The Rous sarcoma virus Gag Polyprotein Forms Biomolecular Condensates Driven by Intrinsically-disordered Regions

Highly accurate protein structure prediction with AlphaFold

Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works

Enzymatic assembly of DNA molecules up to several hundred kilobases

Gibson, D. G., Young, L., Chuang, R.-Y., Venter, J. C., Hutchison, C. A., & Smith, H. O. (2009) · Nature Methods · doi:10.1038/nmeth.1318 · Cited by 9,742 · see citing works

ColabFold - Making protein folding accessible to all

Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works

Protein Identification and Analysis Tools in the ExPASy Server

Wilkins, M. R., Gasteiger, E., Bairoch, A., Sanchez, J., Williams, K. L., Appel, R. D., & Hochstrasser, D. F. (2003) · Humana Press eBooks · doi:10.1385/1-59259-584-7:531 · Cited by 6,209 · 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

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

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

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

Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

Molliex, A., Temirov, J. P., Lee, J., Coughlin, M., Kanagaraj, A., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,658 · see citing works

Coactivator condensation at super-enhancers links phase separation and gene control

Sabari, B. R., Dall’Agnese, A., Boija, A., Klein, I. A., Coffey, E. L., Shrinivas, K., Abraham, B. J., Hannett, N. M., Zamudio, A. V., Manteiga, J. C., et al. (2018) · Science · doi:10.1126/science.aar3958 · Cited by 2,595 · see citing works

Phase transitions in the assembly of multivalent signalling proteins

Li, P., Banjade, S., Cheng, H., Kim, S., Chen, B., Guo, L., Llaguno, M. C., Hollingsworth, J. V., King, D., Banani, S. F., et al. (2012) · Nature · doi:10.1038/nature10879 · Cited by 2,565 · see citing works

Intrinsically disordered proteins in cellular signalling and regulation

Wright, P. E., & Dyson, H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3920 · Cited by 2,371 · 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

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

Intrinsic Disorder and Protein Function

Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731 · see citing works

ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure

Jain, S., Wheeler, J., Walters, R. W., Agrawal, A., Barsic, A. J., & Parker, R. (2016) · Cell · doi:10.1016/j.cell.2015.12.038 · Cited by 1,597 · 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

A general method to improve fluorophores for live-cell and single-molecule microscopy

Grimm, J. B., English, B. P., Chen, J., Slaughter, J. P., Zhang, Z., Revyakin, A. G., Patel, R. H., Macklin, J. J., Normanno, D., Singer, R. H., et al. (2015) · Nature Methods · doi:10.1038/nmeth.3256 · Cited by 1,509 · see citing works

Compositional Control of Phase-Separated Cellular Bodies

Banani, S. F., Rice, A. M., Peeples, W. B., Lin, Y., Jain, S., Parker, R., & Rosen, M. K. (2016) · Cell · doi:10.1016/j.cell.2016.06.010 · Cited by 1,257 · 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

Flexible nets: The roles of intrinsic disorder in protein interaction networks

Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122 · see citing works

RNA buffers the phase separation behavior of prion-like RNA binding proteins

Maharana, S., Wang, J., Papadopoulos, D. K., Richter, D., Pozniakovsky, A., Poser, I., Bickle, M., Rizk, S., Guillén‐Boixet, J., Franzmann, T. M., et al. (2018) · Science · doi:10.1126/science.aar7366 · Cited by 1,111 · see citing works

A SARCOMA OF THE FOWL TRANSMISSIBLE BY AN AGENT SEPARABLE FROM THE TUMOR CELLS

Rous, P. (1911) · Journal of Experimental Medicine · doi:10.1084/jem.13.4.397 · Cited by 1,051 · 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

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 972 · see citing works

Distinct stages in stress granule assembly and disassembly

Wheeler, J., Matheny, T., Jain, S., Abrisch, R. G., & Parker, R. (2016) · eLife · doi:10.7554/elife.18413 · Cited by 806 · see citing works

P-Body Purification Reveals the Condensation of Repressed mRNA Regulons

Hubstenberger, A., Courel, M., Bénard, M., Souquère, S., Ernoult‐Lange, M., Chouaib, R., Zhou, Y., Morlot, J.-B., Munier, A., Fradet, M., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.003 · Cited by 793 · 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

Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains

Murray, D. T., Kato, M., Lin, Y., Thurber, K. R., Hung, I., McKnight, S. L., & Tycko, R. (2017) · Cell · doi:10.1016/j.cell.2017.08.048 · Cited by 740 · see citing works

Phase separation in biology; functional organization of a higher order

Mitrea, D. M., & Kriwacki, R. W. (2016) · Cell Communication and Signaling · doi:10.1186/s12964-015-0125-7 · Cited by 723 · 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

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

C9orf72 Dipeptide Repeats Impair the Assembly, Dynamics, and Function of Membrane-Less Organelles

Lee, K., Zhang, P., Kim, H. J., Mitrea, D. M., Sarkar, M., Freibaum, B. D., Cika, J., Coughlin, M., Messing, J. A., Molliex, A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.002 · Cited by 687 · see citing works

Phase separation in biology

Alberti, S. (2017) · Current Biology · doi:10.1016/j.cub.2017.08.069 · Cited by 654 · 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

Functional Domains of NEAT1 Architectural lncRNA Induce Paraspeckle Assembly through Phase Separation

Yamazaki, T., Souquère, S., Chujo, T., Kobelke, S., Chong, Y. S., Fox, A. H., Bond, C. S., Nakagawa, S., Pierron, G., & Hirose, T. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.019 · Cited by 598 · see citing works

CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins

Holehouse, A. S., Das, R. K., Ahad, J., Richardson, M. O. G., & Pappu, R. V. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2016.11.3200 · Cited by 551 · 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

Form, function, and use of retroviral Gag proteins

Wills, J. W., & Craven, R. C. (1991) · AIDS · doi:10.1097/00002030-199106000-00002 · Cited by 515 · see citing works

Direct visualization of the co-transcriptional assembly of a nuclear body by noncoding RNAs

Mao, Y. S., Sunwoo, H., Zhang, B., & Spector, D. L. (2010) · Nature Cell Biology · doi:10.1038/ncb2140 · Cited by 455 · see citing works

Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS

Sun, Z., Diaz, Z., Fang, X., Hart, M. P., Chesi, A., Shorter, J., & Gitler, A. D. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000614 · Cited by 448 · see citing works

Phase transitions and size scaling of membrane-less organelles

Brangwynne, C. P. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201308087 · Cited by 432 · see citing works

Hexanediol: a chemical probe to investigate the material properties of membrane-less compartments

Kroschwald, S., Maharana, S., & Alberti, S. (2017) · Matters · doi:10.19185/matters.201702000010 · Cited by 416 · see citing works

A TRANSMISSIBLE AVIAN NEOPLASM. (SARCOMA OF THE COMMON FOWL.)

Rous, P. (1910) · The Journal of Experimental Medicine · doi:10.1084/jem.12.5.696 · Cited by 407 · see citing works

Continuous tissue culture cell lines derived from chemically induced tumors of Japanese quail

Moscovici, C., Moscovici, M. G., Jimenez, H., Lai, M. M. C., Hayman, M. J., & Vogt, P. K. (1977) · Cell · doi:10.1016/0092-8674(77)90320-8 · Cited by 402 · see citing works

Formation of Chromatin Subcompartments by Phase Separation

Erdel, F., & Rippe, K. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.03.011 · Cited by 393 · see citing works

An optimized optogenetic clustering tool for probing protein interaction and function

Taslimi, A., Vrana, J. D., Chen, D., Borinskaya, S., Mayer, B. J., Kennedy, M. J., & Tucker, C. L. (2014) · Nature Communications · doi:10.1038/ncomms5925 · Cited by 390 · see citing works

A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation

Peskett, T. R., Rau, F., O’Driscoll, J., Patani, R., Lowe, A. R., & Saibil, H. R. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.007 · Cited by 321 · see citing works

In Vivo Identification of Human Small Ubiquitin-like Modifier Polymerization Sites by High Accuracy Mass Spectrometry and an in Vitro to in Vivo Strategy

Matić, I., van Hagen, M., Schimmel, J., Maček, B., Ogg, S. C., Tatham, M. H., Hay, R. T., Lamond, A. I., Mann, M., & Vertegaal, A. C. O. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700173-mcp200 · Cited by 303 · see citing works

Ubiquitin is part of the retrovirus budding machinery

Patnaik, A., Chau, V., & Wills, J. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.24.13069 · Cited by 292 · see citing works

Negri bodies are viral factories with properties of liquid organelles

Nikolić, J., Bars, R. L., Zoé, L., Scrima, N., Lagaudrière‐Gesbert, C., Gaudin, Y., & Blondel, D. (2017) · Nature Communications · doi:10.1038/s41467-017-00102-9 · Cited by 292 · see citing works

RNA Packaging

Berkowitz, R. D., Fisher, J., & Goff, S. P. (1996) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-80145-7_6 · Cited by 282 · see citing works

Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof

Martin, E. W., & Holehouse, A. S. (2020) · Emerging Topics in Life Sciences · doi:10.1042/etls20190164 · Cited by 272 · see citing works

Evidence for DNA-mediated nuclear compartmentalization distinct from phase separation

McSwiggen, D. T., Hansen, A. S., Marie-Nelly, H., Teves, S. S., Heckert, A. B., Dugast‐Darzacq, C., Hao, Y., Umemoto, K. K., Tjian, R., & Darzacq, X. (2019) · eLife · doi:10.7554/elife.47098 · Cited by 263 · see citing works

Positionally independent and exchangeable late budding functions of the Rous sarcoma virus and human immunodeficiency virus Gag proteins

Parent, L. J., Bennett, R. P., Craven, R. C., Nelle, T. D., Krishna, N. K., Bowzard, J. B., Wilson, C. B., Puffer, B. A., Montelaro, R. C., & Wills, J. W. (1995) · Journal of Virology · doi:10.1128/jvi.69.9.5455-5460.1995 · Cited by 258 · see citing works

Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding

Arai, M., Sugase, K., Dyson, H. J., & Wright, P. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512799112 · Cited by 250 · see citing works

Nuclear bodies: the emerging biophysics of nucleoplasmic phases

Zhu, L., & Brangwynne, C. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.04.003 · Cited by 249 · see citing works

An assembly domain of the Rous sarcoma virus Gag protein required late in budding

Wills, J. W., Cameron, C. E., Wilson, C. B., Xiang, Y., Bennett, R. P., & Leis, J. (1994) · Journal of Virology · doi:10.1128/jvi.68.10.6605-6618.1994 · Cited by 247 · see citing works

P54nrb Forms a Heterodimer with PSP1 That Localizes to Paraspeckles in an RNA-dependent Manner

Fox, A. H., Bond, C. S., & Lamond, A. I. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-06-0587 · Cited by 236 · see citing works

Phase Transitions Drive the Formation of Vesicular Stomatitis Virus Replication Compartments

Heinrich, B. S., Maliga, Z., Stein, D. A., Hyman, A. A., & Whelan, S. P. J. (2018) · mBio · doi:10.1128/mbio.02290-17 · Cited by 222 · see citing works

Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric Gag polyproteins during RNA packaging in vivo

Berkowitz, R., Ohagen, A., Höglund, S., & Goff, S. (1995) · Journal of Virology · doi:10.1128/jvi.69.10.6445-6456.1995 · Cited by 215 · see citing works

1,6-Hexanediol, commonly used to dissolve liquid–liquid phase separated condensates, directly impairs kinase and phosphatase activities

Düster, R., Kaltheuner, I. H., Schmitz, M., & Geyer, M. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100260 · Cited by 206 · see citing works

Functional organization of cytoplasmic inclusion bodies in cells infected by respiratory syncytial virus

Rincheval, V., Lelek, M., Gault, E., Bouillier, C., Sitterlin, D., Blouquit‐Laye, S., Galloux, M., Zimmer, C., Eléouët, J., & Rameix‐Welti, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00655-9 · Cited by 202 · see citing works

EasyFRAP-web: a web-based tool for the analysis of fluorescence recovery after photobleaching data

Koulouras, G., Παναγόπουλος, Α., Rapsomaniki, M., Giakoumakis, N.-N., Taraviras, S. L., & Lygerou, Z. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky508 · Cited by 179 · see citing works

Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation

Martin, E. W., Thomasen, F. E., Milkovic, N. M., Cuneo, M. J., Grace, C. R., Nourse, A., Lindorff‐Larsen, K., & Mittag, T. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab063 · Cited by 167 · see citing works

In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles

Campbell, S., & Vogt, V. (1997) · Journal of Virology · doi:10.1128/jvi.71.6.4425-4435.1997 · Cited by 162 · see citing works

Optogenetic protein clustering through fluorescent protein tagging and extension of CRY2

Park, H., Kim, N. Y., Lee, S., Kim, N., Kim, J.-H., & Heo, W. D. (2017) · Nature Communications · doi:10.1038/s41467-017-00060-2 · Cited by 158 · see citing works

Controlling compartmentalization by non-membrane-bound organelles

Wheeler, R. J., & Hyman, A. A. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2017.0193 · Cited by 153 · see citing works

Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein

Craven, R. C., Leure‐Dupree, A. E., Weldon, R. A., & Wills, J. W. (1995) · Journal of Virology · doi:10.1128/jvi.69.7.4213-4227.1995 · Cited by 152 · see citing works

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 · see citing works

Liquid Biomolecular Condensates and Viral Lifecycles: Review and Perspectives

Etibor, T. A., Yamauchi, Y., & Amorim, M. J. (2021) · Viruses · doi:10.3390/v13030366 · Cited by 140 · see citing works

Suppression of liquid–liquid phase separation by 1,6-hexanediol partially compromises the 3D genome organization in living cells

Ulianov, S. V., Velichko, A. K., Magnitov, M. D., Luzhin, A. V., Golov, A. K., Ovsyannikova, N., Kireev, I. I., Gavrikov, A. S., Mishin, A. S., Garaev, A. K., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab249 · Cited by 137 · see citing works

WW domains and retrovirus budding

Gamier, L., Wills, J., Verderame, M., & Sudol, M. (1996) · Nature · doi:10.1038/381744a0 · Cited by 132 · see citing works

It’s Raining Liquids: RNA Tunes Viscoelasticity and Dynamics of Membraneless Organelles

Guo, L. E., & Shorter, J. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.006 · Cited by 131 · see citing works

Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteins

Bennett, R. P., Nelle, T. D., & Wills, J. W. (1993) · Journal of Virology · doi:10.1128/jvi.67.11.6487-6498.1993 · Cited by 130 · see citing works

Chromosome dynamics near the sol-gel phase transition dictate the timing of remote genomic interactions

Khanna, N., Zhang, Y., Lucas, J., Dudko, O. K., & Murre, C. (2019) · Nature Communications · doi:10.1038/s41467-019-10628-9 · Cited by 123 · see citing works

Importance of Basic Residues in the Nucleocapsid Sequence for Retrovirus Gag Assembly and Complementation Rescue

Bowzard, J. B., Bennett, R., Krishna, N. K., Ernst, S. M., Rein, A., & Wills, J. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.9034-9044.1998 · Cited by 119 · see citing works

Nuclear entry and CRM1-dependent nuclear export of the Rous sarcoma virus Gag polyprotein

Scheifele, L. Z., Garbitt, R. A., Rhoads, J. D., & Parent, L. (2002) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.062652199 · Cited by 114 · see citing works

Suppression of retroviral MA deletions by the amino-terminal membrane-binding domain of p60src

Wills, J. W., Craven, R. C., Weldon, R. A., Nelle, T. D., & Erdie, C. R. (1991) · Journal of Virology · doi:10.1128/jvi.65.7.3804-3812.1991 · Cited by 112 · see citing works

Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo

Fonin, A. V., Darling, A. L., Kuznetsova, I. М., Константинович, Т. К., & Uversky, V. N. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2894-9 · Cited by 107 · see citing works

Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking

Monette, A., Niu, M., Chen, L., Rao, S., Gorelick, R. J., & Mouland, A. J. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.084 · Cited by 107 · see citing works

The Role of RNA in Biological Phase Separations

Fay, M. M., & Anderson, P. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.003 · Cited by 104 · see citing works

Specificity of retroviral RNA packaging

Aronoff, R., & Linial, M. (1991) · Journal of Virology · doi:10.1128/jvi.65.1.71-80.1991 · Cited by 103 · see citing works

Intrinsically disordered proteins: modes of binding with emphasis on disordered domains

Morris, O. M., Torpey, J. H., & Isaacson, R. L. (2021) · Open Biology · doi:10.1098/rsob.210222 · Cited by 99 · see citing works

Visualization of a missing link in retrovirus capsid assembly

Giovanni Cardone, A., Purdy, J. G., Cheng, N., Craven, R. C., & Steven, A. C. (2009) · Nature · doi:10.1038/nature07724 · Cited by 95 · see citing works

1,6-hexanediol rapidly immobilizes and condenses chromatin in living human cells

Itoh, Y., Iida, S., Tamura, S., Nagashima, R., Shiraki, K., Goto, T., Hibino, K., Ide, S., & Maeshima, K. (2021) · Life Science Alliance · doi:10.26508/lsa.202001005 · Cited by 95 · see citing works

Time-dependent effect of 1,6-hexanediol on biomolecular condensates and 3D chromatin organization

Liu, X., Jiang, S., Ma, L., Qu, J., Zhao, L., Zhu, X. Q., & Ding, J. (2021) · Genome biology · doi:10.1186/s13059-021-02455-3 · Cited by 95 · see citing works

Avian retroviral RNA encapsidation: reexamination of functional 5' RNA sequences and the role of nucleocapsid Cys-His motifs

Aronoff, R., Hajjar, A. M., & Linial, M. L. (1993) · Journal of Virology · doi:10.1128/jvi.67.1.178-188.1993 · Cited by 90 · see citing works

Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release

Weldon, R., & Wills, J. W. (1993) · Journal of Virology · doi:10.1128/jvi.67.9.5550-5561.1993 · Cited by 88 · see citing works

Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis

Mishra, P. M., Verma, N. C., Rao, C., Uversky, V. N., & Nandi, C. K. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.03.001 · Cited by 86 · see citing works

INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS

Hsu, W.-L., Oldfield, C. J., Meng, J., Huang, F., Xue, B., Uversky, V. N., Romero, P. R., & Dunker, A. K. (2011) · Pacific Symposium on Biocomputing (PSB) · doi:10.1142/9789814366496_0012 · Cited by 85 · see citing works

Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10–14 June 2012)

Foffi, G., Pastore, A., Piazza, F., & Temussi, P. A. (2013) · Physical Biology · doi:10.1088/1478-3975/10/4/040301 · Cited by 83 · see citing works

Specificity of Rous sarcoma virus nucleocapsid protein in genomic RNA packaging

Dupraz, P., & Spahr, P. (1992) · Journal of Virology · doi:10.1128/jvi.66.8.4662-4670.1992 · Cited by 77 · see citing works

Nuclear architecture by RNA

Caudron‐Herger, M., & Rippe, K. (2012) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.12.005 · Cited by 75 · see citing works

Biophysical characterization of organelle-based RNA/protein liquid phases using microfluidics

Taylor, N. O., Elbaum‐Garfinkle, S., Vaidya, N., Zhang, H., Stone, H. A., & Brangwynne, C. P. (2016) · Soft Matter · doi:10.1039/c6sm01087c · Cited by 72 · see citing works

Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus gag protein

Craven, R. C., Leure‐Dupree, A. E., Erdie, C. R., Wilson, C. B., & Wills, J. W. (1993) · Journal of Virology · doi:10.1128/jvi.67.10.6246-6252.1993 · Cited by 71 · see citing works

Deconstructing virus condensation

López, N., Camporeale, G., Salgueiro, M., Borkosky, S. S., Visentín, A., Peralta-Martinez, R., Loureiro, M. E., & Gay, G. D. P. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009926 · Cited by 69 · see citing works

Definition of a high-affinity Gag recognition structure mediating packaging of a retroviral RNA genome

Gherghe, C., Lombo, T., Leonard, C. W., Datta, S. A. K., Bess, J. W., Gorelick, R. J., Rein, A., & Weeks, K. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006897107 · Cited by 69 · see citing works

Genetic Evidence for a Connection between Rous Sarcoma Virus Gag Nuclear Trafficking and Genomic RNA Packaging

Garbitt, R. A., Kenney, S. P., & Parent, L. J. (2009) · Journal of Virology · doi:10.1128/jvi.00101-09 · Cited by 68 · see citing works

Directionality of nucleocytoplasmic transport of the retroviral gag protein depends on sequential binding of karyopherins and viral RNA

Gudleski-O'Regan, N., Flanagan, J. M., Ryan, E. P., Bewley, M. C., & Parent, L. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000304107 · Cited by 67 · see citing works

Role of Nedd4 and Ubiquitination of Rous Sarcoma Virus Gag in Budding of Virus-Like Particles from Cells

Vana, M. L., Tang, Y., Chen, A., Medina, G. N., Carter, C., & Leis, J. P. (2004) · Journal of Virology · doi:10.1128/jvi.78.24.13943-13953.2004 · Cited by 64 · see citing works

The membrane-binding domain of the Rous sarcoma virus Gag protein

Verderame, M., Nelle, T., & Wills, J. W. (1996) · Journal of Virology · doi:10.1128/jvi.70.4.2664-2668.1996 · Cited by 61 · see citing works

Dynamic multivalent interactions of intrinsically disordered proteins

Weng, J., & Wang, W. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.11.001 · Cited by 61 · see citing works

The Structure of Immature Virus-Like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the p10 Domain in Assembly

Schur, F. K. M., Dick, R. A., Hagen, W. J. H., Vogt, V. M., & Briggs, J. A. G. (2015) · Journal of Virology · doi:10.1128/jvi.01502-15 · Cited by 61 · see citing works

Detailed Mapping of the Nuclear Export Signal in the Rous Sarcoma Virus Gag Protein

Scheifele, L. Z., Ryan, E., & Parent, L. (2005) · Journal of Virology · doi:10.1128/jvi.79.14.8732-8741.2005 · Cited by 58 · see citing works

RRM domain of ALS/FTD-causing FUS characteristic of irreversible unfolding spontaneously self-assembles into amyloid fibrils

Lu, Y., Lim, L., & Song, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-01281-7 · Cited by 58 · see citing works

Formation of adenovirus DNA replication compartments

Hidalgo, P., & González, R. A. (2019) · FEBS Letters · doi:10.1002/1873-3468.13672 · Cited by 58 · see citing works

Gel or Die: Phase Separation as a Survival Strategy

Kroschwald, S., & Alberti, S. (2017) · Cell · doi:10.1016/j.cell.2017.02.029 · Cited by 58 · see citing works

Importin-β Family Members Mediate Alpharetrovirus Gag Nuclear Entry via Interactions with Matrix and Nucleocapsid

Butterfield-Gerson, K. L., Scheifele, L. Z., Ryan, E. P., Hopper, A. K., & Parent, L. J. (2006) · Journal of Virology · doi:10.1128/jvi.80.4.1798-1806.2006 · Cited by 57 · see citing works

Critical Role of Conserved Hydrophobic Residues within the Major Homology Region in Mature Retroviral Capsid Assembly

Purdy, J. G., Flanagan, J. M., Ropson, I. J., Rennoll-Bankert, K. E., & Craven, R. C. (2008) · Journal of Virology · doi:10.1128/jvi.00214-08 · Cited by 50 · see citing works

Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein: μΨ RNA Packaging Signal Complex

Zhou, J., Bean, R. L., Vogt, V. M., & Summers, M. F. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.013 · Cited by 49 · see citing works

Determination of Protein Phase Diagrams by Centrifugation

Milkovic, N. M., & Mittag, T. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0524-0_35 · Cited by 46 · see citing works

Function and Regulation of Phase-Separated Biological Condensates

Li, X., Chavali, P. L., Pancsa, R., Chavali, S., & Babu, M. M. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01228 · Cited by 45 · see citing works

On the origin of non-membrane-bound organelles, and their physiological function

Stroberg, W., & Schnell, S. D. (2017) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2017.04.006 · Cited by 44 · see citing works

When liquid-liquid phase separation meets viral infections

Wei, W., Bai, L., Yan, B., Meng, W., Wang, H., Zhai, J., Si, F., & Zheng, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.985622 · Cited by 43 · see citing works

AN EXPERIMENTAL COMPARISON OF TRANSPLANTED TUMOR AND A TRANSPLANTED NORMAL TISSUE CAPABLE OF GROWTH

Rous, P. (1910) · The Journal of Experimental Medicine · doi:10.1084/jem.12.3.344 · Cited by 42 · see citing works

NC-mediated nucleolar localization of retroviral gag proteins

Lochmann, T. L., Bann, D. V., Ryan, E. P., Beyer, A. R., Mao, A. Y., Cochrane, A., & Parent, L. J. (2012) · Virus Research · doi:10.1016/j.virusres.2012.09.011 · Cited by 42 · see citing works

Intermolecular Interactions between Retroviral Gag Proteins in the Nucleus

Kenney, S. P., Lochmann, T. L., Schmid, C. L., & Parent, L. (2007) · Journal of Virology · doi:10.1128/jvi.02049-07 · Cited by 40 · see citing works

Host RNA Packaging by Retroviruses: A Newly Synthesized Story

Eckwahl, M. J., Telesnitsky, A., & Wolin, S. L. (2016) · mBio · doi:10.1128/mbio.02025-15 · Cited by 40 · see citing works

Structure and Function of Negri Bodies

Nikolić, J., Lagaudrière‐Gesbert, C., Scrima, N., Blondel, D., & Gaudin, Y. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-14741-9_6 · Cited by 40 · see citing works

Membraneless organelles restructured and built by pandemic viruses: HIV-1 and SARS-CoV-2

Scoca, V., & Nunzio, F. D. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab020 · Cited by 39 · see citing works

Nuclear Trafficking of Retroviral RNAs and Gag Proteins during Late Steps of Replication

Stake, M. S., Bann, D. V., Maldonado, R. J. K., & Parent, L. J. (2013) · Viruses · doi:10.3390/v5112767 · Cited by 36 · see citing works

Multivalency enables unidirectional switch-like competition between intrinsically disordered proteins

Berlow, R. B., Dyson, H. J., & Wright, P. E. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2117338119 · Cited by 36 · see citing works

Proteins without unique 3D structures: Biotechnological applications of intrinsically unstable/disordered proteins

Uversky, V. N. (2014) · Biotechnology Journal · doi:10.1002/biot.201400374 · Cited by 35 · see citing works

trans -Acting Inhibition of Genomic RNA Dimerization by Rous Sarcoma Virus Matrix Mutants

Garbitt, R. A., Albert, J. A., Kessler, M. D., & Parent, L. J. (2001) · Journal of Virology · doi:10.1128/jvi.75.1.260-268.2001 · Cited by 35 · see citing works

Overlapping Roles of the Rous Sarcoma Virus Gag p10 Domain in Nuclear Export and Virion Core Morphology

Scheifele, L. Z., Kenney, S. P., Cairns, T. M., Craven, R. C., & Parent, L. J. (2007) · Journal of Virology · doi:10.1128/jvi.01061-07 · Cited by 34 · see citing works

Alterations in the MA and NC Domains Modulate Phosphoinositide-Dependent Plasma Membrane Localization of the Rous Sarcoma Virus Gag Protein

Nadaraia-Hoke, S., Bann, D. V., Lochmann, T. L., Gudleski-O'Regan, N., & Parent, L. J. (2013) · Journal of Virology · doi:10.1128/jvi.03059-12 · Cited by 31 · see citing works

An LYPSL Late Domain in the Gag Protein Contributes to the Efficient Release and Replication of Rous Sarcoma Virus

Dilley, K. A., Gregory, D., Johnson, M. C., & Vogt, V. (2010) · Journal of Virology · doi:10.1128/jvi.00238-10 · Cited by 30 · see citing works

Visualizing Association of the Retroviral Gag Protein with Unspliced Viral RNA in the Nucleus

Maldonado, R. J. K., Rice, B. L., Chen, E. C., Tuffy, K. M., Chiari, E. F., Fahrbach, K. M., Hope, T. J., & Parent, L. J. (2020) · mBio · doi:10.1128/mbio.00524-20 · Cited by 29 · see citing works

The Role of Protein Disorder in Nuclear Transport and in Its Subversion by Viruses

Wubben, J. M., Atkinson, S. C., & Borg, N. A. (2020) · Cells · doi:10.3390/cells9122654 · Cited by 29 · see citing works

Beyond Plasma Membrane Targeting: Role of the MA domain of Gag in Retroviral Genome Encapsidation

Parent, L. J., & Gudleski-O'Regan, N. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.072 · Cited by 28 · see citing works

Analyzing the Sequences of Intrinsically Disordered Regions with CIDER and localCIDER

Ginell, G. M., & Holehouse, A. S. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0524-0_5 · Cited by 22 · see citing works

How Do Intrinsically Disordered Viral Proteins Hijack the Cell?

Dyson, H. J., & Wright, P. E. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00622 · Cited by 22 · see citing works

Functional Equivalence of Retroviral MA Domains in Facilitating Psi RNA Binding Specificity by Gag

Rye-McCurdy, T., Olson, E. D., Liu, S., Binkley, C., Reyes, J. C., Thompson, B., Flanagan, J. M., Parent, L. J., & Musier‐Forsyth, K. (2016) · Viruses · doi:10.3390/v8090256 · Cited by 21 · see citing works

Interplay between the alpharetroviral Gag protein and SR proteins SF2 and SC35 in the nucleus

Rice, B. L., Maldonado, R. J. K., Stake, M. S., Lochmann, T. L., & Parent, L. J. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00925 · Cited by 11 · see citing works

TNPO3-Mediated Nuclear Entry of the Rous Sarcoma Virus Gag Protein Is Independent of the Cargo-Binding Domain

Rice, B. L., Stake, M. S., & Parent, L. J. (2020) · Journal of Virology · doi:10.1128/jvi.00640-20 · Cited by 9 · see citing works

An Optogenetic Toolkit for the Control of Phase Separation in Living Cells

Kim, C., & Shin, Y. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2663-4_19 · Cited by 4 · see citing works

Biomolecular condensates with liquid properties formed during viral infections

Glon, D., Léonardon, B., Guillemot, A., Albertini, A., Lagaudrière‐Gesbert, C., & Gaudin, Y. (2024) · Microbes and Infection · doi:10.1016/j.micinf.2024.105402 · Cited by 14 · see citing works

Evolution of Virus-like Features and Intrinsically Disordered Regions in Retrotransposon-derived Mammalian Genes

Cagliani, R., Forni, D., Mozzi, A., Fuchs, R., Tussia-Cohen, D., Arrigoni, F., Pozzoli, U., GIOIA, L. D., Hagai, T., & Sironi, M. (2024) · Molecular Biology and Evolution · doi:10.1093/molbev/msae154 · Cited by 12 · see citing works

Virus Induced Membraneless Organelles and Biomolecular Condensates

Mouland, A. J., Parent, L. J., Weber, S. C., & Holehouse, A. S. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168213 · Cited by 6 · see citing works

Comparative analysis of retroviral Gag-host cell interactions: focus on the nuclear interactome

Lambert, G. S., Rice, B. L., Maldonado, R. J. K., Chang, J., & Parent, L. J. (2024) · Retrovirology · doi:10.1186/s12977-024-00645-y · Cited by 5 · see citing works

Role of the Psi Packaging Signal and Dimerization Initiation Sequence in the Organization of Rous Sarcoma Virus Gag-gRNA Co-Condensates

Lambert, G. S., Maldonado, R. J. K., & Parent, L. J. (2025) · Viruses · doi:10.3390/v17010097 · Cited by 3 · see citing works

RNA ‐centric world of retroviruses: unravelling the molecular strategies of genomic RNA packaging

Jehad, M. A., Prabhu, S., Ali, L. M., Pillai, V. N., Mustafa, F., & Rizvi, T. A. (2026) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1002/brv.70188 · Cited by 2 · see citing works

Dynamic interactions of retroviral Gag condensates with nascent viral RNA at transcriptional burst sites: implications for genomic RNA packaging

Maldonado, R. J. K., & Parent, L. J. (2025) · mBio · doi:10.1128/mbio.01695-25 · Cited by 1 · see citing works

Methodological approaches to studying phase separation and HIV-1 replication: Current and future perspectives

Mouland, A. J., Chau, B.-A., & Uversky, V. N. (2024) · Methods · doi:10.1016/j.ymeth.2024.07.002 · Cited by 1 · see citing works

Two Peas in a Pod: Retroviral RNA Dimers Organize Gag–RNA Nanoclusters with Novel Biophysical Properties

Lambert, G. S., Siedlecki, C. A., & Parent, L. J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26125679 · Cited by 1 · see citing works

Influence of HIV-1 Genomic RNA on the Formation of Gag Biomolecular Condensates

Monette, A., Niu, M., Maldonado, R. J. K., Chang, J. T., Lambert, G. S., Flanagan, J. M., Cochrane, A., Parent, L. J., & Mouland, A. J. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168190 · Cited by 13 · see citing works

Role of the Psi Packaging Signal and Dimerization Initiation Sequence in the Organization of Rous Sarcoma Virus Gag-gRNA Co-Condensates

Lambert, G. S., Maldonado, R. J. K., & Parent, L. J. (2025) · Viruses · doi:10.3390/v17010097 · Cited by 3 · see citing works

Scaffolding viral protein NC nucleates phase separation of the HIV-1 biomolecular condensate

Monette, A., Niu, M., Asser, M. N., Gorelick, R. J., & Mouland, A. J. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111251 · Cited by 33 · see citing works

Uncovering protein conformational dynamics within two‐component viral biomolecular condensates

Colyer, A., Acker, J., Borodavka, A., & Calabrese, A. N. (2025) · Protein Science · doi:10.1002/pro.70181 · Cited by 3 · see citing works

Two Peas in a Pod: Retroviral RNA Dimers Organize Gag–RNA Nanoclusters with Novel Biophysical Properties

Lambert, G. S., Siedlecki, C. A., & Parent, L. J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26125679 · Cited by 1 · see citing works