Year |
Citation |
Score |
2023 |
Dar F, Cohen SR, Mitrea DM, Phillips AH, Nagy G, Leite WC, Stanley CB, Choi JM, Kriwacki RW, Pappu RV. Biomolecular condensates form spatially inhomogeneous network fluids. Research Square. PMID 37886520 DOI: 10.21203/rs.3.rs-3419423/v1 |
0.677 |
|
2023 |
Dar F, Cohen SR, Mitrea DM, Phillips AH, Nagy G, Leite WC, Stanley CB, Choi JM, Kriwacki RW, Pappu RV. Biomolecular condensates form spatially inhomogeneous network fluids. Biorxiv : the Preprint Server For Biology. PMID 37873180 DOI: 10.1101/2023.10.07.561338 |
0.677 |
|
2023 |
Farag M, Borcherds WM, Bremer A, Mittag T, Pappu RV. Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions. Nature Communications. 14: 5527. PMID 37684240 DOI: 10.1038/s41467-023-41274-x |
0.303 |
|
2023 |
Lalmansingh JM, Keeley AT, Ruff KM, Pappu RV, Holehouse AS. SOURSOP: A Python Package for the Analysis of Simulations of Intrinsically Disordered Proteins. Journal of Chemical Theory and Computation. PMID 37463458 DOI: 10.1021/acs.jctc.3c00190 |
0.337 |
|
2023 |
Lalmansingh JM, Keeley AT, Ruff KM, Pappu RV, Holehouse AS. SOURSOP: A Python package for the analysis of simulations of intrinsically disordered proteins. Biorxiv : the Preprint Server For Biology. PMID 36824878 DOI: 10.1101/2023.02.16.528879 |
0.336 |
|
2022 |
Ruff KM, Choi YH, Cox D, Ormsby AR, Myung Y, Ascher DB, Radford SE, Pappu RV, Hatters DM. Sequence grammar underlying the unfolding and phase separation of globular proteins. Molecular Cell. PMID 35853451 DOI: 10.1016/j.molcel.2022.06.024 |
0.301 |
|
2022 |
Zeng X, Ruff KM, Pappu RV. Competing interactions give rise to two-state behavior and switch-like transitions in charge-rich intrinsically disordered proteins. Proceedings of the National Academy of Sciences of the United States of America. 119: e2200559119. PMID 35512095 DOI: 10.1073/pnas.2200559119 |
0.323 |
|
2021 |
Zeng X, Liu C, Fossat MJ, Ren P, Chilkoti A, Pappu RV. Design of intrinsically disordered proteins that undergo phase transitions with lower critical solution temperatures. Apl Materials. 9. PMID 38362050 DOI: 10.1063/5.0037438 |
0.48 |
|
2020 |
Choi JM, Hyman AA, Pappu RV. Generalized models for bond percolation transitions of associative polymers. Physical Review. E. 102: 042403. PMID 33212590 DOI: 10.1103/PhysRevE.102.042403 |
0.668 |
|
2020 |
Dar F, Pappu R. Phase Separation: Restricting the sizes of condensates Elife. 9. PMID 32662769 DOI: 10.7554/Elife.59663 |
0.341 |
|
2020 |
Zeng X, Holehouse AS, Chilkoti A, Mittag T, Pappu RV. Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins. Biophysical Journal. PMID 32619404 DOI: 10.1016/J.Bpj.2020.06.014 |
0.404 |
|
2020 |
Cohan MC, Pappu RV. Making the Case for Disordered Proteins and Biomolecular Condensates in Bacteria. Trends in Biochemical Sciences. PMID 32456986 DOI: 10.1016/J.Tibs.2020.04.011 |
0.339 |
|
2020 |
Guillén-Boixet J, Kopach A, Holehouse AS, Wittmann S, Jahnel M, Schlüßler R, Kim K, Trussina IREA, Wang J, Mateju D, Poser I, Maharana S, Ruer-Gruß M, Richter D, Zhang X, ... ... Pappu RV, et al. RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation. Cell. 181: 346-361.e17. PMID 32302572 DOI: 10.1016/J.Cell.2020.03.049 |
0.329 |
|
2020 |
Cohan MC, Eddelbuettel AMP, Levin PA, Pappu RV. Dissecting the functional contributions of the intrinsically disordered C-terminal tail of B. subtilis FtsZ. Journal of Molecular Biology. PMID 32198113 DOI: 10.1016/J.Jmb.2020.03.008 |
0.371 |
|
2020 |
Greig JA, Nguyen TA, Lee M, Holehouse AS, Posey AE, Pappu RV, Jedd G. Arginine-Enriched Mixed-Charge Domains Provide Cohesion for Nuclear Speckle Condensation. Molecular Cell. PMID 32048997 DOI: 10.1016/J.Molcel.2020.01.025 |
0.36 |
|
2020 |
Martin EW, Holehouse AS, Peran I, Farag M, Incicco JJ, Bremer A, Grace CR, Soranno A, Pappu RV, Mittag T. Valence and patterning of aromatic residues determine the phase behavior of prion-like domains. Science (New York, N.Y.). 367: 694-699. PMID 32029630 DOI: 10.1126/Science.Aaw8653 |
0.367 |
|
2020 |
Choi JM, Holehouse AS, Pappu RV. Physical Principles Underlying the Complex Biology of Intracellular Phase Transitions. Annual Review of Biophysics. PMID 32004090 DOI: 10.1146/Annurev-Biophys-121219-081629 |
0.698 |
|
2020 |
Pappu RV, Grosberg A. Decision letter: Dynamic metastable long-living droplets formed by sticker-spacer proteins Elife. DOI: 10.7554/Elife.56159.Sa1 |
0.302 |
|
2020 |
Posey AE, Fossat MJ, Pappu RV. Quantifying the Effects of Charge Regulation on Disorder-Order Transitions of Highly Charged Protein Sequences Biophysical Journal. 118: 540a-541a. DOI: 10.1016/J.Bpj.2019.11.2960 |
0.344 |
|
2020 |
Fossat MJ, Posey AE, Pappu RV. Heuristics for the Effects of Sequence and Conformational Contexts on pKA Values of Ionizable Residues Inferred from Q-Canonical Monte Carlo Simulations Biophysical Journal. 118: 539a-540a. DOI: 10.1016/J.Bpj.2019.11.2956 |
0.357 |
|
2020 |
Choi J, Pappu RV. The Stickers and Spacers Framework for Describing Phase Behavior of Multivalent Intrinsically Disordered Proteins Biophysical Journal. 118: 492a. DOI: 10.1016/J.Bpj.2019.11.2723 |
0.699 |
|
2020 |
Martin EW, Holehouse AS, Peran I, Incicco J, Soranno A, Pappu RV, Mittag T. Evolutionarily Conserved Amino Acid Organization in Protein Low Complexity Regions Encodes Conformation, Dynamics and Assembly Biophysical Journal. 118: 6a. DOI: 10.1016/J.Bpj.2019.11.226 |
0.343 |
|
2020 |
Zeng X, Pappu RV. Combined Theoretical and Computational Approach for Calculating Sequence-specific Phase Diagrams of Thermoresponsive Intrinsically Disordered Homopolypeptides Biophysical Journal. 118: 304a. DOI: 10.1016/J.Bpj.2019.11.1721 |
0.336 |
|
2020 |
Dar F, Pappu RV. Multidimensional Phase Diagrams for Multicomponent Systems Comprising Multivalent Proteins Biophysical Journal. 118: 213a. DOI: 10.1016/J.Bpj.2019.11.1270 |
0.31 |
|
2019 |
Choi JM, Dar F, Pappu RV. LASSI: A lattice model for simulating phase transitions of multivalent proteins. Plos Computational Biology. 15: e1007028. PMID 31634364 DOI: 10.1371/Journal.Pcbi.1007028 |
0.726 |
|
2019 |
Powers SK, Holehouse AS, Korasick DA, Schreiber KH, Clark NM, Jing H, Emenecker R, Han S, Tycksen E, Hwang I, Sozzani R, Jez JM, Pappu RV, Strader LC. Nucleo-cytoplasmic Partitioning of ARF Proteins Controls Auxin Responses in Arabidopsis thaliana. Molecular Cell. PMID 31421981 DOI: 10.1016/J.Molcel.2019.06.044 |
0.317 |
|
2019 |
Cohan MC, Ruff KM, Pappu RV. Information theoretic measures for quantifying sequence-ensemble relationships of intrinsically disordered proteins. Protein Engineering, Design & Selection : Peds. PMID 31375817 DOI: 10.1093/Protein/Gzz014 |
0.346 |
|
2019 |
Fossat MJ, Pappu RV. -Canonical Monte Carlo Sampling for Modeling the Linkage between Charge Regulation and Conformational Equilibria of Peptides. The Journal of Physical Chemistry. B. PMID 31362509 DOI: 10.1021/Acs.Jpcb.9B05206 |
0.361 |
|
2019 |
Bai W, Sargent CJ, Choi JM, Pappu RV, Zhang F. Covalently-assembled single-chain protein nanostructures with ultra-high stability. Nature Communications. 10: 3317. PMID 31346167 DOI: 10.1038/S41467-019-11285-8 |
0.717 |
|
2019 |
Cable J, Brangwynne C, Seydoux G, Cowburn D, Pappu RV, Castañeda CA, Berchowitz LE, Chen Z, Jonikas M, Dernburg A, Mittag T, Fawzi NL. Phase separation in biology and disease-a symposium report. Annals of the New York Academy of Sciences. PMID 31199001 DOI: 10.1111/Nyas.14126 |
0.325 |
|
2019 |
Peran I, Holehouse AS, Carrico IS, Pappu RV, Bilsel O, Raleigh DP. Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions. Proceedings of the National Academy of Sciences of the United States of America. PMID 31167941 DOI: 10.1073/Pnas.1818206116 |
0.429 |
|
2019 |
Boeynaems S, Holehouse AS, Weinhardt V, Kovacs D, Van Lindt J, Larabell C, Van Den Bosch L, Das R, Tompa PS, Pappu RV, Gitler AD. Spontaneous driving forces give rise to protein-RNA condensates with coexisting phases and complex material properties. Proceedings of the National Academy of Sciences of the United States of America. PMID 30926670 DOI: 10.1073/Pnas.1821038116 |
0.332 |
|
2019 |
Beveridge R, Migas LG, Das RK, Pappu RV, Kriwacki RW, Barran PE. Ion mobility mass spectrometry uncovers the impact of the patterning of oppositely charged residues on the conformational distributions of intrinsically disordered proteins. Journal of the American Chemical Society. PMID 30823702 DOI: 10.1021/Jacs.8B13483 |
0.387 |
|
2019 |
Choi JM, Pappu RV. Improvements to the ABSINTH forcefield for proteins based on experimentally derived amino-acid specific backbone conformational statistics. Journal of Chemical Theory and Computation. PMID 30633502 DOI: 10.1021/Acs.Jctc.8B00573 |
0.699 |
|
2019 |
Pappu RV. Making and Breaking the Symmetry between Sequence-Specific Conformational and Phase Behaviors of Disordered Proteins Biophysical Journal. 116: 161a. DOI: 10.1016/J.Bpj.2018.11.895 |
0.405 |
|
2019 |
Michnick S, Bergeron-Sandoval L, Pappu R, François P, Hendricks AG, Ehrlicher AJ, Khadivi Heris H. A Protein Condensate Drives Actin-Independent Endocytosis Biophysical Journal. 116: 161a. DOI: 10.1016/J.Bpj.2018.11.894 |
0.304 |
|
2019 |
Lalmansingh JM, Choi J, Pappu RV. Comparison of Forcefields in the Prediction of Intrinsic Residue-Specific Backbone Dihedral Angle Distributions of Blocked Amino Acids Biophysical Journal. 116: 145a. DOI: 10.1016/J.Bpj.2018.11.806 |
0.676 |
|
2019 |
Dar F, Choi J, Pappu RV. Computational Studies of the Phase Transitions and Network Structure of Dense Liquids Formed by Linear Multivalent Proteins Biophysical Journal. 116: 349a. DOI: 10.1016/J.Bpj.2018.11.1900 |
0.683 |
|
2019 |
Choi J, Mitrea DM, Stanley CB, Ruff KM, Holehouse AS, Kriwacki RW, Pappu RV. Internal Structure of Network Fluid Condensates Formed by Liquid-Liquid Phase Separation of a Multivalent Oligomeric Protein and a Disordered Linear Peptide Biophysical Journal. 116: 349a. DOI: 10.1016/J.Bpj.2018.11.1899 |
0.695 |
|
2019 |
Fossat MJ, Posey AE, Pappu RV. Introducing a Novel Multi-Level Method for Simulating the pH Dependence of Charge State Fluctuations and Conformational Ensembles of Intrinsically Disordered Proteins Biophysical Journal. 116: 287a. DOI: 10.1016/J.Bpj.2018.11.1549 |
0.384 |
|
2019 |
Cohan M, Holehouse AS, Pappu RV. Measures Adapted from Information Theory and Energy Landscape Theory for Quantifying Sequence-To-Conformation Relationships of Intrinsically Disordered Regions Biophysical Journal. 116: 200a. DOI: 10.1016/J.Bpj.2018.11.1107 |
0.312 |
|
2019 |
Holehouse AS, Peran I, Stenzoski NE, Zou J, Piserchio A, Ghose R, Carrico IS, Bilsel O, Raleigh DP, Pappu RV. Protein Unfolded States are Characterized by the Duality of Sequence-Specific Conformational Preferences and Ensemble-Averaged Features of Canonical Random Coils Biophysical Journal. 116: 199a-200a. DOI: 10.1016/J.Bpj.2018.11.1104 |
0.394 |
|
2019 |
Ruff KM, Posey AE, Pappu RV. Modeling the Effects of Ligand Binding on the Phase Behavior of Aggregation-Prone Proteins Biophysical Journal. 116: 199a. DOI: 10.1016/J.Bpj.2018.11.1100 |
0.329 |
|
2019 |
Martin EW, Holehouse AS, Peran I, Bremer A, Pappu RV, Mittag T. Correlating Amino Acid Sequence and Solvation to Disordered Protein Collapse Transitions and Phase Separation Biophysical Journal. 116: 194a. DOI: 10.1016/J.Bpj.2018.11.1076 |
0.376 |
|
2018 |
Choi JM, Pappu RV. Experimentally derived and computationally optimized backbone conformational statistics for blocked amino acids. Journal of Chemical Theory and Computation. PMID 30516982 DOI: 10.1021/Acs.Jctc.8B00572 |
0.716 |
|
2018 |
Posey AE, Holehouse AS, Pappu RV. Phase Separation of Intrinsically Disordered Proteins. Methods in Enzymology. 611: 1-30. PMID 30471685 DOI: 10.1016/Bs.Mie.2018.09.035 |
0.403 |
|
2018 |
Ruff KM, Pappu RV, Holehouse AS. Conformational preferences and phase behavior of intrinsically disordered low complexity sequences: insights from multiscale simulations. Current Opinion in Structural Biology. 56: 1-10. PMID 30439585 DOI: 10.1016/J.Sbi.2018.10.003 |
0.422 |
|
2018 |
Roberts S, Harmon TS, Schaal J, Miao V, Li KJ, Hunt A, Wen Y, Oas TG, Collier JH, Pappu RV, Chilkoti A. Injectable tissue integrating networks from recombinant polypeptides with tunable order. Nature Materials. PMID 30323334 DOI: 10.1038/S41563-018-0182-6 |
0.376 |
|
2018 |
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Pappu RV, Svergun DI, Lemke EA. Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water". Science (New York, N.Y.). 361. PMID 30166461 DOI: 10.1126/Science.Aau8230 |
0.355 |
|
2018 |
Yoo TY, Choi JM, Conway W, Yu CH, Pappu RV, Needleman DJ. Measuring NDC80 binding reveals the molecular basis of tension-dependent kinetochore-microtubule attachments. Elife. 7. PMID 30044223 DOI: 10.7554/Elife.36392 |
0.668 |
|
2018 |
Mirbaha H, Chen D, Morazova OA, Ruff KM, Sharma AM, Liu X, Goodarzi M, Pappu RV, Colby DW, Mirzaei H, Joachimiak LA, Diamond MI. Inert and seed-competent tau monomers suggest structural origins of aggregation. Elife. 7. PMID 29988016 DOI: 10.7554/Elife.36584 |
0.321 |
|
2018 |
Posey AE, Pappu RV. A First Glimpse of Nucleation of Phase Transitions in Living Cells. Molecular Cell. 71: 1-3. PMID 29979961 DOI: 10.1016/J.Molcel.2018.06.028 |
0.325 |
|
2018 |
Wang J, Choi JM, Holehouse AS, Lee HO, Zhang X, Jahnel M, Maharana S, Lemaitre R, Pozniakovsky A, Drechsel D, Poser I, Pappu RV, Alberti S, Hyman AA. A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins. Cell. PMID 29961577 DOI: 10.1016/J.Cell.2018.06.006 |
0.727 |
|
2018 |
Ruff KM, Roberts S, Chilkoti A, Pappu RV. Advances in Understanding Stimulus Responsive Phase Behavior of Intrinsically Disordered Protein Polymers. Journal of Molecular Biology. PMID 29949750 DOI: 10.1016/J.Jmb.2018.06.031 |
0.385 |
|
2018 |
Mittal A, Holehouse AS, Cohan MC, Pappu RV. Equation Chapter 1 Section 1Sequence-To-Conformation Relationships of Disordered Regions Tethered to Folded Domains of Proteins. Journal of Molecular Biology. PMID 29763584 DOI: 10.1016/J.Jmb.2018.05.012 |
0.428 |
|
2018 |
Newcombe EA, Ruff KM, Sethi A, Ormsby AR, Ramdzan YM, Fox A, Purcell AW, Gooley PR, Pappu RV, Hatters DM. Tadpole-like conformations of huntingtin exon 1 are characterized by conformational heterogeneity that persists regardless of polyglutamine length. Journal of Molecular Biology. PMID 29627459 DOI: 10.1016/J.Jmb.2018.03.031 |
0.394 |
|
2018 |
Staller MV, Holehouse AS, Swain-Lenz D, Das RK, Pappu RV, Cohen BA. A High-Throughput Mutational Scan of an Intrinsically Disordered Acidic Transcriptional Activation Domain. Cell Systems. PMID 29525204 DOI: 10.1016/J.Cels.2018.01.015 |
0.377 |
|
2018 |
Garai K, Posey AE, Li X, Buxbaum JN, Pappu RV. Inhibition of Amyloid Beta Fibril Formation by Monomeric Human Transthyretin. Protein Science : a Publication of the Protein Society. PMID 29498118 DOI: 10.1002/Pro.3396 |
0.332 |
|
2018 |
Posey AE, Ruff KM, Harmon TS, Crick SL, Li A, Diamond MI, Pappu RV. Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers. The Journal of Biological Chemistry. PMID 29358329 DOI: 10.1074/Jbc.Ra117.000357 |
0.754 |
|
2018 |
Holehouse AS, Pappu RV. Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions. Annual Review of Biophysics. PMID 29345991 DOI: 10.1146/Annurev-Biophys-070317-032838 |
0.456 |
|
2018 |
Holehouse AS, Pappu RV. Functional Implications of Intracellular Phase Transitions. Biochemistry. PMID 29323488 DOI: 10.1021/Acs.Biochem.7B01136 |
0.309 |
|
2018 |
Franzmann TM, Jahnel M, Pozniakovsky A, Mahamid J, Holehouse AS, Nüske E, Richter D, Baumeister W, Grill SW, Pappu RV, Hyman AA, Alberti S. Phase separation of a yeast prion protein promotes cellular fitness. Science (New York, N.Y.). 359. PMID 29301985 DOI: 10.1126/Science.Aao5654 |
0.327 |
|
2018 |
Pappu RV, Hatters DM. Decision letter: A first order phase transition mechanism underlies protein aggregation in mammalian cells Elife. DOI: 10.7554/Elife.39695.018 |
0.332 |
|
2018 |
Yoo TY, Choi J, Conway W, Yu C, Pappu RV, Needleman DJ. Author response: Measuring NDC80 binding reveals the molecular basis of tension-dependent kinetochore-microtubule attachments Elife. DOI: 10.7554/Elife.36392.025 |
0.663 |
|
2018 |
Harmon TS, Holehouse AS, Pappu RV. Differential solvation of intrinsically disordered linkers drives the formation of spatially organized droplets in ternary systems of linear multivalent proteins New Journal of Physics. 20: 045002. DOI: 10.1088/1367-2630/Aab8D9 |
0.355 |
|
2018 |
Richardson MO, Holehouse AS, Langstein I, Korber P, Pappu RV. Large-Scale Analysis of the Evolution of Functions Mediated by Intrinsically Disordered Regions Biophysical Journal. 114: 79a. DOI: 10.1016/J.Bpj.2017.11.480 |
0.301 |
|
2018 |
Cohan M, Posey A, Mittal A, Grigsby S, Holehouse A, Buske PJ, Levin PA, Pappu RV. Sequence-Encoded Charge Patterning of the Intrinsically Disordered Tail of FtsZ Impacts Polymerization and Bacterial Cell Division Biophysical Journal. 114: 590a. DOI: 10.1016/J.Bpj.2017.11.3226 |
0.317 |
|
2018 |
Posey AE, Kandola T, Pappu RV, Halfmann R. Advances in Quantitative Analysis of Intracellular Protein Phase Separation Kinetics and its Modulation by Cellular Interactions Biophysical Journal. 114: 588a. DOI: 10.1016/J.Bpj.2017.11.3219 |
0.336 |
|
2018 |
Choi J, Wang J, Holehouse AS, Alberti S, Hyman AA, Pappu RV. Molecular Grammar Governing Phase Behavior of Intrinsically Disordered Proteins with Prion-like Domains Biophysical Journal. 114: 561a. DOI: 10.1016/J.Bpj.2017.11.3067 |
0.715 |
|
2018 |
Fossat MJ, Harmon TS, Posey AE, Choi J, Pappu RV. Increasing the Accuracy in All-Atom Simulations of Intrinsically Disordered Proteins based on the Absinth Model Biophysical Journal. 114: 432a. DOI: 10.1016/J.Bpj.2017.11.2392 |
0.706 |
|
2018 |
Ruff KM, Fuertes G, Banterle N, Svergun DI, Lemke EA, Pappu RV. Sequence-Encoded Heterogeneity of Interactions Decouples Different Measures of Protein Sizes and Reconciles the Discrepant Inferences from Saxs versus Fret Experiments Biophysical Journal. 114: 368a. DOI: 10.1016/J.Bpj.2017.11.2039 |
0.346 |
|
2018 |
Holehouse AS, Pappu RV. A General Framework for Predicting and Understanding Sequence-Encoded Phase Diagrams of Intrinsically Disordered Proteins Biophysical Journal. 114: 4a. DOI: 10.1016/J.Bpj.2017.11.051 |
0.383 |
|
2017 |
Harmon TS, Holehouse AS, Rosen MK, Pappu RV. Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins. Elife. 6. PMID 29091028 DOI: 10.7554/Elife.30294 |
0.409 |
|
2017 |
Sherry KP, Das RK, Pappu RV, Barrick D. Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor. Proceedings of the National Academy of Sciences of the United States of America. PMID 29078291 DOI: 10.1073/Pnas.1706083114 |
0.365 |
|
2017 |
Wei MT, Elbaum-Garfinkle S, Holehouse AS, Chen CC, Feric M, Arnold CB, Priestley RD, Pappu RV, Brangwynne CP. Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles. Nature Chemistry. 9: 1118-1125. PMID 29064502 DOI: 10.1038/Nchem.2803 |
0.405 |
|
2017 |
Holehouse AS, Pappu RV. FUS Zigzags Its Way to Cross Beta. Cell. 171: 499-500. PMID 29053965 DOI: 10.1016/J.Cell.2017.10.007 |
0.322 |
|
2017 |
Warner JB, Ruff K, Tan PS, Lemke EA, Pappu RV, Lashuel HA. Monomeric huntingtin exon 1 has similar overall structural features for wild type and pathological polyglutamine lengths. Journal of the American Chemical Society. PMID 28937758 DOI: 10.1021/Jacs.7B06659 |
0.404 |
|
2017 |
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, et al. Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proceedings of the National Academy of Sciences of the United States of America. PMID 28716919 DOI: 10.1073/Pnas.1704692114 |
0.385 |
|
2017 |
Sormanni P, Piovesan D, Heller GT, Bonomi M, Kukic P, Camilloni C, Fuxreiter M, Dosztanyi Z, Pappu RV, Babu MM, Longhi S, Tompa P, Dunker AK, Uversky VN, Tosatto SC, et al. Simultaneous quantification of protein order and disorder. Nature Chemical Biology. 13: 339-342. PMID 28328918 DOI: 10.1038/Nchembio.2331 |
0.386 |
|
2017 |
Kalas V, Pinkner JS, Hannan TJ, Hibbing ME, Dodson KW, Holehouse AS, Zhang H, Tolia NH, Gross ML, Pappu RV, Janetka J, Hultgren SJ. Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions. Science Advances. 3: e1601944. PMID 28246638 DOI: 10.1126/Sciadv.1601944 |
0.321 |
|
2017 |
Holehouse AS, Das RK, Ahad JN, Richardson MO, Pappu RV. CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins. Biophysical Journal. 112: 16-21. PMID 28076807 DOI: 10.1016/J.Bpj.2016.11.3200 |
0.403 |
|
2017 |
Harmon TS, Holehouse AS, Rosen MK, Pappu RV. Author response: Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins Elife. DOI: 10.7554/Elife.30294.022 |
0.351 |
|
2017 |
Cohan MC, Posey A, Grigsby S, Holehouse AS, Mittal A, Buske PJ, Levin P, Pappu RV. The Intrinsically Disordered Tail of FtsZ Impacts Polymerization and Bacterial Cell Division Through Sequence-Encoded Charge Patterning Biophysical Journal. 112: 510a-511a. DOI: 10.1016/J.Bpj.2016.11.2760 |
0.317 |
|
2017 |
Holehouse AS, Perana I, Carrico IS, Bilsel O, Raleigh DP, Pappu RV. Simulations and Experiments Provide a Convergent View of Protein Unfolded States under Folding Conditions Biophysical Journal. 112: 315a. DOI: 10.1016/J.Bpj.2016.11.1709 |
0.474 |
|
2017 |
Choi J, Pappu RV. Lattice Models for Modeling Sequence-Specific Phase Behavior of Low Complexity Domains Biophysical Journal. 112: 208a. DOI: 10.1016/J.Bpj.2016.11.1151 |
0.739 |
|
2017 |
Harmon TS, Roberts S, Chilkoti A, Pappu RV. A Model for Hysteresis Observed in Phase Transitions of Thermally Responsive Intrinsically Disordered Protein Polymers Biophysical Journal. 112: 207a. DOI: 10.1016/J.Bpj.2016.11.1143 |
0.383 |
|
2016 |
Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. Sequence determinants of the conformational properties of an intrinsically disordered protein prior to and upon multisite phosphorylation. Journal of the American Chemical Society. PMID 27807972 DOI: 10.1021/Jacs.6B10272 |
0.423 |
|
2016 |
Harmon TS, Crabtree MD, Shammas SL, Posey AE, Clarke J, Pappu RV. GADIS: Algorithm for designing sequences to achieve target secondary structure profiles of intrinsically disordered proteins. Protein Engineering, Design & Selection : Peds. PMID 27503953 DOI: 10.1093/Protein/Gzw034 |
0.389 |
|
2016 |
Pak CW, Kosno M, Holehouse AS, Padrick SB, Mittal A, Ali R, Yunus AA, Liu DR, Pappu RV, Rosen MK. Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein. Molecular Cell. 63: 72-85. PMID 27392146 DOI: 10.1016/J.Molcel.2016.05.042 |
0.409 |
|
2016 |
Feric M, Vaidya N, Harmon TS, Mitrea DM, Zhu L, Richardson TM, Kriwacki RW, Pappu RV, Brangwynne CP. Coexisting Liquid Phases Underlie Nucleolar Subcompartments. Cell. PMID 27212236 DOI: 10.1016/J.Cell.2016.04.047 |
0.306 |
|
2016 |
Das RK, Huang Y, Phillips AH, Kriwacki RW, Pappu RV. Cryptic sequence features within the disordered protein p27Kip1 regulate cell cycle signaling. Proceedings of the National Academy of Sciences of the United States of America. PMID 27140628 DOI: 10.1073/Pnas.1516277113 |
0.355 |
|
2016 |
Holehouse AS, Harmon TS, Pappu RV. Physical Principles that Govern the Sequence-Encoded Phase Behavior of Intrinsically Disordered Block-Copolymeric Proteins Biophysical Journal. 110: 37a. DOI: 10.1016/J.Bpj.2015.11.268 |
0.408 |
|
2016 |
Posey AE, Ruff KM, Harmon TS, Holehouse AS, Pappu RV. Profilin Binding Modulates the Aggregation and Phase Separation of Huntingtin N-Terminal Fragments via Polyphasic Linkage Biophysical Journal. 110: 399a. DOI: 10.1016/J.Bpj.2015.11.2156 |
0.41 |
|
2016 |
Harmon TS, Pappu RV. Charge Patterned Sequences form Helical Structures through Charge Neutralization Biophysical Journal. 110: 358a. DOI: 10.1016/J.Bpj.2015.11.1931 |
0.385 |
|
2016 |
Kalas V, Pinkner JS, Holehouse AS, Zhang H, Gross ML, Pappu RV, Hultgren SJ. Dynamic Sampling of Multiple Conformations in FimH Modulates Bacterial Adhesion Biophysical Journal. 110: 12a-13a. DOI: 10.1016/J.Bpj.2015.11.125 |
0.385 |
|
2016 |
Pappu RV. Impacts of Charge Patterning on Intrinsically Disordered Proteins and Mechanisms of Disorder-To-Order Transitions Biophysical Journal. 110: 196a. DOI: 10.1016/J.Bpj.2015.11.1094 |
0.401 |
|
2015 |
Ruff KM, Harmon TS, Pappu RV. CAMELOT: A machine learning approach for coarse-grained simulations of aggregation of block-copolymeric protein sequences. The Journal of Chemical Physics. 143: 243123. PMID 26723608 DOI: 10.1063/1.4935066 |
0.41 |
|
2015 |
Banjade S, Wu Q, Mittal A, Peeples WB, Pappu RV, Rosen MK. Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck. Proceedings of the National Academy of Sciences of the United States of America. PMID 26553976 DOI: 10.1073/Pnas.1508778112 |
0.376 |
|
2015 |
Holehouse AS, Pappu RV. Protein polymers: Encoding phase transitions. Nature Materials. 14: 1083-4. PMID 26490213 DOI: 10.1038/Nmat4459 |
0.337 |
|
2015 |
Das RK, Ruff KM, Pappu RV. Relating sequence encoded information to form and function of intrinsically disordered proteins. Current Opinion in Structural Biology. 32: 102-12. PMID 25863585 DOI: 10.1016/J.Sbi.2015.03.008 |
0.427 |
|
2015 |
Pappu RV. Cell signaling, division, and organization mediated by intrinsically disordered proteins. Seminars in Cell & Developmental Biology. 37: 1-2. PMID 25703796 DOI: 10.1016/J.Semcdb.2015.01.003 |
0.315 |
|
2015 |
Diamond MI, Cai S, Boudreau A, Carey CJ, Lyle N, Pappu RV, Swamidass SJ, Bissell M, Piwnica-Worms H, Shao J. Subcellular localization and Ser-137 phosphorylation regulate tumor-suppressive activity of profilin-1. The Journal of Biological Chemistry. 290: 9075-86. PMID 25681442 DOI: 10.1074/Jbc.M114.619874 |
0.718 |
|
2015 |
Holehouse AS, Garai K, Lyle N, Vitalis A, Pappu RV. Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation. Journal of the American Chemical Society. 137: 2984-95. PMID 25664638 DOI: 10.1021/Ja512062H |
0.817 |
|
2015 |
Buske PJ, Mittal A, Pappu RV, Levin PA. An intrinsically disordered linker plays a critical role in bacterial cell division. Seminars in Cell & Developmental Biology. 37: 3-10. PMID 25305578 DOI: 10.1016/J.Semcdb.2014.09.017 |
0.371 |
|
2015 |
Brangwynne CP, Tompa P, Pappu RV. Polymer physics of intracellular phase transitions Nature Physics. 11: 899-904. DOI: 10.1038/Nphys3532 |
0.303 |
|
2015 |
Ruff KM, Pappu RV. Multiscale Simulations Provide Mechanistic Insights into the Effects of Sequence Contexts on Early-Stage Polyglutamine-Mediated Aggregation Biophysical Journal. 108: 495a. DOI: 10.1016/J.Bpj.2014.11.2710 |
0.408 |
|
2015 |
Holehouse AS, Ahad J, Das RK, Pappu RV. CIDER: Classification of Intrinsically Disordered Ensemble Regions Biophysical Journal. 108: 228a. DOI: 10.1016/J.Bpj.2014.11.1260 |
0.422 |
|
2015 |
Harmon TS, Pappu RV. An Evolutionary Algorithm for the Design of Different Degrees of Secondary Structure in Intrinsically Disordered Proteins (IDPs) Biophysical Journal. 108: 228a. DOI: 10.1016/J.Bpj.2014.11.1259 |
0.412 |
|
2015 |
Sherry K, Das R, Pappu R, Barrick D. Effects of Charge Interactions and Transient Secondary Structure Elements on the Function of the Disordered RAM Region of the Notch Receptor Biophysical Journal. 108: 193a-194a. DOI: 10.1016/J.Bpj.2014.11.1071 |
0.35 |
|
2014 |
Ripaud L, Chumakova V, Antonin M, Hastie AR, Pinkert S, Körner R, Ruff KM, Pappu RV, Hornburg D, Mann M, Hartl FU, Hipp MS. Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome. Proceedings of the National Academy of Sciences of the United States of America. 111: 18219-24. PMID 25489109 DOI: 10.1073/Pnas.1421313111 |
0.42 |
|
2014 |
Ruff KM, Khan SJ, Pappu RV. A coarse-grained model for polyglutamine aggregation modulated by amphipathic flanking sequences. Biophysical Journal. 107: 1226-35. PMID 25185558 DOI: 10.1016/J.Bpj.2014.07.019 |
0.411 |
|
2014 |
Pappu RV. Frozen in beta. Biophysical Journal. 107: 795-7. PMID 25140412 DOI: 10.1016/J.Bpj.2014.07.007 |
0.415 |
|
2014 |
Mittal A, Lyle N, Harmon TS, Pappu RV. Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins. Journal of Chemical Theory and Computation. 10: 3550-3562. PMID 25136274 DOI: 10.1021/Ct5002297 |
0.787 |
|
2014 |
Vitalis A, Pappu RV. A simple molecular mechanics integrator in mixed rigid body and dihedral angle space. The Journal of Chemical Physics. 141: 034105. PMID 25053299 DOI: 10.1063/1.4887339 |
0.645 |
|
2014 |
van der Lee R, Buljan M, Lang B, Weatheritt RJ, Daughdrill GW, Dunker AK, Fuxreiter M, Gough J, Gsponer J, Jones DT, Kim PM, Kriwacki RW, Oldfield CJ, Pappu RV, Tompa P, et al. Classification of intrinsically disordered regions and proteins. Chemical Reviews. 114: 6589-631. PMID 24773235 DOI: 10.1021/Cr400525M |
0.376 |
|
2014 |
Luan B, Lyle N, Pappu RV, Raleigh DP. Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts. Biochemistry. 53: 39-47. PMID 24280003 DOI: 10.1021/Bi4008337 |
0.775 |
|
2014 |
Holehouse AS, Lyle N, Vitalis A, Thirumalai D, Pappu RV. Parsing the Contributions of Polypeptide Backbones and Sidechains to Denaturation in Concentrated Aqueous Solutions of Urea and Guanidinium Chloride Biophysical Journal. 106: 484a. DOI: 10.1016/J.Bpj.2013.11.2731 |
0.801 |
|
2014 |
Ruff KM, Garai K, Pappu RV. Role of Intrinsic Helicity Within N-Terminal Flanking Sequences on Huntingtin Aggregation Mechanisms Biophysical Journal. 106: 483a. DOI: 10.1016/J.Bpj.2013.11.2727 |
0.368 |
|
2014 |
Harmon TS, Rosen MK, Pappu RV. Coarse Grain Models Highlight the Importance of Flexible Disordered Linkers as Determinants of the Phase Behavior in Polyvalent Proteins Biophysical Journal. 106: 481a. DOI: 10.1016/J.Bpj.2013.11.2718 |
0.395 |
|
2014 |
Mittal A, Garai K, Pappu RV. How Do Interactions in Cis with Ordered Domains Influence Sequence-Ensemble Relationships of Intrinsically Disordered Regions? Biophysical Journal. 106: 425a-426a. DOI: 10.1016/J.Bpj.2013.11.2398 |
0.388 |
|
2014 |
Garai K, Li X, Powers EM, Buxbaum J, Pappu R. Transthyretin Interacts with Amyloid-β Oligomers to Delay Amyloid Aggregation Biophysical Journal. 106: 270a. DOI: 10.1016/J.Bpj.2013.11.1581 |
0.338 |
|
2014 |
Pappu R. Decoding Sequence-Ensemble Relationships of IDPS Biophysical Journal. 106: 5a. DOI: 10.1016/J.Bpj.2013.11.063 |
0.398 |
|
2013 |
Crick SL, Ruff KM, Garai K, Frieden C, Pappu RV. Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation. Proceedings of the National Academy of Sciences of the United States of America. 110: 20075-80. PMID 24282292 DOI: 10.1073/Pnas.1320626110 |
0.782 |
|
2013 |
Lyle N, Das RK, Pappu RV. A quantitative measure for protein conformational heterogeneity. The Journal of Chemical Physics. 139: 121907. PMID 24089719 DOI: 10.1063/1.4812791 |
0.787 |
|
2013 |
Das RK, Pappu RV. Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. Proceedings of the National Academy of Sciences of the United States of America. 110: 13392-7. PMID 23901099 DOI: 10.1073/Pnas.1304749110 |
0.416 |
|
2013 |
Meng W, Luan B, Lyle N, Pappu RV, Raleigh DP. The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry. 52: 2662-71. PMID 23480024 DOI: 10.1021/Bi301667U |
0.78 |
|
2013 |
Meng W, Lyle N, Luan B, Raleigh DP, Pappu RV. Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 110: 2123-8. PMID 23341588 DOI: 10.1073/Pnas.1216979110 |
0.787 |
|
2013 |
Mao AH, Lyle N, Pappu RV. Describing sequence-ensemble relationships for intrinsically disordered proteins. The Biochemical Journal. 449: 307-18. PMID 23240611 DOI: 10.1042/Bj20121346 |
0.811 |
|
2013 |
Das RK, Mittal A, Pappu RV. How is functional specificity achieved through disordered regions of proteins? Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 35: 17-22. PMID 23138868 DOI: 10.1002/Bies.201200115 |
0.372 |
|
2013 |
Crick SL, Ruff KM, Garai K, Frieden C, Pappu RV. Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation Proceedings of the National Academy of Sciences of the United States of America. 110: 20075-20080. DOI: 10.1073/pnas.1320626110 |
0.765 |
|
2013 |
Lyle NJ, Pappu RV. Quantifying Disorder using Simulated Ensembles for Different Classes of Polypeptides Biophysical Journal. 104: 53a. DOI: 10.1016/J.Bpj.2012.11.335 |
0.796 |
|
2013 |
Das RK, Ruff K, Pappu RV. Functional Implications of Intrinsic Helicities within Basic Regions of bZIP Transcription Factors Biophysical Journal. 104: 53a. DOI: 10.1016/J.Bpj.2012.11.334 |
0.374 |
|
2013 |
Mittal A, Das RK, Pappu RV. Assessing the Coupling in cis between Disordered Regions and Ordered Domains Biophysical Journal. 104: 53a. DOI: 10.1016/J.Bpj.2012.11.333 |
0.386 |
|
2013 |
Khan S, Lyle N, Pappu RV. Coarse Grain Simulations Providing a Unifying Framework for Explaining Polyglutamine Aggregation Mechanism Biophysical Journal. 104: 388a-389a. DOI: 10.1016/J.Bpj.2012.11.2166 |
0.778 |
|
2013 |
Pappu RV. Connecting Sequence to Conformational Properties of Intrinsically Disordered Proteins: A Charged Relationship Biophysical Journal. 104: 355a. DOI: 10.1016/J.Bpj.2012.11.1969 |
0.427 |
|
2013 |
Ruff K, Lyle N, Pappu RV. Modulation of Polyglutamine Conformations and Associations by C-Terminal Proline Rich Regions from Exon 1 of Huntingtin Biophysical Journal. 104: 233a. DOI: 10.1016/J.Bpj.2012.11.1317 |
0.774 |
|
2012 |
Babu MM, Kriwacki RW, Pappu RV. Structural biology. Versatility from protein disorder. Science (New York, N.Y.). 337: 1460-1. PMID 22997313 DOI: 10.1126/Science.1228775 |
0.393 |
|
2012 |
Mao AH, Pappu RV. Crystal lattice properties fully determine short-range interaction parameters for alkali and halide ions. The Journal of Chemical Physics. 137: 064104. PMID 22897252 DOI: 10.1063/1.4742068 |
0.71 |
|
2012 |
Das RK, Mao AH, Pappu RV. Unmasking functional motifs within disordered regions of proteins. Science Signaling. 5: pe17. PMID 22510467 DOI: 10.1126/Scisignal.2003091 |
0.743 |
|
2012 |
Radhakrishnan A, Vitalis A, Mao AH, Steffen AT, Pappu RV. Improved atomistic Monte Carlo simulations demonstrate that poly-L-proline adopts heterogeneous ensembles of conformations of semi-rigid segments interrupted by kinks. The Journal of Physical Chemistry. B. 116: 6862-71. PMID 22329658 DOI: 10.1021/Jp212637R |
0.803 |
|
2012 |
Das RK, Crick SL, Pappu RV. N-terminal segments modulate the α-helical propensities of the intrinsically disordered basic regions of bZIP proteins. Journal of Molecular Biology. 416: 287-99. PMID 22226835 DOI: 10.1016/J.Jmb.2011.12.043 |
0.779 |
|
2012 |
Lyle NJ, Meng W, Raleigh DP, Pappu RV. Simulations of Denatured Protein Ensembles Reproduce and Rationalize Experimental Observations of Persistent Contacts Between Residues Distal in Protein Sequence Biophysical Journal. 102: 630a. DOI: 10.1016/J.Bpj.2011.11.3433 |
0.798 |
|
2012 |
Das RK, Pappu RV. Conformational Ensembles of Intrinsically Disordered Proteins are Determined by Charge Patterning Biophysical Journal. 102: 630a. DOI: 10.1016/J.Bpj.2011.11.3432 |
0.445 |
|
2012 |
Ruff K, Lyle N, Pappu RV. Implications Of Cis Interactions Between Expanded Polyglutamine and the Proline Rich C-Terminal Domain of Huntingtin Exon 1 For the Loss- Versus Gain-Of-Function Models of Huntington's Disease Biophysical Journal. 102: 256a. DOI: 10.1016/J.Bpj.2011.11.1411 |
0.774 |
|
2012 |
Crick SL, Mao AH, Pappu RV. Inferring Aggregation Mechanisms of Polyglutamine Through Quantitative Studies of Phase Behavior Biophysical Journal. 102: 11a. DOI: 10.1016/J.Bpj.2011.11.081 |
0.816 |
|
2012 |
Crick SL, Pappu RV. Thermodynamic and Kinetic Models for Aggregation of Intrinsically Disordered Proteins Protein and Peptide Folding, Misfolding, and Non-Folding. 413-440. DOI: 10.1002/9781118183373.ch14 |
0.75 |
|
2011 |
Halfmann R, Alberti S, Krishnan R, Lyle N, O'Donnell CW, King OD, Berger B, Pappu RV, Lindquist S. Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Molecular Cell. 43: 72-84. PMID 21726811 DOI: 10.1016/J.Molcel.2011.05.013 |
0.79 |
|
2011 |
Vitalis A, Pappu RV. Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides. Biophysical Chemistry. 159: 14-23. PMID 21530061 DOI: 10.1016/J.Bpc.2011.04.006 |
0.695 |
|
2011 |
Mao AH, Pappu RV. Exact recording of metropolis-hastings-class Monte Carlo simulations using one bit per sample Computer Physics Communications. 182: 1452-1454. DOI: 10.1016/J.Cpc.2011.03.013 |
0.709 |
|
2011 |
Das RK, Crick SL, Pappu RV. Intrinsic Helicity of Disordered Basic Regions of Bzip Transcription Factors: Implications For Mechanisms of DNA Binding Biophysical Journal. 100: 63a. DOI: 10.1016/J.Bpj.2010.12.544 |
0.745 |
|
2011 |
Lyle NJ, Crick SL, Pappu RV. Alterations to the Conformational Ensemble and Intermolecular Associations of Polyglutamine Due to Charged Side Chains at the N- and C-Termini Biophysical Journal. 100: 63a. DOI: 10.1016/J.Bpj.2010.12.543 |
0.816 |
|
2011 |
Das RK, Crick SL, Pappu RV. Intrinsic Disorder in the Basic Regions of bZIP Transcription Factors: What it Means to Be Disordered and Why it Might Matter! Biophysical Journal. 100: 519a. DOI: 10.1016/J.Bpj.2010.12.3033 |
0.738 |
|
2011 |
Das RK, Barrick D, Pappu RV. Conformational Fluctuations within the Intrinsically Disordered RAM Domain of the Notch Receptor are Governed by the Patterning of Charged Residues within the Primary Sequence Biophysical Journal. 100: 13a. DOI: 10.1016/J.Bpj.2010.12.282 |
0.389 |
|
2011 |
Radhakrishnan A, Vitalis A, Mao AH, Steffen AT, Pappu RV. Accurate Atomistic Modeling of Conformational Equilibria of Proline-Rich Sequences Biophysical Journal. 100: 378a-379a. DOI: 10.1016/J.Bpj.2010.12.2254 |
0.807 |
|
2011 |
Mao AH, Pappu RV. Intrinsically Disordered Protein Regions Modeled as Isolated Entities Commonly Adopt Ensembles of Collapsed, Globular Conformations Biophysical Journal. 100: 228a. DOI: 10.1016/J.Bpj.2010.12.1461 |
0.774 |
|
2011 |
Crick SL, Pappu RV. Establishing a Reference State for Studying the Aggregation Kinetics of Polyglutamine Containing Systems Biophysical Journal. 100: 201a. DOI: 10.1016/J.Bpj.2010.12.1310 |
0.756 |
|
2010 |
Wyczalkowski MA, Vitalis A, Pappu RV. New estimators for calculating solvation entropy and enthalpy and comparative assessments of their accuracy and precision. The Journal of Physical Chemistry. B. 114: 8166-80. PMID 20503993 DOI: 10.1021/Jp103050U |
0.754 |
|
2010 |
Mao AH, Crick SL, Vitalis A, Chicoine CL, Pappu RV. Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proceedings of the National Academy of Sciences of the United States of America. 107: 8183-8. PMID 20404210 DOI: 10.1073/Pnas.0911107107 |
0.823 |
|
2010 |
Williamson TE, Vitalis A, Crick SL, Pappu RV. Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. Journal of Molecular Biology. 396: 1295-309. PMID 20026071 DOI: 10.1016/J.Jmb.2009.12.017 |
0.825 |
|
2010 |
Lyle NJ, Pappu RV. Parameter Refinement, Optimization, and Extension of the Absinth Implicit Solvation Model Biophysical Journal. 98: 574a. DOI: 10.1016/J.Bpj.2009.12.3118 |
0.778 |
|
2010 |
Crick S, Pappu RV. Probing the Conformational Ensemble of Polyglutamine During the Initial Stages of Aggregation Biophysical Journal. 98: 424a. DOI: 10.1016/J.Bpj.2009.12.2297 |
0.775 |
|
2010 |
Mao AH, Crick SL, Chicoine CL, Pappu RV. Effects of pH on Conformational Equilibria of Intrinsically Disordered Proteins Biophysical Journal. 98: 256a. DOI: 10.1016/J.Bpj.2009.12.1390 |
0.818 |
|
2009 |
Chen AA, Marucho M, Baker NA, Pappu RV. Simulations of RNA interactions with monovalent ions. Methods in Enzymology. 469: 411-32. PMID 20946801 DOI: 10.1016/S0076-6879(09)69020-0 |
0.555 |
|
2009 |
Vitalis A, Pappu RV. Methods for Monte Carlo simulations of biomacromolecules. Annual Reports in Computational Chemistry. 5: 49-76. PMID 20428473 DOI: 10.1016/S1574-1400(09)00503-9 |
0.666 |
|
2009 |
Hu X, Crick SL, Bu G, Frieden C, Pappu RV, Lee JM. Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide Proceedings of the National Academy of Sciences of the United States of America. 106: 20324-20329. PMID 19910533 DOI: 10.1073/Pnas.0911281106 |
0.762 |
|
2009 |
Lashuel HA, Pappu RV. Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies. Chembiochem : a European Journal of Chemical Biology. 10: 1951-4. PMID 19598186 DOI: 10.1002/Cbic.200900373 |
0.305 |
|
2009 |
Vitalis A, Lyle N, Pappu RV. Thermodynamics of beta-sheet formation in polyglutamine. Biophysical Journal. 97: 303-11. PMID 19580768 DOI: 10.1016/J.Bpj.2009.05.003 |
0.795 |
|
2009 |
Chen AA, Draper DE, Pappu RV. Molecular simulation studies of monovalent counterion-mediated interactions in a model RNA kissing loop. Journal of Molecular Biology. 390: 805-19. PMID 19482035 DOI: 10.1016/J.Jmb.2009.05.071 |
0.573 |
|
2009 |
Vitalis A, Pappu RV. ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions. Journal of Computational Chemistry. 30: 673-99. PMID 18506808 DOI: 10.1002/Jcc.21005 |
0.717 |
|
2009 |
Lee J, Crick S, Pappu R, Frieden C, Hu X. P1-004: Amyloid seeds formed by cellular uptake, concentration, and aggergation of the Abeta1-42
peptide Alzheimer's & Dementia. 5: P173-P173. DOI: 10.1016/J.Jalz.2009.04.007 |
0.758 |
|
2009 |
Chen AA, Draper DE, Pappu RV. Mechanism Of Monovalent Counterion Specificity In A RNA Kissing Loop Complex Biophysical Journal. 96: 576a. DOI: 10.1016/J.Bpj.2008.12.3008 |
0.556 |
|
2009 |
Pappu R. Effects Of Sequence And Conformational Contexts In Polyglutamine Aggregation Biophysical Journal. 96: 552a. DOI: 10.1016/J.Bpj.2008.12.2993 |
0.461 |
|
2009 |
Mao A, Vitalis A, Pappu RV. How Does Charge Content Modulate Conformational Equilibria of Intrinsically Disordered Proteins? An Illustration Using Protamines Biophysical Journal. 96: 220a. DOI: 10.1016/J.Bpj.2008.12.1920 |
0.825 |
|
2009 |
Vitalis A, Pappu RV. Introducing A Software Package For The Simulation Of Biomacromolecules Using The ABSINTH Implicit Solvation Model Biophysical Journal. 96: 303a. DOI: 10.1016/J.Bpj.2008.12.1508 |
0.679 |
|
2009 |
Wyczalkowski MA, Pappu RV. Assessing the Driving Forces for Collapse of Archetypal Intrinsically Disordered Polypeptides Biophysical Journal. 96: 301a. DOI: 10.1016/J.Bpj.2008.12.1495 |
0.69 |
|
2008 |
Vitalis A, Wang X, Pappu RV. Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization. Journal of Molecular Biology. 384: 279-97. PMID 18824003 DOI: 10.1016/J.Jmb.2008.09.026 |
0.73 |
|
2008 |
Tran HT, Mao A, Pappu RV. Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins. Journal of the American Chemical Society. 130: 7380-92. PMID 18481860 DOI: 10.1021/Ja710446S |
0.784 |
|
2008 |
Wyczalkowski MA, Pappu RV. Satisfying the fluctuation theorem in free-energy calculations with Hamiltonian replica exchange. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics. 77: 026104. PMID 18352087 DOI: 10.1103/Physreve.77.026104 |
0.633 |
|
2008 |
Pappu RV, Wang X, Vitalis A, Crick SL. A polymer physics perspective on driving forces and mechanisms for protein aggregation. Archives of Biochemistry and Biophysics. 469: 132-41. PMID 17931593 DOI: 10.1016/J.Abb.2007.08.033 |
0.799 |
|
2008 |
Wyczalkowski MA, Pappu RV. Publisher's Note: Satisfying the fluctuation theorem in free-energy calculations with Hamiltonian replica exchange (Physical Review e (2008) 77 (026104)) Physical Review E - Statistical, Nonlinear, and Soft Matter Physics. 77. DOI: 10.1103/Physreve.77.029905 |
0.618 |
|
2007 |
Chen AA, Pappu RV. Parameters of monovalent ions in the AMBER-99 forcefield: assessment of inaccuracies and proposed improvements. The Journal of Physical Chemistry. B. 111: 11884-7. PMID 17887792 DOI: 10.1021/Jp0765392 |
0.535 |
|
2007 |
Vitalis A, Wang X, Pappu RV. Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories. Biophysical Journal. 93: 1923-37. PMID 17526581 DOI: 10.1529/Biophysj.107.110080 |
0.735 |
|
2007 |
Chen AA, Pappu RV. Quantitative characterization of ion pairing and cluster formation in strong 1:1 electrolytes. The Journal of Physical Chemistry. B. 111: 6469-78. PMID 17518490 DOI: 10.1021/Jp0708547 |
0.533 |
|
2006 |
Crick SL, Jayaraman M, Frieden C, Wetzel R, Pappu RV. Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions Proceedings of the National Academy of Sciences of the United States of America. 103: 16764-16769. PMID 17075061 DOI: 10.1073/Pnas.0608175103 |
0.79 |
|
2006 |
Tran HT, Pappu RV. Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions. Biophysical Journal. 91: 1868-86. PMID 16766618 DOI: 10.1529/Biophysj.106.086264 |
0.44 |
|
2006 |
Wang X, Vitalis A, Wyczalkowski MA, Pappu RV. Characterizing the conformational ensemble of monomeric polyglutamine. Proteins. 63: 297-311. PMID 16299774 DOI: 10.1002/Prot.20761 |
0.81 |
|
2006 |
Lee J, Hu X, Crick S, Song H, Yin K, Cirrito J, Bateman R, Hsu CY, Xu J, Hsu FF, Turk J, Pappu R, Holtzman DM, Yan P. O4-06-07: MMP-9 degrades fibrilllar abeta in vitro and compact plaques In situ Alzheimer's & Dementia. 2: S89-S89. DOI: 10.1016/J.Jalz.2006.05.342 |
0.701 |
|
2005 |
Tran HT, Wang X, Pappu RV. Reconciling observations of sequence-specific conformational propensities with the generic polymeric behavior of denatured proteins. Biochemistry. 44: 11369-80. PMID 16114874 DOI: 10.1021/Bi050196L |
0.45 |
|
2004 |
Patriciu A, Chirikjian GS, Pappu RV. Analysis of the conformational dependence of mass-metric tensor determinants in serial polymers with constraints. The Journal of Chemical Physics. 121: 12708-20. PMID 15606297 DOI: 10.1063/1.1821492 |
0.324 |
|
2004 |
Drozdov AN, Grossfield A, Pappu RV. Role of solvent in determining conformational preferences of alanine dipeptide in water. Journal of the American Chemical Society. 126: 2574-81. PMID 14982467 DOI: 10.1021/Ja039051X |
0.35 |
|
2002 |
Pappu RV, Rose GD. A simple model for polyproline II structure in unfolded states of alanine-based peptides. Protein Science : a Publication of the Protein Society. 11: 2437-55. PMID 12237465 DOI: 10.1110/Ps.0217402 |
0.647 |
|
2000 |
Pappu RV, Srinivasan R, Rose GD. The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding Proceedings of the National Academy of Sciences of the United States of America. 97: 12565-12570. PMID 11070081 DOI: 10.1073/Pnas.97.23.12565 |
0.656 |
|
2000 |
Hart RK, Pappu RV, Ponder JW. Exploring the Similarities between Potential Smoothing and Simulated Annealing Journal of Computational Chemistry. 21: 531-552. DOI: 10.1002/(Sici)1096-987X(200005)21:7<531::Aid-Jcc3>3.0.Co;2-C |
0.652 |
|
1999 |
Pappu RV. Review of the Fourth Johns Hopkins Protein Folding Meeting Proteins: Structure, Function and Genetics. 36: 263-269. PMID 10409820 DOI: 10.1002/(Sici)1097-0134(19990815)36:3<263::Aid-Prot1>3.0.Co;2-Q |
0.318 |
|
1999 |
Pappu RV, Marshall GR, Ponder JW. A potential smoothing algorithm accurately predicts transmembrane helix packing. Nature Structural Biology. 6: 50-5. PMID 9886292 DOI: 10.1038/4922 |
0.642 |
|
1998 |
Huang ES, Koehl P, Levitt M, Pappu RV, Ponder JW. Accuracy of side-chain prediction upon near-native protein backbones generated by Ab initio folding methods. Proteins. 33: 204-17. PMID 9779788 DOI: 10.1002/(Sici)1097-0134(19981101)33:2<204::Aid-Prot5>3.0.Co;2-I |
0.673 |
|
1998 |
Pappu RV, Weaver DL. The early folding kinetics of apomyoglobin Protein Science. 7: 480-490. PMID 9521125 DOI: 10.1002/Pro.5560070229 |
0.572 |
|
1998 |
Pappu RV, Hart RK, Ponder JW. Analysis and application of potential energy smoothing and search methods for global optimization Journal of Physical Chemistry B. 102: 9725-9742. DOI: 10.1021/Jp982255T |
0.613 |
|
1996 |
Pappu RV, Schneller WJ, Weaver DL. Electrostatic multipole representation of a polypeptide chain: An algorithm for simulation of polypeptide properties Journal of Computational Chemistry. 17: 1033-1055. DOI: 10.1002/(Sici)1096-987X(199606)17:8<1033::Aid-Jcc12>3.0.Co;2-F |
0.609 |
|
Low-probability matches (unlikely to be authored by this person) |
2017 |
Boothby TC, Piszkiewicz S, Mehta A, Brozena A, Tapia H, Koshland D, Holehouse A, Pappu R, Goldstein B, Pielak G. Tardigrade Disordered Proteins Mediate Desiccation Tolerance Biophysical Journal. 112: 480a. DOI: 10.1016/J.Bpj.2016.11.2600 |
0.297 |
|
2016 |
Ruff KM, Holehouse AS, Richardson MG, Pappu RV. Proteomic and Biophysical Analysis of Polar Tracts Biophysical Journal. 110: 556a. DOI: 10.1016/J.Bpj.2015.11.2975 |
0.296 |
|
2015 |
Kozlov AG, Weiland E, Mittal A, Waldman V, Antony E, Fazio N, Pappu RV, Lohman TM. Intrinsically disordered C-terminal tails of E. coli single-stranded DNA binding protein regulate cooperative binding to single-stranded DNA. Journal of Molecular Biology. 427: 763-74. PMID 25562210 DOI: 10.1016/J.Jmb.2014.12.020 |
0.295 |
|
2022 |
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, ... Pappu RV, et al. Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nature Structural & Molecular Biology. 29: 781-790. PMID 35948766 DOI: 10.1038/s41594-022-00811-w |
0.295 |
|
2017 |
Clarke J, Pappu RV. Editorial overview: Protein Folding and Binding, Complexity Comes of Age. Current Opinion in Structural Biology. 42: v-vii. PMID 28351535 DOI: 10.1016/J.Sbi.2017.03.004 |
0.294 |
|
2017 |
Fei J, Jadaliha M, Harmon TS, Li ITS, Hua B, Hao Q, Holehouse AS, Reyer M, Sun Q, Freier SM, Pappu RV, Prasanth KV, Ha T. Quantitative analysis of multilayer organization of proteins and RNA in nuclear speckles at super resolution. Journal of Cell Science. PMID 29133588 DOI: 10.1242/Jcs.206854 |
0.293 |
|
2018 |
Mirbaha H, Chen D, Morazova OA, Ruff KM, Sharma AM, Liu X, Goodarzi M, Pappu RV, Colby DW, Mirzaei H, Joachimiak LA, Diamond MI. Author response: Inert and seed-competent tau monomers suggest structural origins of aggregation Elife. DOI: 10.7554/Elife.36584.035 |
0.292 |
|
2023 |
Pappu R, Farag M, Borcherds W, Bremer A, Mittag T. Phase Separation in Mixtures of Prion-Like Low Complexity Domains is Driven by the Interplay of Homotypic and Heterotypic Interactions. Research Square. PMID 37205474 DOI: 10.21203/rs.3.rs-2870258/v1 |
0.291 |
|
2023 |
Farag M, Borcherds WM, Bremer A, Mittag T, Pappu RV. Phase Separation in Mixtures of Prion-Like Low Complexity Domains is Driven by the Interplay of Homotypic and Heterotypic Interactions. Biorxiv : the Preprint Server For Biology. PMID 36993212 DOI: 10.1101/2023.03.15.532828 |
0.291 |
|
2022 |
Farag M, Cohen SR, Borcherds WM, Bremer A, Mittag T, Pappu RV. Condensates formed by prion-like low-complexity domains have small-world network structures and interfaces defined by expanded conformations. Nature Communications. 13: 7722. PMID 36513655 DOI: 10.1038/s41467-022-35370-7 |
0.289 |
|
2023 |
Patil A, Strom AR, Paulo JA, Collings CK, Ruff KM, Shinn MK, Sankar A, Cervantes KS, Wauer T, St Laurent JD, Xu G, Becker LA, Gygi SP, Pappu RV, Brangwynne CP, et al. A disordered region controls cBAF activity via condensation and partner recruitment. Cell. 186: 4936-4955.e26. PMID 37788668 DOI: 10.1016/j.cell.2023.08.032 |
0.287 |
|
2017 |
Chatterjee S, Luthra P, Esaulova E, Agapov E, Yen BC, Borek DM, Edwards MR, Mittal A, Jordan DS, Ramanan P, Moore ML, Pappu RV, Holtzman MJ, Artyomov MN, Basler CF, et al. Structural basis for human respiratory syncytial virus NS1-mediated modulation of host responses. Nature Microbiology. 2: 17101. PMID 28665409 DOI: 10.1038/Nmicrobiol.2017.101 |
0.286 |
|
2017 |
Posey AE, Harmon TS, Pappu RV. Charge Neutralization, Not Salt Bridges, Stabilizes Alpha Helices in Repeating Blocks of Acidic and Basic Residues Biophysical Journal. 112: 345a-346a. DOI: 10.1016/J.Bpj.2016.11.1874 |
0.284 |
|
2019 |
Zeng X, Fossat MJ, Tang N, Chilkoti A, Pappu RV. A High Throughput Method for Exploring the Sequence Space of Polypeptides That Exhibit Thermoresponsive Phase Behavior Biophysical Journal. 116: 200a. DOI: 10.1016/J.Bpj.2018.11.1105 |
0.279 |
|
2020 |
Lalmansingh JM, Posey AE, Kandola T, Halfmann R, Pappu RV. Basin Mapping Method for Extracting Comparative Assessments of Protein Phase Behavior from In Vivo Measurements Biophysical Journal. 118: 538a. DOI: 10.1016/J.Bpj.2019.11.2949 |
0.273 |
|
2021 |
Ruff KM, Pappu RV. AlphaFold and implications for intrinsically disordered proteins. Journal of Molecular Biology. 167208. PMID 34418423 DOI: 10.1016/j.jmb.2021.167208 |
0.27 |
|
2021 |
Kar M, Posey AE, Dar F, Hyman AA, Pappu RV. Glycine-Rich Peptides from FUS Have an Intrinsic Ability to Self-Assemble into Fibers and Networked Fibrils. Biochemistry. PMID 34648275 DOI: 10.1021/acs.biochem.1c00501 |
0.269 |
|
2009 |
Pappu RV, Nussinov R. Protein folding: lessons learned and new frontiers. Preface. Physical Biology. 6: 010301. PMID 19208944 DOI: 10.1088/1478-3975/6/1/010301 |
0.268 |
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2017 |
Harmon TS, Holehouse AS, Pappu RV. To Mix, or To Demix, That Is the Question. Biophysical Journal. 112: 565-567. PMID 28256216 DOI: 10.1016/J.Bpj.2016.12.031 |
0.258 |
|
2023 |
Farag M, Holehouse AS, Zeng X, Pappu RV. FIREBALL: A tool to fit protein phase diagrams based on mean-field theories for polymer solutions. Biophysical Journal. PMID 37161095 DOI: 10.1016/j.bpj.2023.05.007 |
0.257 |
|
2017 |
Ruff KM, Warner JB, Posey AE, Siong Tan P, Lemke EA, Pappu RV, Lashuel HA. Polyglutamine Length Dependent Structural Properties and Phase Behavior of Huntingtin Exon 1 Biophysical Journal. 112: 511a. DOI: 10.1016/J.Bpj.2016.11.2762 |
0.254 |
|
2019 |
Posey AE, Holehouse AS, Ruff KM, Pappu RV. Experimental and Theoretical Methods for Mapping Coexistence Curves of Phase-Separating Biological Macromolecules Biophysical Journal. 116: 349a. DOI: 10.1016/J.Bpj.2018.11.1901 |
0.253 |
|
2013 |
Dunker AK, Babu MM, Barbar E, Blackledge M, Bondos SE, Dosztányi Z, Dyson HJ, Forman-Kay J, Fuxreiter M, Gsponer J, Han KH, Jones DT, Longhi S, Metallo SJ, Nishikawa K, ... ... Pappu RV, et al. What's in a name? Why these proteins are intrinsically disordered: Why these proteins are intrinsically disordered. Intrinsically Disordered Proteins. 1: e24157. PMID 28516007 DOI: 10.4161/idp.24157 |
0.253 |
|
2014 |
Tubbs AT, Dorsett Y, Chan E, Helmink B, Lee BS, Hung P, George R, Bredemeyer AL, Mittal A, Pappu RV, Chowdhury D, Mosammaparast N, Krangel MS, Sleckman BP. KAP-1 promotes resection of broken DNA ends not protected by γ-H2AX and 53BP1 in G₁-phase lymphocytes. Molecular and Cellular Biology. 34: 2811-21. PMID 24842905 DOI: 10.1128/Mcb.00441-14 |
0.251 |
|
2022 |
Shinn MK, Cohan MC, Bullock JL, Ruff KM, Levin PA, Pappu RV. Connecting sequence features within the disordered C-terminal linker of FtsZ to functions and bacterial cell division. Proceedings of the National Academy of Sciences of the United States of America. 119: e2211178119. PMID 36215496 DOI: 10.1073/pnas.2211178119 |
0.25 |
|
2023 |
Farag M, Holehouse AS, Zeng X, Pappu RV. FIREBALL: A tool to fit protein phase diagrams based on mean-field theories for polymer solutions. Biorxiv : the Preprint Server For Biology. PMID 36993371 DOI: 10.1101/2023.03.19.533322 |
0.249 |
|
2021 |
Posey AE, Ruff KM, Lalmansingh JM, Kandola TS, Lange JJ, Halfmann R, Pappu RV. Mechanistic inferences from analysis of measurements of protein phase transitions in live cells. Journal of Molecular Biology. 166848. PMID 33539877 DOI: 10.1016/j.jmb.2021.166848 |
0.244 |
|
2023 |
Fossat MJ, Posey AE, Pappu RV. Uncovering the Contributions of Charge Regulation to the Stability of Single Alpha Helices. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. e202200746. PMID 36599672 DOI: 10.1002/cphc.202200746 |
0.236 |
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2020 |
Lazar T, Martínez-Pérez E, Quaglia F, Hatos A, Chemes LB, Iserte JA, Méndez NA, Garrone NA, Saldaño TE, Marchetti J, Rueda AJV, Bernadó P, Blackledge M, Cordeiro TN, Fagerberg E, ... ... Pappu RV, et al. PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins. Nucleic Acids Research. PMID 33305318 DOI: 10.1093/nar/gkaa1021 |
0.234 |
|
2020 |
Ruff KM, Dar F, Posey AE, Pappu RV. Principles of Ligand Modulation of Phase Behavior in Multicomponent Systems Biophysical Journal. 118: 371a. DOI: 10.1016/J.Bpj.2019.11.2126 |
0.231 |
|
2022 |
Seim I, Posey AE, Snead WT, Stormo BM, Klotsa D, Pappu RV, Gladfelter AS. Dilute phase oligomerization can oppose phase separation and modulate material properties of a ribonucleoprotein condensate. Proceedings of the National Academy of Sciences of the United States of America. 119: e2120799119. PMID 35333653 DOI: 10.1073/pnas.2120799119 |
0.229 |
|
2021 |
Fossat MJ, Zeng X, Pappu RV. Uncovering Differences in Hydration Free Energies and Structures for Model Compound Mimics of Charged Side Chains of Amino Acids. The Journal of Physical Chemistry. B. 125: 4148-4161. PMID 33877835 DOI: 10.1021/acs.jpcb.1c01073 |
0.228 |
|
2023 |
Pappu RV, Cohen SR, Dar F, Farag M, Kar M. Phase Transitions of Associative Biomacromolecules. Chemical Reviews. PMID 36881934 DOI: 10.1021/acs.chemrev.2c00814 |
0.228 |
|
2014 |
Xu W, Edwards MR, Borek DM, Feagins AR, Mittal A, Alinger JB, Berry KN, Yen B, Hamilton J, Brett TJ, Pappu RV, Leung DW, Basler CF, Amarasinghe GK. Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of phosphorylated STAT1. Cell Host & Microbe. 16: 187-200. PMID 25121748 DOI: 10.1016/J.Chom.2014.07.008 |
0.227 |
|
2021 |
Cohan MC, Shinn MK, Lalmansingh JM, Pappu RV. Uncovering Non-random Binary Patterns Within Sequences of Intrinsically Disordered Proteins. Journal of Molecular Biology. 434: 167373. PMID 34863777 DOI: 10.1016/j.jmb.2021.167373 |
0.223 |
|
2011 |
Thomas DG, Pappu RV, Baker NA. NanoParticle Ontology for cancer nanotechnology research. Journal of Biomedical Informatics. 44: 59-74. PMID 20211274 DOI: 10.1016/J.Jbi.2010.03.001 |
0.221 |
|
2018 |
Boothby TC, Piszkiewicz S, Mehta A, Brozena A, Tapia H, Koshland D, Holehouse A, Pappu R, Goldstein B, Pielak G. Gelation and Vitrification of Tardigrade IDPs Biophysical Journal. 114: 560a-561a. DOI: 10.1016/J.Bpj.2017.11.3065 |
0.219 |
|
2023 |
Zeng X, Pappu RV. Developments in describing equilibrium phase transitions of multivalent associative macromolecules. Current Opinion in Structural Biology. 79: 102540. PMID 36804705 DOI: 10.1016/j.sbi.2023.102540 |
0.218 |
|
2021 |
Bremer A, Farag M, Borcherds WM, Peran I, Martin EW, Pappu RV, Mittag T. Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains. Nature Chemistry. 14: 196-207. PMID 34931046 DOI: 10.1038/s41557-021-00840-w |
0.217 |
|
2019 |
Pappu RV. Decision letter: Ion counting demonstrates a high electrostatic field generated by the nucleosome Elife. DOI: 10.7554/Elife.44993.019 |
0.212 |
|
2023 |
Kar M, Vogel LT, Chauhan G, Ausserwöger H, Welsh TJ, Kamath AR, Knowles TPJ, Hyman AA, Seidel CAM, Pappu RV. Glutamate helps unmask the differences in driving forces for phase separation versus clustering of FET family proteins in sub-saturated solutions. Research Square. PMID 37790538 DOI: 10.21203/rs.3.rs-3252197/v1 |
0.211 |
|
2023 |
Kar M, Vogel LT, Chauhan G, Ausserwöger H, Welsh TJ, Kamath AR, Knowles TPJ, Hyman AA, Seidel CAM, Pappu RV. Glutamate helps unmask the differences in driving forces for phase separation versus clustering of FET family proteins in sub-saturated solutions. Biorxiv : the Preprint Server For Biology. PMID 37609232 DOI: 10.1101/2023.08.11.552963 |
0.211 |
|
2021 |
Fossat MJ, Posey AE, Pappu RV. Quantifying charge state heterogeneity for proteins with multiple ionizable residues. Biophysical Journal. 120: 5438-5453. PMID 34826385 DOI: 10.1016/j.bpj.2021.11.2886 |
0.208 |
|
2018 |
Roberts S, Harmon TS, Schaal JL, Miao V, Li KJ, Hunt A, Wen Y, Oas TG, Collier JH, Pappu RV, Chilkoti A. Author Correction: Injectable tissue integrating networks from recombinant polypeptides with tunable order. Nature Materials. PMID 30382194 DOI: 10.1038/S41563-018-0233-Z |
0.201 |
|
2022 |
Kar M, Dar F, Welsh TJ, Vogel LT, Kühnemuth R, Majumdar A, Krainer G, Franzmann TM, Alberti S, Seidel CAM, Knowles TPJ, Hyman AA, Pappu RV. Phase-separating RNA-binding proteins form heterogeneous distributions of clusters in subsaturated solutions. Proceedings of the National Academy of Sciences of the United States of America. 119: e2202222119. PMID 35787038 DOI: 10.1073/pnas.2202222119 |
0.198 |
|
2023 |
Dai Y, Farag M, Lee D, Zeng X, Kim K, Son HI, Guo X, Su J, Peterson N, Mohammed J, Ney M, Shapiro DM, Pappu RV, Chilkoti A, You L. Programmable synthetic biomolecular condensates for cellular control. Nature Chemical Biology. PMID 36747054 DOI: 10.1038/s41589-022-01252-8 |
0.194 |
|
2021 |
Bergeron-Sandoval LP, Kumar S, Heris HK, Chang CLA, Cornell CE, Keller SL, François P, Hendricks AG, Ehrlicher AJ, Pappu RV, Michnick SW. Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34887356 DOI: 10.1073/pnas.2113789118 |
0.19 |
|
2023 |
Chauhan G, Bremer A, Dar F, Mittag T, Pappu RV. Crowder titrations enable the quantification of driving forces for macromolecular phase separation. Biophysical Journal. PMID 37717144 DOI: 10.1016/j.bpj.2023.09.006 |
0.179 |
|
2022 |
Mittag T, Pappu RV. A conceptual framework for understanding phase separation and addressing open questions and challenges. Molecular Cell. 82: 2201-2214. PMID 35675815 DOI: 10.1016/j.molcel.2022.05.018 |
0.178 |
|
2023 |
Chauhan G, Bremer A, Dar F, Mittag T, Pappu RV. Crowder titrations enable the quantification of driving forces for macromolecular phase separation. Biorxiv : the Preprint Server For Biology. PMID 37461587 DOI: 10.1101/2023.07.03.547544 |
0.177 |
|
2009 |
Thomas D, Pappu R, Baker N. NPO: Ontology for Cancer Nanotechnology Research Nature Precedings. 4: 1-1. DOI: 10.1038/Npre.2009.3514.1 |
0.169 |
|
2020 |
Mathieu C, Pappu RV, Taylor JP. Beyond aggregation: Pathological phase transitions in neurodegenerative disease. Science (New York, N.Y.). 370: 56-60. PMID 33004511 DOI: 10.1126/science.abb8032 |
0.168 |
|
2022 |
Staller MV, Ramirez E, Kotha SR, Holehouse AS, Pappu RV, Cohen BA. Directed mutational scanning reveals a balance between acidic and hydrophobic residues in strong human activation domains. Cell Systems. PMID 35120642 DOI: 10.1016/j.cels.2022.01.002 |
0.166 |
|
2023 |
Pappu R, Lin A, Ruff K, Jalihal A, Dar F, King M, Lalmansingh J, Posey A, Seim I, Gladfelter A. Dynamical control enables the formation of demixed biomolecular condensates. Research Square. PMID 36798397 DOI: 10.21203/rs.3.rs-2440278/v1 |
0.16 |
|
2023 |
Lin AZ, Ruff KM, Jalihal A, Dar F, King MR, Lalmansingh JM, Posey AE, Seim I, Gladfelter AS, Pappu RV. Dynamical control enables the formation of demixed biomolecular condensates. Biorxiv : the Preprint Server For Biology. PMID 36711465 DOI: 10.1101/2023.01.04.522702 |
0.16 |
|
2022 |
Bremer A, Posey AE, Borgia MB, Borcherds WM, Farag M, Pappu RV, Mittag T. Quantifying Coexistence Concentrations in Multi-Component Phase-Separating Systems Using Analytical HPLC. Biomolecules. 12. PMID 36291688 DOI: 10.3390/biom12101480 |
0.158 |
|
2022 |
Feric M, Sarfallah A, Dar F, Temiakov D, Pappu RV, Misteli T. Mesoscale structure-function relationships in mitochondrial transcriptional condensates. Proceedings of the National Academy of Sciences of the United States of America. 119: e2207303119. PMID 36191226 DOI: 10.1073/pnas.2207303119 |
0.156 |
|
2023 |
Alshareedah I, Borcherds WM, Cohen SR, Farag M, Singh A, Bremer A, Pappu RV, Mittag T, Banerjee PR. Sequence-encoded grammars determine material properties and physical aging of protein condensates. Biorxiv : the Preprint Server For Biology. PMID 37066350 DOI: 10.1101/2023.04.06.535902 |
0.149 |
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2023 |
Wu T, King MR, Farag M, Pappu RV, Lew MD. Single fluorogen imaging reveals spatial inhomogeneities within biomolecular condensates. Biorxiv : the Preprint Server For Biology. PMID 36747818 DOI: 10.1101/2023.01.26.525727 |
0.145 |
|
2021 |
Ruff KM, Dar F, Pappu RV. Ligand effects on phase separation of multivalent macromolecules. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33653957 DOI: 10.1073/pnas.2017184118 |
0.143 |
|
2021 |
Kahn JD, Lemke EA, Pappu RV. Faces, facets, and functions of biomolecular condensates driven by multivalent proteins and nucleic acids. Biophysical Journal. PMID 33730551 DOI: 10.1016/j.bpj.2021.03.003 |
0.136 |
|
2023 |
Wadsworth GM, Zahurancik WJ, Zeng X, Pullara P, Lai LB, Sidharthan V, Pappu RV, Gopalan V, Banerjee PR. RNAs undergo phase transitions with lower critical solution temperatures. Nature Chemistry. PMID 37932412 DOI: 10.1038/s41557-023-01353-4 |
0.132 |
|
2021 |
Ruff KM, Dar F, Pappu RV. Polyphasic linkage and the impact of ligand binding on the regulation of biomolecular condensates. Biophysics Reviews. 2: 021302. PMID 34179888 DOI: 10.1063/5.0050059 |
0.121 |
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2024 |
Das T, Zaidi F, Farag M, Ruff KM, Messing J, Taylor JP, Pappu RV, Mittag T. Metastable condensates suppress conversion to amyloid fibrils. Biorxiv : the Preprint Server For Biology. PMID 38464104 DOI: 10.1101/2024.02.28.582569 |
0.12 |
|
2024 |
King MR, Ruff KM, Pappu RV. Emergent microenvironments of nucleoli. Nucleus (Austin, Tex.). 15: 2319957. PMID 38443761 DOI: 10.1080/19491034.2024.2319957 |
0.12 |
|
2024 |
Aguilar Pérez G, Pappu RV, Milovanovic D. Tear down this wall: phosphorylation regulates the internal interfaces of postsynaptic condensates. Trends in Cell Biology. PMID 38429121 DOI: 10.1016/j.tcb.2024.02.007 |
0.12 |
|
2023 |
Lin AZ, Ruff KM, Dar F, Jalihal A, King MR, Lalmansingh JM, Posey AE, Erkamp NA, Seim I, Gladfelter AS, Pappu RV. Dynamical control enables the formation of demixed biomolecular condensates. Nature Communications. 14: 7678. PMID 37996438 DOI: 10.1038/s41467-023-43489-4 |
0.11 |
|
2020 |
Pappu RV. Phase Separation-A Physical Mechanism for Organizing Information and Biochemical Reactions. Developmental Cell. 55: 1-3. PMID 33049210 DOI: 10.1016/j.devcel.2020.09.023 |
0.083 |
|
2021 |
Keating CD, Pappu RV. Liquid-Liquid Phase Separation: A Widespread and Versatile Way to Organize Aqueous Solutions. The Journal of Physical Chemistry Letters. 12: 10994-10995. PMID 34788997 DOI: 10.1021/acs.jpclett.1c03352 |
0.079 |
|
2021 |
Keating CD, Pappu RV. Liquid-Liquid Phase Separation: A Widespread and Versatile Way to Organize Aqueous Solutions. The Journal of Physical Chemistry. B. 125: 12399-12400. PMID 34788996 DOI: 10.1021/acs.jpcb.1c08831 |
0.079 |
|
2023 |
Shinn MK, Pappu RV. Soaping up transcriptional condensates. Developmental Cell. 58: 915-916. PMID 37279696 DOI: 10.1016/j.devcel.2023.05.002 |
0.062 |
|
2009 |
Thomas DG, Pappu RV, Baker NA. Ontologies for cancer nanotechnology research. Conference Proceedings : ... Annual International Conference of the Ieee Engineering in Medicine and Biology Society. Ieee Engineering in Medicine and Biology Society. Annual Conference. 2009: 4158-61. PMID 19964619 DOI: 10.1109/IEMBS.2009.5333941 |
0.06 |
|
2021 |
Lorenzini M, Burel S, Lesage A, Wagner E, Charrière C, Chevillard PM, Evrard B, Maloney D, Ruff KM, Pappu RV, Wagner S, Nerbonne JM, Silva JR, Townsend RR, Maier LS, et al. Proteomic and functional mapping of cardiac NaV1.5 channel phosphorylation sites. The Journal of General Physiology. 153. PMID 33410863 DOI: 10.1085/jgp.202012646 |
0.047 |
|
1973 |
Pappu RV, Boothroyd AR. Memory behavior of metal-plasma-anodized Al2O3 and SiO2-semiconductor (MAOS) capacitors Applied Physics Letters. 22: 72-74. DOI: 10.1063/1.1654561 |
0.036 |
|
1978 |
Pappu RV, Harris E, Yates M. Screening methods and experience with MOS memory Microelectronics Reliability. 17: 193-199. DOI: 10.1016/0026-2714(78)91154-X |
0.034 |
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Hide low-probability matches. |