| Year |
Citation |
Score |
| 2018 |
Custer GS, Xu H, Matysiak S, Das P. How Hydrophobic Hydration Destabilizes Surfactant Micelle at Low Temperature: A Coarse-grained Simulation Study. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 30247911 DOI: 10.1021/Acs.Langmuir.8B01994 |
0.668 |
|
| 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 |
0.447 |
|
| 2018 |
Das P, Matysiak S, Mittal J. Looking at the Disordered Proteins through the Computational Microscope. Acs Central Science. 4: 534-542. PMID 29805999 DOI: 10.1021/Acscentsci.7B00626 |
0.662 |
|
| 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 |
0.39 |
|
| 2017 |
Chakraborty S, Das P. Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors. Scientific Reports. 7: 9941. PMID 28855598 DOI: 10.1038/S41598-017-10212-5 |
0.332 |
|
| 2017 |
Kang H, Vázquez FX, Zhang L, Das P, Toledo-Sherman LM, Luan B, Levitt M, Zhou R. Emerging β-sheet rich conformations in super-compact Huntingtin exon-1 mutant structures. Journal of the American Chemical Society. PMID 28609090 DOI: 10.1021/Jacs.7B00838 |
0.427 |
|
| 2017 |
Das P, Chacko AR, Belfort G. Alzheimer's Protective Cross-Interaction between Wild-Type and A2T Variants Alters Aβ42 Dimer Structure. Acs Chemical Neuroscience. 8: 606-618. PMID 28292185 DOI: 10.1021/Acschemneuro.6B00357 |
0.401 |
|
| 2017 |
Custer GS, Das P, Matysiak S. Interplay between Conformational Heterogeneity and Hydration in the Folding Landscape of a Designed 3-Helix Bundle. The Journal of Physical Chemistry. B. PMID 28282142 DOI: 10.1021/Acs.Jpcb.6B12286 |
0.696 |
|
| 2017 |
Das P, Chacko A, Belfort G. Alzheimer's Protective Cross-Interaction Between Wild-Type and A2T Variants Changes Aβ42 Dimer Structure Biophysical Journal. 112: 363. DOI: 10.1016/J.Bpj.2016.11.1969 |
0.392 |
|
| 2016 |
Murray B, Sorci M, Rosenthal J, Lippens J, Isaacson D, Das P, Fabris D, Li S, Belfort G. A2T and A2V Aβ Peptides Exhibit Different Aggregation Kinetics, Primary Nucleation, Morphology, Structure and LTP Inhibition. Proteins. PMID 26799157 DOI: 10.1002/Prot.24995 |
0.353 |
|
| 2015 |
Das P, Murray B, Belfort G. Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation. Biophysical Journal. 108: 738-47. PMID 25650940 DOI: 10.1016/J.Bpj.2014.12.013 |
0.369 |
|
| 2014 |
Das P, Kang SG, Temple S, Belfort G. Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations. Plos One. 9: e113041. PMID 25422897 DOI: 10.1371/Journal.Pone.0113041 |
0.39 |
|
| 2014 |
Dasgupta A, Udgaonkar JB, Das P. Multistage unfolding of an SH3 domain: an initial urea-filled dry molten globule precedes a wet molten globule with non-native structure. The Journal of Physical Chemistry. B. 118: 6380-92. PMID 24661021 DOI: 10.1021/Jp410019F |
0.499 |
|
| 2013 |
Matysiak S, Das P. Effects of sequence and solvation on the temperature-pressure conformational landscape of proteinlike heteropolymers. Physical Review Letters. 111: 058103. PMID 23952449 DOI: 10.1103/Physrevlett.111.058103 |
0.652 |
|
| 2013 |
Das P, Kapoor D, Halloran KT, Zhou R, Matthews CR. Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study. Journal of the American Chemical Society. 135: 1882-90. PMID 23293932 DOI: 10.1021/Ja310544T |
0.4 |
|
| 2013 |
Das P, Belfort G, Temple S. Understanding the Protective Role of Alphab Crystallin, a Molecular Chaperone, in Toxic Amyloid Beta Oligomer Formation at an Atomic Level Biophysical Journal. 104: 391a. DOI: 10.1016/J.Bpj.2012.11.2179 |
0.384 |
|
| 2012 |
Xia Z, Das P, Shakhnovich EI, Zhou R. Collapse of unfolded proteins in a mixture of denaturants. Journal of the American Chemical Society. 134: 18266-74. PMID 23057830 DOI: 10.1021/Ja3031505 |
0.497 |
|
| 2012 |
Das P, Matysiak S. Direct characterization of hydrophobic hydration during cold and pressure denaturation. The Journal of Physical Chemistry. B. 116: 5342-8. PMID 22512347 DOI: 10.1016/J.Bpj.2011.11.2484 |
0.65 |
|
| 2012 |
Das P. Effect of cosolvents on nano-confined water: a molecular dynamics study. Nanoscale. 4: 2931-6. PMID 22441726 DOI: 10.1039/C2Nr30070B |
0.35 |
|
| 2012 |
Das P. Differential Dehydration of Hydrophobic Nanotubes in Aqueous Urea and Guanidinium Chloride Solutions: Implications for Protein Denaturation Mechanism Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.3983 |
0.449 |
|
| 2011 |
Das P, King JA, Zhou R. Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands. Proceedings of the National Academy of Sciences of the United States of America. 108: 10514-9. PMID 21670251 DOI: 10.1073/Pnas.1019152108 |
0.401 |
|
| 2011 |
Xiu P, Yang Z, Zhou B, Das P, Fang H, Zhou R. Urea-induced drying of hydrophobic nanotubes: comparison of different urea models. The Journal of Physical Chemistry. B. 115: 2988-94. PMID 21384841 DOI: 10.1021/Jp108303Q |
0.465 |
|
| 2010 |
Li J, Das P, Zhou R. Single mutation effects on conformational change and membrane deformation of influenza hemagglutinin fusion peptides. The Journal of Physical Chemistry. B. 114: 8799-806. PMID 20552971 DOI: 10.1021/Jp1029163 |
0.333 |
|
| 2010 |
Das P, Zhou R. Urea-induced drying of carbon nanotubes suggests existence of a dry globule-like transient state during chemical denaturation of proteins. The Journal of Physical Chemistry. B. 114: 5427-30. PMID 20361766 DOI: 10.1021/Jp911444Q |
0.402 |
|
| 2010 |
Das P, King JA, Zhou R. beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin. Protein Science : a Publication of the Protein Society. 19: 131-40. PMID 19937657 DOI: 10.1002/Pro.296 |
0.457 |
|
| 2008 |
Zhou R, Das P, Royyuru AK. Single mutation induced H3N2 hemagglutinin antibody neutralization: a free energy perturbation study. The Journal of Physical Chemistry. B. 112: 15813-20. PMID 19367871 DOI: 10.1021/Jp805529Z |
0.331 |
|
| 2006 |
Das P, Moll M, Stamati H, Kavraki LE, Clementi C. Low-dimensional, free-energy landscapes of protein-folding reactions by nonlinear dimensionality reduction. Proceedings of the National Academy of Sciences of the United States of America. 103: 9885-90. PMID 16785435 DOI: 10.1073/Pnas.0603553103 |
0.627 |
|
| 2005 |
Wilson CJ, Das P, Clementi C, Matthews KS, Wittung-Stafshede P. The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates. Proceedings of the National Academy of Sciences of the United States of America. 102: 14563-8. PMID 16203983 DOI: 10.1073/Pnas.0505808102 |
0.638 |
|
| 2005 |
Das P, Wilson CJ, Fossati G, Wittung-Stafshede P, Matthews KS, Clementi C. Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experiment. Proceedings of the National Academy of Sciences of the United States of America. 102: 14569-74. PMID 16203982 DOI: 10.1073/Pnas.0505844102 |
0.666 |
|
| 2005 |
Das P, Matysiak S, Clementi C. Balancing energy and entropy: a minimalist model for the characterization of protein folding landscapes. Proceedings of the National Academy of Sciences of the United States of America. 102: 10141-6. PMID 16006532 DOI: 10.1073/Pnas.0409471102 |
0.705 |
|
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