The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Protein Phase Separation Provides Long-Term Memory of Transient Spatial Stimuli
Open accessPublished version of a preprint
Abstract
Protein/RNA clusters arise frequently in spatially regulated biological processes, from the asymmetric distribution of P granules and PAR proteins in developing embryos to localized receptor oligomers in migratory cells. This co-occurrence suggests that protein clusters might possess intrinsic properties that make them a useful substrate for spatial regulation. Here, we demonstrate that protein droplets show a robust form of spatial memory, maintaining the spatial pattern of an inhibitor of droplet formation long after it has been removed. Despite this persistence, droplets can be highly dynamic, continuously exchanging monomers with the diffuse phase. We investigate the principles of biophysical spatial memory in three contexts: a computational model of phase separation; a novel optogenetic system where light can drive rapid, localized dissociation of liquid-like protein droplets; and membrane-localized signal transduction from clusters of receptor tyrosine kinases. Our results suggest that the persistent polarization underlying many cellular and developmental processes could arise through a simple biophysical process, without any additional biochemical feedback loops.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In our experiments with either passive or active coacervate droplets, we did not observe any shrinkage of small droplets, suggesting that Ostwald ripening is being slowed down or prevented by an opposing force closely linked to the nature of our droplets28.”
From Active coacervate droplets are protocells that grow and resist Ostwald ripening (2021) · cites this paper as [28]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The kinetics of precipitation from supersaturated solid solutions
Lifshitz, I. M., & Slyozov, V. V. (1961) · Journal of Physics and Chemistry of Solids · doi:10.1016/0022-3697(61)90054-3 · Cited by 8,558
Liquid phase condensation in cell physiology and disease
Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,143
Self-citationGermline 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
Self-citationA theory of biological pattern formation
Gierer, A., & Meinhardt, H. (1972) · Kybernetik · doi:10.1007/bf00289234 · Cited by 3,158
Collective cell migration in morphogenesis, regeneration and cancer
Friedl, P., & Gilmour, D. T. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2720 · Cited by 2,804
A Guide to Monte Carlo Simulations in Statistical Physics
Landau, D. P., & Binder, K. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781139696463 · Cited by 2,346
Theory of precipitate change by redissolution
Wagner, C. (1961) · Medical Entomology and Zoology · Cited by 1,943
Phase separation of signaling molecules promotes T cell receptor signal transduction
Su, X., Ditlev, J. A., Hui, E., Xing, W., Banjade, S., Okrut, J., King, D., Taunton, J., Rosen, M. K., & Vale, R. D. (2016) · Science · doi:10.1126/science.aad9964 · Cited by 1,260
The chemical basis of morphogenesis
Turing, A. M. (1990) · Bulletin of Mathematical Biology · doi:10.1016/s0092-8240(05)80008-4 · Cited by 997
Spatiotemporal Control of Intracellular Phase Transitions Using Light-Activated optoDroplets
Shin, Y., Berry, J. M., Pannucci, N. L., Haataja, M., Toettcher, J. E., & Brangwynne, C. P. (2016) · Cell · doi:10.1016/j.cell.2016.11.054 · Cited by 953
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Alberti, S., Gladfelter, A., & Mittag, T. (2019) · Cell · doi:10.1016/j.cell.2018.12.035 · Cited by 2,856
Physical Principles Underlying the Complex Biology of Intracellular Phase Transitions
Choi, J., Holehouse, A. S., & Pappu, R. V. (2020) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-121219-081629 · Cited by 908
Liquid Nuclear Condensates Mechanically Sense and Restructure the Genome
Shin, Y., Chang, Y.-C., Lee, D. S. W., Berry, J., Sanders, D. W., Ronceray, P., Wingreen, N. S., Haataja, M., & Brangwynne, C. P. (2018) · Cell · doi:10.1016/j.cell.2018.10.057 · Cited by 676
Self-citationEvaluating phase separation in live cells: diagnosis, caveats, and functional consequencesPreprint
McSwiggen, D. T., Mir, M., Darzacq, X., & Tjian, R. (2019) · Genes & Development · doi:10.1101/gad.331520.119 · Cited by 600
Probing and engineering liquid-phase organelles
Bracha, D., Walls, M. T., & Brangwynne, C. P. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0341-6 · Cited by 320
Self-citationLight-based control of metabolic flux through assembly of synthetic organelles
Zhao, E. M., Suek, N., Wilson, M. Z., Dine, E., Pannucci, N. L., Gitai, Z., Avalos, J. L., & Toettcher, J. E. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0284-8 · Cited by 290
Self-citationCapillary forces generated by biomolecular condensates
Gouveia, B., Kim, Y., Shaevitz, J. W., Petry, S., Stone, H. A., & Brangwynne, C. P. (2022) · Nature · doi:10.1038/s41586-022-05138-6 · Cited by 269
Self-citationEngineered Living Materials For Sustainability
An, B., Wang, Y., Huang, Y., Wang, X., Liu, Y., Xun, D., Church, G. M., Dai, Z., Yi, X., Tang, T., et al. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00512 · Cited by 256
Phase separation in immune signalling
Xiao, Q., McAtee, C. K., & Su, X. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00572-5 · Cited by 232
The liquid nucleome – phase transitions in the nucleus at a glance
Strom, A. R., & Brangwynne, C. P. (2019) · Journal of Cell Science · doi:10.1242/jcs.235093 · Cited by 224
Self-citationNavarro, M. G.-J., Kashida, S., Chouaib, R., Souquère, S., Pierron, G., Barbieri-Weill, D., & Gueroui, Z. (2019) · Nature Communications · doi:10.1038/s41467-019-11241-6 · Cited by 211
Active coacervate droplets are protocells that grow and resist Ostwald ripening
Nakashima, K. K., van Haren, M. H. I., André, A. A. M., Robu, I., & Spruijt, E. (2021) · Nature Communications · doi:10.1038/s41467-021-24111-x · Cited by 209
Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods
Pignataro, M. F., Herrera, M. G., & Dodero, V. I. (2020) · Molecules · doi:10.3390/molecules25204854 · Cited by 224
Engineering synthetic biomolecular condensates
Dai, Y., You, L., & Chilkoti, A. (2023) · Nature Reviews Bioengineering · doi:10.1038/s44222-023-00052-6 · Cited by 198
Zhang, H., Shao, S., Zeng, Y., Wang, X., Qin, Y., Ren, Q., Xiang, S., Wang, Y., Xiao, J., & Sun, Y. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00846-7 · Cited by 189
Dynamic metastable long-living droplets formed by sticker-spacer proteins
Ranganathan, S., & Shakhnovich, E. I. (2020) · eLife · doi:10.7554/elife.56159 · Cited by 169
Ma, L., Gao, Z.-Y., Wu, J., Zhong, B., Xie, Y., Huang, W. L., & Lin, Y. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.031 · Cited by 164
Optogenetic control of protein binding using light-switchable nanobodies
Gil, A. A., Carrasco‐López, C., Zhu, L., Zhao, E. M., Ravindran, P. T., Wilson, M. Z., Goglia, A. G., Avalos, J. L., & Toettcher, J. E. (2020) · Nature Communications · doi:10.1038/s41467-020-17836-8 · Cited by 162
Self-citationPrion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
McAlary, L., Plotkin, S. S., Yerbury, J. J., & Cashman, N. R. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00262 · Cited by 160
Membraneless nuclear organelles and the search for phases within phases
Sawyer, I. A., Sturgill, D. M., & Dundr, M. (2018) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1514 · Cited by 149
Designer membraneless organelles sequester native factors for control of cell behavior
Garabedian, M. V., Wang, W., Dabdoub, J. B., Tong, M., Caldwell, R. M., Benman, W. K. J., Schuster, B. S., Deiters, A., & Good, M. C. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00840-4 · Cited by 147
Optophysiology: Illuminating cell physiology with optogenetics
Tan, P., He, L., Huang, Y., & Zhou, Y. (2022) · Physiological Reviews · doi:10.1152/physrev.00021.2021 · Cited by 141
Synthetic protein condensates for cellular and metabolic engineering
Qian, Z., Huang, S.-C., & Xia, X. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01203-3 · Cited by 131
Signaling Dynamics Control Cell Fate in the Early Drosophila Embryo
Johnson, H. E., Shvartsman, S. Y., & Toettcher, J. E. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.01.009 · Cited by 127
Self-citationAntifeeva, I. A., Fonin, A. V., Fefilova, A. S., Stepanenko, O. V., Povarova, O. I., Silonov, S. A., Kuznetsova, I. М., Uversky, V. N., & Константинович, Т. К. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04276-4 · Cited by 138
Watanabe, K., Morishita, K., Zhou, X., Shiizaki, S., Uchiyama, Y., Koike, M., Naguro, I., & Ichijo, H. (2021) · Nature Communications · doi:10.1038/s41467-021-21614-5 · Cited by 117
Biomolecular condensates in neurodegeneration and cancer
Spannl, S., Tereshchenko, M., Mastromarco, G. J., Ihn, S. J., & Lee, H. O. (2019) · Traffic · doi:10.1111/tra.12704 · Cited by 116
Molecular determinants of condensate composition
Holehouse, A. S., & Alberti, S. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.12.021 · Cited by 107
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 101
Controlling the material properties and rRNA processing function of the nucleolus using light
Zhu, L., Richardson, T. M., Wacheul, L., Wei, M.-T., Feric, M., Whitney, G., Lafontaine, D. L. J., & Brangwynne, C. P. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903870116 · Cited by 94
Self-citationA bright future: optogenetics to dissect the spatiotemporal control of cell behavior
Goglia, A. G., & Toettcher, J. E. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.11.010 · Cited by 90
Self-citationA Live-Cell Screen for Altered Erk Dynamics Reveals Principles of Proliferative Control
Goglia, A. G., Wilson, M. Z., Jena, S. G., Silbert, J., Basta, L. P., Devenport, D., & Toettcher, J. E. (2020) · Cell Systems · doi:10.1016/j.cels.2020.02.005 · Cited by 84
Self-citationKubota, R., Tanaka, W., & Hamachi, I. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01334 · Cited by 86
Synthetic Protein Condensates That Inducibly Recruit and Release Protein Activity in Living Cells
Yoshikawa, M., Yoshii, T., Ikuta, M., & Tsukiji, S. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c12375 · Cited by 81
Protein Phase Separation Arising from Intrinsic Disorder: First-Principles to Bespoke Applications
Shapiro, D. M., Ney, M. R., Eghtesadi, S. A., & Chilkoti, A. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c01146 · Cited by 77
Phase Separation during Germline Development
So, C., Cheng, S., & Schuh, M. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.12.004 · Cited by 79
Optimized Vivid-derived Magnets photodimerizers for subcellular optogenetics in mammalian cells
Benedetti, L., Marvin, J. S., Falahati, H., Guillén-Samander, A., Looger, L. L., & Camilli, P. V. D. (2020) · eLife · doi:10.7554/elife.63230 · Cited by 75
Protein Mediated Enzyme Immobilization
Caparco, A. A., Dautel, D. R., & Champion, J. A. (2022) · Small · doi:10.1002/smll.202106425 · Cited by 74
Biomolecular condensates in membrane receptor signaling
Jaqaman, K., & Ditlev, J. A. (2021) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.12.006 · Cited by 74
Physical Chemistry of Cellular Liquid‐Phase Separation
Bentley, E. P., Frey, B. B., & Deniz, A. A. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201805093 · Cited by 67
MolPhase, an advanced prediction algorithm for protein phase separation
Liang, Q., Peng, N., Xie, Y., Kumar, N., Gao, W., & Miao, Y. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00090-9 · Cited by 64
Optogenetics and biosensors set the stage for metabolic cybergenetics
Carrasco‐López, C., Echauri, S. A. G., Kichuk, T., & Avalos, J. L. (2020) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2020.07.012 · Cited by 63
SPLIT: Stable Protein Coacervation Using a Light Induced Transition
Reed, E. H., Schuster, B. S., Good, M. C., & Hammer, D. A. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.9b00503 · Cited by 59
Kim, Y. J., Lee, M., Lee, Y., Ji, J., Sanders, J. T., Botten, G. A., He, L., Lyu, J., Zhang, Y., Mettlen, M., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg1123 · Cited by 55
Polyphasic linkage and the impact of ligand binding on the regulation of biomolecular condensates
Ruff, K. M., Dar, F., & Pappu, R. V. (2021) · Biophysics Reviews · doi:10.1063/5.0050059 · Cited by 51
Designer Condensates: A Toolkit for the Biomolecular Architect
Hastings, R., & Boeynaems, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166837 · Cited by 53
Substratum stiffness regulates Erk signaling dynamics through receptor-level control
Farahani, P. E., Lemke, S. B., Dine, E., Uribe, G. A., Toettcher, J. E., & Nelson, C. M. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110181 · Cited by 51
Self-citationProgrammable de novo designed coiled coil-mediated phase separation in mammalian cells
Ramšak, M., Ramirez, D. A., Hough, L. E., Shirts, M. R., Vidmar, S., Eleršič, K., Anderluh, G., & Jerala, R. (2023) · Nature Communications · doi:10.1038/s41467-023-43742-w · Cited by 50
Peptide-mediated liquid–liquid phase separation and biomolecular condensates
Li, G., Yuan, C., & Yan, X. (2025) · Soft Matter · doi:10.1039/d4sm01477d · Cited by 53
Ölçücü, G., Klaus, O., Jaeger, K., Drepper, T., & Krauß, U. (2021) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.1c02045 · Cited by 50
Liquid–liquid phase separation in innate immunity
Liu, D., Yang, J., & Cristea, I. M. (2024) · Trends in Immunology · doi:10.1016/j.it.2024.04.009 · Cited by 54
Emerging Implications of Phase Separation in Cancer
Ren, J., Zhang, Z., Zong, Z., Zhang, L., & Zhou, F. (2022) · Advanced Science · doi:10.1002/advs.202202855 · Cited by 48
Ligand-independent receptor clustering modulates transmembrane signaling: a new paradigm
Sánchez, M. F., & Tampé, R. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.08.002 · Cited by 49
Optogenetic tools for microbial synthetic biology
Chia, N., Lee, S. Y., & Tong, Y. (2022) · Biotechnology Advances · doi:10.1016/j.biotechadv.2022.107953 · Cited by 47
Farahani, P. E., Reed, E. H., Underhill, E. J., Aoki, K., & Toettcher, J. E. (2021) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-083120-111648 · Cited by 46
Self-citationOptobiochemistry: Genetically Encoded Control of Protein Activity by Light
Seong, J., & Lin, M. Z. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072420-112431 · Cited by 45
Synthetic biomolecular condensates to engineer eukaryotic cells
Reinkemeier, C. D., & Lemke, E. A. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.08.005 · Cited by 40
Optogenetics Illuminates Applications in Microbial Engineering
Hoffman, S. M., Tang, A. Y., & Avalos, J. L. (2022) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-092120-092340 · Cited by 42
Light-regulated gene expression in Bacteria: Fundamentals, advances, and perspectives
Ohlendorf, R., & Möglich, A. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.1029403 · Cited by 37
Bhopatkar, A. A., Uversky, V. N., & Rangachari, V. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011501 · Cited by 40
Wang, Q., Fan, H., Li, F., Skeeters, S. S., Krishnamurthy, V. V., Song, Y., & Zhang, K. (2020) · eLife · doi:10.7554/elife.57395 · Cited by 40
Reed, E. H., Gao, Y., Aoki, K., & Toettcher, J. E. (2024) · Nature Communications · doi:10.1038/s41467-024-50858-0 · Cited by 39
Self-citationComplex Coacervate-Based Materials for Biomedicine: Recent Advancements and Future Prospects
Roy, P. S. (2024) · Industrial & Engineering Chemistry Research · doi:10.1021/acs.iecr.3c03830 · Cited by 36
Understanding and Engineering Chromatin as a Dynamical System across Length and Timescales
Johnstone, C. P., Wang, N., Sevier, S. A., & Galloway, K. E. (2020) · Cell Systems · doi:10.1016/j.cels.2020.09.011 · Cited by 36
Photodimerization systems for regulating protein–protein interactions with light
Spiltoir, J. I., & Tucker, C. L. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.01.021 · Cited by 36
Light-switchable transcription factors obtained by direct screening in mammalian cells
Zhu, L., McNamara, H. M., & Toettcher, J. E. (2023) · Nature Communications · doi:10.1038/s41467-023-38993-6 · Cited by 35
Self-citationPhysics 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 43
Genetically-encoded biosensors for analyzing and controlling cellular process in yeast
Marsafari, M., Ma, J., Koffas, M. A. G., & Xu, P. (2020) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2020.04.006 · Cited by 35
Levin, M. (2025) · BioEssays · doi:10.1002/bies.202400196 · Cited by 34
Spatiotemporal organization of coacervate microdroplets
Wang, X., Zhang, P., & Tian, L. (2021) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2021.101420 · Cited by 34
Synthetic developmental biology: New tools to deconstruct and rebuild developmental systems
McNamara, H. M., Ramm, B., & Toettcher, J. E. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.04.013 · Cited by 33
Self-citationSodium ion influx regulates liquidity of biomolecular condensates in hyperosmotic stress response
Morishita, K., Watanabe, K., Naguro, I., & Ichijo, H. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112315 · Cited by 33
A platform to induce and mature biomolecular condensates using chemicals and light
Hernández-Candia, C. N., Brady, B. R., Harrison, E., & Tucker, C. L. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01520-1 · Cited by 32
Roles of Phase Separation for Cellular Redox Maintenance
Saito, Y., & Kimura, W. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.691946 · Cited by 30
A synthetic gene circuit for imaging-free detection of signaling pulses
Ravindran, P. T., McFann, S. E., Thornton, R. H., & Toettcher, J. E. (2021) · Cell Systems · doi:10.1016/j.cels.2021.10.002 · Cited by 27
Self-citationModulating gene regulation function by chemically controlled transcription factor clustering
Wu, J., Chen, B., Liu, Y., Ma, L., Huang, W. L., & Lin, Y. (2022) · Nature Communications · doi:10.1038/s41467-022-30397-2 · Cited by 31
Perspectives of RAS and RHEB GTPase Signaling Pathways in Regenerating Brain Neurons
Schöneborn, H., Raudzus, F., Coppey, M., Neumann, S., & Heumann, R. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19124052 · Cited by 32
Optogenetic strategies for the control of gene expression in yeasts
Pérez, A. L. A., Piva, L. C., Fulber, J. P. C., de Moraes, L. M. P., Marco, J. L. D., Vieira, H. L. D. A., Coelho, C. M., Reis, V. C. B., & Torres, F. A. G. (2021) · Biotechnology Advances · doi:10.1016/j.biotechadv.2021.107839 · Cited by 31
Liquid-liquid phase separation (LLPS) in synthetic biosystems
Kang, W., Ma, X., Liu, C., Wang, S., Zhou, Y. P., Xue, C., Xu, Y., & Li, B. (2023) · Materials Science and Engineering R Reports · doi:10.1016/j.mser.2023.100762 · Cited by 31
Light-induced targeting enables proteomics on endogenous condensates
Lee, C., Quintana, A., Suppanz, I., Gomez‐Auli, A., Mittler, G., & Cissé, I. I. (2024) · Cell · doi:10.1016/j.cell.2024.09.040 · Cited by 33
Memorizing environmental signals through feedback and feedforward loops
Jiang, Y., & Hao, N. (2021) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.11.008 · Cited by 30
Modulating liquid–liquid phase separation of FUS: mechanisms and strategies
Ji, Y., Li, F., & Qiao, Y. (2022) · Journal of Materials Chemistry B · doi:10.1039/d2tb01688e · Cited by 28
Harnessing biomolecular condensates in living cells
Nakamura, H., DeRose, R., & Inoue, T. (2019) · The Journal of Biochemistry · doi:10.1093/jb/mvz028 · Cited by 27
The rise and shine of yeast optogenetics
Figueroa, D., Rojas, V., Romero, A., Larrondo, L. F., & Salinas, F. (2020) · Yeast · doi:10.1002/yea.3529 · Cited by 29
Switching states: dynamic remodelling of polarity complexes as a toolkit for cell polarization
Péglion, F., & Goehring, N. W. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.05.002 · Cited by 30
Interactions between Phase-Separated Liquids and Membrane Surfaces
Botterbusch, S., & Baumgart, T. (2021) · Applied Sciences · doi:10.3390/app11031288 · Cited by 29
Protein Condensation, Cellular Organization, and Spatiotemporal Regulation of Cytoplasmic Properties
van Tartwijk, F. W., & Kaminski, C. F. (2022) · Advanced Biology · doi:10.1002/adbi.202101328 · Cited by 28
A protein kinase A–regulated network encodes short- and long-lived cellular memories
Jiang, Y., AkhavanAghdam, Z., Li, Y., Zid, B. M., & Hao, N. (2020) · Science Signaling · doi:10.1126/scisignal.aay3585 · Cited by 29
A modular tool to query and inducibly disrupt biomolecular condensates
Hernández-Candia, C. N., Pearce, S., & Tucker, C. L. (2021) · Nature Communications · doi:10.1038/s41467-021-22096-1 · Cited by 25
Lights up on organelles: Optogenetic tools to control subcellular structure and organization
Kichuk, T., Carrasco‐López, C., & Avalos, J. L. (2020) · WIREs Mechanisms of Disease · doi:10.1002/wsbm.1500 · Cited by 24
Steering Molecular Activity with Optogenetics: Recent Advances and Perspectives
Oh, T., Fan, H., Skeeters, S. S., & Zhang, K. (2021) · Advanced Biology · doi:10.1002/adbi.202000180 · Cited by 24
Different states and the associated fates of biomolecular condensates
Ranganathan, S., Liu, J., & Shakhnovich, E. I. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220054 · Cited by 25
Recent advances in engineering synthetic biomolecular condensates
Wan, L., Ke, J., Zhu, Y., Zhang, W., & Mu, W. (2024) · Biotechnology Advances · doi:10.1016/j.biotechadv.2024.108452 · Cited by 24
Liquid–Liquid Phase Separation in Cancer Signaling, Metabolism and Anticancer Therapy
Igelmann, S., Lessard, F., & Ferbeyre, G. (2022) · Cancers · doi:10.3390/cancers14071830 · Cited by 22
Shedding light on current trends in molecular optogenetics
Fischer, A., Kramer, M. M., Radziwill, G., & Weber, W. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102196 · Cited by 21
Recent advances in design and application of synthetic membraneless organelles
Wan, L., Zhu, Y., Zhang, W., & Mu, W. (2024) · Biotechnology Advances · doi:10.1016/j.biotechadv.2024.108355 · Cited by 20
Optical Control over Liquid–Liquid Phase Separation
Jia, L., Gao, S., & Qiao, Y. (2024) · Small Methods · doi:10.1002/smtd.202301724 · Cited by 22
Optogenetic approaches to investigate spatiotemporal signaling during development
Rogers, K. W., & Müller, P. (2019) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2019.11.009 · Cited by 23
IDPs and IDRs in biomolecular condensates
Holehouse, A. S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816348-1.00007-7 · Cited by 21
Dine, E., Reed, E. H., & Toettcher, J. E. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109280 · Cited by 19
Self-citation
Metadata
- Authors
- Dine, E., Gil, A. A., Uribe, G., Brangwynne, C. P., & Toettcher, J. E.
- Affiliations
- Princeton University (US)
- Corresponding author
- Toettcher, Jared E.
- Venue
- Cell Systems
- Publisher
- Elsevier BV
- Published
- 2018-06
- Volume
- 6
- Issue
- 6
- Pages
- 655-663.e5
- ISSN
- 2405-4712 (ISSN-L)
- PMC
- PMC6023754
- OpenAlex
- W2952516695
- Cited by
- 182
- References
- 38
- Citations by year
- 2026: 13 · 2025: 24 · 2024: 26 · 2023: 16 · 2022: 29 · 2021: 32 · 2020: 19 · 2019: 17 · 2018: 6
- FWCI
- 6.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Systems (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Stony Brook University
- Children's Hospital Los Angeles (DP2EB024247, U01DA040601)
- Doris Duke Charitable Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- protein phase separation, liquid-liquid phase separation, protein droplets, spatial memory, spatial regulation, receptor tyrosine kinase signaling, polarization, P granules, PAR proteins, asymmetric cell division
- MeSH terms
- Computer Simulation, Membrane Proteins, Neoplasm Proteins, Proteins, RNA, Organelles, Signal Transduction, Feedback, Physiological, Memory, Long-Term, Optogenetics, Spatial Memory
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
