{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T05:23:39Z","timestamp":1787289819195,"version":"build-2736575974"},"reference-count":163,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T00:00:00Z","timestamp":1787097600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100024250","name":"Israel innovation authority","doi-asserted-by":"crossref","award":["89600"],"award-info":[{"award-number":["89600"]}],"id":[{"id":"10.13039\/501100024250","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Genes"],"abstract":"<jats:p>Biomolecular condensates are dynamic membraneless organelles composed of proteins and RNAs that assemble through multivalent interactions and provide cells with powerful means to regulate gene expression in space and time. Different epitranscriptomic marks such as m6A, m1A, and m5C can reshape RNA structure\u2014binding interfaces and multivalency and, in this manner, tuning which transcripts nucleate or partition into specific condensates and influencing their material state. This review summarizes how individual RNA modifications and their associated proteins regulate the formation and function of BMCs such as stress granules, P-bodies, nuclear bodies and disease-linked condensates in cancer and neurodegeneration. It highlights emerging concepts of combinatorial \u201cepitranscriptomic codes\u201d and bidirectional feedback between condensates and RNA-modifying enzymes and discusses the current experimental and technical gaps that still limit our understanding of modification crosstalk and condensate topology.<\/jats:p>","DOI":"10.3390\/genes17080973","type":"journal-article","created":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T11:04:12Z","timestamp":1787137452000},"page":"973","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["RNA Modifications Modulate Biomolecular Condensates in Stress and Disease"],"prefix":"10.3390","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2391-9947","authenticated-orcid":false,"given":"Y.","family":"Sprecher","sequence":"first","affiliation":[{"name":"Sheba Cancer Research Center, Sheba Medical Center, Tel Hashomer, Ramat Gan 5266202, Israel"},{"name":"Gray Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv 6997801, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9092-0411","authenticated-orcid":false,"given":"M.","family":"Sevilla-Sharon","sequence":"additional","affiliation":[{"name":"Sheba Cancer Research Center, Sheba Medical Center, Tel Hashomer, Ramat Gan 5266202, Israel"},{"name":"Gray Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv 6997801, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2465-6664","authenticated-orcid":false,"given":"S.","family":"Moshitch-Moshkovitz","sequence":"additional","affiliation":[{"name":"Sheba Cancer Research Center, Sheba Medical Center, Tel Hashomer, Ramat Gan 5266202, Israel"},{"name":"Gray Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv 6997801, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,8,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"EMBJ2021110137","DOI":"10.15252\/embj.2021110137","article-title":"RNA is required for the integrity of multiple nuclear and cytoplasmic membrane-less RNP granules","volume":"41","author":"Decker","year":"2022","journal-title":"EMBO J."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"4737","DOI":"10.1016\/j.cell.2023.09.006","article-title":"Formation, function, and pathology of RNP granules","volume":"186","author":"Ripin","year":"2023","journal-title":"Cell"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1016\/j.cell.2006.11.026","article-title":"SnapShot: Cellular bodies","volume":"127","author":"Spector","year":"2006","journal-title":"Cell"},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Uversky, V.N. (2023). Biological Liquid-Liquid Phase Separation, Biomolecular Condensates, and Membraneless Organelles: Now You See Me, Now You Don\u2019t. Int. J. Mol. Sci., 24.","DOI":"10.3390\/books978-3-0365-8930-5"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1800085","DOI":"10.1002\/bies.201800085","article-title":"RNAs, phase separation, and membrane-less organelles: Are post-transcriptional modifications modulating organelle dynamics?","volume":"40","author":"Drino","year":"2018","journal-title":"Bioessays"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: Organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"7115","DOI":"10.1074\/jbc.TM118.001192","article-title":"The molecular language of membraneless organelles","volume":"294","author":"Gomes","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2202855","DOI":"10.1002\/advs.202202855","article-title":"Emerging Implications of Phase Separation in Cancer","volume":"9","author":"Ren","year":"2022","journal-title":"Adv. Sci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"4636","DOI":"10.1016\/j.jmb.2018.08.005","article-title":"Multiple Modes of Protein-Protein Interactions Promote RNP Granule Assembly","volume":"430","author":"Mittag","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"135907","DOI":"10.1016\/j.ijbiomac.2024.135907","article-title":"The role of phase separation in RNA modification: Both cause and effect","volume":"280","author":"Lu","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.ncrna.2026.01.003","article-title":"Noncoding RNAs are indispensable architects and regulators of biomolecular condensates","volume":"18","author":"Chen","year":"2026","journal-title":"Non-Coding RNA Res."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Arsi\u00e8, R., Tartaglia, G.G., and Vabulas, R.M. (2025). Methyladenine as a regulator of biomolecular condensation. Front. Mol. Biosci., 12.","DOI":"10.3389\/fmolb.2025.1722147"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"4683","DOI":"10.7150\/thno.99019","article-title":"The role of m6A-associated membraneless organelles in the RNA metabolism processes and human diseases","volume":"14","author":"Bu","year":"2024","journal-title":"Theranostics"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/s41580-020-0264-6","article-title":"RNA contributions to the form and function of biomolecular condensates","volume":"22","author":"Roden","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Su, Y., Maimaitiyiming, Y., Wang, L., Cheng, X., and Hsu, C.-H. (2021). Modulation of Phase Separation by RNA: A Glimpse on N6-Methyladenosine Modification. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.786454"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1016\/j.jmb.2019.01.028","article-title":"RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43","volume":"431","author":"Zacco","year":"2019","journal-title":"J. Mol. Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"7730","DOI":"10.1038\/s41467-025-62055-8","article-title":"Current practices in the study of biomolecular condensates: A community comment","volume":"16","author":"Alberti","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1038\/s41589-020-0524-y","article-title":"m6A-binding YTHDF proteins promote stress granule formation","volume":"16","author":"Fu","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1038\/s41586-019-1374-1","article-title":"m6A enhances the phase separation potential of mRNA","volume":"571","author":"Ries","year":"2019","journal-title":"Nature"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1038\/s41422-019-0210-3","article-title":"Multivalent m6A motifs promote phase separation of YTHDF proteins","volume":"29","author":"Gao","year":"2019","journal-title":"Cell Res."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"3735","DOI":"10.1038\/s41467-022-31358-5","article-title":"Limited effects of m6A modification on mRNA partitioning into stress granules","volume":"13","author":"Khong","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1016\/j.ccell.2021.04.017","article-title":"N6-Methyladenosine on mRNA facilitates a phase-separated nuclear body that suppresses myeloid leukemic differentiation","volume":"39","author":"Cheng","year":"2021","journal-title":"Cancer Cell"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3368","DOI":"10.1016\/j.molcel.2021.07.024","article-title":"Enhancer RNA m6A methylation facilitates transcriptional condensate formation and gene activation","volume":"81","author":"Lee","year":"2021","journal-title":"Mol. Cell"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"3816","DOI":"10.1093\/nar\/gkaa048","article-title":"The m6A reader YTHDF1 promotes ovarian cancer progression via augmenting EIF3C translation","volume":"48","author":"Liu","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"e2410532","DOI":"10.1002\/advs.202410532","article-title":"CircDNA2-Educated YTHDF2 Phase Separation Promotes PM(2.5)-Induced Malignant Transformation Through the Blunting of GADD45A Expression","volume":"12","author":"Xu","year":"2025","journal-title":"Adv. Sci."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/s41556-018-0045-z","article-title":"Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation","volume":"20","author":"Huang","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"9054","DOI":"10.1038\/s41467-024-53400-4","article-title":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism","volume":"15","author":"Hornegger","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"e26","DOI":"10.1093\/nar\/gku1275","article-title":"Stress granules are dispensable for mRNA stabilization during cellular stress","volume":"43","author":"Bley","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"6051","DOI":"10.1093\/nar\/gkx141","article-title":"N6-methyladenosine alters RNA structure to regulate binding of a low-complexity protein","volume":"45","author":"Liu","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1038\/nature14234","article-title":"N6-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions","volume":"518","author":"Liu","year":"2015","journal-title":"Nature"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1093\/jmcb\/mjaa023","article-title":"The protective role of m1A during stress-induced granulation","volume":"12","author":"Alriquet","year":"2021","journal-title":"J. Mol. Cell Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1038\/s41586-023-06701-5","article-title":"m1A in CAG repeat RNA binds to TDP-43 and induces neurodegeneration","volume":"623","author":"Sun","year":"2023","journal-title":"Nature"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1093\/nar\/gkad1193","article-title":"Histone lactylation-boosted ALKBH3 potentiates tumor progression and diminished promyelocytic leukemia protein nuclear condensates by m1A demethylation of SP100A","volume":"52","author":"Gu","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Liu, X.M., Ma, L., and Schekman, R. (2021). Selective sorting of microRNAs into exosomes by phase-separated YBX1 condensates. eLife, 10.","DOI":"10.7554\/eLife.71982"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"e70270","DOI":"10.1002\/ctm2.70270","article-title":"Targeting YBX1-m5C mediates RNF115 mRNA circularisation and translation to enhance vulnerability of ferroptosis in hepatocellular carcinoma","volume":"15","author":"Li","year":"2025","journal-title":"Clin. Transl. Med."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"143288","DOI":"10.1016\/j.ijbiomac.2025.143288","article-title":"HuMSCs-derived exosomal YBX1 participates in oxidative damage repair in granulosa cells by stabilizing COX5B mRNA in an m5C-dependent manner","volume":"310","author":"Zhu","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.fmre.2021.10.008","article-title":"RNA 5-methylcytosine regulates YBX2-dependent liquid-liquid phase separation","volume":"2","author":"Wang","year":"2022","journal-title":"Fundam. Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1038\/cr.2017.55","article-title":"5-methylcytosine promotes mRNA export\u2014NSUN2 as the methyltransferase and ALYREF as an m5C reader","volume":"27","author":"Yang","year":"2017","journal-title":"Cell Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/s41698-024-00737-0","article-title":"ALYREF recruits ELAVL1 to promote colorectal tumorigenesis via facilitating RNA m5C recognition and nuclear export","volume":"8","author":"Zhong","year":"2024","journal-title":"npj Precis. Oncol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"D299","DOI":"10.1093\/nar\/gkae951","article-title":"RPS 2.0: An updated database of RNAs involved in liquid\u2013liquid phase separation","volume":"53","author":"He","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"D347","DOI":"10.1093\/nar\/gkab986","article-title":"RPS: A comprehensive database of RNAs involved in liquid\u2013liquid phase separation","volume":"50","author":"Liu","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.bbagrm.2018.10.011","article-title":"ADAR RNA editing in innate immune response phasing, in circadian clocks and in sleep","volume":"1862","author":"Sinigaglia","year":"2019","journal-title":"Biochim. Biophys. Acta (BBA)\u2014Gene Regul. Mech."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/j.omtn.2023.01.003","article-title":"Internal m7G methylation: A novel epitranscriptomic contributor in brain development and diseases","volume":"31","author":"Xia","year":"2023","journal-title":"Mol. Ther. Nucleic Acids"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2088","DOI":"10.1111\/j.1742-4658.2005.04650.x","article-title":"Protein families and RNA recognition","volume":"272","author":"Chen","year":"2005","journal-title":"FEBS J."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1186\/s43556-025-00350-y","article-title":"Biomolecular condensates: Molecular structure, biological functions, diseases, and therapeutic targets","volume":"6","author":"Choi","year":"2025","journal-title":"Mol. Biomed."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1016\/j.cell.2012.04.031","article-title":"Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins","volume":"149","author":"Castello","year":"2012","journal-title":"Cell"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1038\/nphys3532","article-title":"Polymer physics of intracellular phase transitions","volume":"11","author":"Brangwynne","year":"2015","journal-title":"Nat. Phys."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"e24360","DOI":"10.4161\/idp.24360","article-title":"The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins","volume":"1","author":"Theillet","year":"2013","journal-title":"Intrinsically Disord. Proteins"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1038\/s41594-021-00601-w","article-title":"It\u2019s not just a phase: Function and characteristics of RNA-binding proteins in phase separation","volume":"28","author":"Wiedner","year":"2021","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Xiao, L., and Xia, K. (2025). Functions of Intrinsically Disordered Regions. Biology, 14.","DOI":"10.3390\/biology14070810"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1038\/s41594-021-00677-4","article-title":"Molecular interactions contributing to FUS SYGQ LC-RGG phase separation and co-partitioning with RNA polymerase II heptads","volume":"28","author":"Murthy","year":"2021","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.molcel.2015.09.006","article-title":"Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II","volume":"60","author":"Burke","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"5383","DOI":"10.1091\/mbc.e04-08-0715","article-title":"Stress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1","volume":"15","author":"Gilks","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1016\/j.cell.2018.03.056","article-title":"FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-\u03c0 Interactions","volume":"173","author":"Qamar","year":"2018","journal-title":"Cell"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.cell.2018.06.006","article-title":"A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins","volume":"174","author":"Wang","year":"2018","journal-title":"Cell"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.brainres.2018.04.036","article-title":"The physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration","volume":"1693","author":"Lin","year":"2018","journal-title":"Brain Res."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1093\/hmg\/ddt408","article-title":"Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40\/70 chaperones","volume":"23","author":"Bengoechea","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"9491","DOI":"10.1093\/nar\/gkaa681","article-title":"RNA-binding and prion domains: The Yin and Yang of phase separation","volume":"48","author":"Gotor","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"7189","DOI":"10.1073\/pnas.1504822112","article-title":"The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics","volume":"112","author":"Kim","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"EMBR202153632","DOI":"10.15252\/embr.202153632","article-title":"Specific RNA interactions promote TDP-43 multivalent phase separation and maintain liquid properties","volume":"22","author":"Grese","year":"2021","journal-title":"EMBO Rep."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"West, D.L., Loughlin, F.E., Rivero-Rodr\u00edguez, F., Vankadari, N., Vel\u00e1zquez-Cruz, A., Corrales-Guerrero, L., D\u00edaz-Moreno, I., and Wilce, J.A. (2022). Regulation of TIA-1 Condensates: Zn2+ and RGG Motifs Promote Nucleic Acid Driven LLPS and Inhibit Irreversible Aggregation. Front. Mol. Biosci., 9.","DOI":"10.3389\/fmolb.2022.960806"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1016\/j.molcel.2020.01.025","article-title":"Arginine-Enriched Mixed-Charge Domains Provide Cohesion for Nuclear Speckle Condensation","volume":"77","author":"Greig","year":"2020","journal-title":"Mol. Cell"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"e64004","DOI":"10.7554\/eLife.64004","article-title":"Charge-driven condensation of RNA and proteins suggests broad role of phase separation in cytoplasmic environments","volume":"10","author":"Dutagaci","year":"2021","journal-title":"eLife"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0301-4622(98)00208-7","article-title":"Oligomerization and phase separation in globular protein solutions","volume":"75","author":"Asherie","year":"1998","journal-title":"Biophys. Chem."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2443","DOI":"10.1021\/acs.biochem.2c00210","article-title":"Principles Governing the Phase Separation of Multidomain Proteins","volume":"61","author":"Mohanty","year":"2022","journal-title":"Biochemistry"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/nature10879","article-title":"Phase transitions in the assembly of multivalent signalling proteins","volume":"483","author":"Li","year":"2012","journal-title":"Nature"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2015.09.015","article-title":"Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization","volume":"163","author":"Molliex","year":"2015","journal-title":"Cell"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/j.jmb.2016.12.011","article-title":"Methylarginines within the RGG-Motif Region of hnRNP A1 Affect Its IRES Trans-Acting Factor Activity and Are Required for hnRNP A1 Stress Granule Localization and Formation","volume":"429","author":"Wall","year":"2017","journal-title":"J. Mol. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/s43556-022-00075-2","article-title":"Post-translational modifications in liquid-liquid phase separation: A comprehensive review","volume":"3","author":"Li","year":"2022","journal-title":"Mol. Biomed."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.molcel.2017.10.015","article-title":"The stress granule transcriptome reveals principles of mRNA accumulation in stress granules","volume":"68","author":"Khong","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"2734","DOI":"10.1073\/pnas.1800038115","article-title":"RNA self-assembly contributes to stress granule formation and defining the stress granule transcriptome","volume":"115","author":"Protter","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1038\/s41594-023-01089-2","article-title":"m6A governs length-dependent enrichment of mRNAs in stress granules","volume":"30","author":"Ries","year":"2023","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/j.molcel.2009.01.026","article-title":"An Architectural Role for a Nuclear Noncoding RNA: NEAT1 RNA Is Essential for the Structure of Paraspeckles","volume":"33","author":"Clemson","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"4020","DOI":"10.1038\/emboj.2012.251","article-title":"Alternative 3\u2019-end processing of long noncoding RNA initiates construction of nuclear paraspeckles","volume":"31","author":"Naganuma","year":"2012","journal-title":"EMBO J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1261\/rna.059477.116","article-title":"Functional dissection of NEAT1 using genome editing reveals substantial localization of the NEAT1_1 isoform outside paraspeckles","volume":"23","author":"Li","year":"2017","journal-title":"RNA"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1261\/rna.028639.111","article-title":"Identification of cis-and trans-acting factors involved in the localization of MALAT-1 noncoding RNA to nuclear speckles","volume":"18","author":"Miyagawa","year":"2012","journal-title":"RNA"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"6630","DOI":"10.1093\/nar\/gku290","article-title":"Identification and characterization of RNA guanine-quadruplex binding proteins","volume":"42","author":"Hacht","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"2127","DOI":"10.1016\/j.jmb.2017.05.017","article-title":"RNA G-quadruplexes in biology: Principles and molecular mechanisms","volume":"429","author":"Fay","year":"2017","journal-title":"J. Mol. Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"3246","DOI":"10.1038\/s41467-019-10923-5","article-title":"RNA structure drives interaction with proteins","volume":"10","author":"Armaos","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/sj.embor.7400325","article-title":"RNA sequence-and shape-dependent recognition by proteins in the ribonucleoprotein particle","volume":"6","author":"Stefl","year":"2005","journal-title":"EMBO Rep."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/nature22386","article-title":"RNA phase transitions in repeat expansion disorders","volume":"546","author":"Jain","year":"2017","journal-title":"Nature"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1126\/science.aar7432","article-title":"mRNA structure determines specificity of a polyQ-driven phase separation","volume":"360","author":"Langdon","year":"2018","journal-title":"Science"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"e64252","DOI":"10.7554\/eLife.64252","article-title":"In vivo reconstitution finds multivalent RNA\u2013RNA interactions as drivers of mesh-like condensates","volume":"10","author":"Ma","year":"2021","journal-title":"eLife"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1038\/s41580-023-00628-5","article-title":"Cellular functions of eukaryotic RNA helicases and their links to human diseases","volume":"24","author":"Bohnsack","year":"2023","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"e18746","DOI":"10.7554\/eLife.18746","article-title":"ATPase activity of the DEAD-box protein Dhh1 controls processing body formation","volume":"5","author":"Mugler","year":"2016","journal-title":"elife"},{"key":"ref_86","first-page":"1","article-title":"Selective RNA sequestration in biomolecular condensates directs cell fate transitions","volume":"28","author":"Pessina","year":"2025","journal-title":"Nat. Biotechnol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"10817","DOI":"10.1093\/nar\/gkac866","article-title":"A sePARate phase? Poly(ADP-ribose) versus RNA in the organization of biomolecular condensates","volume":"50","author":"Alemasova","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.cell.2020.03.049","article-title":"RNA-induced conformational switching and clustering of G3BP drive stress granule assembly by condensation","volume":"181","author":"Kopach","year":"2020","journal-title":"Cell"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2655","DOI":"10.1002\/j.1460-2075.1992.tb05331.x","article-title":"Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box","volume":"11","author":"Kiledjian","year":"1992","journal-title":"EMBO J."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"6244","DOI":"10.1038\/s41467-024-50003-x","article-title":"Modular RNA motifs for orthogonal phase separated compartments","volume":"15","author":"Stewart","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/j.molcel.2024.11.012","article-title":"G3BP1 promotes intermolecular RNA-RNA interactions during RNA condensation","volume":"85","author":"Parker","year":"2025","journal-title":"Mol. Cell"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1038\/s43586-024-00365-9","article-title":"mRNA m6A detection","volume":"4","author":"Rechavi","year":"2024","journal-title":"Nat. Rev. Methods Primers"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1007\/s13238-019-00660-2","article-title":"Binding to m6A RNA promotes YTHDF2-mediated phase separation","volume":"11","author":"Wang","year":"2020","journal-title":"Protein Cell"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1676","DOI":"10.1038\/s41556-023-01258-x","article-title":"O-GlcNAcylation determines the translational regulation and phase separation of YTHDF proteins","volume":"25","author":"Chen","year":"2023","journal-title":"Nat. Cell Biol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2070","DOI":"10.1111\/jcmm.14847","article-title":"m6A facilitates YTHDF-independent phase separation","volume":"24","author":"Liu","year":"2020","journal-title":"J. Cell Mol. Med."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"eadp5689","DOI":"10.1126\/sciadv.adp5689","article-title":"Decoding the interplay between m6A modification and stress granule stability by live-cell imaging","volume":"10","author":"Li","year":"2024","journal-title":"Sci. Adv."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.tig.2021.11.005","article-title":"The multifaceted effects of YTHDC1-mediated nuclear m6A recognition","volume":"38","author":"Widagdo","year":"2022","journal-title":"Trends Genet."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"e2524579123","DOI":"10.1073\/pnas.2524579123","article-title":"YTHDC1 recognizes METTL16-dependent m6A on caRNAs and coordinates cotranscriptional splicing","volume":"123","author":"Zhang","year":"2026","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1126\/science.aay6018","article-title":"N6-methyladenosine of chromosome-associated regulatory RNA regulates chromatin state and transcription","volume":"367","author":"Liu","year":"2020","journal-title":"Science"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1038\/s41419-025-07608-x","article-title":"YTHDC1 phase separation drives the nuclear export of m6A-modified lncNONMMUT062668.2 through the transport complex SRSF3\u2013ALYREF\u2013XPO5 to aggravate pulmonary fibrosis","volume":"16","author":"Chen","year":"2025","journal-title":"Cell Death Dis."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2657","DOI":"10.1007\/s00018-012-1186-z","article-title":"Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs): Post-transcriptional drivers of cancer progression?","volume":"70","author":"Bell","year":"2013","journal-title":"Cell Mol. Life Sci."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1016\/j.gendis.2023.06.017","article-title":"IGF2BPs as novel m6A readers: Diverse roles in regulating cancer cell biological functions, hypoxia adaptation, metabolism, and immunosuppressive tumor microenvironment","volume":"11","author":"Duan","year":"2024","journal-title":"Genes. Dis."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"118795","DOI":"10.1016\/j.bbamcr.2020.118795","article-title":"Initiation of stress granule assembly by rapid clustering of IGF2BP proteins upon osmotic shock","volume":"1867","author":"Zeng","year":"2020","journal-title":"Biochim. Biophys. Acta (BBA)\u2014Mol. Cell Res."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"105071","DOI":"10.1016\/j.jbc.2023.105071","article-title":"The disordered C terminus of ALKBH5 promotes phase separation and paraspeckles assembly","volume":"299","author":"Qin","year":"2023","journal-title":"J. Biol. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"e107976","DOI":"10.15252\/embj.2021107976","article-title":"m6A modification of HSATIII lncRNAs regulates temperature-dependent splicing","volume":"40","author":"Ninomiya","year":"2021","journal-title":"EMBO J."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1038\/s41467-022-28547-7","article-title":"Dynamic FMR1 granule phase switch instructed by m6A modification contributes to maternal RNA decay","volume":"13","author":"Zhang","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1093\/jmcb\/mjaa073","article-title":"Granulation of m1A-modified mRNAs protects their functionality through cellular stress","volume":"12","author":"Jiang","year":"2021","journal-title":"J. Mol. Cell Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/nature16998","article-title":"The dynamic N 1-methyladenosine methylome in eukaryotic messenger RNA","volume":"530","author":"Dominissini","year":"2016","journal-title":"Nature"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1038\/nchembio.2040","article-title":"Transcriptome-wide mapping reveals reversible and dynamic N1-methyladenosine methylome","volume":"12","author":"Li","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/nature24456","article-title":"The m1A landscape on cytosolic and mitochondrial mRNA at single-base resolution","volume":"551","author":"Safra","year":"2017","journal-title":"Nature"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"5126","DOI":"10.1038\/s41467-019-13146-w","article-title":"Antibody cross-reactivity accounts for widespread appearance of m1A in 5\u2019UTRs","volume":"10","author":"Grozhik","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/j.molcel.2017.11.029","article-title":"Loud and clear epitranscriptomic m1A signals: Now in single-base resolution","volume":"68","author":"Dominissini","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_113","first-page":"429","article-title":"Advances in the Structural and Functional Understanding of m1A RNA Modification","volume":"57","author":"Smoczynski","year":"2024","journal-title":"Acc. Chem. Res."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3112","DOI":"10.1093\/hmg\/ddt166","article-title":"The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation","volume":"22","author":"Zhang","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Chien, H.M., Lee, C.C., and Huang, J.J. (2021). The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22158213"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"13583","DOI":"10.1073\/pnas.212483099","article-title":"Higher order arrangement of the eukaryotic nuclear bodies","volume":"99","author":"Wang","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1042\/BST20231447","article-title":"TDP-43 in nuclear condensates: Where, how, and why","volume":"52","author":"Lang","year":"2024","journal-title":"Biochem. Soc. Trans."},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Zhao, T., Zhang, Z., Chen, Z., Xu, G., Wang, Y., and Wang, F. (2025). Biological functions of 5-methylcytosine RNA-binding proteins and their potential mechanisms in human cancers. Front. Oncol., 15.","DOI":"10.3389\/fonc.2025.1534948"},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Zheng, X., Zeng, F., Lei, Y., Li, Y., Deng, J., Luo, G., He, Q., and Zhou, Y. (2025). YBX1: An RNA\/DNA-binding protein that affects disease progression. Front. Oncol., 15.","DOI":"10.3389\/fonc.2025.1635209"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"111797","DOI":"10.1016\/j.cellsig.2025.111797","article-title":"Y-box binding protein 1: A critical target for understanding and treating cardiovascular disease","volume":"132","author":"Liu","year":"2025","journal-title":"Cell. Signal."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1038\/s12276-024-01184-4","article-title":"RNA m5C modification upregulates E2F1 expression in a manner dependent on YBX1 phase separation and promotes tumor progression in ovarian cancer","volume":"56","author":"Liu","year":"2024","journal-title":"Exp. Mol. Med."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1038\/s41416-023-02275-1","article-title":"RNA modifications in cancer","volume":"129","author":"Tang","year":"2023","journal-title":"Br. J. Cancer"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/nature11112","article-title":"Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq","volume":"485","author":"Dominissini","year":"2012","journal-title":"Nature"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"3189","DOI":"10.1021\/acs.analchem.5c06757","article-title":"Single-Cell Multimodal Profiling of m6A mRNA Modification under Oxidative Stress","volume":"98","author":"Ren","year":"2026","journal-title":"Anal. Chem."},{"key":"ref_125","doi-asserted-by":"crossref","unstructured":"Chen, X., Yuan, Y., Zhou, F., Huang, X., Li, L., Pu, J., Zeng, Y., and Jiang, X. (2025). RNA m5C modification: From physiology to pathology and its biological significance. Front. Immunol., 16.","DOI":"10.3389\/fimmu.2025.1599305"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/s41698-026-01361-w","article-title":"TRMT6-directed m1A modification initiates lung squamous cell carcinoma via YTHDF3-stabilized cell cycle genes","volume":"10","author":"Xue","year":"2026","journal-title":"npj Precis. Oncol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1038\/s41586-021-03313-9","article-title":"The RNA m6A reader YTHDC1 silences retrotransposons and guards ES cell identity","volume":"591","author":"Liu","year":"2021","journal-title":"Nature"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1111\/cas.16137","article-title":"YTHDC1-dependent m6A modification modulated FOXM1 promotes glycolysis and tumor progression through CENPA in triple-negative breast cancer","volume":"115","author":"Shen","year":"2024","journal-title":"Cancer Sci."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1186\/s13059-025-03526-5","article-title":"ASPM mediates nuclear entrapment of FOXM1 via liquid-liquid phase separation to promote progression of hepatocarcinoma","volume":"26","author":"Jiang","year":"2025","journal-title":"Genome Biol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"4917","DOI":"10.1093\/nar\/gkac233","article-title":"A histidine cluster determines YY1-compartmentalized coactivators and chromatin elements in phase-separated enhancer clusters","volume":"50","author":"Wang","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"4672","DOI":"10.7150\/ijbs.81595","article-title":"Low expression of m6A reader YTHDC1 promotes progression of ovarian cancer via PIK3R1\/STAT3\/GANAB axis","volume":"19","author":"Wang","year":"2023","journal-title":"Int. J. Biol. Sci."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1007\/s00018-025-05850-2","article-title":"APEX1-STAT3 signaling mediates the force-coordinated endothelial regeneration","volume":"82","author":"Liu","year":"2025","journal-title":"Cell Mol. Life Sci."},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Wang, F., Zhao, Z., Li, Z., Chen, X., Lu, W., Yao, S., Xi, J., Sun, Y., Luo, H., and Feng, Q. (2026). YTHDC1 drives senescence evasion in ovarian cancer through m6A-mediated TERT stabilization. Cell Death Dis.","DOI":"10.1038\/s41419-026-08896-7"},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Xu, Y., Zhang, W., Shen, F., Yang, X., Liu, H., Dai, S., Sun, X., Huang, J., and Guo, Q. (2021). YTH Domain Proteins: A Family of m6A Readers in Cancer Progression. Front. Oncol., 11.","DOI":"10.3389\/fonc.2021.629560"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/s40364-023-00452-1","article-title":"The function and clinical implication of YTHDF1 in the human system development and cancer","volume":"11","author":"Ren","year":"2023","journal-title":"Biomark. Res."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"136243","DOI":"10.1016\/j.jhazmat.2024.136243","article-title":"YTHDF2 phase separation promotes arsenic-induced keratinocyte transformation in a poly-m6A-dependent manner by inhibiting translational initiation of the key tumor suppressor PTEN","volume":"480","author":"Zhao","year":"2024","journal-title":"J. Hazard. Mater."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1186\/s12943-021-01398-4","article-title":"N6-methyladenosine-modified circIGF2BP3 inhibits CD8+ T-cell responses to facilitate tumor immune evasion by promoting the deubiquitination of PD-L1 in non-small cell lung cancer","volume":"20","author":"Liu","year":"2021","journal-title":"Mol. Cancer"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Elcheva, I.A., Gowda, C.P., Bogush, D., Gornostaeva, S., Fakhardo, A., Sheth, N., Kokolus, K.M., Sharma, A., Dovat, S., and Uzun, Y. (2023). IGF2BP family of RNA-binding proteins regulate innate and adaptive immune responses in cancer cells and tumor microenvironment. Front. Immunol., 14.","DOI":"10.3389\/fimmu.2023.1224516"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1021\/acscentsci.2c00107","article-title":"Allosteric Regulation of IGF2BP1 as a Novel Strategy for the Activation of Tumor Immune Microenvironment","volume":"8","author":"Liu","year":"2022","journal-title":"ACS Cent. Sci."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1186\/s13041-026-01297-z","article-title":"m6A RNA methylation in neural plasticity, brain aging, and neurodegenerative vulnerability","volume":"19","author":"Zhou","year":"2026","journal-title":"Mol. Brain"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/s41531-026-01362-3","article-title":"The epitranscriptomic m6A RNA modification modulates the synapse in ageing and in a mouse model of synucleinopathy","volume":"12","author":"Chopra","year":"2026","journal-title":"npj Park. Dis."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/s41583-019-0244-z","article-title":"The m6A epitranscriptome: Transcriptome plasticity in brain development and function","volume":"21","author":"Livneh","year":"2020","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Huang, H., Camats-Perna, J., Medeiros, R., Anggono, V., and Widagdo, J. (2020). Altered expression of the m6A methyltransferase METTL3 in Alzheimer\u2019s disease. Eneuro, 7.","DOI":"10.1523\/ENEURO.0125-20.2020"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"5033","DOI":"10.1038\/s41467-024-49416-5","article-title":"M6A reduction relieves FUS-associated ALS granules","volume":"15","author":"Giuliani","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.molcel.2022.12.019","article-title":"RNA methylation influences TDP43 binding and disease pathogenesis in models of amyotrophic lateral sclerosis and frontotemporal dementia","volume":"83","author":"McMillan","year":"2023","journal-title":"Mol. Cell"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Carey, J.L., and Guo, L. (2022). Liquid-Liquid Phase Separation of TDP-43 and FUS in Physiology and Pathology of Neurodegenerative Diseases. Front. Mol. Biosci., 9.","DOI":"10.3389\/fmolb.2022.826719"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/s12953-024-00231-2","article-title":"Spatial proteomics: Unveiling the multidimensional landscape of protein localization in human diseases","volume":"22","author":"Wu","year":"2024","journal-title":"Proteome Sci."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"3322","DOI":"10.1038\/s41467-024-47435-w","article-title":"Local environment in biomolecular condensates modulates enzymatic activity across length scales","volume":"15","author":"Papp","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1021\/acs.jpcb.2c07684","article-title":"Biomolecular Condensates Regulate Enzymatic Activity under a Crowded Milieu: Synchronization of Liquid-Liquid Phase Separation and Enzymatic Transformation","volume":"127","author":"Saini","year":"2023","journal-title":"J. Phys. Chem. B"},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Verdile, V., De Paola, E., and Paronetto, M.P. (2019). Aberrant Phase Transitions: Side Effects and Novel Therapeutic Strategies in Human Disease. Front. Genet., 10.","DOI":"10.3389\/fgene.2019.00173"},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Naskar, A., Nayak, A., Salaikumaran, M.R., Vishal, S.S., and Gopal, P.P. (2023). Phase separation and pathologic transitions of RNP condensates in neurons: Implications for amyotrophic lateral sclerosis, frontotemporal dementia and other neurodegenerative disorders. Front. Mol. Neurosci., 16.","DOI":"10.3389\/fnmol.2023.1242925"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1261\/rna.079001.121","article-title":"Pathological phase transitions in ALS-FTD impair dynamic RNA-protein granules","volume":"28","author":"Nedelsky","year":"2022","journal-title":"RNA"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.molcel.2018.08.027","article-title":"Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments","volume":"72","author":"Bouchard","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1038\/s41556-020-0550-8","article-title":"Biophysical properties of AKAP95 protein condensates regulate splicing and tumorigenesis","volume":"22","author":"Li","year":"2020","journal-title":"Nat. Cell Biol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"2586","DOI":"10.1200\/JCO.2024.42.16_suppl.2586","article-title":"Phase 1 dose escalation and cohort expansion study evaluating safety, PK, PD and clinical activity of STC-15, a METTL-3 inhibitor, in patients with advanced malignancies","volume":"42","author":"Moser","year":"2024","journal-title":"J. Clin. Oncol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"100247","DOI":"10.1016\/j.mocell.2025.100247","article-title":"Optogenetics to biomolecular phase separation in neurodegenerative diseases","volume":"48","author":"Park","year":"2025","journal-title":"Mol. Cells"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"6717","DOI":"10.1038\/s41467-024-50858-0","article-title":"Rapid and reversible dissolution of biomolecular condensates using light-controlled recruitment of a solubility tag","volume":"15","author":"Gao","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"064017","DOI":"10.1103\/PhysRevApplied.23.064017","article-title":"Molecular mechanisms of condensate modulation from energy-dominance analysis","volume":"23","author":"Qian","year":"2025","journal-title":"Phys. Rev. Appl."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.3724\/abbs.2023106","article-title":"Small molecules in regulating protein phase separation","volume":"55","author":"Li","year":"2023","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1038\/s41467-021-22096-1","article-title":"A modular tool to query and inducibly disrupt biomolecular condensates","volume":"12","author":"Pearce","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1016\/j.cell.2022.02.007","article-title":"The epitranscriptome toolbox","volume":"185","author":"Dominissini","year":"2022","journal-title":"Cell"},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Xue, Z., Mukherjee, O., Mi, L., Guo, Y., Zheng, R., Yuan, C., and You, M. (2026). Programmable and Switchable RNA Scaffolds for Synthetic Condensate Engineering in Mammalian Cells. bioRxiv.","DOI":"10.64898\/2026.02.14.705909"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1038\/s41565-026-02164-7","article-title":"Programmable artificial RNA condensates in mammalian cells","volume":"21","author":"Li","year":"2026","journal-title":"Nat. Nanotechnol."}],"container-title":["Genes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4425\/17\/8\/973\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T04:25:16Z","timestamp":1787286316000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4425\/17\/8\/973"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,19]]},"references-count":163,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2026,8]]}},"alternative-id":["genes17080973"],"URL":"https:\/\/doi.org\/10.3390\/genes17080973","relation":{},"ISSN":["2073-4425"],"issn-type":[{"value":"2073-4425","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,19]]}}}