{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T20:44:06Z","timestamp":1792097046807,"version":"4.4.0"},"reference-count":160,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T00:00:00Z","timestamp":1789430400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100006984","name":"Irma T Hirschl Charitable Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006984","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100003566","name":"ALS Therapy Development Foundation Inc","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100003566","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Chemical Biology"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.chembiol.2026.09.011","type":"journal-article","created":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T14:42:19Z","timestamp":1792075339000},"page":"1404-1421","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Protein arginine methylation rewires molecular interactions"],"prefix":"10.1016","volume":"33","author":[{"given":"Joseph D.","family":"DeAngelo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aliza M.","family":"Silverstein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9388-6004","authenticated-orcid":false,"given":"David","family":"Shechter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.chembiol.2026.09.011_bib1","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1038\/srep01311","article-title":"Loss of the major Type I arginine methyltransferase PRMT1 causes substrate scavenging by other PRMTs","volume":"3","author":"Dhar","year":"2013","journal-title":"Sci. Rep."},{"key":"10.1016\/j.chembiol.2026.09.011_bib2","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1074\/mcp.O113.027870","article-title":"Immunoaffinity enrichment and mass spectrometry analysis of protein methylation","volume":"13","author":"Guo","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.chembiol.2026.09.011_bib3","doi-asserted-by":"crossref","first-page":"2072","DOI":"10.1074\/mcp.O113.032748","article-title":"Proteomic analysis of arginine methylation sites in human cells reveals dynamic regulation during transcriptional arrest","volume":"13","author":"Sylvestersen","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.chembiol.2026.09.011_bib4","article-title":"Global analysis of protein arginine methylation","volume":"1","author":"Zhang","year":"2021","journal-title":"Cell Rep. Methods"},{"key":"10.1016\/j.chembiol.2026.09.011_bib5","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.molcel.2005.04.003","article-title":"Arginine methylation an emerging regulator of protein function","volume":"18","author":"Bedford","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib6","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.molcel.2016.11.003","article-title":"Arginine Methylation: The Coming of Age","volume":"65","author":"Blanc","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib7","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1038\/s41580-019-0155-x","article-title":"The regulation, functions and clinical relevance of arginine methylation","volume":"20","author":"Guccione","year":"2019","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib8","doi-asserted-by":"crossref","first-page":"2933","DOI":"10.1007\/s00018-019-03140-2","article-title":"Cellular consequences of arginine methylation","volume":"76","author":"Lorton","year":"2019","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.chembiol.2026.09.011_bib9","article-title":"Crystal structure of TDRD3 and methyl-arginine binding characterization of TDRD3, SMN and SPF30","volume":"7","author":"Liu","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.chembiol.2026.09.011_bib10","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-pi Interactions","volume":"173","author":"Qamar","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib11","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1016\/j.cell.2018.03.004","article-title":"Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation","volume":"173","author":"Hofweber","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2021.102971","article-title":"Independent transcriptomic and proteomic regulation by type I and II protein arginine methyltransferases","volume":"24","author":"Maron","year":"2021","journal-title":"iScience"},{"key":"10.1016\/j.chembiol.2026.09.011_bib13","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.cell.2016.06.010","article-title":"Compositional Control of Phase-Separated Cellular Bodies","volume":"166","author":"Banani","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib14","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1007028","article-title":"LASSI: A lattice model for simulating phase transitions of multivalent proteins","volume":"15","author":"Choi","year":"2019","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib15","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2017184118","article-title":"Ligand effects on phase separation of multivalent macromolecules","volume":"118","author":"Ruff","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib16","doi-asserted-by":"crossref","first-page":"2201","DOI":"10.1016\/j.molcel.2022.05.018","article-title":"A conceptual framework for understanding phase separation and addressing open questions and challenges","volume":"82","author":"Mittag","year":"2022","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib17","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/nrc3409","article-title":"Protein arginine methyltransferases and cancer","volume":"13","author":"Yang","year":"2013","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.chembiol.2026.09.011_bib18","doi-asserted-by":"crossref","first-page":"4258","DOI":"10.1038\/emboj.2012.261","article-title":"Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS","volume":"31","author":"Dormann","year":"2012","journal-title":"EMBO J."},{"key":"10.1016\/j.chembiol.2026.09.011_bib19","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.ccell.2019.05.014","article-title":"Anti-tumor Activity of the Type I PRMT Inhibitor, GSK3368715, Synergizes with PRMT5 Inhibition through MTAP Loss","volume":"36","author":"Fedoriw","year":"2019","journal-title":"Cancer Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib20","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1074\/mcp.RA119.001888","article-title":"Arginine in C9ORF72 Dipolypeptides Mediates Promiscuous Proteome Binding and Multiple Modes of Toxicity","volume":"19","author":"Radwan","year":"2020","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.chembiol.2026.09.011_bib21","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":"10.1016\/j.chembiol.2026.09.011_bib22","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/j.molcel.2013.05.021","article-title":"Defining the RGG\/RG motif","volume":"50","author":"Thandapani","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib23","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":"10.1016\/j.chembiol.2026.09.011_bib24","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1126\/science.aaw8653","article-title":"Valence and patterning of aromatic residues determine the phase behavior of prion-like domains","volume":"367","author":"Martin","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib25","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1038\/nsmb.2185","article-title":"Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins","volume":"18","author":"Tripsianes","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib26","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1038\/nrm.2017.10","article-title":"The code and beyond: transcription regulation by the RNA polymerase II carboxy-terminal domain","volume":"18","author":"Harlen","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib27","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1038\/s41586-019-1464-0","article-title":"Pol II phosphorylation regulates a switch between transcriptional and splicing condensates","volume":"572","author":"Guo","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.09.011_bib28","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1038\/nsmb0205-110","article-title":"Reading signals on the nucleosome with a new nomenclature for modified histones","volume":"12","author":"Turner","year":"2005","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib29","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1002\/cbic.201700521","article-title":"Kinetic Analysis of PRMT1 Reveals Multifactorial Processivity and a Sequential Ordered Mechanism","volume":"19","author":"Brown","year":"2018","journal-title":"Chembiochem"},{"key":"10.1016\/j.chembiol.2026.09.011_bib30","doi-asserted-by":"crossref","first-page":"4775","DOI":"10.1021\/acs.biochem.0c00554","article-title":"Characterization of the Kinetic Mechanism of Human Protein Arginine Methyltransferase 5","volume":"59","author":"Eddershaw","year":"2020","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2026.09.011_bib31","doi-asserted-by":"crossref","first-page":"22902","DOI":"10.1074\/jbc.M312904200","article-title":"PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity","volume":"279","author":"Miranda","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib32","doi-asserted-by":"crossref","first-page":"7859","DOI":"10.1074\/jbc.M111.336271","article-title":"Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues","volume":"287","author":"Zurita-Lopez","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib33","doi-asserted-by":"crossref","first-page":"5430","DOI":"10.1021\/bi4005123","article-title":"Substrate specificity, processivity, and kinetic mechanism of protein arginine methyltransferase 5","volume":"52","author":"Wang","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2026.09.011_bib34","doi-asserted-by":"crossref","first-page":"26722","DOI":"10.1074\/jbc.M116.757625","article-title":"Transient Kinetics Define a Complete Kinetic Model for Protein Arginine Methyltransferase 1","volume":"291","author":"Hu","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib35","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/S0969-2126(03)00071-6","article-title":"Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides","volume":"11","author":"Zhang","year":"2003","journal-title":"Structure"},{"key":"10.1016\/j.chembiol.2026.09.011_bib36","doi-asserted-by":"crossref","first-page":"17960","DOI":"10.1073\/pnas.1209814109","article-title":"Crystal structure of the human PRMT5:MEP50 complex","volume":"109","author":"Antonysamy","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib37","doi-asserted-by":"crossref","first-page":"32604","DOI":"10.1074\/jbc.M114.609271","article-title":"Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop","volume":"289","author":"Feng","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib38","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1038\/s41573-021-00159-8","article-title":"Protein arginine methylation: from enigmatic functions to therapeutic targeting","volume":"20","author":"Wu","year":"2021","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.chembiol.2026.09.011_bib39","doi-asserted-by":"crossref","first-page":"2068","DOI":"10.1073\/pnas.1525783113","article-title":"A glutamate\/aspartate switch controls product specificity in a protein arginine methyltransferase","volume":"113","author":"Debler","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib40","doi-asserted-by":"crossref","first-page":"3509","DOI":"10.1093\/emboj\/19.14.3509","article-title":"Crystal structure of the conserved core of protein arginine methyltransferase PRMT3","volume":"19","author":"Zhang","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.chembiol.2026.09.011_bib41","doi-asserted-by":"crossref","first-page":"2917","DOI":"10.1007\/s00018-019-03145-x","article-title":"Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level","volume":"76","author":"Tewary","year":"2019","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.chembiol.2026.09.011_bib42","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1039\/D3CB00018D","article-title":"Chemical probes and methods for the study of protein arginine methylation","volume":"4","author":"Brown","year":"2023","journal-title":"RSC Chem. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib43","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1093\/protein\/6.3.247","article-title":"Atomic environments of arginine side chains in proteins","volume":"6","author":"Nandi","year":"1993","journal-title":"Protein Eng."},{"key":"10.1016\/j.chembiol.2026.09.011_bib44","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1002\/pro.5560030402","article-title":"A structural role for arginine in proteins: multiple hydrogen bonds to backbone carbonyl oxygens","volume":"3","author":"Borders","year":"1994","journal-title":"Protein Sci."},{"key":"10.1016\/j.chembiol.2026.09.011_bib45","doi-asserted-by":"crossref","first-page":"9459","DOI":"10.1073\/pnas.96.17.9459","article-title":"Cation-pi interactions in structural biology","volume":"96","author":"Gallivan","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib46","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1126\/science.252.5009.1167","article-title":"Arginine-mediated RNA recognition: the arginine fork","volume":"252","author":"Calnan","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib47","doi-asserted-by":"crossref","first-page":"7421","DOI":"10.1021\/acs.jpcb.5c02168","article-title":"Arginine: I. Interactions of Its Guanidinium Moiety with Branched Aliphatic Side Chains","volume":"129","author":"Ng","year":"2025","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.chembiol.2026.09.011_bib48","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1002\/pro.2838","article-title":"Effect of methylation on the side-chain pKa value of arginine","volume":"25","author":"Evich","year":"2016","journal-title":"Protein Sci."},{"key":"10.1016\/j.chembiol.2026.09.011_bib49","doi-asserted-by":"crossref","first-page":"41576","DOI":"10.1074\/jbc.R112.418574","article-title":"Carbon-oxygen hydrogen bonding in biological structure and function","volume":"287","author":"Horowitz","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib50","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1146\/annurev.bb.22.060193.001215","article-title":"The effects of phosphorylation on the structure and function of proteins","volume":"22","author":"Johnson","year":"1993","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.chembiol.2026.09.011_bib51","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.molcel.2006.06.026","article-title":"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey","volume":"23","author":"Kim","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib52","doi-asserted-by":"crossref","first-page":"2879","DOI":"10.1021\/ja3108214","article-title":"Site-specific and regiospecific installation of methylarginine analogues into recombinant histones and insights into effector protein binding","volume":"135","author":"Le","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2026.09.011_bib53","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1111\/j.1432-1033.1982.tb06847.x","article-title":"Effect of acetylation on the binding of N-terminal peptides of histone H4 to DNA","volume":"127","author":"Cary","year":"1982","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib54","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/S0021-9258(18)54150-8","article-title":"Studies of the DNA binding properties of histone H4 amino terminus. Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 \u201ctail\u201d to DNA","volume":"268","author":"Hong","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib55","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/0092-8674(93)90051-Q","article-title":"A positive role for histone acetylation in transcription factor access to nucleosomal DNA","volume":"72","author":"Lee","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib56","doi-asserted-by":"crossref","first-page":"17857","DOI":"10.1073\/pnas.1201805109","article-title":"Regulation of the H4 tail binding and folding landscapes via Lys-16 acetylation","volume":"109","author":"Potoyan","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib57","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature722","article-title":"Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9","volume":"416","author":"Nielsen","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.09.011_bib58","doi-asserted-by":"crossref","first-page":"2080","DOI":"10.1126\/science.1069473","article-title":"Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail","volume":"295","author":"Jacobs","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib59","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1038\/nature04802","article-title":"Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF","volume":"442","author":"Li","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.09.011_bib60","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/182186a0","article-title":"Content of citrulline and other amino-acids in a protein of hair follicles","volume":"182","author":"Rogers","year":"1958","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.09.011_bib61","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1046\/j.1432-1327.1999.00083.x","article-title":"Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse","volume":"259","author":"Rus'd","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib62","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1002\/bies.10357","article-title":"PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease","volume":"25","author":"Vossenaar","year":"2003","journal-title":"Bioessays"},{"key":"10.1016\/j.chembiol.2026.09.011_bib63","doi-asserted-by":"crossref","first-page":"1662","DOI":"10.1016\/j.biocel.2006.03.008","article-title":"Citrullination: a posttranslational modification in health and disease","volume":"38","author":"Gy\u00f6rgy","year":"2006","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib64","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.molcel.2018.10.016","article-title":"Arginine Citrullination at the C-Terminal Domain Controls RNA Polymerase II Transcription","volume":"73","author":"Sharma","year":"2019","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib65","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/j.cell.2004.08.020","article-title":"Histone deimination antagonizes arginine methylation","volume":"118","author":"Cuthbert","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib66","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1126\/science.1101400","article-title":"Human PAD4 regulates histone arginine methylation levels via demethylimination","volume":"306","author":"Wang","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib67","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.ccell.2019.07.003","article-title":"Therapeutic Targeting of RNA Splicing Catalysis through Inhibition of Protein Arginine Methylation","volume":"36","author":"Fong","year":"2019","journal-title":"Cancer Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib68","doi-asserted-by":"crossref","first-page":"D512","DOI":"10.1093\/nar\/gku1267","article-title":"PhosphoSitePlus, 2014: mutations, PTMs and recalibrations","volume":"43","author":"Hornbeck","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib69","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.aaf7329","article-title":"Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells","volume":"9","author":"Larsen","year":"2016","journal-title":"Sci. Signal."},{"key":"10.1016\/j.chembiol.2026.09.011_bib70","doi-asserted-by":"crossref","first-page":"1946","DOI":"10.1038\/s41467-021-21963-1","article-title":"Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth","volume":"12","author":"Li","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.chembiol.2026.09.011_bib71","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/s12953-020-00162-8","article-title":"Proteome-wide identification of arginine methylation in colorectal cancer tissues from patients","volume":"18","author":"Lim","year":"2020","journal-title":"Proteome Sci."},{"key":"10.1016\/j.chembiol.2026.09.011_bib72","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.aat8388","article-title":"Proteomics profiling of arginine methylation defines PRMT5 substrate specificity","volume":"12","author":"Musiani","year":"2019","journal-title":"Sci. Signal."},{"key":"10.1016\/j.chembiol.2026.09.011_bib73","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2020.545934","article-title":"Proteome-Wide Alterations of Asymmetric Arginine Dimethylation Associated With Pancreatic Ductal Adenocarcinoma Pathogenesis","volume":"8","author":"Wei","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib74","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.molcel.2006.11.019","article-title":"The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing","volume":"25","author":"Cheng","year":"2007","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib75","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1074\/mcp.M111.015883","article-title":"PTMScan direct: identification and quantification of peptides from critical signaling proteins by immunoaffinity enrichment coupled with LC-MS\/MS","volume":"11","author":"Stokes","year":"2012","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.chembiol.2026.09.011_bib76","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1038\/s41594-019-0313-z","article-title":"PRMT5 methylome profiling uncovers a direct link to splicing regulation in acute myeloid leukemia","volume":"26","author":"Radzisheuskaya","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib77","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1021\/acs.jproteome.9b00633","article-title":"Middle-Down Proteomics Reveals Dense Sites of Methylation and Phosphorylation in Arginine-Rich RNA-Binding Proteins","volume":"19","author":"Kundinger","year":"2020","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib78","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.cell.2009.02.044","article-title":"A systematic survey identifies prions and illuminates sequence features of prionogenic proteins","volume":"137","author":"Alberti","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib79","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","article-title":"The amyloid state of proteins in human diseases","volume":"148","author":"Eisenberg","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib80","doi-asserted-by":"crossref","first-page":"11504","DOI":"10.1073\/pnas.93.21.11504","article-title":"Structural studies of p21Waf1\/Cip1\/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity","volume":"93","author":"Kriwacki","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib81","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.molcel.2015.08.018","article-title":"Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins","volume":"60","author":"Lin","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib82","doi-asserted-by":"crossref","first-page":"7984","DOI":"10.1093\/nar\/gkx460","article-title":"Intrinsically disordered RGG\/RG domains mediate degenerate specificity in RNA binding","volume":"45","author":"Ozdilek","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib83","doi-asserted-by":"crossref","DOI":"10.26508\/lsa.201800178","article-title":"Interaction modulation through arrays of clustered methyl-arginine protein modifications","volume":"1","author":"Woodsmith","year":"2018","journal-title":"Life Sci. Alliance"},{"key":"10.1016\/j.chembiol.2026.09.011_bib84","doi-asserted-by":"crossref","first-page":"6811","DOI":"10.1093\/nar\/gkae329","article-title":"CARM1 hypermethylates the NuRD chromatin remodeling complex to promote cell cycle gene expression and breast cancer development","volume":"52","author":"Chen","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib85","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":"10.1016\/j.chembiol.2026.09.011_bib86","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2205255119","article-title":"Global profiling of arginine dimethylation in regulating protein phase separation by a steric effect-based chemical-enrichment method","volume":"119","author":"Wang","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib87","article-title":"Arginine methylation-enabled FUS phase separation with SMN contributes to neuronal granule formation","volume":"43","author":"Wang","year":"2024","journal-title":"Cell Rep."},{"key":"10.1016\/j.chembiol.2026.09.011_bib88","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1016\/j.yexcr.2008.12.008","article-title":"PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function","volume":"315","author":"Jobert","year":"2009","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib89","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1002\/pro.3354","article-title":"Differential interaction of PRMT1 with RGG-boxes of the FET family proteins EWS and TAF15","volume":"27","author":"Li","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.chembiol.2026.09.011_bib90","doi-asserted-by":"crossref","first-page":"2507","DOI":"10.1126\/science.1065961","article-title":"A transcriptional switch mediated by cofactor methylation","volume":"294","author":"Xu","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib91","doi-asserted-by":"crossref","first-page":"2174","DOI":"10.1126\/science.284.5423.2174","article-title":"Regulation of transcription by a protein methyltransferase","volume":"284","author":"Chen","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib92","doi-asserted-by":"crossref","first-page":"40810","DOI":"10.1074\/jbc.M005459200","article-title":"Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300","volume":"275","author":"Chen","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib93","doi-asserted-by":"crossref","first-page":"5457","DOI":"10.1093\/emboj\/cdf548","article-title":"Control of CBP co-activating activity by arginine methylation","volume":"21","author":"Chevillard-Briet","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.chembiol.2026.09.011_bib94","doi-asserted-by":"crossref","first-page":"7846","DOI":"10.1128\/MCB.00568-06","article-title":"Signaling within a coactivator complex: methylation of SRC-3\/AIB1 is a molecular switch for complex disassembly","volume":"26","author":"Feng","year":"2006","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib95","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1128\/MCB.00815-06","article-title":"The activity and stability of the transcriptional coactivator p\/CIP\/SRC-3 are regulated by CARM1-dependent methylation","volume":"27","author":"Naeem","year":"2007","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib96","doi-asserted-by":"crossref","first-page":"4327","DOI":"10.1093\/nar\/gky240","article-title":"The arginine methyltransferase CARM1 represses p300\u2217ACT\u2217CREMtau activity and is required for spermiogenesis","volume":"46","author":"Bao","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib97","doi-asserted-by":"crossref","first-page":"11115","DOI":"10.1074\/jbc.M513053200","article-title":"Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src","volume":"281","author":"Ostareck-Lederer","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib98","doi-asserted-by":"crossref","first-page":"16030","DOI":"10.1074\/jbc.M909368199","article-title":"Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains","volume":"275","author":"Bedford","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib99","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/S0022-2836(03)00148-7","article-title":"High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues","volume":"327","author":"Sprangers","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib100","doi-asserted-by":"crossref","first-page":"11748","DOI":"10.1093\/nar\/gks929","article-title":"Recognition of asymmetrically dimethylated arginine by TDRD3","volume":"40","author":"Sikorsky","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib101","doi-asserted-by":"crossref","first-page":"8289","DOI":"10.1128\/MCB.21.24.8289-8300.2001","article-title":"The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins","volume":"21","author":"Friesen","year":"2001","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib102","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1017\/S135583820101442X","article-title":"Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B\/B' and the Sm-like protein LSm4, and their interaction with the SMN protein","volume":"7","author":"Brahms","year":"2001","journal-title":"RNA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib103","article-title":"SART3 reads methylarginine-marked glycine- and arginine-rich motifs","volume":"43","author":"Wang","year":"2024","journal-title":"Cell Rep."},{"key":"10.1016\/j.chembiol.2026.09.011_bib104","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1021\/acs.biochem.0c00035","article-title":"A Binary Arginine Methylation Switch on Histone H3 Arginine 2 Regulates Its Interaction with WDR5","volume":"59","author":"Lorton","year":"2020","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2026.09.011_bib105","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1038\/nsmb1116","article-title":"Molecular recognition of histone H3 by the WD40 protein WDR5","volume":"13","author":"Couture","year":"2006","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib106","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1042\/BCJ20230384","article-title":"Loss of the methylarginine reader function of SND1 confers resistance to hepatocellular carcinoma","volume":"480","author":"Wright","year":"2023","journal-title":"Biochem. J."},{"key":"10.1016\/j.chembiol.2026.09.011_bib107","doi-asserted-by":"crossref","first-page":"18398","DOI":"10.1073\/pnas.1013106107","article-title":"Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain","volume":"107","author":"Liu","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib108","doi-asserted-by":"crossref","first-page":"1876","DOI":"10.1101\/gad.1956010","article-title":"Structural basis for methylarginine-dependent recognition of Aubergine by Tudor","volume":"24","author":"Liu","year":"2010","journal-title":"Genes Dev."},{"key":"10.1016\/j.chembiol.2026.09.011_bib109","doi-asserted-by":"crossref","first-page":"28476","DOI":"10.1074\/jbc.M414328200","article-title":"Tudor domains bind symmetrical dimethylated arginines","volume":"280","author":"C\u00f4t\u00e9","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib110","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1002\/anie.201708233","article-title":"Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain","volume":"57","author":"Supekar","year":"2018","journal-title":"Angew. Chem., Int. Ed. Engl."},{"key":"10.1016\/j.chembiol.2026.09.011_bib111","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1016\/j.molcel.2010.11.024","article-title":"TDRD3 is an effector molecule for arginine-methylated histone marks","volume":"40","author":"Yang","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib112","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1126\/science.1202663","article-title":"The C-terminal domain of RNA polymerase II is modified by site-specific methylation","volume":"332","author":"Sims","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib113","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.ads6385","article-title":"BRD9 functions as a methylarginine reader to regulate AKT-EZH2 signaling","volume":"11","author":"Yin","year":"2025","journal-title":"Sci. Adv."},{"key":"10.1016\/j.chembiol.2026.09.011_bib114","doi-asserted-by":"crossref","first-page":"3006","DOI":"10.1074\/jbc.C700192200","article-title":"Arginine methylation of the histone H3 tail impedes effector binding","volume":"283","author":"Iberg","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib115","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1038\/nsmb.2209","article-title":"Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance","volume":"19","author":"Migliori","year":"2012","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib116","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1093\/hmg\/ddq007","article-title":"Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA","volume":"19","author":"Blackwell","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.chembiol.2026.09.011_bib117","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1038\/nsmb.2064","article-title":"Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction","volume":"18","author":"Phan","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib118","doi-asserted-by":"crossref","first-page":"E5391","DOI":"10.1073\/pnas.1515737112","article-title":"Crystal structure reveals specific recognition of a G-quadruplex RNA by a beta-turn in the RGG motif of FMRP","volume":"112","author":"Vasilyev","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib119","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1111\/j.1742-4658.2011.08020.x","article-title":"Identification of Ewing's sarcoma protein as a G-quadruplex DNA- and RNA-binding protein","volume":"278","author":"Takahama","year":"2011","journal-title":"FEBS J."},{"key":"10.1016\/j.chembiol.2026.09.011_bib120","doi-asserted-by":"crossref","first-page":"7225","DOI":"10.1093\/nar\/gkae319","article-title":"PRMT5-mediated arginine methylation of FXR1 is essential for RNA binding in cancer cells","volume":"52","author":"Vijayakumar","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib121","doi-asserted-by":"crossref","first-page":"1834","DOI":"10.4161\/cc.4.12.2250","article-title":"The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity","volume":"4","author":"Boisvert","year":"2005","journal-title":"Cell Cycle"},{"key":"10.1016\/j.chembiol.2026.09.011_bib122","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1261\/rna.055269.115","article-title":"Arginine methylation enhances the RNA chaperone activity of the West Nile virus host factor AUF1 p45","volume":"22","author":"Friedrich","year":"2016","journal-title":"RNA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib123","doi-asserted-by":"crossref","first-page":"2564","DOI":"10.1021\/acschembio.5b00566","article-title":"G-Quadruplex DNA- and RNA-Specific-Binding Proteins Engineered from the RGG Domain of TLS\/FUS","volume":"10","author":"Takahama","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib124","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1261\/rna.062547.117","article-title":"Sbp1 modulates the translation of Pab1 mRNA in a poly(A)- and RGG-dependent manner","volume":"24","author":"Brandariz-N\u00fa\u00f1ez","year":"2018","journal-title":"RNA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib125","doi-asserted-by":"crossref","first-page":"22671","DOI":"10.1074\/jbc.M116.739573","article-title":"Arginine Demethylation of G3BP1 Promotes Stress Granule Assembly","volume":"291","author":"Tsai","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib126","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/s41418-019-0350-5","article-title":"UBAP2L arginine methylation by PRMT1 modulates stress granule assembly","volume":"27","author":"Huang","year":"2020","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.chembiol.2026.09.011_bib127","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":"10.1016\/j.chembiol.2026.09.011_bib128","doi-asserted-by":"crossref","DOI":"10.1126\/science.aar2555","article-title":"Imaging dynamic and selective low-complexity domain interactions that control gene transcription","volume":"361","author":"Chong","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib129","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1005941","article-title":"Sequence determinants of protein phase behavior from a coarse-grained model","volume":"14","author":"Dignon","year":"2018","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib130","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2021.688973","article-title":"Systematic Analysis of the Impact of R-Methylation on RBPs-RNA Interactions: A Proteomic Approach","volume":"8","author":"Maniaci","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.chembiol.2026.09.011_bib131","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1038\/s41557-021-00840-w","article-title":"Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains","volume":"14","author":"Bremer","year":"2022","journal-title":"Nat. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib132","doi-asserted-by":"crossref","first-page":"4016","DOI":"10.1016\/j.molcel.2025.09.021","article-title":"Productive mRNA chromatin escape is promoted by PRMT5 activity","volume":"85","author":"DeAngelo","year":"2025","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib133","doi-asserted-by":"crossref","first-page":"899","DOI":"10.14348\/molcells.2020.0186","article-title":"Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder","volume":"43","author":"Hong","year":"2020","journal-title":"Mol. Cells"},{"key":"10.1016\/j.chembiol.2026.09.011_bib134","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1038\/s42004-025-01687-9","article-title":"Sequence-based prediction of condensate composition reveals that specificity can emerge from multivalent interactions among disordered regions","volume":"8","author":"Wess\u00e9n","year":"2025","journal-title":"Commun. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib135","doi-asserted-by":"crossref","first-page":"4626","DOI":"10.1038\/s41467-021-24798-y","article-title":"PRMT1-dependent regulation of RNA metabolism and DNA damage response sustains pancreatic ductal adenocarcinoma","volume":"12","author":"Giuliani","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.chembiol.2026.09.011_bib136","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/j.molcel.2017.12.022","article-title":"Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation","volume":"69","author":"Ryan","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.09.011_bib137","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1126\/science.1134108","article-title":"Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis","volume":"314","author":"Neumann","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib138","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1126\/science.aab0983","article-title":"TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD","volume":"349","author":"Ling","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib139","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/nature11922","article-title":"Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS","volume":"495","author":"Kim","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.09.011_bib140","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2024.115205","article-title":"Opposing roles of p38alpha-mediated phosphorylation and PRMT1-mediated arginine methylation in driving TDP-43 proteinopathy","volume":"44","author":"Aikio","year":"2025","journal-title":"Cell Rep."},{"key":"10.1016\/j.chembiol.2026.09.011_bib141","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.aaz5683","article-title":"PRMT5 control of cGAS\/STING and NLRC5 pathways defines melanoma response to antitumor immunity","volume":"12","author":"Kim","year":"2020","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.chembiol.2026.09.011_bib142","doi-asserted-by":"crossref","first-page":"884","DOI":"10.4049\/immunohorizons.2100076","article-title":"PRMT5 Promotes Symmetric Dimethylation of RNA Processing Proteins and Modulates Activated T Cell Alternative Splicing and Ca(2+)\/NFAT Signaling","volume":"5","author":"Sengupta","year":"2021","journal-title":"ImmunoHorizons"},{"key":"10.1016\/j.chembiol.2026.09.011_bib143","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1515\/hsz-2022-0136","article-title":"NF90\/NFAR (nuclear factors associated with dsRNA) - a new methylation substrate of the PRMT5-WD45-RioK1 complex","volume":"403","author":"Cox","year":"2022","journal-title":"Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib144","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.4049\/jimmunol.1601702","article-title":"PRMT5-Selective Inhibitors Suppress Inflammatory T Cell Responses and Experimental Autoimmune Encephalomyelitis","volume":"198","author":"Webb","year":"2017","journal-title":"J. Immunol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib145","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.abm6265","article-title":"The lncRNA PILA promotes NF-kappaB signaling in osteoarthritis by stimulating the activity of the protein arginine methyltransferase PRMT1","volume":"15","author":"Tang","year":"2022","journal-title":"Sci. Signal."},{"key":"10.1016\/j.chembiol.2026.09.011_bib146","doi-asserted-by":"crossref","first-page":"4326","DOI":"10.1073\/pnas.1522372113","article-title":"Asymmetric arginine dimethylation of RelA provides a repressive mark to modulate TNFalpha\/NF-kappaB response","volume":"113","author":"Reintjes","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2026.09.011_bib147","doi-asserted-by":"crossref","first-page":"4779","DOI":"10.1158\/1078-0432.CCR-24-3610","article-title":"MTA-Cooperative PRMT5 Inhibitors Are Efficacious in MTAP-Deleted Malignant Peripheral Nerve Sheath Tumor Models","volume":"31","author":"Zhang","year":"2025","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib148","doi-asserted-by":"crossref","first-page":"2412","DOI":"10.1158\/2159-8290.CD-23-0669","article-title":"MRTX1719 Is an MTA-Cooperative PRMT5 Inhibitor That Exhibits Synthetic Lethality in Preclinical Models and Patients with MTAP-Deleted Cancer","volume":"13","author":"Engstrom","year":"2023","journal-title":"Cancer Discov."},{"key":"10.1016\/j.chembiol.2026.09.011_bib149","doi-asserted-by":"crossref","first-page":"5097","DOI":"10.1021\/acs.jmedchem.4c03067","article-title":"Discovery of TNG462: A Highly Potent and Selective MTA-Cooperative PRMT5 Inhibitor to Target Cancers with MTAP Deletion","volume":"68","author":"Cottrell","year":"2025","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib150","doi-asserted-by":"crossref","first-page":"1138","DOI":"10.1016\/j.annonc.2024.08.2339","article-title":"First-in-human study of AMG 193, an MTA-cooperative PRMT5 inhibitor, in patients with MTAP-deleted solid tumors: results from phase I dose exploration","volume":"35","author":"Rodon","year":"2024","journal-title":"Ann. Oncol."},{"key":"10.1016\/j.chembiol.2026.09.011_bib151","doi-asserted-by":"crossref","first-page":"3383","DOI":"10.1158\/0008-5472.CAN-18-1010","article-title":"MTAP Loss Promotes Stemness in Glioblastoma and Confers Unique Susceptibility to Purine Starvation","volume":"79","author":"Hansen","year":"2019","journal-title":"Cancer Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib152","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.aad5944","article-title":"Disordered methionine metabolism in MTAP\/CDKN2A-deleted cancers leads to dependence on PRMT5","volume":"351","author":"Mavrakis","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.09.011_bib153","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1038\/s41420-025-02545-2","article-title":"Combined inhibition by PRMT5 and MAT2A demonstrates a strong synthetic lethality in MTAP homozygous-deficient glioma models","volume":"11","author":"Jiang","year":"2025","journal-title":"Cell Death Discov."},{"key":"10.1016\/j.chembiol.2026.09.011_bib154","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.105492","article-title":"Combined inhibition of MTAP and MAT2a mimics synthetic lethality in tumor models via PRMT5 inhibition","volume":"300","author":"Bedard","year":"2024","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.09.011_bib155","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1186\/s13046-024-03237-y","article-title":"Targeting PRMT5 through PROTAC for the treatment of triple-negative breast cancer","volume":"43","author":"Guo","year":"2024","journal-title":"J. Exp. Clin. Cancer Res."},{"key":"10.1016\/j.chembiol.2026.09.011_bib156","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/s41416-023-02276-0","article-title":"Phase 1 study of GSK3368715, a type I PRMT inhibitor, in patients with advanced solid tumors","volume":"129","author":"El-Khoueiry","year":"2023","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.chembiol.2026.09.011_bib157","doi-asserted-by":"crossref","DOI":"10.1016\/j.esmoop.2024.102961","article-title":"A phase I study to evaluate the safety, pharmacokinetics, and pharmacodynamics of PF-06939999 (PRMT5 inhibitor) in patients with selected advanced or metastatic tumors with high incidence of splicing factor gene mutations","volume":"9","author":"Rodon","year":"2024","journal-title":"ESMO Open"},{"key":"10.1016\/j.chembiol.2026.09.011_bib158","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1038\/nature09504","article-title":"Selective inhibition of BET bromodomains","volume":"468","author":"Filippakopoulos","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.09.011_bib159","doi-asserted-by":"crossref","first-page":"4504","DOI":"10.1038\/s41467-023-40124-0","article-title":"Pharmacological perturbation of the phase-separating protein SMNDC1","volume":"14","author":"Enders","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.chembiol.2026.09.011_bib160","doi-asserted-by":"crossref","DOI":"10.15252\/emmm.202317683","article-title":"PRMT inhibitor promotes SMN2 exon 7 inclusion and synergizes with nusinersen to rescue SMA mice","volume":"15","author":"Kordala","year":"2023","journal-title":"EMBO Mol. Med."}],"container-title":["Cell Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2451945626003600?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2451945626003600?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T19:46:48Z","timestamp":1792093608000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2451945626003600"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":160,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2026,10]]}},"alternative-id":["S2451945626003600"],"URL":"https:\/\/doi.org\/10.1016\/j.chembiol.2026.09.011","relation":{},"ISSN":["2451-9456"],"issn-type":[{"value":"2451-9456","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Protein arginine methylation rewires molecular interactions","name":"articletitle","label":"Article Title"},{"value":"Cell Chemical Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.chembiol.2026.09.011","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Author(s). Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}