Cell-free Formation of RNA Granules: Bound RNAs Identify Features and Components of Cellular Assemblies

Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation

Trapnell, C., Williams, B. A., Pertea, G., Mortazavi, A., Kwan, G., van Baren, M. J., Salzberg, S. L., Wold, B. J., & Pachter, L. (2010) · Nature Biotechnology · doi:10.1038/nbt.1621 · Cited by 15,556

Mapping and quantifying mammalian transcriptomes by RNA-Seq

Mortazavi, A., Williams, B. A., McCue, K., Schaeffer, L., & Wold, B. (2008) · Nature Methods · doi:10.1038/nmeth.1226 · Cited by 13,696

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576

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

A brain-specific microRNA regulates dendritic spine development

Schratt, G. M., Tuebing, F., Nigh, E. A., Kane, C. G., Sabatini, M. E., Kiebler, M., & Greenberg, M. E. (2006) · Nature · doi:10.1038/nature04367 · Cited by 1,786

Abnormal dendritic spines in fragile X knockout mice: Maturation and pruning deficits

Comery, T. A., Harris, J. B., Willems, P. J., Oostra, B. A., Irwin, S. A., Weiler, I. J., & Greenough, W. T. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5401 · Cited by 1,046

Global Analysis of mRNA Localization Reveals a Prominent Role in Organizing Cellular Architecture and Function

Lécuyer, E., Yoshida, H., Parthasarathy, N., Alm, C., Babak, T., Cerovina, T., Hughes, T. R., Tomancak, P., & Krause, H. M. (2007) · Cell · doi:10.1016/j.cell.2007.08.003 · Cited by 967

The Fragile X Syndrome Protein FMRP Associates with BC1 RNA and Regulates the Translation of Specific mRNAs at Synapses

Zalfa, F., Giorgi, M., Primerano, B., Moro, A., Di Penta, A., Reis, S., Oostra, B., & Bagni, C. (2003) · Cell · doi:10.1016/s0092-8674(03)00079-5 · Cited by 676

Prions as adaptive conduits of memory and inheritance

Shorter, J., & Lindquist, S. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1616 · Cited by 555

TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling

Zinszner, H., Sok, J., Immanuel, D., Yin, Y., & Ron, D. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.15.1741 · Cited by 350

Liquid-Liquid Phase Separation in Biology

Hyman, A. A., Weber, C. A., & Jülicher, F. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013325 · Cited by 3,155

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

Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811

A brave new world of RNA-binding proteins

Hentze, M. W., Castello, A., Schwarzl, T., & Preiss, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,821

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

Context-dependent control of alternative splicing by RNA-binding proteins

Fu, X.-D., & Ares, M. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3778 · Cited by 1,044

The Mediator complex: a central integrator of transcription

Allen, B. L., & Taatjes, D. J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3951 · Cited by 922

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

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

Eukaryotic core promoters and the functional basis of transcription initiation

Haberle, V., & Stark, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0028-8 · Cited by 774

Regulation by 3′-Untranslated Regions

Mayr, C. (2017) · Annual Review of Genetics · doi:10.1146/annurev-genet-120116-024704 · Cited by 588

RNA transcription modulates phase transition-driven nuclear body assembly

Berry, J., Weber, S. C., Vaidya, N., Haataja, M., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509317112 · Cited by 501

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

Mapping Local and Global Liquid Phase Behavior in Living Cells Using Photo-Oligomerizable Seeds

Bracha, D., Walls, M. T., Wei, M.-T., Zhu, L., Kurian, M., Avalos, J. L., Toettcher, J. E., & Brangwynne, C. P. (2018) · Cell · doi:10.1016/j.cell.2018.10.048 · Cited by 462

Dynamic integration of splicing within gene regulatory pathways

Braunschweig, U., Gueroussov, S., Plocik, A. M., Graveley, B. R., & Blencowe, B. J. (2013) · Cell · doi:10.1016/j.cell.2013.02.034 · Cited by 406

Relationship of sequence and phase separation in protein low-complexity regions

Martin, E. W., & Mittag, T. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00008 · Cited by 389

YB ‐1 protein: functions and regulation

Lyabin, D. N., Eliseeva, I. A., & Ovchinnikov, L. P. (2014) · WIREs RNA · doi:10.1002/wrna.1200 · Cited by 381

Neurodegenerative Diseases: Expanding the Prion Concept

Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361

Astrocytes locally translate transcripts in their peripheral processes

Sakers, K., Lake, A. M., Khazanchi, R., Ouwenga, R., Vasek, M. J., Dani, A., & Dougherty, J. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617782114 · Cited by 202

FUS is Phosphorylated by DNA-PK and Accumulates in the Cytoplasm after DNA Damage

Deng, Q., Holler, C. J., Taylor, G., Hudson, K. F., Watkins, W., Gearing, M., Ito, D., Murray, M. E., Dickson, D. W., Seyfried, N. T., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0172-14.2014 · Cited by 161

Pathological stress granules in Alzheimer’s disease

Ash, P. E. A., Vanderweyde, T. E., Youmans, K. L., Apicco, D. J., & Wolozin, B. (2014) · Brain Research · doi:10.1016/j.brainres.2014.05.052 · Cited by 129

SUMOylation Is an Inhibitory Constraint that Regulates the Prion-like Aggregation and Activity of CPEB3

Drisaldi, B., Colnaghi, L., Fioriti, L., Rao, N., Myers, C., Snyder, A. M., Metzger, D. J., Tarasoff, J., Konstantinov, E., Fraser, P. E., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.061 · Cited by 120

RNA-binding proteins with basic-acidic dipeptide (BAD) domains self-assemble and aggregate in Alzheimer's disease

Bishof, I., Dammer, E. B., Duong, D. M., Kundinger, S. R., Gearing, M., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001747 · Cited by 80

Chromatin dependencies in cancer and inflammation

Marazzi, I., Greenbaum, B. D., Low, D. H. P., & Guccione, E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.113 · Cited by 80

Aggregation Properties of the Small Nuclear Ribonucleoprotein U1-70K in Alzheimer Disease

Diner, I., Hales, C. M., Bishof, I., Rabenold, L., Duong, D. M., Yi, H., Laur, O., Gearing, M., Troncoso, J., Thambisetty, M., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.562959 · Cited by 63

Liquid-liquid phase separation of protein tau: An emerging process in Alzheimer's disease pathogenesis

Ainani, H., Bouchmaa, N., Ben Mrid, R., & El Fatimy, R. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106011 · Cited by 54

Integration of Data from Liquid–Liquid Phase Separation Databases Highlights Concentration and Dosage Sensitivity of LLPS Drivers

Farahi, N., Lazar, T., Wodak, S. J., Tompa, P., & Pancsa, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063017 · Cited by 46

Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy

Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28

A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity

Gu, J., Zhou, X., Sutherland, L., Liszczak, G., & McKnight, S. L. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2503382122