{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T03:25:19Z","timestamp":1793762719027,"version":"4.6.1"},"reference-count":58,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Japan Society for the Promotion of Science Kakenhi","award":["23K06597"],"award-info":[{"award-number":["23K06597"]}],"id":[{"id":"https:\/\/ror.org\/00hhkn466","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Research Support Project for Life Science and Drug Discovery"},{"DOI":"10.13039\/100009619","name":"Japan Agency for Medical Research and Development","doi-asserted-by":"publisher","award":["JP25ama121025"],"award-info":[{"award-number":["JP25ama121025"]}],"id":[{"id":"10.13039\/100009619","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Regnase-1 is an essential RNase that suppresses immune cell activation by targeting the mRNA of pro-inflammatory cytokines such as interleukin 6 (IL-6). Although genetic inhibition of Regnase-1 activity in CD8+ T cells has been shown to enhance antitumor immunity, no molecular inhibitors of Regnase-1 have been reported. By exploiting a library of nucleic acid analogs in conjunction with an RNA displacement assay, we identified multiple candidate competitors of Regnase-1 RNA substrates. Among these, suramin\u2014an approved drug for treating African sleeping sickness\u2014and several of its derivatives displaced Regnase-1 RNA targets with submicromolar affinity, competitively inhibited Regnase-1\u2013mediated degradation of RNA in vitro, and enhanced Il6 mRNA levels and IL-6 production in mouse embryonic fibroblasts. A 2.62 \u00c5 crystal structure revealed that suramin bound to the Regnase-1 active site, coordinating with the catalytic Mg2+. Quantum chemical calculations further elucidated qualitative interactions between suramin and surrounding residues of Regnase-1. These findings establish suramin as a small-molecule inhibitor of Regnase-1\u2013mediated RNA decay.<\/jats:p>","DOI":"10.1093\/narmme\/ugag043","type":"journal-article","created":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T13:32:15Z","timestamp":1790861535000},"source":"Crossref","is-referenced-by-count":0,"title":["Identification of small-molecule inhibitors of the immune system repressor Regnase-1"],"prefix":"10.1093","volume":"3","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5280-6730","authenticated-orcid":false,"given":"Arthur","family":"Millius","sequence":"first","affiliation":[{"name":"Department of Genome Informatics, Research Institute for Microbial Diseases (RIMD), The University of Osaka , 565-0871Osaka ,","place":["Japan"]},{"name":"Laboratory for Systems Immunology, Immunology Frontier Research Center (WPI-iFReC), The University of Osaka , 565-0871Osaka ,","place":["Japan"]},{"name":"Laboratory of Host Defense, WPI-iFReC, The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8735-0665","authenticated-orcid":false,"given":"Chee-Hong Takahiro","family":"Yew","sequence":"additional","affiliation":[{"name":"Department of Genome Informatics, Research Institute for Microbial Diseases (RIMD), The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuko","family":"Misumi","sequence":"additional","affiliation":[{"name":"TechnoPro, Inc. TechnoPro R&D, Company , 650-0047Kobe ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2854-9225","authenticated-orcid":false,"given":"Jian","family":"Yu","sequence":"additional","affiliation":[{"name":"Protein Crystallography Laboratory, Institute for Protein Research, The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6020-8151","authenticated-orcid":false,"given":"Daisuke","family":"Takaya","sequence":"additional","affiliation":[{"name":"Graduate School of Pharmaceutical Sciences, The University of Osaka , 565-0871Osaka,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-6275-5550","authenticated-orcid":false,"given":"Shuhei","family":"Miyakawa","sequence":"additional","affiliation":[{"name":"Graduate School of Pharmaceutical Sciences, The University of Osaka , 565-0871Osaka,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eun-Sol","family":"Choi","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Kunsan National University , 54150Gunsan ,","place":["Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6790-5160","authenticated-orcid":false,"given":"Hyo-Jun","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Kunsan National University , 54150Gunsan ,","place":["Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-7865-2506","authenticated-orcid":false,"given":"Tatum Melati","family":"Andini","sequence":"additional","affiliation":[{"name":"Department of Genome Informatics, Research Institute for Microbial Diseases (RIMD), The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-3677-8774","authenticated-orcid":false,"given":"Fahad","family":"Khalaf","sequence":"additional","affiliation":[{"name":"Department of Genome Informatics, Research Institute for Microbial Diseases (RIMD), The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0305-8163","authenticated-orcid":false,"given":"Kazuhiko","family":"Maeda","sequence":"additional","affiliation":[{"name":"Laboratory of Host Defense, WPI-iFReC, The University of Osaka , 565-0871Osaka ,","place":["Japan"]},{"name":"Department of Host Defense, RIMD, The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5357-8250","authenticated-orcid":false,"given":"Kaori","family":"Fukuzawa","sequence":"additional","affiliation":[{"name":"Graduate School of Pharmaceutical Sciences, The University of Osaka , 565-0871Osaka,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5354-0807","authenticated-orcid":false,"given":"Genji","family":"Kurisu","sequence":"additional","affiliation":[{"name":"Protein Crystallography Laboratory, Institute for Protein Research, The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7602-9617","authenticated-orcid":false,"given":"Shizuo","family":"Akira","sequence":"additional","affiliation":[{"name":"Laboratory of Host Defense, WPI-iFReC, The University of Osaka , 565-0871Osaka ,","place":["Japan"]},{"name":"Department of Host Defense, RIMD, The University of Osaka , 565-0871Osaka ,","place":["Japan"]},{"name":"Center for Advanced Modalities and Drug Delivery System (CAMaD), The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7855-1302","authenticated-orcid":false,"given":"Soyoung","family":"Park","sequence":"additional","affiliation":[{"name":"Laboratory for Systems Immunology, Immunology Frontier Research Center (WPI-iFReC), The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4078-0817","authenticated-orcid":false,"given":"Daron M","family":"Standley","sequence":"additional","affiliation":[{"name":"Department of Genome Informatics, Research Institute for Microbial Diseases (RIMD), The University of Osaka , 565-0871Osaka ,","place":["Japan"]},{"name":"Laboratory for Systems Immunology, Immunology Frontier Research Center (WPI-iFReC), The University of Osaka , 565-0871Osaka ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,10,1]]},"reference":[{"key":"2026110321314273800_B1","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1038\/s41568-021-00347-z","article-title":"Systemic immunity in cancer","volume":"21","author":"Hiam-Galvez","year":"2021","journal-title":"Nat Rev Cancer"},{"key":"2026110321314273800_B2","doi-asserted-by":"publisher","first-page":"3335","DOI":"10.1172\/JCI83871","article-title":"Cancer immunotherapy: harnessing the immune system to battle cancer","volume":"125","author":"Yang","year":"2015","journal-title":"J Clin Invest"},{"key":"2026110321314273800_B3","doi-asserted-by":"publisher","first-page":"314","DOI":"10.1016\/j.annonc.2025.10.1239","article-title":"Intratumoral heterogeneity and immunotherapy resistance: clinical implications","volume":"37","author":"Keenan","year":"2026","journal-title":"Ann Oncol"},{"key":"2026110321314273800_B4","doi-asserted-by":"publisher","first-page":"11","DOI":"10.4049\/jimmunol.1800991","article-title":"The next generation of immunotherapy for cancer: small molecules could make big waves","volume":"202","author":"Kerr","year":"2019","journal-title":"J Immunol"},{"key":"2026110321314273800_B5","doi-asserted-by":"publisher","first-page":"450","DOI":"10.1002\/cmdc.201500566","article-title":"Cancer immunotherapy: selected targets and small-molecule modulators","volume":"11","author":"Weinmann","year":"2016","journal-title":"ChemMedChem"},{"key":"2026110321314273800_B6","doi-asserted-by":"publisher","first-page":"1185","DOI":"10.1038\/nature07924","article-title":"Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay","volume":"458","author":"Matsushita","year":"2009","journal-title":"Nature"},{"key":"2026110321314273800_B7","doi-asserted-by":"publisher","first-page":"1036","DOI":"10.1016\/j.cell.2013.04.034","article-title":"Malt1-induced cleavage of regnase-1 in CD4(+) helper T cells regulates immune activation","volume":"153","author":"Uehata","year":"2013","journal-title":"Cell"},{"key":"2026110321314273800_B8","doi-asserted-by":"publisher","first-page":"1167","DOI":"10.1038\/ni.2137","article-title":"The I\u03baB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR\u2013IL-1R by controlling degradation of regnase-1","volume":"12","author":"Iwasaki","year":"2011","journal-title":"Nat Immunol"},{"key":"2026110321314273800_B9","doi-asserted-by":"publisher","first-page":"859","DOI":"10.1093\/intimm\/dxab048","article-title":"Post-transcriptional regulation of immunological responses by Regnase-1-related RNases","volume":"33","author":"Uehata","year":"2021","journal-title":"Int Immunol"},{"key":"2026110321314273800_B10","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1111\/gtc.13018","article-title":"Breaking self-regulation of Regnase-1 promotes its own protein expression","volume":"28","author":"Piboonprai","year":"2023","journal-title":"Genes Cells"},{"key":"2026110321314273800_B11","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1038\/s41586-019-1821-z","article-title":"Targeting REGNASE-1 programs long-lived effector T cells for cancer therapy","volume":"576","author":"Wei","year":"2019","journal-title":"Nature"},{"key":"2026110321314273800_B12","doi-asserted-by":"publisher","first-page":"e2218632120","DOI":"10.1073\/pnas.2218632120","article-title":"Combined disruption of T cell inflammatory regulators Regnase-1 and Roquin-1 enhances antitumor activity of engineered human T cells","volume":"120","author":"Mai","year":"2023","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026110321314273800_B13","doi-asserted-by":"publisher","first-page":"103008","DOI":"10.1016\/j.xcrm.2026.103008","article-title":"Targeting Regnase-1 in B7-H3-CAR T cells reprograms the tumor microenvironment and enhances antitumor efficacy for osteosarcoma","volume":"7","author":"Adeshakin","year":"2026","journal-title":"Cell Rep Med"},{"key":"2026110321314273800_B14","doi-asserted-by":"publisher","first-page":"113589","DOI":"10.1016\/j.biopha.2022.113589","article-title":"Small-molecule screening of ribonuclease L binders for RNA degradation","volume":"154","author":"Borgelt","year":"2022","journal-title":"Biomed Pharmacother"},{"key":"2026110321314273800_B15","doi-asserted-by":"publisher","first-page":"8531","DOI":"10.1038\/s41467-025-64291-4","article-title":"Harnessing indole scaffolds to identify small-molecule IRE1\u03b1 inhibitors modulating XBP1 mRNA splicing","volume":"16","author":"Liu","year":"2025","journal-title":"Nat Commun"},{"key":"2026110321314273800_B16","doi-asserted-by":"publisher","first-page":"6425","DOI":"10.1093\/nar\/gkz285","article-title":"A screening platform to monitor RNA processing and protein\u2013RNA interactions in ribonuclease P uncovers a small molecule inhibitor","volume":"47","author":"Madrigal-Carrillo","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"2026110321314273800_B17","doi-asserted-by":"publisher","first-page":"1431","DOI":"10.1084\/jem.20181078","article-title":"Phosphorylation-dependent Regnase-1 release from endoplasmic reticulum is critical in IL-17 response","volume":"216","author":"Tanaka","year":"2019","journal-title":"J Exp Med"},{"key":"2026110321314273800_B18","doi-asserted-by":"publisher","first-page":"22324","DOI":"10.1038\/srep22324","article-title":"Structural basis for the regulation of enzymatic activity of Regnase-1 by domain\u2013domain interactions","volume":"6","author":"Yokogawa","year":"2016","journal-title":"Sci Rep"},{"key":"2026110321314273800_B19","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1089\/adt.2021.133","article-title":"A new spectral shift-based method to characterize molecular interactions","volume":"20","author":"Langer","year":"2022","journal-title":"Assay Drug Dev Technol"},{"key":"2026110321314273800_B20","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"2026110321314273800_B21","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1107\/S0907444912001308","article-title":"Towards automated crystallographic structure refinement with phenix.refine","volume":"68","author":"Afonine","year":"2012","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"2026110321314273800_B22","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1107\/S0907444911047834","article-title":"Use of knowledge-based restraints in phenix.refine to improve macromolecular refinement at low resolution","volume":"68","author":"Headd","year":"2012","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"2026110321314273800_B23","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"2026110321314273800_B24","doi-asserted-by":"publisher","first-page":"701","DOI":"10.1016\/S0009-2614(99)00874-X","article-title":"Fragment molecular orbital method: an approximate computational method for large molecules","volume":"313","author":"Kitaura","year":"1999","journal-title":"Chem Phys Lett"},{"key":"2026110321314273800_B25","doi-asserted-by":"publisher","DOI":"10.1007\/978-981-15-9235-5","volume-title":"Recent Advances of the Fragment Molecular Orbital Method: Enhanced Performance and Applicability","author":"Mochizuki","year":"2021"},{"key":"2026110321314273800_B26","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1002\/jcc.20496","article-title":"Pair interaction energy decomposition analysis","volume":"28","author":"Fedorov","year":"2007","journal-title":"J Comput Chem"},{"key":"2026110321314273800_B27","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1007\/978-1-0716-0282-9_3","article-title":"Guiding medicinal chemistry with fragment molecular orbital (FMO) method","volume":"2114","author":"Heifetz","year":"2020","journal-title":"Methods Mol Biol"},{"key":"2026110321314273800_B28"},{"key":"2026110321314273800_B29","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1007\/s00214-004-0602-3","article-title":"A parallelized integral-direct second-order M\u00f8ller\u2013Plesset perturbation theory method with a fragment molecular orbital scheme","volume":"112","author":"Mochizuki","year":"2004","journal-title":"Theor Chem Acc"},{"key":"2026110321314273800_B30","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1016\/j.sbi.2021.08.010","article-title":"Fragment molecular orbital calculations for biomolecules","volume":"72","author":"Fukuzawa","year":"2022","journal-title":"Curr Opin Struct Biol"},{"key":"2026110321314273800_B31","doi-asserted-by":"publisher","first-page":"60874","DOI":"10.1021\/acsomega.5c09502","article-title":"Dynamical fragment molecular orbital interaction analysis of SARS-CoV\u20132 RNA-dependent RNA polymerase and remdesivir","volume":"10","author":"Miyakawa","year":"2025","journal-title":"ACS Omega"},{"key":"2026110321314273800_B32","doi-asserted-by":"publisher","first-page":"777","DOI":"10.1021\/acs.jcim.0c01062","article-title":"FMODB: the world\u2019s first database of quantum mechanical calculations for biomacromolecules based on the fragment molecular orbital method","volume":"61","author":"Takaya","year":"2021","journal-title":"J Chem Inf Model"},{"key":"2026110321314273800_B33","doi-asserted-by":"publisher","first-page":"3891","DOI":"10.1021\/acs.jcim.1c00203","article-title":"AutoDock vina 1.2.0: new docking methods, expanded force field, and python bindings","volume":"61","author":"Eberhardt","year":"2021","journal-title":"J Chem Inf Model"},{"key":"2026110321314273800_B34","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J Comput Chem"},{"key":"2026110321314273800_B35","doi-asserted-by":"publisher","first-page":"962","DOI":"10.1101\/gr.258848.119","article-title":"Binding specificities of human RNA-binding proteins toward structured and linear RNA sequences","volume":"30","author":"Jolma","year":"2020","journal-title":"Genome Res"},{"key":"2026110321314273800_B36","doi-asserted-by":"publisher","first-page":"1058","DOI":"10.1016\/j.cell.2015.04.029","article-title":"Regnase-1 and roquin regulate a common element in inflammatory mRNAs by spatiotemporally distinct mechanisms","volume":"161","author":"Mino","year":"2015","journal-title":"Cell"},{"key":"2026110321314273800_B37","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1093\/intimm\/dxx015","article-title":"Regulation of mRNA stability by CCCH-type zinc-finger proteins in immune cells","volume":"29","author":"Maeda","year":"2017","journal-title":"Int Immunol"},{"key":"2026110321314273800_B38","doi-asserted-by":"publisher","first-page":"23672","DOI":"10.3390\/ijms151223672","article-title":"P2X and P2Y receptors\u2014role in the pathophysiology of the nervous system","volume":"15","author":"Pucha\u0142owicz","year":"2014","journal-title":"Int J Mol Sci"},{"key":"2026110321314273800_B39","doi-asserted-by":"publisher","first-page":"7381","DOI":"10.1038\/s41598-018-25765-2","article-title":"Substrate specificity of human MCPIP1 endoribonuclease","volume":"8","author":"Wilamowski","year":"2018","journal-title":"Sci Rep"},{"key":"2026110321314273800_B40","doi-asserted-by":"publisher","first-page":"8838","DOI":"10.1093\/nar\/gkz628","article-title":"Translation-dependent unwinding of stem-loops by UPF1 licenses Regnase-1 to degrade inflammatory mRNAs","volume":"47","author":"Mino","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"2026110321314273800_B41","doi-asserted-by":"publisher","first-page":"e71966","DOI":"10.7554\/eLife.71966","article-title":"IRAK1-dependent Regnase-1-14-3-3 complex formation controls Regnase-1-mediated mRNA decay","volume":"10","author":"Akaki","year":"2021","journal-title":"eLife"},{"key":"2026110321314273800_B42","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1016\/j.chembiol.2014.11.021","article-title":"Small-molecule modulators of methyl-lysine binding for the CBX7 chromodomain","volume":"22","author":"Ren","year":"2015","journal-title":"Chem Biol"},{"key":"2026110321314273800_B43","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1016\/j.str.2007.02.002","article-title":"Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin","volume":"15","author":"Schuetz","year":"2007","journal-title":"Structure"},{"key":"2026110321314273800_B44","doi-asserted-by":"publisher","first-page":"E2011","DOI":"10.1073\/pnas.1601089113","article-title":"Suramin inhibits cullin-RING E3 ubiquitin ligases","volume":"113","author":"Wu","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"key":"2026110321314273800_B45","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1038\/s41594-021-00570-0","article-title":"Structural basis for inhibition of the SARS-CoV-2 RNA polymerase by suramin","volume":"28","author":"Yin","year":"2021","journal-title":"Nat Struct Mol Biol"},{"key":"2026110321314273800_B46","doi-asserted-by":"publisher","first-page":"392","DOI":"10.1038\/s41564-020-00844-1","article-title":"Structure of trypanosome coat protein VSGsur and function in suramin resistance","volume":"6","author":"Zeelen","year":"2021","journal-title":"Nat Microbiol"},{"key":"2026110321314273800_B47","doi-asserted-by":"publisher","first-page":"489","DOI":"10.1007\/s12576-019-00666-9","article-title":"Suramin protects hepatocytes from LPS-induced apoptosis by regulating mitochondrial stress and inactivating the JNK-Mst1 signaling pathway","volume":"69","author":"Wang","year":"2019","journal-title":"J Physiol Scien"},{"key":"2026110321314273800_B48","doi-asserted-by":"publisher","first-page":"1301","DOI":"10.4155\/fmc-2017-0322","article-title":"Suramin potently inhibits cGAMP synthase, cGAS, in THP1 cells to modulate IFN-\u03b2 levels","volume":"10","author":"Wang","year":"2018","journal-title":"Future Med Chem"},{"key":"2026110321314273800_B49","doi-asserted-by":"publisher","first-page":"851","DOI":"10.1016\/S0006-2952(99)00150-1","article-title":"Inhibition of tumor necrosis factor-alpha (TNF-alpha)\/TNF-alpha receptor binding by structural analogues of suramin","volume":"58","author":"Mancini","year":"1999","journal-title":"Biochem Pharmacol"},{"key":"2026110321314273800_B50","doi-asserted-by":"publisher","first-page":"931","DOI":"10.1016\/0192-0561(94)00054-9","article-title":"Suramin blocks the binding of interleukin-1 to its receptor and neutralizes IL-1 biological activities","volume":"16","author":"Strassmann","year":"1994","journal-title":"Int J Immunopharmacol"},{"key":"2026110321314273800_B51","doi-asserted-by":"publisher","first-page":"6957","DOI":"10.1093\/nar\/gks359","article-title":"Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase","volume":"40","author":"Xu","year":"2012","journal-title":"Nucleic Acids Res"},{"key":"2026110321314273800_B52","doi-asserted-by":"publisher","first-page":"1721","DOI":"10.1080\/15476286.2020.1795584","article-title":"The immunomodulatory role of regnase family RNA-binding proteins","volume":"17","author":"Fischer","year":"2020","journal-title":"RNA Biol"},{"key":"2026110321314273800_B53","doi-asserted-by":"publisher","first-page":"473","DOI":"10.1016\/j.cplett.2004.08.082","article-title":"Large scale MP2 calculations with fragment molecular orbital scheme","volume":"396","author":"Mochizuki","year":"2004","journal-title":"Chem Phys Lett"},{"key":"2026110321314273800_B54","doi-asserted-by":"publisher","first-page":"190117","DOI":"10.1098\/rsob.190117","article-title":"The anti-parasitic agent suramin and several of its analogues are inhibitors of the DNA binding protein Mcm10","volume":"9","author":"Paulson","year":"2019","journal-title":"Open Biol"},{"key":"2026110321314273800_B55","doi-asserted-by":"publisher","first-page":"10281","DOI":"10.1074\/jbc.RA120.014375","article-title":"Suramin and NF449 are IP5K inhibitors that disrupt inositol hexakisphosphate-mediated regulation of cullin-RING ligase and sensitize cancer cells to MLN4924\/pevonedistat","volume":"295","author":"Zhang","year":"2020","journal-title":"J Biol Chem"},{"key":"2026110321314273800_B56","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1016\/j.ejmech.2004.01.007","article-title":"Structure-activity relationships of analogues of NF449 confirm NF449 as the most potent and selective known P2X1 receptor antagonist","volume":"39","author":"Kassack","year":"2004","journal-title":"Eur J Med Chem"},{"key":"2026110321314273800_B57","doi-asserted-by":"publisher","first-page":"e01168","DOI":"10.1128\/AAC.01168-19","article-title":"100 Years of Suramin","volume":"64","author":"Wiedemar","year":"2020","journal-title":"Antimicrob Agents Chemother"},{"key":"2026110321314273800_B58","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1080\/15476286.2025.2581385","article-title":"Targeting RNA-binding proteins Roquin-1 and Regnase-1 could enhance CAR-iPSC-derived macrophage immunotherapy for solid tumors: a perspective and challenges","volume":"22","author":"Mirzaei","year":"2025","journal-title":"RNA Biol"}],"container-title":["NAR Molecular Medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/narmolmed\/advance-article-pdf\/doi\/10.1093\/narmme\/ugag043\/71559908\/ugag043.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/narmolmed\/article-pdf\/3\/4\/ugag043\/71559908\/ugag043.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/narmolmed\/article-pdf\/3\/4\/ugag043\/71559908\/ugag043.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T02:31:50Z","timestamp":1793759510000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/narmolmed\/article\/doi\/10.1093\/narmme\/ugag043\/8859098"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,1]]},"references-count":58,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2026,10,21]]}},"URL":"https:\/\/doi.org\/10.1093\/narmme\/ugag043","relation":{},"ISSN":["2976-856X"],"issn-type":[{"value":"2976-856X","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2026,10]]},"published":{"date-parts":[[2026,10,1]]},"article-number":"ugag043"}}