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 11,141

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. D. (2016) · Nature Methods · doi:10.1038/nmeth.4067 · Cited by 7,334

Biomolecular condensates: organizers of cellular biochemistry

Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,058

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

Liquid phase condensation in cell physiology and disease

Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,143

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

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

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

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 3,230

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

Harder, E. D., Damm, W., Maple, J. R., Wu, C., Reboul, M., Xiang, J. Y., Wang, L., Lupyan, D., Dahlgren, M. K., Knight, J. L., et al. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00864 · Cited by 3,104

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

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

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 2,628

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 2,249

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

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

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 2,001

Coexisting Liquid Phases Underlie Nucleolar Subcompartments

Feric, M., Vaidya, N., Harmon, T. S., Mitrea, D. M., Zhu, L., Richardson, T. M., Kriwacki, R. W., Pappu, R. V., & Brangwynne, C. P. (2016) · Cell · doi:10.1016/j.cell.2016.04.047 · Cited by 1,934

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

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

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 1,789

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

Magde, D., Elson, E. L., & Webb, W. W. (1972) · Physical Review Letters · doi:10.1103/physrevlett.29.705 · Cited by 1,783

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

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

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 1,593

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 1,519

Fluorescence correlation spectroscopy. I. Conceptual basis and theory

Elson, E. L., & Magde, D. (1974) · Biopolymers · doi:10.1002/bip.1974.360130102 · Cited by 1,456

Polymer physics of intracellular phase transitions

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

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

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

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

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

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

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 1,089

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

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

Some Properties of Solutions of Long-chain Compounds.

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

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

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 992

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 970

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

Robustelli, P. J., Piana, S., & Shaw, D. (2018) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1800690115 · Cited by 962

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 948

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 936

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

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

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

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

NMR Characterization of the Dynamics of Biomacromolecules

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

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 881

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 872

Liquid–Liquid Phase Separation in Disease

Alberti, S., & Dormann, D. (2019) · Annual Review of Genetics · doi:10.1146/annurev-genet-112618-043527 · Cited by 871

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 869

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

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 858

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

Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides

Best, R., & Hummer, G. (2009) · Journal of Physical Chemistry B · doi:10.1021/jp901540t · Cited by 826

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

The molecular language of membraneless organelles

Gomes, E., & Shorter, J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.001192 · Cited by 804

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

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

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

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 709

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

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

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

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

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. O., Even, A., Fenton, C. H., et al. (2014) · International Conference for High Performance Computing, Networking, Storage and Analysis (SC) · doi:10.1109/sc.2014.9 · Cited by 677

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 672

Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties

Dignon, G. L., Best, R. B., & Mittal, J. (2020) · Annual Review of Physical Chemistry · doi:10.1146/annurev-physchem-071819-113553 · Cited by 657

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

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

Unfolded Proteins and Protein Folding Studied by NMR

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

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

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

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

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

RNA polymerase II clustering through carboxy-terminal domain phase separation

Boehning, M., Dugast‐Darzacq, C., Rankovic, M., Hansen, A. S., Yu, T., Marie-Nelly, H., McSwiggen, D. T., Kokić, G., Dailey, G. M., Cramer, P., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0112-y · Cited by 610

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 584

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

The plurifunctional nucleolus

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

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 531

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 521

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

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 516

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

Uversky, V. N. (2013) · Protein Science · doi:10.1002/pro.2261 · Cited by 512

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 510

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

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

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 497

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

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

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

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

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 416

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 415

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 405

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 398

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

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 393

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

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 384

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

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 377

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 372

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

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

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

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

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 353

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 352

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

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 343

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 335

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 321

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

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 312

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 308

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 307

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 300

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

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

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

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 290

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

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 269

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

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 263

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

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 260

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 257

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

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

Matter over mind: Liquid phase separation and neurodegeneration

Elbaum‐Garfinkle, S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.001188 · Cited by 247

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 239

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 235

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

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

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 215

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 210

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

General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation.

Prompers, J., & Brüschweiler, R. (2002) · Journal of the American Chemical Society · doi:10.1021/ja012750u · Cited by 194

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 193

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

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

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 174

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

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 173

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 166

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 166

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 164

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 162

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

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

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 159

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 157

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

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 153

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

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

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

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

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

An NMR View of Protein Dynamics in Health and Disease.

Sekhar, A., & Kay, L. (2019) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115647 · Cited by 143

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

Fluorescence correlation spectroscopy and Brownian rotational diffusion

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

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

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 138

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

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

Simulation methods for liquid–liquid phase separation of disordered proteins

Dignon, G. L., Zheng, W., & Mittal, J. (2019) · Current Opinion in Chemical Engineering · doi:10.1016/j.coche.2019.03.004 · Cited by 132

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 127

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

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

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

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

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 114

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 110

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

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

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 108

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

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 106

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

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 105

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

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

Salvi, N., Abyzov, A., & Blackledge, M. (2016) · Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.6b00885 · Cited by 100

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 95

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

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

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

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 92

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

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

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

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

Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy

Delaforge, E., Kragelj, J., Tengo, L., Palencia, A., Milles, S., Bouvignies, G., Salvi, N., Blackledge, M. J., & Jensen, M. R. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b12407 · Cited by 85

Phase Separation in Cell Division

Ong, J. Y., & Torres, J. Z. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.08.007 · Cited by 85

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 84

Long-Range Correlated Dynamics in Intrinsically Disordered Proteins

Parigi, G., Rezaei‐Ghaleh, N., Giachetti, A., Becker, S., Fernández, C. O., Blackledge, M. J., Griesinger, C., Zweckstetter, M., & Luchinat, C. (2014) · Journal of the American Chemical Society · doi:10.1021/ja506820r · Cited by 83

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

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

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 174

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

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 142

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 119

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

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

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 76