The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
Open accessAbstract
Eukaryotic cells contain assemblies of RNAs and proteins termed RNA granules. Many proteins within these bodies contain KH or RRM RNA-binding domains as well as low complexity (LC) sequences of unknown function. We discovered that exposure of cell or tissue lysates to a biotinylated isoxazole (b-isox) chemical precipitated hundreds of RNA-binding proteins with significant overlap to the constituents of RNA granules. The LC sequences within these proteins are both necessary and sufficient for b-isox-mediated aggregation, and these domains can undergo a concentration-dependent phase transition to a hydrogel-like state in the absence of the chemical. X-ray diffraction and EM studies revealed the hydrogels to be composed of uniformly polymerized amyloid-like fibers. Unlike pathogenic fibers, the LC sequence-based polymers described here are dynamic and accommodate heterotypic polymerization. These observations offer a framework for understanding the function of LC sequences as well as an organizing principle for cellular structures that are not membrane bound.
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?
In the citing paper
“This module contained proteins often found in RNA granules [48]”
From Deep proteomic network analysis of Alzheimer’s disease brain reveals alterations in RNA binding proteins and RNA splicing associated with disease (2018) · cites this paper as [48]
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
Sheldrick, G. M. (2007) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767307043930 · Cited by 88,113
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
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
Natively unfolded proteins: A point where biology waits for physics
Uversky, V. N. (2002) · Protein Science · doi:10.1110/ps.4210102 · Cited by 1,852
Eukaryotic Stress Granules: The Ins and Outs of Translation
Buchan, J. R., & Parker, R. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.11.020 · Cited by 1,535
Kedersha, N., Gupta, M., Li, W., Miller, I. J., & Anderson, P. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.7.1431 · Cited by 1,260
[URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae
Wickner, R. B. (1994) · Science · doi:10.1126/science.7909170 · Cited by 1,216
Kanai, Y., Dohmae, N., & Hirokawa, N. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.022 · Cited by 1,109
Stress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1
Farny, N. G., Kedersha, N., Ayodele, M. O., Shen, L., Stoecklin, G., Dember, L. M., & Anderson, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0715 · Cited by 1,017
Flagged first, then by citations
Research works printed but not linked: 3
- Sheffield, P., Garrard, S., and Derewenda, Z. (1999). Overcoming expression and purification problems of RhoGDI using a family of “parallel” expression vectors. Protein Expr. Purif. 15, 34–39. · DOI
- Sheldrick, G.M. (2008). A short history of SHELX. Acta Crystallogr. A 64, 112–122. · DOI
- Wootton, J.C., and Federhen, S. (1996). Analysis of compositionally biased regions in sequence databases. Methods Enzymol. 266, 554–571. · DOI
Cited by
Sorted by citations
Items 901–1,000 of 1,003
Falkenberg, C. V., Blinov, M. L., & Loew, L. M. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.10.016 · Cited by 38
Smad4 sequestered in SFPQ condensates prevents TGF-β tumor-suppressive signaling
Xiao, M., Wang, F., Chen, N., Zhang, H., Cao, J., Yu, Y., Zhao, B., Ji, J., Xu, P., Li, L., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.11.020 · Cited by 39
Self-citationFunctional specificity in biomolecular condensates revealed by genetic complementation
Sabari, B. R., Hyman, A. A., & Hnisz, D. (2024) · Nature Reviews Genetics · doi:10.1038/s41576-024-00780-4 · Cited by 35
Assessing amyloid fibrils and amorphous aggregates: A review
Basha, S., Mukunda, D. C., Pai, A. R., & Mahato, K. K. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143725 · Cited by 40
Linser, R., Sarkar, R., Krushelnitzky, A., Mainz, A., & Reif, B. (2014) · Journal of Biomolecular NMR · doi:10.1007/s10858-014-9822-6 · Cited by 36
The role of cold shock domain proteins in inflammatory diseases
Lindquist, J. A., Brandt, S., Bernhardt, A., Zhu, C., & Mertens, P. R. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1136-3 · Cited by 38
Molecular Origin of pH‐Dependent Fibril Formation of a Functional Amyloid
McGlinchey, R. P., Jiang, Z., & Lee, J. C. (2014) · ChemBioChem · doi:10.1002/cbic.201402074 · Cited by 37
Computational analysis of candidate prion-like proteins in bacteria and their role
Iglesias, V., de Groot, N. S., & Ventura, S. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01123 · Cited by 36
Binding of NUFIP2 to Roquin promotes recognition and regulation of ICOS mRNA
Rehage, N., Davydova, E., Conrad, C., Behrens, G., Maiser, A., Stehklein, J. E., Brenner, S., Klein, J., Jeridi, A., Hoffmann, A., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02582-1 · Cited by 36
Sun, Y., Cruz, A. M., Hadley, K. C., Galant, N. J., Law, R., Vernon, R. M., Morris, V. K., Robertson, J., & Chakrabartty, A. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00842 · Cited by 37
Holt, C., Raynes, J. K., & Carver, J. A. (2019) · Biopolymers · doi:10.1002/bip.23319 · Cited by 37
Age‐related neurodegenerative diseases
Duggan, M. R., Torkzaban, B., Ahooyi, T. M., Khalili, K., & Gordon, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29248 · Cited by 40
The expanding world of metabolic enzymes moonlighting as RNA binding proteins
Curtis, N. J., & Jeffery, C. J. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200664 · Cited by 37
Targeted modulation of protein liquid–liquid phase separation by evolution of amino-acid sequence
Lichtinger, S. M., Garaizar, A., Collepardo‐Guevara, R., & Reinhardt, A. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009328 · Cited by 37
Biomolecular condensates in cancer biology
Suzuki, H. I., & Onimaru, K. (2021) · Cancer Science · doi:10.1111/cas.15232 · Cited by 37
Molecular Investigations of Protein Aggregation in the Pathogenesis of Amyotrophic Lateral Sclerosis
Duranti, E., & Villa, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010704 · Cited by 40
Zhang, H., Gu, J., Zhang, Y., Guo, H., Zhang, S., Song, J., Liu, C., Wang, L. F., Li, D., & Dai, B. (2023) · ACS Nano · doi:10.1021/acsnano.3c00001 · Cited by 36
Heterologous Aggregates Promote De Novo Prion Appearance via More than One Mechanism
Arslan, F., Hong, J. Y., Kanneganti, V., Park, S.-K., & Liebman, S. W. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1004814 · Cited by 36
Hutten, S., Sharangdhar, T., & Kiebler, M. A. (2014) · RNA Biology · doi:10.4161/rna.32091 · Cited by 37
Scherrer, K. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.09.011 · Cited by 38
Shi, M., Zhang, P., Vora, S. M., & Wu, H. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.03.002 · Cited by 39
Kankel, M. W., Sen, A., Lü, L., Theodorou, M., Dimlich, D. N., McCampbell, A., Henderson, C. E., Shneider, N. A., & Artavanis‐Tsakonas, S. (2020) · Genetics · doi:10.1534/genetics.119.302985 · Cited by 35
Application of yeast to studying amyloid and prion diseases
Chernoff, Y. O., Grizel, A. V., Rubel, A. A., Zelinsky, A. А., Chandramowlishwaran, P., & Chernova, T. A. (2020) · Advances in genetics · doi:10.1016/bs.adgen.2020.01.002 · Cited by 41
Pal, T., Wessén, J., Das, S., & Chan, H. S. (2021) · Physical review. E · doi:10.1103/physreve.103.042406 · Cited by 36
Roles of protein arginine methyltransferase 1 (PRMT1) in brain development and disease
Hashimoto, M., Fukamizu, A., Nakagawa, T., & Kizuka, Y. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129776 · Cited by 36
Amyotrophic Lateral Sclerosis Genes in Drosophila melanogaster
Layalle, S., They, L., Ourghani, S., Raoul, C., & Soustelle, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020904 · Cited by 36
Distinct roles of hnRNPH1 low-complexity domains in splicing and transcription
Kim, G. H., & Kwon, I. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2109668118 · Cited by 36
Paxman, J., Zhou, Z., O’Laughlin, R., Liu, Y., Li, Y., Tian, W., Su, H., Jiang, Y., Holness, S. E., Stasiowski, E., et al. (2022) · eLife · doi:10.7554/elife.75978 · Cited by 37
Duran-Arqué, B., Cañete, M., Castellazzi, C. L., Bartomeu, A., Ferrer-Caelles, A., Reina, Ó., Caballé, A., Gay, M., Arauz‐Garofalo, G., Belloc, E., et al. (2022) · Genome biology · doi:10.1186/s13059-022-02759-y · Cited by 35
Biomolecular condensation involving the cytoskeleton
Mohapatra, S., & Wegmann, S. (2023) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2023.01.009 · Cited by 37
Towards sequence-based principles for protein phase separation predictions
Vendruscolo, M., & Fuxreiter, M. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102317 · Cited by 38
Bish, R. A., Cuevas-Polo, N., Cheng, Z., Hambardzumyan, D., Munschauer, M., Landthaler, M., & Vogel, C. (2015) · Biomolecules · doi:10.3390/biom5031441 · Cited by 34
The Y-Box Binding Protein 1 Suppresses Alzheimer’s Disease Progression in Two Animal Models
Бобкова, Н. В., Lyabin, D. N., Medvinskaya, N. I., Samokhin, A. N., Nekrasov, P. V., Nesterova, I. V., Aleksandrova, I. Y., Tatarnikova, O. G., Bobylev, A. G., Vikhlyantsev, I. M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138867 · Cited by 35
Idiosyncrasies of hnRNP A1-RNA recognition: Can binding mode influence function
Levengood, J. D., & Tolbert, B. S. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.04.001 · Cited by 34
Protein phase separation in mitosis
Tiwary, A. K., & Zheng, Y. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.04.011 · Cited by 35
Amyloid and Amyloid-Like Aggregates: Diversity and the Term Crisis
Matiiv, A. B., Trubitsina, N. P., Matveenko, A. G., Barbitoff, Y. A., Zhouravleva, G. A., & Bondarev, S. A. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920090035 · Cited by 33
Jo, Y., Jang, J., Song, D., Park, H., & Jung, Y. (2021) · Chemical Science · doi:10.1039/d1sc05672g · Cited by 35
Klein, M. E., Monday, H. R., & Jordan, B. A. (2016) · Neural Plasticity · doi:10.1155/2016/3857934 · Cited by 37
DEAD-box ATPases as regulators of biomolecular condensates and membrane-less organelles
Overwijn, D., & Hondele, M. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.10.001 · Cited by 34
Synaptic control of local translation: the plot thickens with new characters
Thomas, M. G., Pascual, M. L., Maschi, D., Luchelli, L., & Boccaccio, G. L. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1506-y · Cited by 38
An Atypical Tropomyosin in Drosophila with Intermediate Filament-like Properties
Cho, A., Kato, M., Whitwam, T., Kim, J. H., & Montell, D. J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.054 · Cited by 34
Self-citationDynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide
Jean, L., Lee, C. F., Hodder, P., Hawkins, N., & Vaux, D. J. (2016) · Scientific Reports · doi:10.1038/srep32124 · Cited by 34
Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1
Paul, K. R., Molliex, A., Cascarina, S., Boncella, A. E., Taylor, J., & Ross, E. D. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00652-16 · Cited by 33
Prion-based nanomaterials and their emerging applications
Díaz-Caballero, M., Fernández, M. R., Navarro, S., & Ventura, S. (2018) · Prion · doi:10.1080/19336896.2018.1521235 · Cited by 34
Prieto, C., Nguyen, D. T. T., Liu, Z., Wheat, J. C., Perez, A. R., Gourkanti, S., Chou, T., Barin, E., Velleca, A., Rohwetter, T. M., et al. (2021) · Nature Cancer · doi:10.1038/s43018-021-00220-w · Cited by 38
Johnson, R. M., Vu, N., Griffin, B. P., Gentry, A. E., Archer, K. J., Chalfant, C. E., & Park, M. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.671206 · Cited by 34
Vulnerability of microRNA biogenesis in FTD–ALS
Eitan, C., & Hornstein, E. (2016) · Brain Research · doi:10.1016/j.brainres.2015.12.063 · Cited by 38
Prions, amyloids, and RNA: Pieces of a puzzle
Nizhnikov, A., Antonets, K., Bondarev, S., Inge-Vechtomov, S., & Derkatch, I. L. (2016) · Prion · doi:10.1080/19336896.2016.1181253 · Cited by 32
Regulation of nucleolus assembly by non-coding RNA polymerase II transcripts
Caudron‐Herger, M., Pankert, T., & Rippe, K. (2016) · Nucleus · doi:10.1080/19491034.2016.1190890 · Cited by 33
Mechanisms of Vertebrate Germ Cell Determination
Aguero, T. H., Kassmer, S. H., Alberio, R., Johnson, A. D., & King, M. L. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-46095-6_8 · Cited by 34
Arginine-rich Peptides Can Actively Mediate Liquid-liquid Phase Separation
Boeynaems, S., Decker, M. D., Tompa, P., & Bosch, L. V. D. (2017) · BIO-PROTOCOL · doi:10.21769/bioprotoc.2525 · Cited by 34
Self-Assembly of Spider Silk-Fusion Proteins Comprising Enzymatic and Fluorescence Activity
Humeník, M., Mohrand, M., & Scheibel, T. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.7b00759 · Cited by 33
Grignaschi, E., Cereghetti, G., Grigolato, F., Kopp, M. R. G., Caimi, S., Faltova, L., Saad, S., Peter, M., & Arosio, P. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001628 · Cited by 34
Order/Disorder in Protein and Peptide‐Based Biomaterials
Ulijn, R. V., & Lampel, A. (2019) · Israel Journal of Chemistry · doi:10.1002/ijch.201900051 · Cited by 33
Effect of additives on liquid droplets and aggregates of proteins
Shiraki, K., Mimura, M., Nishinami, S., & Ura, T. (2020) · Biophysical Reviews · doi:10.1007/s12551-020-00682-9 · Cited by 33
Zhu, M., Kuechler, E. R., Zhang, J., Matalon, O., Dubreuil, B., Hofmann, A., Loewen, C., Levy, E. D., Gsponer, J., & Mayor, T. (2020) · Journal of Cell Science · doi:10.1242/jcs.244657 · Cited by 33
Antagonistic roles for Ataxin-2 structured and disordered domains in RNP condensation
Singh, A., Huelsmeier, J., Kandi, A. R., Pothapragada, S. S., Hillebrand, J., Petrauskas, A., Agrawal, K., Krishnan, R., Thiagarajan, D., Jayaprakashappa, D., et al. (2021) · eLife · doi:10.7554/elife.60326 · Cited by 32
Egea, P. F. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.784367 · Cited by 35
Liquid-Liquid Phase Separation in Nucleation Process of Biomineralization
Qin, D., He, Z., Li, P., & Zhang, S. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.834503 · Cited by 34
Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils
Garg, D. K., & Bhat, R. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.05.042 · Cited by 33
Kalwat, M. A., Huang, Z., Wichaidit, C., McGlynn, K., Earnest, S. A., Savoia, C., Dioum, E. M., Schneider, J. W., Hutchison, M. R., & Cobb, M. H. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00993 · Cited by 33
Self-citationMittal, A., Lyle, N. J., Harmon, T. S., & Pappu, R. V. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct5002297 · Cited by 33
Liquid-liquid phase separation as a major mechanism of plant abiotic stress sensing and responses
Liu, X., Zhu, J., & Zhao, C. (2023) · Stress Biology · doi:10.1007/s44154-023-00141-x · Cited by 32
Verde, E. M., Secco, V., Ghezzi, A., Mandrioli, J., & Carra, S. (2025) · Cells · doi:10.3390/cells14100680 · Cited by 35
3′UTRs take a long shot in the brain
Wang, L., & Yi, R. (2013) · BioEssays · doi:10.1002/bies.201300100 · Cited by 30
Beyond the cytoskeleton: mesoscale assemblies and their function in spatial organization
Wilson, M. Z., & Gitai, Z. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.03.008 · Cited by 32
Modifiers of solid RNP granules control normal RNP dynamics and mRNA activity in early development
Hubstenberger, A., Cameron, C., Noble, S. L., Keenan, S., & Evans, T. C. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201504044 · Cited by 35
Baloh, R. H. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a269b · Cited by 33
A glass menagerie of low complexity sequences
Halfmann, R. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.05.002 · Cited by 32
PRMT1-mediated methylation of the microprocessor-associated proteins regulates microRNA biogenesis
Spadotto, V., Giambruno, R., Massignani, E., Mihailovich, M., Maniaci, M., Patuzzo, F., Ghini, F., Nicassio, F., & Bonaldi, T. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1051 · Cited by 32
Periphilin self-association underpins epigenetic silencing by the HUSH complex
Prigozhin, D. M., Douse, C. H., Farleigh, L. E., Albecka, A., Tchasovnikarova, I. A., Timms, R. T., Oda, S.-I., Adolf, F., Freund, S. M. V., Maslen, S., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa785 · Cited by 38
Fomicheva, A., & Ross, E. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031251 · Cited by 30
Emerging Roles for Phase Separation of RNA-Binding Proteins in Cellular Pathology of ALS
Milicevic, K. D., Ranković, B., Anđjus, P. R., Bataveljić, D., & Milovanović, D. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.840256 · Cited by 32
Lin, Y., Wessén, J., Pal, T., Das, S., & Chan, H. S. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2663-4_3 · Cited by 32
Staples, M. I., Frazer, C., Fawzi, N. L., & Bennett, R. J. (2023) · Nature Microbiology · doi:10.1038/s41564-022-01314-6 · Cited by 37
Holehouse, A. S., & Pappu, R. V. (2015) · Nature Materials · doi:10.1038/nmat4459 · Cited by 32
Synaptic control of mRNA translation by reversible assembly of XRN1 bodies
Luchelli, L., Thomas, M. G., & Boccaccio, G. L. (2015) · Journal of Cell Science · doi:10.1242/jcs.163295 · Cited by 31
Characterization of Soft Amyloid Cores in Human Prion-Like Proteins
Batlle, C., de Groot, N. S., Iglesias, V., Navarro, S., & Ventura, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-09714-z · Cited by 32
Li, M., Fan, Y., Li, Q., Wang, X., Zhao, L., & Zhu, M. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7165387 · Cited by 32
RNA granules in flux: dynamics to balance physiology and pathology
Kiebler, M. A., & Bauer, K. E. (2024) · Nature reviews. Neuroscience · doi:10.1038/s41583-024-00859-1 · Cited by 37
Udayakumar, D., & Dynan, W. S. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.05.024 · Cited by 31
Perspective on SOD1 mediated toxicity in Amyotrophic Lateral Sclerosis
Sangwan, S., & Eisenberg, D. S. (2016) · Postępy Biochemii · doi:10.18388/pb.2016_37 · Cited by 31
Self-citationTargeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology
Fujita, K., Chen, X., Homma, H., Tagawa, K., Amano, M., Saito, A., Imoto, S., Akatsu, H., Hashizume, Y., Kaibuchi, K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-02821-z · Cited by 31
FMRP regulates presynaptic localization of neuronal voltage gated calcium channels
Ferron, L., Novazzi, C. G., Pilch, K. S., Moreno, C., Ramgoolam, K., & DOLPHIN, A. C. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104779 · Cited by 31
Peptide-based Interaction Proteomics
Meyer, K., & Selbach, M. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r120.002034 · Cited by 32
Zhang, M., Shi, H., Zhang, X., Zhang, X., & Huang, Y. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000748 · Cited by 31
Advances in the phase separation-organized membraneless organelles in cells: a narrative review
Li, W., Jiang, C., & Zhang, E. (2021) · Translational Cancer Research · doi:10.21037/tcr-21-1111 · Cited by 31
Graham, L. D., Glattauer, V., Li, D., Tyler, M. J., & Ramshaw, J. A. M. (2013) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2013.04.008 · Cited by 31
The role of FLI-1-EWS, a fusion gene reciprocal to EWS-FLI-1, in Ewing sarcoma
Elzi, D. J., Song, M., Houghton, P. J., Chen, Y., & Shiio, Y. (2015) · Genes & Cancer · doi:10.18632/genesandcancer.86 · Cited by 34
Jim's View: Is the Golgi stack a phase‐separated liquid crystal?
Rothman, J. E. (2019) · FEBS Letters · doi:10.1002/1873-3468.13609 · Cited by 31
Lewis, B. A., Das, S., Jha, R. K., & Levens, D. (2023) · Science Advances · doi:10.1126/sciadv.adi4565 · Cited by 30
Nickerson, J. A., & Momen‐Heravi, F. (2024) · Nucleus · doi:10.1080/19491034.2024.2350180 · Cited by 33
Phase Separation and Aggregation of α‐Synuclein Diverge at Different Salt Conditions
Sternke‐Hoffmann, R., Sun, X., Menzel, A., Pinto, M. D. S., Venclovaitė, U., Wördehoff, M. M., Hoyer, W., Zheng, W., & Luo, J. (2024) · Advanced Science · doi:10.1002/advs.202308279 · Cited by 30
Translation and silencing in RNA granules: a tale of sand grains
Pimentel, J. N., & Boccaccio, G. L. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00068 · Cited by 30
Krüger, T., Hofweber, M., & Krämer, S. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-01-0068 · Cited by 30
Nucleoli and Stress Granules: Connecting Distant Relatives
Mahboubi, H., & Stochaj, U. (2014) · Traffic · doi:10.1111/tra.12191 · Cited by 33
Manna, S. L., Scognamiglio, P. L., Roviello, V., Borbone, F., Florio, D., Natale, C. D., Bigi, A., Cecchi, C., Cascella, R., Giannini, C., et al. (2019) · FEBS Journal · doi:10.1111/febs.14815 · Cited by 30
Exploiting Replication Stress as a Novel Therapeutic Intervention
Martin, J. C., Hoegel, T. J., Lynch, M. L., Woloszynska‐Read, A., Melendy, T., & Ohm, J. E. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0651 · Cited by 32
Altered Phase Separation and Cellular Impact in C9orf72-Linked ALS/FTD
Solomon, D. A., Smikle, R., Reid, M. J., & Mizielinska, S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.664151 · Cited by 33
Salladini, E., Gondelaud, F., Nilsson, J. F., Pesce, G., Bignon, C., Murrali, M. G., Fabre, R., Pierattelli, R., Kajava, A. V., Horvat, B., et al. (2021) · Biomolecules · doi:10.3390/biom11091324 · Cited by 30
Metadata
- Authors
- Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., Grishin, N. V., Frantz, D. E., Schneider, J. W., Chen, S., Li, L., Sawaya, M. R., Eisenberg, D., Tycko, R., & McKnight, S. L.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Howard Hughes Medical Institute (US)
- National Institute of Biological Sciences, Beijing (CN)
- National Institutes of Health (US)
- Corresponding author
- McKnight, Steven L.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 149
- Issue
- 4
- Pages
- 753-767
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC6347373
- OpenAlex
- W2120156669
- Cited by
- 2,012
- References
- 51
- Citations by year
- 2026: 100 · 2025: 104 · 2024: 130 · 2023: 139 · 2022: 195 · 2021: 227 · 2020: 198 · 2019: 167 · 2018: 177 · 2017: 128 · 2016: 127 · 2015: 120 · 2014: 91 · 2013: 83 · 2012: 22
- FWCI
- 40.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (ZIADK075031)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- RNA granules, low-complexity sequences, RNA-binding proteins, KH domain, RRM domain, protein aggregation, hydrogels, phase separation, cell-free system, protein condensates
- MeSH terms
- Animals, Brain, Cell-Free System, Cytoplasmic Granules, Male, Models, Molecular, RNA, Testis, X-Ray Diffraction, RNA-Binding Proteins, Caenorhabditis elegans, Hydrogel, Polyethylene Glycol Dimethacrylate, NIH 3T3 Cells, Mice, Embryonic Stem Cells
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