb.2006.02.006 |
0.644 |
|
2004 |
Mukhopadhyay S, Maitra U, Ira I, Krishnamoorthy G, Schmidt J, Talmon Y. Structure and dynamics of a molecular hydrogel derived from a tripodal cholamide. Journal of the American Chemical Society. 126: 15905-14. PMID 15571416 DOI: 10.1021/Ja046788T |
0.702 |
|
2004 |
Mukhopadhyay S, Maitra U. Facile synthesis, aggregation behavior, and cholesterol solubilization ability of avicholic acid. Organic Letters. 6: 31-4. PMID 14703343 DOI: 10.1021/Ol036073F |
0.559 |
|
2003 |
Gundiah G, Mukhopadhyay S, Tumkurkar UG, Govindaraj A, Maitra U, Rao CNR. Hydrogel route to nanotubes of metal oxides and sulfates Journal of Materials Chemistry. 13: 2118-2122. DOI: 10.1039/B304007K |
0.529 |
|
2003 |
Mukhopadhyay S, Ira, Krishnamoorthy G, Maitra U. Dynamics of bound dyes in a nonpolymeric aqueous gel derived from a tripodal bile salt Journal of Physical Chemistry B. 107: 2189-2192. DOI: 10.1021/Jp027079+ |
0.626 |
|
2001 |
Maitra U, Mukhopadhyay S, Sarkar A, Rao P, Indi SS. Hydrophobic Pockets in a Nonpolymeric Aqueous Gel: Observation of such a Gelation Process by Color Change. Angewandte Chemie (International Ed. in English). 40: 2281-2283. PMID 29711840 DOI: 10.1002/1521-3773(20010618)40:12<2281::Aid-Anie2281>3.0.Co;2-L |
0.566 |
|
2001 |
Maitra U, Mukhopadhyay S, Sarkar A, Rao P, Indi SS. Hydrophobic Pockets in a Nonpolymeric Aqueous Gel: Observation of such a Gelation Process by Color Change We thank the Jawaharlal Nehru Center for Advanced Scientific Research (Bangalore), and Mitokor, Inc. (San Diego) for supporting this work through unrestricted research grants. Angewandte Chemie (International Ed. in English). 40: 2281-2283. PMID 11433494 DOI: 10.1002/1521-3773(20010618)40:12<2281::AID-ANIE2281>3.0.CO;2-L |
0.485 |
|
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