Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry

ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB

Maier, J., Martinez, C., Kasavajhala, K., Wickstrom, L., Hauser, K., & Simmerling, C. L. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00255 · Cited by 10,971 · see citing works

CHARMM36m: An Improved Force Field for Folded and Intrinsically Disordered Proteins

Huang, J., Rauscher, S., Nawrocki, G., Ran, T., Feig, M., de Groot, B. L., Grubmüller, H., & MacKerell, A. (2016) · Nature Methods · doi:10.1038/nmeth.4067 · Cited by 6,708 · see citing works

Biomolecular condensates: organizers of cellular biochemistry

Banani, S. F., Lee, H. O., Hyman, A., & Rosen, M. (2017) · Nature reviews. Molecular cell biology · doi:10.1038/nrm.2017.7 · Cited by 5,574 · see citing works

A theory of the linear viscoelastic properties of dilute solutions of coiling polymers

Rouse, P. E. (1953) · The Journal of Chemical Physics · doi:10.1063/1.1699180 · Cited by 4,203 · see citing works

Liquid phase condensation in cell physiology and disease

Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,184 · see citing works

Thermodynamics of High Polymer Solutions

Flory, P., & Krigbaum, W. R. (1941) · The Journal of Chemical Physics · doi:10.1063/1.1723621 · Cited by 4,126 · see citing works

Intrinsically unstructured proteins and their functions

Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871 · see citing works

Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity

Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777 · see citing works

Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation

Brangwynne, C. P., Eckmann, C. R., Courson, D. S., Rybarska, A., Hoege, C., Gharakhani, J., Jülicher, F., & Hyman, A. A. (2009) · Science · doi:10.1126/science.1172046 · Cited by 3,215 · see citing works

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · see citing works

Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates

Alberti, S., Gladfelter, A., & Mittag, T. (2019) · Cell · doi:10.1016/j.cell.2018.12.035 · Cited by 2,856 · see citing works

OPLS3: A Force Field Providing Broad Coverage of Drug-like Small Molecules and Proteins.

Harder, E. D., Damm, W., Maple, J., Wu, C., Reboul, M., Xiang, J.-Y., Wang, L.-L., Lupyan, D., Dahlgren, M. K., Knight, J. L., et al. (2016) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00864 · Cited by 2,826 · see citing works

Cyclic GMP-AMP Is an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA

Wu, J., Sun, L., Chen, X., Du, F., Shi, H., Chen, C., & Chen, Z. J. (2012) · Science · doi:10.1126/science.1229963 · Cited by 2,574 · see citing works

Classification of Intrinsically Disordered Regions and Proteins

van der Lee, R., Buljan, M., Lang, B., Weatheritt, R. J., Daughdrill, G. W., Dunker, A. K., Fuxreiter, M., Gough, J., Gsponer, J., Jones, D. T., et al. (2014) · Chemical Reviews · doi:10.1021/cr400525m · Cited by 2,155 · see citing works

Dynamic light scattering: a practical guide and applications in biomedical sciences

Stetefeld, J., McKenna, S. A., & Patel, T. R. (2016) · Biophysical Reviews · doi:10.1007/s12551-016-0218-6 · Cited by 2,058 · see citing works

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012 · see citing works

Protein Phase Separation: A New Phase in Cell Biology

Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 1,954 · see citing works

A molecular grammar governing the driving forces for phase separation of prion-like RNA binding proteins

Wang, J., Choi, J.-M., Holehouse, A., Lee, H. O., Zhang, X., Jahnel, M., Maharana, S., Lemaitre, R., Pozniakovsky, A., Drechsel, D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.06.006 · Cited by 1,876 · see citing works

Phase separation drives heterochromatin domain formation

Strom, A. R., Emelyanov, A. V., Mir, M., Fyodorov, D. V., Darzacq, X., & Karpen, G. H. (2017) · Nature · doi:10.1038/nature22989 · Cited by 1,813 · see citing works

Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles

Nott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803 · see citing works

Coexisting liquid phases underlie nucleolar sub-compartments

Feric, M., Vaidya, N., Harmon, T., Mitrea, D. M., Zhu, L., Richardson, T. M., Kriwacki, R., Pappu, R., & Brangwynne, C. (2016) · Cell · doi:10.1016/j.cell.2016.04.047 · Cited by 1,798 · see citing works

Thermodynamic Fluctuations in a Reacting System—Measurement by Fluorescence Correlation Spectroscopy

Magde, D., Elson, E., & Webb, W. W. (1972) · Physical Review Letters · doi:10.1103/physrevlett.29.705 · Cited by 1,773 · see citing works

A Phase Separation Model for Transcriptional Control

Hnisz, D., Shrinivas, K., Young, R. A., Chakraborty, A. K., & Sharp, P. A. (2017) · Cell · doi:10.1016/j.cell.2017.02.007 · Cited by 1,753 · see citing works

Principles and Properties of Stress Granules

Protter, D. S. W., & Parker, R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.05.004 · Cited by 1,738 · see citing works

Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins

Lin, Y., Protter, D. S. W., Rosen, M. K., & Parker, R. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.018 · Cited by 1,594 · see citing works

Fluorescence correlation spectroscopy. II. An experimental realization

Magde, D., Elson, E. L., & Webb, W. W. (1974) · Biopolymers · doi:10.1002/bip.1974.360130103 · Cited by 1,515 · see citing works

Fluorescence correlation spectroscopy. I. Conceptual basis and theory

Elson, E. L., & Magde, D. (1974) · Biopolymers · doi:10.1002/bip.1974.360130102 · Cited by 1,436 · see citing works

Polymer physics of intracellular phase transitions

Brangwynne, C., Tompa, P., & Pappu, R. (2015) · Nature Physics · doi:10.1038/nphys3532 · Cited by 1,415 · see citing works

P bodies and the control of mRNA translation and degradation

Parker, R., & Sheth, U. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.011 · Cited by 1,335 · see citing works

Coupling of folding and binding for unstructured proteins

Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327 · see citing works

The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics

Elbaum-Garfinkle, S., Kim, Y., Szczepaniak, K., Chen, C. C.-H., Eckmann, C. R., Myong, S., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504822112 · Cited by 1,278 · see citing works

Valence and patterning of aromatic residues determine the phase behavior of prion-like domains

Martin, E. W., Holehouse, A. S., Peran, I., Farag, M., Incicco, J. J., Bremer, A., Grace, C. R., Soranno, A., Pappu, R. V., & Mittag, T. (2020) · Science · doi:10.1126/science.aaw8653 · Cited by 1,147 · see citing works

Tau protein liquid–liquid phase separation can initiate tau aggregation

Wegmann, S., Eftekharzadeh, B., Tepper, K., Zoltowska, K. M., Bennett, R. E., Dujardin, S., Laskowski, P. R., MacKenzie, D., Kamath, T., Commins, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798049 · Cited by 1,102 · see citing works

Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions

Tompa, P., & Fuxreiter, M. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.10.003 · Cited by 1,080 · see citing works

DNA-induced liquid phase condensation of cGAS activates innate immune signaling

Du, M., & Chen, Z. J. (2018) · Science · doi:10.1126/science.aat1022 · Cited by 1,068 · see citing works

Developing a molecular dynamics force field for both folded and disordered protein states

Robustelli, P., Piana, S., & Shaw, D. E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800690115 · Cited by 1,047 · see citing works

Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins

Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., & Gronenborn, A. M. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00168a070 · Cited by 1,046 · see citing works

Some Properties of Solutions of Long-chain Compounds.

Huggins, M. (1942) · The Journal of Physical Chemistry · doi:10.1021/j150415a018 · Cited by 1,043 · see citing works

Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

Das, R. K., & Pappu, R. V. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304749110 · Cited by 1,008 · see citing works

Speeding molecular recognition by using the folding funnel: The fly-casting mechanism

Shoemaker, B. A., Portman, J. J., & Wolynes, P. G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160259697 · Cited by 971 · see citing works

P bodies: at the crossroads of post-transcriptional pathways

Eulálio, A., Behm‐Ansmant, I., & Izaurralde, E. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2080 · Cited by 939 · see citing works

Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II

Burke, K. A., Janke, A. M., Rhine, C. L., & Fawzi, N. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.006 · Cited by 932 · see citing works

Folding dynamics and mechanism of β-hairpin formation

Muñoz, V., Thompson, P. A., Hofrichter, J., & Eaton, W. A. (1997) · Nature · doi:10.1038/36626 · Cited by 929 · see citing works

Stress granules as crucibles of ALS pathogenesis

Li, Y. R., King, O. D., Shorter, J., & Gitler, A. D. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302044 · Cited by 913 · see citing works

Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response

Riback, J. A., Katanski, C. D., Kear‐Scott, J. L., Pilipenko, E. V., Rojek, A. E., Sosnick, T. R., & Drummond, D. A. (2017) · Cell · doi:10.1016/j.cell.2017.02.027 · Cited by 913 · see citing works

A framework for understanding the functions of biomolecular condensates across scales

Lyon, A. S., Peeples, W. B., & Rosen, M. K. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00303-z · Cited by 895 · see citing works

Statistical Thermodynamics of Chain Molecule Liquids. I. An Equation of State for Normal Paraffin Hydrocarbons

Flory, P. J., Orwoll, R. A., & Vrij, A. (1964) · Journal of the American Chemical Society · doi:10.1021/ja01071a023 · Cited by 892 · see citing works

NMR Characterization of the Dynamics of Biomacromolecules

Palmer, A. G. I. (2004) · Chemical Reviews · doi:10.1021/cr030413t · Cited by 889 · see citing works

α‐Synuclein aggregation nucleates through liquid‐liquid phase separation

Ray, S., Singh, N., Kumar, R., Patel, K., Pandey, S., Datta, D., Mahato, J., Panigrahi, R., Navalkar, A., Mehra, S., et al. (2020) · Nature Chemistry · doi:10.1038/s41557-020-0465-9 · Cited by 863 · see citing works

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain

Conicella, A. E., Zerze, G. H., Mittal, J., & Fawzi, N. L. (2016) · Structure · doi:10.1016/j.str.2016.07.007 · Cited by 860 · see citing works

Improved Peptide and Protein Torsional Energetics with the OPLS-AA Force Field

Robertson, M. J., Tirado‐Rives, J., & Jorgensen, W. L. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00356 · Cited by 858 · see citing works

Water Dispersion Interactions Strongly Influence Simulated Structural Properties of Disordered Protein States

Piana, S., Donchev, A., Robustelli, P., & Shaw, D. E. (2015) · The Journal of Physical Chemistry B · doi:10.1021/jp508971m · Cited by 855 · see citing works

Liquid–Liquid Phase Separation in Disease

Alberti, S., & Dormann, D. (2019) · Annual Review of Genetics · doi:10.1146/annurev-genet-112618-043527 · Cited by 849 · see citing works

ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function

Murakami, T., Qamar, S., Lin, J. Q., Schierle, G. S. K., Rees, E. J., Miyashita, A., Costa, A. R., Dodd, R. B., Chan, F. T. S., Michel, C. H., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.10.030 · Cited by 848 · see citing works

Optimized Molecular Dynamics Force Fields Applied to the Helix−Coil Transition of Polypeptides

Best, R. B., & Hummer, G. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp901540t · Cited by 836 · see citing works

The protein folding ‘speed limit’

Kubelka, J., Hofrichter, J., & Eaton, W. A. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.01.013 · Cited by 832 · see citing works

Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821 · see citing works

Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

Ambadipudi, S., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00480-0 · Cited by 782 · see citing works

The molecular language of membraneless organelles

Gomes, E., & Shorter, J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.001192 · Cited by 763 · see citing works

Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein

Pak, C. W., Kosno, M., Holehouse, A., Padrick, S., Mittal, A., Ali, R., Yunus, A., Liu, D. R., Pappu, R., & Rosen, M. (2016) · Molecules and Cells · doi:10.1016/j.molcel.2016.05.042 · Cited by 747 · see citing works

Phase separation of a yeast prion protein promotes cellular fitness

Franzmann, T. M., Jahnel, M., Pozniakovsky, A., Mahamid, J., Holehouse, A. S., Nüske, E., Richter, D., Baumeister, W. P., Grill, S. W., Pappu, R. V., et al. (2018) · Science · doi:10.1126/science.aao5654 · Cited by 741 · see citing works

RNA Controls PolyQ Protein Phase Transitions

Zhang, H., Elbaum‐Garfinkle, S., Langdon, E. M., Taylor, N. O., Occhipinti, P., Bridges, A. A., Brangwynne, C. P., & Gladfelter, A. S. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.017 · Cited by 712 · see citing works

Intrinsically disordered proteins in overcrowded milieu: Membrane-less organelles, phase separation, and intrinsic disorder

Uversky, V. N. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.10.015 · Cited by 707 · see citing works

Random-coil behavior and the dimensions of chemically unfolded proteins

Kohn, J. E., Millett, I. S., Jacob, J., Žagrović, B., Dillon, T. M., Cingel, N., Dothager, R. S., Seifert, S., Thiyagarajan, P., Sosnick, T. R., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403643101 · Cited by 706 · see citing works

Molecular interactions underlying liquid‐liquid phase separation of the FUS low‐complexity domain

Murthy, A. C., Dignon, G. L., Kan, Y., Zerze, G. H., Parekh, S. H., Mittal, J., & Fawzi, N. L. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0250-x · Cited by 698 · see citing works

The Centrosome Is a Selective Condensate that Nucleates Microtubules by Concentrating Tubulin

Woodruff, J. B., Gomes, B. F., Widlund, P. O., Mahamid, J., Honigmann, A., & Hyman, A. A. (2017) · Cell · doi:10.1016/j.cell.2017.05.028 · Cited by 685 · see citing works

Mammalian Stress Granules and Processing Bodies

Kedersha, N., & Anderson, P. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)31005-7 · Cited by 664 · see citing works

Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation

Hofweber, M., Hutten, S., Bourgeois, B. M. R., Spreitzer, E., Niedner, A., Schifferer, M., Ruepp, M., Simons, M., Niessing, D., Madl, T., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.004 · Cited by 654 · see citing works

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652 · see citing works

Unfolded Proteins and Protein Folding Studied by NMR

Dyson, H. J., & Wright, P. E. (2004) · Chemical Reviews · doi:10.1021/cr030403s · Cited by 628 · see citing works

Phase separation in polyelectrolyte solutions. Theory of complex coacervation

Overbeek, J. T. G., & Voorn, M. J. (1957) · Journal of Cellular and Comparative Physiology · doi:10.1002/jcp.1030490404 · Cited by 626 · see citing works

Sequence determinants of protein phase behavior from a coarse-grained model

Dignon, G., Zheng, W.-W., Kim, Y. C., Best, R., & Mittal, J. (2017) · bioRxiv · doi:10.1371/journal.pcbi.1005941 · Cited by 621 · see citing works

Long-Range Interactions Within a Nonnative Protein

Klein‐Seetharaman, J., Oikawa, M., Grimshaw, S. B., Wirmer, J., Duchardt, E., Ueda, T., Imoto, T., Smith, L. J., Dobson, C. M., & Schwalbe, H. (2002) · Science · doi:10.1126/science.1067680 · Cited by 615 · see citing works

Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles

Wei, M.-T., Elbaum‐Garfinkle, S., Holehouse, A. S., Chen, C. C.-H., Feric, M., Arnold, C. B., Priestley, R. D., Pappu, R. V., & Brangwynne, C. P. (2017) · Nature Chemistry · doi:10.1038/nchem.2803 · Cited by 612 · see citing works

Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties

Dignon, G., Best, R., & Mittal, J. (2020) · Annual review of physical chemistry (Print) · doi:10.1146/annurev-physchem-071819-113553 · Cited by 599 · see citing works

Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose)

Altmeyer, M., Neelsen, K. J., Teloni, F., Pozdnyakova, I., Pellegrino, S., Grøfte, M., Rask, M., Streicher, W. W., Jungmichel, S., Nielsen, M. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms9088 · Cited by 581 · see citing works

Microtubule dynamics: an interplay of biochemistry and mechanics

Brouhard, G. J., & Rice, L. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0009-y · Cited by 569 · see citing works

Anton 2: Raising the Bar for Performance and Programmability in a Special-Purpose Molecular Dynamics Supercomputer

Shaw, D. E., Grossman, J. P., Bank, J. A., Batson, B., Butts, J. A., Chao, J. C., Deneroff, M. M., Dror, R., Even, A., Fenton, C. H., et al. (2014) · International Conference for High Performance Computing, Networking, Storage and Analysis · doi:10.1109/sc.2014.9 · Cited by 567 · see citing works

The plurifunctional nucleolus

Pederson, T. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.17.3871 · Cited by 536 · see citing works

Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation

Brady, J. P., Farber, P. J., Sekhar, A., Lin, Y., Huang, R., Bah, A., Nott, T. J., Chan, H. S., Baldwin, A. J., Forman-Kay, J. D., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706197114 · Cited by 534 · see citing works

RNA polymerase II clustering through carboxy-terminal domain phase separation

Boehning, M., Dugast-Darzacq, C., Rankovic, M., Hansen, A., Yu, T., Marie-Nelly, H., McSwiggen, D., Kokic, G., Dailey, G., Cramer, P., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0112-y · Cited by 528 · see citing works

Preformed structural elements feature in partner recognition by intrinsically unstructured proteins

Fuxreiter, M., Simon, I., Friedrich, P., & Tompa, P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.017 · Cited by 518 · see citing works

Assessing the accuracy of physical models used in protein-folding simulations: quantitative evidence from long molecular dynamics simulations

Piana, S., Klepeis, J. L., & Shaw, D. E. (2014) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.12.006 · Cited by 513 · see citing works

Partitioning of cancer therapeutics in nuclear condensates

Klein, I. A., Boija, A., Afeyan, L. K., Hawken, S. W., Fan, M., Dall’Agnese, A., Oksuz, O., Henninger, J. E., Shrinivas, K., Sabari, B. R., et al. (2020) · Science · doi:10.1126/science.aaz4427 · Cited by 508 · see citing works

The Cytosolic DNA Sensor cGAS Forms an Oligomeric Complex with DNA and Undergoes Switch-like Conformational Changes in the Activation Loop

Zhang, X., Wu, J., Du, F., Xu, H., Sun, L., Chen, Z., Brautigam, C. A., Zhang, X., & Chen, Z. J. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.01.003 · Cited by 505 · see citing works

Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)

Theillet, F., Binolfi, A., Frembgen-Kesner, T., Hingorani, K. S., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L. M., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 504 · see citing works

Phase separation and neurodegenerative diseases: a disturbance in the force

Zbinden, A., Pérez-Berlanga, M., De Rossi, P., & Polymenidou, M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.09.014 · Cited by 500 · see citing works

Precise Measurement of Diffusion Coefficients using Scanning Fluorescence Correlation Spectroscopy

Petrášek, Z., & Schwille, P. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.108811 · Cited by 498 · see citing works

Protein condensates as aging Maxwell fluids

Jawerth, L. M., Fischer‐Friedrich, E., Saha, S., Wang, J., Franzmann, T. M., Zhang, X., Sachweh, J., Ruer, M., Ijavi, M., Saha, S., et al. (2020) · Science · doi:10.1126/science.aaw4951 · Cited by 488 · see citing works

A decade and a half of protein intrinsic disorder: Biology still waits for physics

Uversky, V. (2013) · Protein Science · doi:10.1002/pro.2261 · Cited by 478 · see citing works

Coarse master equations for peptide folding dynamics

Buchete, N.-V., & Hummer, G. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp0761665 · Cited by 477 · see citing works

Spontaneous driving forces give rise to protein−RNA condensates with coexisting phases and complex material properties

Boeynaems, S., Holehouse, A. S., Weinhardt, V., Kovács, D., Lindt, J. V., Larabell, C. A., Bosch, L. V. D., Das, R., Tompa, P., Pappu, R. V., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821038116 · Cited by 460 · see citing works

Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein Folding

Yang, D., & Kay, L. E. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0581 · Cited by 459 · see citing works

Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates

Savastano, A., de Opakua, A. I., Rankovic, M., & Zweckstetter, M. (2020) · Nature Communications · doi:10.1038/s41467-020-19843-1 · Cited by 418 · see citing works

Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation

Ryan, V. H., Dignon, G. L., Zerze, G. H., Chabata, C. V., Silva, R., Conicella, A. E., Amaya, J., Burke, K. A., Mittal, J., & Fawzi, N. L. (2018) · Molecular Cell · doi:10.1016/j.molcel.2017.12.022 · Cited by 417 · see citing works

Structural Ensembles of Intrinsically Disordered Proteins Depend Strongly on Force Field: A Comparison to Experiment

Rauscher, S., Gapsys, V., Gajda, M. J., Zweckstetter, M., de Groot, B. L., & Grubmüller, H. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00736 · Cited by 408 · see citing works

Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties

Tesei, G., Schulze, T. K., Crehuet, R., & Lindorff‐Larsen, K. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2111696118 · Cited by 407 · see citing works

The Eukaryotic CO2-Concentrating Organelle Is Liquid-like and Exhibits Dynamic Reorganization

Rosenzweig, E. S. F., Xu, B., Cuellar, L. K., Martínez-Sánchez, A., Schaffer, M., Strauss, M., Cartwright, H. N., Ronceray, P., Plitzko, J. M., Förster, F. G., et al. (2017) · Cell · doi:10.1016/j.cell.2017.08.008 · Cited by 402 · see citing works

Local Nucleation of Microtubule Bundles through Tubulin Concentration into a Condensed Tau Phase

Hernández-Vega, A., Braun, M., Scharrel, L., Jahnel, M., Wegmann, S., Hyman, B. T., Alberti, S., Diez, S., & Hyman, A. A. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.042 · Cited by 395 · see citing works

To be or not to be in the nucleolus

Carmo‐Fonseca, M., Mendes-Soares, L., & Campos, I. (2000) · Nature Cell Biology · doi:10.1038/35014078 · Cited by 384 · see citing works

Membraneless organelles can melt nucleic acid duplexes and act as biomolecular filters

Nott, T. J., Craggs, T. D., & Baldwin, A. J. (2016) · Nature Chemistry · doi:10.1038/nchem.2519 · Cited by 382 · see citing works

TDP-43 α-helical structure tunes liquid–liquid phase separation and function

Conicella, A. E., Dignon, G. L., Zerze, G. H., Schmidt, H. B., D’Ordine, A. M., Kim, Y. C., Rohatgi, R., Ayala, Y. M., Mittal, J., & Fawzi, N. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912055117 · Cited by 376 · see citing works

Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding

Eliezer, D., Yao, J. S., Dyson, H. J., & Wright, P. E. (1998) · Nature Structural Biology · doi:10.1038/nsb0298-148 · Cited by 371 · see citing works

Genomic RNA Elements Drive Phase Separation of the SARS-CoV-2 Nucleocapsid

Iserman, C., Roden, C., Boerneke, M. A., Sealfon, R. S. G., McLaughlin, G. A., Jungreis, I., Fritch, E. J., Hou, Y. J., Ekena, J., Weidmann, C. A., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.041 · Cited by 371 · see citing works

Rotational brownian motion and fluorescence intensify fluctuations

Ehrenberg, M., & Rigler, R. W. (1974) · Chemical Physics · doi:10.1016/0301-0104(74)85005-6 · Cited by 367 · see citing works

CAJAL BODIES: A Long History of Discovery

Cioce, M., & Lamond, A. I. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.103738 · Cited by 359 · see citing works

Ultrafast dynamics of protein collapse from single-molecule photon statistics

Nettels, D., Gopich, I. V., Hoffmann, A., & Schuler, B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611093104 · Cited by 356 · see citing works

Characterization of the Dynamics of Biomacromolecules Using Rotating-Frame Spin Relaxation NMR Spectroscopy

Palmer, A. G. I., & Massi, F. (2006) · Chemical Reviews · doi:10.1021/cr0404287 · Cited by 355 · see citing works

Quantifying Dynamics in Phase-Separated Condensates Using Fluorescence Recovery after Photobleaching

Taylor, N. O., Wei, M.-T., Stone, H. A., & Brangwynne, C. P. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.08.030 · Cited by 354 · see citing works

ABSINTH: A new continuum solvation model for simulations of polypeptides in aqueous solutions

Vitalis, A., & Pappu, R. V. (2008) · Journal of Computational Chemistry · doi:10.1002/jcc.21005 · Cited by 349 · see citing works

SARS‐CoV‐2 nucleocapsid protein phase‐separates with RNA and with human hnRNPs

Perdikari, T. M., Murthy, A. C., Ryan, V. H., Watters, S., Naik, M. T., & Fawzi, N. L. (2020) · The EMBO Journal · doi:10.15252/embj.2020106478 · Cited by 345 · see citing works

Phosphoregulated FMRP phase separation models activity-dependent translation through bidirectional control of mRNA granule formation

Tsang, B., Arsenault, J., Vernon, R. M., Lin, H., Sonenberg, N., Wang, L., Bah, A., & Forman-Kay, J. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814385116 · Cited by 328 · see citing works

Identifying sequence perturbations to an intrinsically disordered protein that determine its phase-separation behavior

Schuster, B. S., Dignon, G. L., Tang, W. S., Kelley, F. M., Ranganath, A. K., Jahnke, C. N., Simpkins, A. G., Regy, R. M., Hammer, D. A., Good, M. C., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000223117 · Cited by 324 · see citing works

FUS and TDP-43 Phases in Health and Disease

Portz, B., Lee, B. L., & Shorter, J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.12.005 · Cited by 323 · see citing works

Balanced Protein–Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association

Best, R., Zheng, W.-W., & Mittal, J. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct500569b · Cited by 312 · see citing works

RNA stores tau reversibly in complex coacervates

Zhang, X., Lin, Y., Eschmann, N. A., Zhou, H., Rauch, J. N., Hernández, I., Guzman, E., Kosik, K. S., & Han, S. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2002183 · Cited by 308 · see citing works

Stress- and ubiquitylation-dependent phase separation of the proteasome

Yasuda, S., Tsuchiya, H., Kaiho, A., Guo, Q., Ikeuchi, K., Endo, A., Arai, N., Ohtake, F., Murata, S., Inada, T., et al. (2020) · Nature · doi:10.1038/s41586-020-1982-9 · Cited by 301 · see citing works

Exploring Free-Energy Landscapes of Intrinsically Disordered Proteins at Atomic Resolution Using NMR Spectroscopy

Jensen, M. R., Zweckstetter, M., Huang, J., & Blackledge, M. J. (2014) · Chemical Reviews · doi:10.1021/cr400688u · Cited by 298 · see citing works

Template-directed RNA polymerization and enhanced ribozyme catalysis inside membraneless compartments formed by coacervates

Poudyal, R. R., Guth-Metzler, R., Veenis, A. J., Frankel, E. A., Keating, C. D., & Bevilacqua, P. C. (2019) · Nature Communications · doi:10.1038/s41467-019-08353-4 · Cited by 298 · see citing works

Structural and Dynamical Properties of a Denatured Protein. Heteronuclear 3D NMR Experiments and Theoretical Simulations of Lysozyme in 8 M Urea

Schwalbe, H., Fiebig, K. M., Buck, M., Jones, J. A., Grimshaw, S. B., Spencer, A., Glaser, S. J., Smith, L. J., & Dobson, C. M. (1997) · Biochemistry · doi:10.1021/bi970049q · Cited by 292 · see citing works

Mouse Heterochromatin Adopts Digital Compaction States without Showing Hallmarks of HP1-Driven Liquid-Liquid Phase Separation

Erdel, F., Rademacher, A., Vlijm, R., Tünnermann, J., Frank, L., Weinmann, R., Schweigert, E., Yserentant, K., Hummert, J., Bauer, C., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.02.005 · Cited by 292 · see citing works

Phase Transitions of Spindle-Associated Protein Regulate Spindle Apparatus Assembly

Jiang, H., Wang, S., Huang, Y., He, X.-N., Cui, H., Zhu, X.-L., & Zheng, Y.-X. (2015) · Cell · doi:10.1016/j.cell.2015.08.010 · Cited by 291 · see citing works

Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions

Crick, S. L., Jayaraman, M., Frieden, C., Wetzel, R. B., & Pappu, R. V. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608175103 · Cited by 289 · see citing works

Liquid–Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation

Babinchak, W. M., & Surewicz, W. K. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.03.004 · Cited by 287 · see citing works

Molecular Dynamics Simulations of Intrinsically Disordered Proteins: Force Field Evaluation and Comparison with Experiment

Henriques, J., Cragnell, C., & Skepö, M. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/ct501178z · Cited by 265 · see citing works

Direct observation of structure and dynamics during phase separation of an elastomeric protein

Reichheld, S. E., Muiznieks, L. D., Keeley, F. W., & Sharpe, S. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701877114 · Cited by 265 · see citing works

Liquid network connectivity regulates the stability and composition of biomolecular condensates with many components

Espinosa, J. R., Joseph, J. A., Sanchez‐Burgos, I., Garaizar, A., Frenkel, D., & Collepardo‐Guevara, R. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917569117 · Cited by 262 · see citing works

Phase separation at the synapse

Chen, X., Wu, X., Wu, H., & Zhang, M. (2020) · Nature Neuroscience · doi:10.1038/s41593-019-0579-9 · Cited by 261 · see citing works

Comparative Analysis of Viscosity of Complex Liquids and Cytoplasm of Mammalian Cells at the Nanoscale

Kalwarczyk, T., Ziębacz, N., Bielejewska, A., Zaboklicka, E., Koynov, K., Szymański, J., Wilk, A., Patkowski, A., Gapiński, J., Butt, H., et al. (2011) · Nano Letters · doi:10.1021/nl2008218 · Cited by 256 · see citing works

Cajal Bodies, Nucleoli, and Speckles in the Xenopus Oocyte Nucleus Have a Low-Density, Sponge-like Structure

Handwerger, K. E., Cordero, J. A., & Gall, J. G. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0742 · Cited by 256 · see citing works

Residual Structure and Dynamics in Parkinson's Disease-associated Mutants of α-Synuclein

Bussell, R., & Eliezer, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106777200 · Cited by 253 · see citing works

Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells

König, I., Zarrine‐Afsar, A., Aznauryan, M. G., Soranno, A., Wunderlich, B., Dingfelder, F., Stüber, J. C., Plückthun, A., Nettels, D., & Schuler, B. (2015) · Nature Methods · doi:10.1038/nmeth.3475 · Cited by 250 · see citing works

Matter over mind: Liquid phase separation and neurodegeneration

Elbaum‐Garfinkle, S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.001188 · Cited by 244 · see citing works

Rubisco condensate formation by CcmM in β-carboxysome biogenesis

Wang, H., Yan, X., Aigner, H., Bracher, A., Nguyen, N. D., Hee, W. Y., Long, B. M., Price, G. D., Hartl, F. U., & Hayer-Hartl, M. K. (2019) · Nature · doi:10.1038/s41586-019-0880-5 · Cited by 242 · see citing works

New developments in force fields for biomolecular simulations

Nerenberg, P. S., & Head-Gordon, T. L. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.02.002 · Cited by 236 · see citing works

Phase separation of TPX2 enhances and spatially coordinates microtubule nucleation

King, M. R., & Petry, S. (2020) · Nature Communications · doi:10.1038/s41467-019-14087-0 · Cited by 230 · see citing works

Performance of Fluorescence Correlation Spectroscopy for Measuring Diffusion and Concentration

Enderlein, J., Gregor, I., Patra, D., Dertinger, T., & Kaupp, U. B. (2005) · ChemPhysChem · doi:10.1002/cphc.200500414 · Cited by 221 · see citing works

Molecular Details of Protein Condensates Probed by Microsecond Long Atomistic Simulations

Zheng, W., Dignon, G. L., Jovic, N., Xu, X., Regy, R. M., Fawzi, N. L., Kim, Y. C., Best, R. B., & Mittal, J. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c10489 · Cited by 213 · see citing works

General Framework for Studying the Dynamics of Folded and Nonfolded Proteins by NMR Relaxation Spectroscopy and MD Simulation

Prompers, J. J., & Brüschweiler, R. (2002) · Journal of the American Chemical Society · doi:10.1021/ja012750u · Cited by 205 · see citing works

Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling

Csizmók, V., Follis, A. V., Kriwacki, R. W., & Forman-Kay, J. D. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00548 · Cited by 201 · see citing works

Understanding the key factors that control the rate of β-hairpin folding

Du, D., Zhu, Y., Huang, C., & Gai, F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405904101 · Cited by 195 · see citing works

Liquid–Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus–Host Interactions

Brocca, S., Grandori, R., Longhi, S., & Uversky, V. N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239045 · Cited by 189 · see citing works

Unfolded Protein and Peptide Dynamics Investigated with Single-Molecule FRET and Correlation Spectroscopy from Picoseconds to Seconds

Nettels, D., Hoffmann, A., & Schuler, B. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp076971j · Cited by 183 · see citing works

Dynamic cluster formation determines viscosity and diffusion in dense protein solutions

von Bülow, S., Siggel, M., Linke, M., & Hummer, G. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1817564116 · Cited by 183 · see citing works

Backbone Dynamics and Structural Characterization of the Partially Folded A State of Ubiquitin by 1H, 13C, and 15N Nuclear Magnetic Resonance Spectroscopy

Brutscher, B., Brüschweiler, R., & Ernst, R. R. (1997) · Biochemistry · doi:10.1021/bi971538t · Cited by 179 · see citing works

An NMR View of Protein Dynamics in Health and Disease

Sekhar, A., & Kay, L. E. (2019) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115647 · Cited by 178 · see citing works

Force field development and simulations of intrinsically disordered proteins

Huang, J., & MacKerell, A. D. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.10.008 · Cited by 173 · see citing works

Methods for Physical Characterization of Phase-Separated Bodies and Membrane-less Organelles

Mitrea, D. M., Chandra, B., Ferrolino, M. C., Gibbs, E. B., Tolbert, M., White, M. R., & Kriwacki, R. W. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.07.006 · Cited by 173 · see citing works

Liquid–Liquid Phase Separation Is Driven by Large-Scale Conformational Unwinding and Fluctuations of Intrinsically Disordered Protein Molecules

Majumdar, A., Dogra, P., Maity, S., & Mukhopadhyay, S. (2019) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.9b01731 · Cited by 165 · see citing works

LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation

von Appen, A., LaJoie, D., Johnson, I. E., Trnka, M. J., Pick, S. M., Burlingame, A. L., Ullman, K. S., & Frost, A. S. (2020) · Nature · doi:10.1038/s41586-020-2232-x · Cited by 165 · see citing works

Conformational Expansion of Tau in Condensates Promotes Irreversible Aggregation

Wen, J., Hong, L., Krainer, G., Yao, Q.-Q., Knowles, T. P. J., Wu, S., & Perrett, S. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c03078 · Cited by 164 · see citing works

From Induced Fit to Conformational Selection: A Continuum of Binding Mechanism Controlled by the Timescale of Conformational Transitions

Zhou, H. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.11.029 · Cited by 161 · see citing works

Narrow equilibrium window for complex coacervation of tau and RNA under cellular conditions

Lin, Y., McCarty, J., Rauch, J. N., Delaney, K. T., Kosik, K. S., Fredrickson, G. H., Shea, J., & Han, S. (2019) · eLife · doi:10.7554/elife.42571 · Cited by 160 · see citing works

The phase separation underlying the pyrenoid-based microalgal Rubisco supercharger

Wunder, T., Cheng, S. L. H., Lai, S.-K., Li, H., & Mueller‐Cajar, O. (2018) · Nature Communications · doi:10.1038/s41467-018-07624-w · Cited by 159 · see citing works

Protein intrinsic disorder and structure-function continuum

Uversky, V. N. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.05.003 · Cited by 155 · see citing works

Interactions by disorder – A matter of context

Bugge, K., Brakti, I., Fernandes, C. B., Dreier, J. E., Lundsgaard, J. E., Olsen, J. G., Skriver, K., & Kragelund, B. B. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00110 · Cited by 155 · see citing works

Unraveling Molecular Interactions in Liquid–Liquid Phase Separation of Disordered Proteins by Atomistic Simulations

Paloni, M., Bailly, R., Ciandrini, L., & Barducci, A. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c06288 · Cited by 151 · see citing works

Depletion interactions modulate the binding between disordered proteins in crowded environments

Zosel, F., Soranno, A., Buholzer, K., Nettels, D., & Schuler, B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921617117 · Cited by 150 · see citing works

The Helix-Coil Kinetics of a Heteropeptide

Thompson, P. A., Muñoz, V., Jas, G. S., Henry, E. R., Eaton, W. A., & Hofrichter, J. (1999) · The Journal of Physical Chemistry B · doi:10.1021/jp990292u · Cited by 149 · see citing works

Identification of an Aggregation-Prone Structure of Tau

Elbaum-Garfinkle, S., & Rhoades, E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305206m · Cited by 149 · see citing works

Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation

Oltrogge, L. M., Chaijarasphong, T., Chen, A. W., Bolin, E. R., Marqusee, S., & Savage, D. F. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0387-7 · Cited by 146 · see citing works

First-generation predictors of biological protein phase separation

Vernon, R. M., & Forman-Kay, J. D. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.05.016 · Cited by 145 · see citing works

Physics-based computational and theoretical approaches to intrinsically disordered proteins

Shea, J., Best, R. B., & Mittal, J. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.12.012 · Cited by 144 · see citing works

Temperature-Dependent Helix−Coil Transition of an Alanine Based Peptide

Huang, C., Klemke, J. W., Getahun, Z., DeGrado, W. F., & Gai, F. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0158814 · Cited by 141 · see citing works

Fluorescence correlation spectroscopy and Brownian rotational diffusion

Aragón, S. R., & Pecora, R. (1975) · Biopolymers · doi:10.1002/bip.1975.360140110 · Cited by 140 · see citing works

Backbone Dynamics of a Highly Disordered 131 Residue Fragment of Staphylococcal Nuclease

Alexandrescu, A. T., & Shortlet, D. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1598 · Cited by 140 · see citing works

Describing sequence–ensemble relationships for intrinsically disordered proteins

Mao, A. H., Lyle, N., & Pappu, R. V. (2013) · Biochemical Journal · doi:10.1042/bj20121346 · Cited by 135 · see citing works

The (un)structural biology of biomolecular liquid-liquid phase separation using NMR spectroscopy

Murthy, A. C., & Fawzi, N. L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.009847 · Cited by 135 · see citing works

Disordered Proteinaceous Machines

Fuxreiter, M., Tóth-Petróczy, Á., Kraut, D. A., Matouschek, A. T., Lim, R. Y. H., Xue, B., Kurgan, L., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr4007329 · Cited by 133 · see citing works

Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor

Sherry, K. P., Das, R. K., Pappu, R. V., & Barrick, D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706083114 · Cited by 127 · see citing works

Measuring Conformational Dynamics: A New FCS-FRET Approach

Torres, T., & Levitus, M. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp070659s · Cited by 126 · see citing works

New Force Field on Modeling Intrinsically Disordered Proteins

Wang, W., Ye, W., Jiang, C., Luo, R., & Chen, H. (2014) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12314 · Cited by 126 · see citing works

Residue-Specific Force Field Based on Protein Coil Library. RSFF2: Modification of AMBER ff99SB

Zhou, C., Jiang, F., & Wu, Y. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp5064676 · Cited by 120 · see citing works

Identification of Dynamic Modes in an Intrinsically Disordered Protein Using Temperature-Dependent NMR Relaxation

Abyzov, A., Salvi, N., Schneider, R., Maurin, D., Ruigrok, R. W. H., Jensen, M. R., & Blackledge, M. J. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b02424 · Cited by 117 · see citing works

AWSEM-IDP: A Coarse-Grained Force Field for Intrinsically Disordered Proteins

Hao, W., Wolynes, P. G., & Papoian, G. A. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b05791 · Cited by 116 · see citing works

Simulation methods for liquid-liquid phase separation of disordered proteins

Dignon, G., Zheng, W.-W., & Mittal, J. (2019) · Current Opinion in Chemical Engineering · doi:10.1016/j.coche.2019.03.004 · Cited by 113 · see citing works

PEG 400, a hydrophilic molecular probe for measuring intestinal permeability

Ma, T. Y., Hollander, D., Krugliak, P., & Katz, K. D. (1990) · Gastroenterology · doi:10.1016/0016-5085(90)91288-h · Cited by 109 · see citing works

The physical basis of model-free analysis of NMR relaxation data from proteins and complex fluids

Halle, B. (2009) · The Journal of Chemical Physics · doi:10.1063/1.3269991 · Cited by 109 · see citing works

Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation

Salvi, N., Abyzov, A., & Blackledge, M. J. (2016) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.6b00885 · Cited by 109 · see citing works

Interaction hot spots for phase separation revealed by NMR studies of a CAPRIN1 condensed phase

Kim, T. H., Payliss, B. J., Nosella, M. L., Lee, I. T. W., Toyama, Y., Forman-Kay, J. D., & Kay, L. E. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2104897118 · Cited by 109 · see citing works

Helix nucleation kinetics from molecular simulations in explicit solvent

Hummer, G., Garcı́a, A. E., & Garde, S. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20010101)42:1 · Cited by 107 · see citing works

Filtered FCS: Species Auto‐ and Cross‐Correlation Functions Highlight Binding and Dynamics in Biomolecules

Felekyan, S., Kalinin, S., Sanabria, H., Valeri, A., & Seidel, C. A. M. (2012) · ChemPhysChem · doi:10.1002/cphc.201100897 · Cited by 107 · see citing works

Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations

Soranno, A., Holla, A., Dingfelder, F., Nettels, D., Makarov, D. E., & Schuler, B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616672114 · Cited by 106 · see citing works

Crossover regime for the diffusion of nanoparticles in polyethylene glycol solutions: influence of the depletion layer

Ziębacz, N., Wieczorek, S. A., Kalwarczyk, T., Fiałkowski, M., & Hołyst, R. (2011) · Soft Matter · doi:10.1039/c0sm01357a · Cited by 105 · see citing works

Residue-Specific Force Field Based on the Protein Coil Library. RSFF1: Modification of OPLS-AA/L

Jiang, F., Zhou, C., & Wu, Y. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp5017449 · Cited by 105 · see citing works

Reentrant Phase Transitions and Non-Equilibrium Dynamics in Membraneless Organelles

Milin, A. N., & Deniz, A. A. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00001 · Cited by 104 · see citing works

Elucidating binding mechanisms and dynamics of intrinsically disordered protein complexes using NMR spectroscopy

Schneider, R. C., Blackledge, M. J., & Jensen, M. R. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.09.007 · Cited by 104 · see citing works

Nanosecond Time Scale Motions in Proteins Revealed by High-Resolution NMR Relaxometry

Charlier, C., Khan, S. N., Marquardsen, T., Pelupessy, P., Reiss, V., Sakellariou, D., Bodenhausen, G., Engelke, F., & Ferrage, F. (2013) · Journal of the American Chemical Society · doi:10.1021/ja409820g · Cited by 100 · see citing works

Nanosecond timescale folding dynamics of a pentapeptide in water

Tobias, D. J., Mertz, J. E., & Brooks, C. L. (1991) · Biochemistry · doi:10.1021/bi00238a032 · Cited by 93 · see citing works

Distribution of Pico- and Nanosecond Motions in Disordered Proteins from Nuclear Spin Relaxation

Khan, S. N., Charlier, C., Augustyniak, R., Salvi, N., Déjean, V., Bodenhausen, G., Lequin, O., Pelupessy, P., & Ferrage, F. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.06.069 · Cited by 93 · see citing works

NMR Experiments for Studies of Dilute and Condensed Protein Phases: Application to the Phase-Separating Protein CAPRIN1

Wong, L. E., Kim, T. H., Muhandiram, D. R., Forman-Kay, J. D., & Kay, L. E. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b12208 · Cited by 93 · see citing works

The effect of macromolecular crowding on mobility of biomolecules, association kinetics, and gene expression in living cells

Tabaka, M., Kalwarczyk, T., Szymański, J., Hou, S., & Hołyst, R. (2014) · Frontiers in Physics · doi:10.3389/fphy.2014.00054 · Cited by 92 · see citing works

A Model of Interdomain Mobility in a Multidomain Protein

Ryabov, Y., & Fushman, D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja067667r · Cited by 91 · see citing works

Hairpin folding rates reflect mutations within and remote from the turn region

Olsen, K. A., Fesinmeyer, R. M., Stewart, J. M., & Andersen, N. H. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504392102 · Cited by 88 · see citing works

Phase Separation in Cell Division

Ong, J. Y., & Torres, J. Z. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.08.007 · Cited by 88 · see citing works

Intermolecular Charge-Transfer Modulates Liquid–Liquid Phase Separation and Liquid-to-Solid Maturation of an Intrinsically Disordered pH-Responsive Domain

Dogra, P., Joshi, A., Majumdar, A., & Mukhopadhyay, S. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10892 · Cited by 87 · see citing works

Coupled binding and folding of intrinsically disordered proteins: what can we learn from kinetics?

Gianni, S., Dogan, J., & Jemth, P. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.11.012 · Cited by 85 · see citing works

ff14IDPs force field improving the conformation sampling of intrinsically disordered proteins

Song, D., Wang, W., Ye, W., Ji, D., Luo, R., & Chen, H. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12832 · Cited by 85 · see citing works

Protein dynamics from single-molecule fluorescence intensity correlation functions

Gopich, I. V., Nettels, D., Schuler, B., & Szabó, A. (2009) · The Journal of Chemical Physics · doi:10.1063/1.3212597 · Cited by 81 · see citing works

Chemical Exchange

Palmer, A. G. I., & Koss, H. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.09.028 · Cited by 81 · see citing works

AlphaFold, Artificial Intelligence (AI), and Allostery

Nussinov, R., Zhang, M., Liu, Y., & Jang, H. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04346 · Cited by 190 · see citing works

Learning the chemical grammar of biomolecular condensates

Kilgore, H. R., & Young, R. A. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01046-y · Cited by 172 · see citing works

Micropolarity governs the structural organization of biomolecular condensates

Ye, S., Latham, A. P., Tang, Y., Hsiung, C., Chen, J., Luo, F., Liu, Y., Zhang, B., & Zhang, X. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01477-1 · Cited by 144 · see citing works

The role of biomolecular condensates in protein aggregation

Visser, B. S., Lipiński, W. P., & Spruijt, E. (2024) · Nature Reviews Chemistry · doi:10.1038/s41570-024-00635-w · Cited by 138 · see citing works

Principles Governing the Phase Separation of Multidomain Proteins

Mohanty, P., Kapoor, U., Devarajan, D. S., Phan, T. M., Rizuan, A., & Mittal, J. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00210 · Cited by 120 · see citing works

Stress-related biomolecular condensates in plants

Solís-Miranda, J., Chodasiewicz, M., Skirycz, A., Fernie, A. R., Moschou, P. N., Bozhkov, P. V., & Gutiérrez-Beltrán, E. (2023) · The Plant Cell · doi:10.1093/plcell/koad127 · Cited by 98 · see citing works

Condensed-phase signaling can expand kinase specificity and respond to macromolecular crowding

Sang, D., Shu, T., Pantoja, C. F., de Opakua, A. I., Zweckstetter, M., & Holt, L. J. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.08.016 · Cited by 96 · see citing works

Liquid–Liquid Phase Separation Modifies the Dynamic Properties of Intrinsically Disordered Proteins

Guseva, S., Schnapka, V., Adamski, W., Maurin, D., Ruigrok, R. W. H., Salvi, N., & Blackledge, M. J. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c13647 · Cited by 94 · see citing works

Cellular Protein Aggregates: Formation, Biological Effects, and Ways of Elimination

Wen, J.-H., He, X., Feng, Z.-S., Li, D.-Y., Tang, J., & Liu, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108593 · Cited by 81 · see citing works

Biological soft matter: intrinsically disordered proteins in liquid–liquid phase separation and biomolecular condensates

Fonin, A. V., Antifeeva, I. A., Kuznetsova, I. М., Константинович, Т. К., Zaslavsky, B. Y., Kulkarni, P., & Uversky, V. N. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220052 · Cited by 77 · see citing works

In situ formation of biomolecular condensates as intracellular drug reservoirs for augmenting chemotherapy

Liang, T., Dong, Y., Cheng, I., Wen, P., Li, F., Liu, F., Wu, Q. Y., Ren, E., Liu, P., Li, H., et al. (2024) · Nature Biomedical Engineering · doi:10.1038/s41551-024-01254-y · Cited by 67 · see citing works

Towards Accurate Simulation of Coupling between Protein Secondary Structure and Phase Separation

Zhang, Y.-M., Li, S.-L., Gong, X., & Chen, J.-H. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c09195 · Cited by 53 · see citing works

Biological condensates form percolated networks with molecular motion properties distinctly different from dilute solutions

Shen, Z., Jia, B., Xu, Y., Wessén, J., Pal, T., Chan, H. S., Du, S., & Zhang, M. (2023) · eLife · doi:10.7554/elife.81907 · Cited by 58 · see citing works

Peptide-mediated liquid–liquid phase separation and biomolecular condensates

Li, G., Yuan, C., & Yan, X. (2025) · Soft Matter · doi:10.1039/d4sm01477d · Cited by 51 · see citing works

Protein conformation and biomolecular condensates

Vazquez, D. S., Toledo, P. L., Gianotti, A. R., & Ermácora, M. R. (2022) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2022.09.004 · Cited by 41 · see citing works

Challenges in studying the liquid-to-solid phase transitions of proteins using computer simulations

Szała-Mendyk, B., Phan, T. M., Mohanty, P., & Mittal, J. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102333 · Cited by 41 · see citing works

Theory and Simulation of Multiphase Coexistence in Biomolecular Mixtures

Jacobs, W. M. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.3c00198 · Cited by 39 · see citing works

Supramolecular Switching of Liquid‐Liquid Phase Separation for Orchestrating Enzyme Kinetics

Wang, D., Zhou, L., Zhang, X.-K., Zhou, Z., Huang, Z., & Gao, N. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202422601 · Cited by 39 · see citing works

Functional specificity in biomolecular condensates revealed by genetic complementation

Sabari, B. R., Hyman, A. A., & Hnisz, D. (2024) · Nature Reviews Genetics · doi:10.1038/s41576-024-00780-4 · Cited by 37 · see citing works

Peptide-Based Biomimetic Condensates via Liquid–Liquid Phase Separation as Biomedical Delivery Vehicles

Song, S., Ivanov, T., Yuan, D., Wang, J., da Silva, L. C., Xie, J., & Cao, S. (2024) · Biomacromolecules · doi:10.1021/acs.biomac.4c00814 · Cited by 36 · see citing works

Synthetic Biomolecular Condensates: Phase‐Separation Control, Cytomimetic Modelling and Emerging Biomedical Potential

Song, S., Ivanov, T., Doan‐Nguyen, T. P., da Silva, L. C., Xie, J., Landfester, K., & Cao, S. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202418431 · Cited by 38 · see citing works

Benchmarking residue-resolution protein coarse-grained models for simulations of biomolecular condensates

Feito, A., Sanchez‐Burgos, I., Tejero, I., Sanz, E., Rey, A., Collepardo‐Guevara, R., Tejedor, A. R., & Espinosa, J. R. (2025) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1012737 · Cited by 36 · see citing works

Macromolecular crowding effects on protein dynamics

Das, N., Khan, T., Halder, B., Ghosh, S., & Sen, P. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136248 · Cited by 35 · see citing works

Physics of droplet regulation in biological cells

Zwicker, D., Paulin, O. W., & ter Burg, C. (2025) · Reports on Progress in Physics · doi:10.1088/1361-6633/ae12a7 · Cited by 35 · see citing works

Current perspectives in drug targeting intrinsically disordered proteins and biomolecular condensates

Qin, C., Wang, Y., Zheng, J., Wan, X., & Fan, X. (2025) · BMC Biology · doi:10.1186/s12915-025-02214-x · Cited by 39 · see citing works

The roles of intrinsically disordered proteins in neurodegeneration

Utami, K. H., Morimoto, S., Mitsukura, Y., & Okano, H. (2025) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2025.130772 · Cited by 34 · see citing works

Highly Charged Proteins and Their Repulsive Interactions Antagonize Biomolecular Condensation

Tan, C., Niitsu, A., & Sugita, Y. (2023) · JACS Au · doi:10.1021/jacsau.2c00646 · Cited by 30 · see citing works

Model biomolecular condensates have heterogeneous structure quantitatively dependent on the interaction profile of their constituent macromolecules

Shillcock, J. C., Lagisquet, C., Alexandre, J., Vuillon, L., & Ipsen, J. H. (2022) · Soft Matter · doi:10.1039/d2sm00387b · Cited by 29 · see citing works

The mechanobiology of biomolecular condensates

Sanfeliu-Cerdán, N., & Krieg, M. (2025) · Biophysics Reviews · doi:10.1063/5.0236610 · Cited by 28 · see citing works

Progress, Challenges and Opportunities of NMR and XL-MS for Cellular Structural Biology

Zhang, Z., Zhao, Q., Gong, Z., Du, R., Liu, M., Zhang, Y., Zhang, L., & Li, C. (2024) · JACS Au · doi:10.1021/jacsau.3c00712 · Cited by 27 · see citing works

Contributions of the N‐terminal intrinsically disordered region of the severe acute respiratory syndrome coronavirus 2 nucleocapsid protein to RNA‐induced phase separation

Zachrdla, M., Savastano, A., de Opakua, A. I., Cima‐Omori, M., & Zweckstetter, M. (2022) · Protein Science · doi:10.1002/pro.4409 · Cited by 27 · see citing works

Representing structures of the multiple conformational states of proteins

Ramelot, T. A., Tejero, R., & Montelione, G. T. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102703 · Cited by 26 · see citing works

Identifying protein conformational states in the Protein Data Bank: Toward unlocking the potential of integrative dynamics studies

Ellaway, J. I. J., Anyango, S., Nair, S. S., Zaki, H. A., Nadzirin, N., Powell, H. R., Gutmanas, A., Váradi, M., & Velankar, S. S. (2024) · Structural Dynamics · doi:10.1063/4.0000251 · Cited by 27 · see citing works

Multiphasic condensates formed with mono-component of tetrapeptides via phase separation

Zhou, L., Zhu, L., Wang, C., Xu, T., Wang, J., Zhang, B., Zhang, X., & Wang, H. (2025) · Nature Communications · doi:10.1038/s41467-025-58060-6 · Cited by 26 · see citing works

Genetically-encoded targeted protein degradation technology to remove endogenous condensation-prone proteins and improve crop performance

Luo, M., Zhu, S., Dang, H., Wen, Q., Niu, R., Long, J., Wang, Z., Tong, Y., Ning, Y., Yuan, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56570-x · Cited by 24 · see citing works

Modulation of biophysical properties of nucleocapsid protein in the mutant spectrum of SARS-CoV-2

Nguyen, A., Zhao, H., Myagmarsuren, D., Srinivasan, S., Wu, D., Chen, J., Piszczek, G., & Schuck, P. (2024) · eLife · doi:10.7554/elife.94836 · Cited by 32 · see citing works

Size-controlled assembly of phase separated protein condensates with interfacial protein cages

Oh, H. J., Lee, Y., Hwang, H., Hong, K., Choi, H., Kang, J. Y., & Jung, Y. (2025) · Nature Communications · doi:10.1038/s41467-025-56391-y · Cited by 22 · see citing works

Conformations, interactions and functions of intrinsically disordered syndecans

Ricard‐Blum, S., & Couchman, J. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221085 · Cited by 22 · see citing works

Conformational Dynamics in Proteins: Entangled Slow Fluctuations and Nonequilibrium Reaction Events

Ono, J., Matsumura, Y., Mori, T., & Saito, S. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c05307 · Cited by 20 · see citing works

Capturing single-molecule properties does not ensure accurate prediction of biomolecular phase diagrams

Feito, A., Sanchez‐Burgos, I., Rey, A., Collepardo‐Guevara, R., Espinosa, J. R., & Tejedor, A. R. (2024) · Molecular Physics · doi:10.1080/00268976.2024.2425757 · Cited by 20 · see citing works

Use of AI-methods over MD simulations in the sampling of conformational ensembles in IDPs

Sil, S., Datta, I., & Basu, S. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1542267 · Cited by 20 · see citing works

Molecular Simulations Integrated with Experiments for Probing the Interaction Dynamics and Binding Mechanisms of Intrinsically Disordered Proteins

Ghosh, C., Nagpal, S., & Muñoz, V. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102756 · Cited by 16 · see citing works

Predicting Conformational Ensembles of Intrinsically Disordered Proteins: From Molecular Dynamics to Machine Learning

Aupič, J., Pokorná, P., Ruthstein, S., & Magistrato, A. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c01544 · Cited by 18 · see citing works

Microphase separation produces interfacial environment within diblock biomolecular condensatesPreprint

Latham, A. P., Zhu, L.-C., Sharon, D. A., Ye, S.-T., Willard, A. P., Zhang, X., & Zhang, B. (2023) · bioRxiv · doi:10.7554/elife.90750 · Cited by 18 · see citing works

Solution NMR goes big: Atomic resolution studies of protein components of molecular machines and phase-separated condensates

Sever, A. I. M., Ahmed, R., Rößler, P., & Kay, L. E. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102976 · Cited by 16 · see citing works

Modulation of biophysical properties of nucleocapsid protein in the mutant spectrum of SARS-CoV-2

Nguyen, A., Zhao, H., Myagmarsuren, D., Srinivasan, S., Wu, D., Chen, J., Piszczek, G., & Schuck, P. (2024) · eLife · doi:10.7554/elife.94836.3 · Cited by 15 · see citing works

Synthetic Membraneless Droplets for Synaptic‐Like Clustering of Lipid Vesicles

Li, Q., Song, Q., Guo, W., Cao, Y., Cui, X., Chen, D., & Shum, H. C. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202313096 · Cited by 14 · see citing works

Backbone Interactions and Secondary Structures in Phase Separation of Disordered Proteins

Li, S.-L., Zhang, Y.-M., & Chen, J.-H. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230618 · Cited by 10 · see citing works

Sequence Sensitivity in Membrane Remodeling by Polyampholyte Condensates

Mondal, S., & Cui, Q. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c08149 · Cited by 14 · see citing works

Hierarchical Structural Organization in Bioinspired Peptide Coacervate Microdroplets

Lim, J., Gudlur, S., Buchanan, C., Perrin, Q. M., Boyd, H., Moulin, M., Iwase, H., Porcar, L., Cárdenas, M., Miserez, A., et al. (2025) · ACS Nano · doi:10.1021/acsnano.5c12015 · Cited by 13 · see citing works

Repulsive vs Attractive Crowding Distinctly Regulate TDP-43 Condensates through Region-specific Structural Dynamics

Zhang, G., Feng, C., & Chu, X. (2025) · JACS Au · doi:10.1021/jacsau.5c00876 · Cited by 13 · see citing works

Protein nanocondensates: the next frontier

Toledo, P. L., Gianotti, A. R., Vazquez, D. S., & Ermácora, M. R. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01105-1 · Cited by 13 · see citing works

Submillisecond Atomistic Molecular Dynamics Simulations Reveal Hydrogen Bond-Driven Diffusion of a Guest Peptide in Protein–RNA Condensate

Unarta, I. C., Cao, S., Goonetilleke, E. C., Niu, J., Gellman, S. H., & Huang, X. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c08126 · Cited by 13 · see citing works

Small molecule fluorescent probes for the study of protein phase separation

Owyong, T. C., Zhao, J., & Hong, Y. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102354 · Cited by 13 · see citing works

Diversity of hydrodynamic radii of intrinsically disordered proteins

Białobrzewski, M. K., Klepka, B. P., Michaś, A., Cieplak-Rotowska, M. K., Staszałek, Z., & Niedźwiecka, A. (2023) · European Biophysics Journal · doi:10.1007/s00249-023-01683-8 · Cited by 12 · see citing works

Balancing thermodynamic stability, dynamics, and kinetics in phase separation of intrinsically disordered proteins

Zhang, G., & Chu, X. (2024) · The Journal of Chemical Physics · doi:10.1063/5.0220861 · Cited by 12 · see citing works

Heterogeneous Slowdown of Dynamics in the Condensate of an Intrinsically Disordered Protein

Mukherjee, S., & Schäfer, L. V. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c02142 · Cited by 12 · see citing works

Remote on–off switching of protein activity by intrinsically disordered region

Ji, T., Ge, P., Zhang, S., Wan, C., Liu, H., Qu, X., Zhu, F., Gong, Q., Xu, W., Wang, C., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01585-7 · Cited by 12 · see citing works

Microphase separation produces interfacial environment within diblock biomolecular condensates

Latham, A. P., Zhu, L., Sharon, D. A., Ye, S., Willard, A. P., Zhang, X., & Zhang, B. (2025) · eLife · doi:10.7554/elife.90750.4 · Cited by 11 · see citing works

Navigating condensate micropolarity to enhance small-molecule drug targeting

Ouyang, J., Chen, J., Wu, Z., You, K., Chen, T., Gao, Y. Q., Li, P., Zhang, X., & Li, T. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-02017-9 · Cited by 11 · see citing works

Unravelling the microscopic characteristics of intrinsically disordered proteins upon liquid–liquid phase separation

Wu, S., Wen, J., & Perrett, S. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220148 · Cited by 11 · see citing works

Structural Insights into ATP-Sensitive Potassium Channel Mechanics: A Role of Intrinsically Disordered Regions

Walczewska-Szewc, K., & Nowak, W. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c01196 · Cited by 11 · see citing works

Biological Liquid–Liquid Phase Separation, Biomolecular Condensates, and Membraneless Organelles: Now You See Me, Now You Don’t

Uversky, V. N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713150 · Cited by 11 · see citing works

The role of intrinsically disordered regions of SARS-CoV-2 nucleocapsid and non-structural protein 1 proteins

Shitaye, G., Ventserova, N., D’Abrosca, G., Dragone, M., Maina, E. W., Fattorusso, R., Iacovino, R., Russo, L., Isernia, C., & Malgieri, G. (2025) · Frontiers in Chemistry · doi:10.3389/fchem.2025.1597656 · Cited by 10 · see citing works

To What Extent is Anfinsen’s Thermodynamic Hypothesis Consistent With the Formation and Polymorphism of Amyloid Fibrils?

Jiang, Y. X., & Eisenberg, D. S. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169364 · Cited by 10 · see citing works

The emerging roles of liquid–liquid phase separation in tumor immunity

Liu, Y., Cao, L.-Y., & Sun, Z. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113212 · Cited by 9 · see citing works

Liquid–liquid phase separation of peptides: a molecular foundation for next-generation biomaterials

Lu, L., & Wang, H. (2025) · Chemical Science · doi:10.1039/d5sc07607b · Cited by 9 · see citing works

Fluorescence-based mapping of condensate dielectric permittivity uncovers hydrophobicity-driven membrane interactions

Sabri, E., Mangiarotti, A., & Dimova, R. (2026) · Nature Communications · doi:10.1038/s41467-026-71273-7 · Cited by 9 · see citing works

Unveiling the potential of metal-organic framework-based membranes: Transforming material science for a sustainable future

Abboud, M., Chaouiki, A., Chafiq, M., Fatimah, S., Elboughdiri, N. A., Kang, J.-H., & Ko, Y. G. (2024) · Separation and Purification Technology · doi:10.1016/j.seppur.2024.131332 · Cited by 8 · see citing works

ROS-mediated cell death and phase separation in gynecological malignancies

Wei, H., Xiong, M., & Min, L. (2025) · European journal of medical research · doi:10.1186/s40001-025-02846-3 · Cited by 8 · see citing works

Biomolecular condensates as cellular memory modules: Thermodynamic principles and plant stress adaptation

Maity, S., & Moschou, P. N. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.11.2681 · Cited by 8 · see citing works

From the Catastrophic Objective Irreproducibility of Cancer Research and Unavoidable Failures of Molecular Targeted Therapies to the Sparkling Hope of Supramolecular Targeted Strategies

Алексеенко, И. В., Kondratyeva, L. G., Чернов, И. П., & Sverdlov, E. D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032796 · Cited by 8 · see citing works

Atomic Resolution Interactions Regulating Partitioning of a FUS Folded RRM Domain into Model CAPRIN1 Condensates

Ahmed, R., Bonin, J. P., Forman-Kay, J. D., & Kay, L. E. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c10918 · Cited by 7 · see citing works

Poxvirus H5 mediates the formation of liquid-liquid phase separation condensates which promote virus factory assembly

Zhu, J., Zhang, Z., Fang, Y., Xu, J., Jiang, Z., Li, H., Xie, S., Niu, K., Jing, Z., Song, B., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013708 · Cited by 7 · see citing works

Structural and dynamic properties of IL1 receptors

Zhukova, J., Lopatnikova, J., & Sennikov, S. V. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1714624 · Cited by 7 · see citing works

Insights into de-mixing and morphology modulation in coacervate-membrane interactions from integrating experiments and simulations

Mondal, S., Mangiarotti, A., Dimova, R., & Cui, Q. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01810-w · Cited by 7 · see citing works

Liquid-Liquid Phase Separation Associated with Intrinsically Disordered Proteins: Experimental and Computational Tools

Coskuner‐Weber, O., & Uversky, V. N. (2024) · Current Protein and Peptide Science · doi:10.2174/0113892037314062240618193044 · Cited by 7 · see citing works

Ribosome Tunnel Environment Drives the Formation of α-Helix during Cotranslational Folding

Yasuda, T., Morita, R., Shigeta, Y., & Harada, R. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c00901 · Cited by 7 · see citing works

Recent advances in protein conformation sampling by combining machine learning with molecular simulation

唐, Y. 一. T., 杨, Z. 中. Y., 姚, Y. 逸. Y., 周, Y. 运. Z., 谈, Y. 圆. T., 王, Z. 子. W., 潘, T. 瞳. P., 熊, R. 瑞. X., 孙, J. 俊. S., & Wei, G. (2024) · Chinese Physics B · doi:10.1088/1674-1056/ad1a92 · Cited by 7 · see citing works

Emerging connections: Poly(ADP-ribose), FET proteins and RNA in the regulation of DNA damage condensates

Lombardi, S., Zilocchi, M., Nicsanu, R., & Barabino, S. M. L. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103846 · Cited by 6 · see citing works

Molecular mechanisms mediated by liquid-liquid phase separation in chronic liver disease progression

Qiu, X., Tian, H., Gao, Y., Wang, J., Bao, Z., Qiu, N., Zhang, F., Zhang, Z., Wang, F., Zheng, S., et al. (2025) · iScience · doi:10.1016/j.isci.2025.113843 · Cited by 6 · see citing works

Modulating hierarchical self-assembly in thermoresponsive intrinsically disordered proteins through high-temperature incubation time

Sethi, V., Cohen-Gerassi, D., Meir, S., Ney, M., Shmidov, Y., Koren, G., Adler-Abramovich, L., Chilkoti, A., & Beck, R. (2023) · Scientific Reports · doi:10.1038/s41598-023-48483-w · Cited by 6 · see citing works

Synthetic Biomolecular Condensates: Phase‐Separation Control, Cytomimetic Modelling and Emerging Biomedical Potential

Song, S., Ivanov, T., Doan‐Nguyen, T. P., da Silva, L. C., Xie, J., Landfester, K., & Cao, S. (2024) · Angewandte Chemie · doi:10.1002/ange.202418431 · Cited by 5 · see citing works

Perspective: fluorescence lifetime imaging and single-molecule spectroscopy for studying biological condensates

Loidolt-Krüger, M. (2025) · Methods in microscopy · doi:10.1515/mim-2024-0018 · Cited by 6 · see citing works

Solidarity of the Coordination Helix and Water Helix in the Nucleotide Coordination Polymer

Zohaib, H. M., Saqlain, M., Khan, M. A., Qamar, S., Masood, S., Ilyas, M., Xu, Y., & Li, H. (2024) · Crystal Growth & Design · doi:10.1021/acs.cgd.4c00515 · Cited by 6 · see citing works

Protein Profiling by Nanopore-Based Technology

Meng, F., Li, X., Zou, N., & Wang, X. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c00992 · Cited by 5 · see citing works

Tetrel bond involving -CH3group in HnXCH3(X = F, Cl, and Br, n = 0; X = O, S, and Se, n = 1; X = N, P, and As, n = 2). Cooperativity with triel bond and beryllium bond

Wu, Q., An, X., & Li, Q. (2023) · Molecular Physics · doi:10.1080/00268976.2023.2186721 · Cited by 5 · see citing works

Proteomic tools to study phosphorylation of intrinsically disordered proteins

Spolaore, B., Secco, L., Rocca, G., Manfioletti, G., Arrigoni, G., & Sgarra, R. (2023) · Expert Review of Proteomics · doi:10.1080/14789450.2023.2217359 · Cited by 5 · see citing works

Advances in probing single biomolecules: From DNA bases to glycans

Hou, B., Zhang, T., Yang, H., Han, X., Liu, L., Li, L., Grazioli, C., Wu, X., Jiang, N., & Wang, Y. (2023) · Interdisciplinary materials · doi:10.1002/idm2.12106 · Cited by 5 · see citing works

Wet Conformation of Prion-Like Domain and Intimate Correlation of Hydration and Conformational Fluctuations

Hu, G., Song, H., Chen, X., & Li, J. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c01476 · Cited by 5 · see citing works

Modulation of Biophysical Properties of Nucleocapsid Protein in the Mutant Spectrum of SARS-CoV-2Preprint

Nguyen, A., Zhao, H., Myagmarsuren, D., Srinivasan, S., Wu, D., Chen, J., Piszczek, G., & Schuck, P. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.21.568093 · Cited by 5 · see citing works

Liquid-liquid phase separation in cancer therapy resistance

Hu, P., Ding, H., Yue, N., Ye, J., Ruan, S., Qian, Y., Wang, C., & Song, D. (2026) · iScience · doi:10.1016/j.isci.2026.115420 · Cited by 4 · see citing works

Transient Structural Properties of the Rho GDP‐Dissociation Inhibitor

Gomez, S. M., Visco, I., Merino, F., Bieling, P., & Linser, R. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202403941 · Cited by 4 · see citing works

Genetically Engineered Liposwitch-Based Nanomaterials

Hossain, M. S., Wang, A., Anika, S., Zhang, Z., & Mozhdehi, D. (2024) · Biomacromolecules · doi:10.1021/acs.biomac.4c01388 · Cited by 4 · see citing works

Driving Forces in the Formation of Biocondensates of Highly Charged Proteins: A Thermodynamic Analysis of the Binary Complex Formation

Ballauff, M. (2024) · Biomolecules · doi:10.3390/biom14111421 · Cited by 4 · see citing works

Supramolecular Switching of Liquid‐Liquid Phase Separation for Orchestrating Enzyme Kinetics

Wang, D., Zhou, L., Zhang, X., Zhou, Z., Huang, Z., & Gao, N. (2025) · Angewandte Chemie · doi:10.1002/ange.202422601 · Cited by 4 · see citing works

Conformation and Dynamics of Monomeric, Phase-Separated, and Cross-Linked Resilin Biomaterials

Otis, J., Reichenwallner, J., Reichheld, S. E., Au, A., Yip, C. M., Ernst, O. P., & Sharpe, S. J. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12305 · Cited by 4 · see citing works

Advances in artificial cells capable of metabolic mimicry: from fundamentals to applications

Jia, Y., Zhao, J., Xu, W., Zhang, X., Li, S., & Han, X. (2026) · Chemical Society Reviews · doi:10.1039/d5cs01330e · Cited by 4 · see citing works

Structural characterization of codon 129 polymorphism in prion peptide segments (PrP127-132) using the Markov State Models.

Omwansu, W., Musembi, R., & Derese, S. (2024) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2024.108927 · Cited by 3 · see citing works

Integrating chemical artificial intelligence and cognitive computing for predictive analysis of biological pathways: a case for intrinsically disordered proteins

Coskuner‐Weber, O., Gentili, P. L., & Uversky, V. N. (2025) · Biophysical Reviews · doi:10.1007/s12551-025-01286-x · Cited by 4 · see citing works

Unravelling the microscopic characteristics of intrinsically disordered proteins upon liquid–liquid phase separation

Wu, S., Wen, J., & Perrett, S. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220148 · Cited by 11 · see citing works

Intrinsically disordered proteins and biomolecular condensates as drug targets

Biesaga, M., Frigolé-Vivas, M., & Salvatella, X. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.02.009 · Cited by 115 · see citing works

Model shows the role of intrinsically disordered proteins in biomolecular condensate viscoelasticity

Liebendorfer, A. (2026) · Scilight · doi:10.1063/10.0042657

Intrinsically disordered proteins and liquid–liquid phase separation: Molecular grammar, condensate physiology, and disease-relevant phase transitions

Abinawanto, A., & Sophian, A. (2026) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2026.141183

Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid–Liquid Phase Separation

Garaizar, A., Sanchez‐Burgos, I., Collepardo‐Guevara, R., & Espinosa, J. R. (2020) · Molecules · doi:10.3390/molecules25204705 · Cited by 78 · see citing works