{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T13:05:25Z","timestamp":1785416725678,"version":"3.56.0"},"reference-count":161,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T00:00:00Z","timestamp":1785110400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100019232","name":"Lincoln Memorial University","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100019232","id-type":"DOI","asserted-by":"crossref"}]},{"id":[{"id":"https:\/\/ror.org\/02qma2225","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Vaccines"],"abstract":"<jats:p>The innate immune system provides the first line of defense against invading pathogens and relies on tightly regulated mechanisms to initiate and resolve inflammatory responses. In addition to transcriptional control, post-transcriptional regulation of messenger RNA (mRNA) plays a critical role in determining the magnitude and duration of immune responses. Among those key regulators, the ZFP36 family of CCCH-type zinc-finger RNA-binding proteins, including ZFP36, ZFP36L1, and ZFP36L2, plays a central role in controlling the stability and translation of inflammatory, immune-related, and viral RNAs. This review focuses on the ZFP36 family of RNA-binding proteins and highlights their emerging roles in inflammation, immune cell development and differentiation, and antiviral immunity, with a particular focus on ZFP36L1 and ZFP36L2. Recent evidence has identified ZFP36L1 as a broad-spectrum antiviral factor that restricts multiple RNA viruses through distinct molecular mechanisms. A detailed understanding of the molecular mechanisms underlying ZFP36L1- and ZFP36L2-mediated antiviral activity and immune regulation will facilitate rational development of host-directed antiviral therapeutics and their strategic integration with vaccination strategies to limit viral replication, shedding, and transmission, thereby improving the control of emerging and re-emerging viral diseases.<\/jats:p>","DOI":"10.3390\/vaccines14080656","type":"journal-article","created":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T09:47:41Z","timestamp":1785145661000},"page":"656","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["ZFP36 Family Proteins as Critical Regulators of Inflammation, Immune Cell Development, and Antiviral Responses"],"prefix":"10.3390","volume":"14","author":[{"given":"Malabika","family":"Bhowmik","sequence":"first","affiliation":[{"name":"Richard A. Gillespie College of Veterinary Medicine, Lincoln Memorial University, Harrogate, TN 37752, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tooba","family":"Momin","sequence":"additional","affiliation":[{"name":"Richard A. Gillespie College of Veterinary Medicine, Lincoln Memorial University, Harrogate, TN 37752, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neelu","family":"Thakur","sequence":"additional","affiliation":[{"name":"Richard A. Gillespie College of Veterinary Medicine, Lincoln Memorial University, Harrogate, TN 37752, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neeraj","family":"Singh","sequence":"additional","affiliation":[{"name":"Department of Physiological Sciences, College of Veterinary Medicine, Oklahoma State University, Stillwater, OK 74078, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mrigendra","family":"Rajput","sequence":"additional","affiliation":[{"name":"Richard A. Gillespie College of Veterinary Medicine, Lincoln Memorial University, Harrogate, TN 37752, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,7,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0065-2776(04)86004-8","article-title":"Innate autoimmunity","volume":"86","author":"Carroll","year":"2005","journal-title":"Adv. Immunol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"e714","DOI":"10.1002\/mco2.714","article-title":"The interaction of innate immune and adaptive immune system","volume":"5","author":"Wang","year":"2024","journal-title":"MedComm"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1128\/CMR.00046-08","article-title":"Pathogen recognition and inflammatory signaling in innate immune defenses","volume":"22","author":"Mogensen","year":"2009","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1111\/j.1365-2796.2007.01821.x","article-title":"Role of the innate immune system in host defence against bacterial infections: Focus on the Toll-like receptors","volume":"261","author":"Albiger","year":"2007","journal-title":"J. Intern. Med."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"114316","DOI":"10.1016\/j.bcp.2020.114316","article-title":"Detection of Viral Infections by Innate Immunity","volume":"183","author":"Carty","year":"2021","journal-title":"Biochem. Pharmacol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1146\/annurev-immunol-032713-120145","article-title":"Chemokines and chemokine receptors: Positioning cells for host defense and immunity","volume":"32","author":"Griffith","year":"2014","journal-title":"Annu. Rev. Immunol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"16","DOI":"10.3109\/08830185.2010.529976","article-title":"Pathogen recognition by the innate immune system","volume":"30","author":"Kumar","year":"2011","journal-title":"Int. Rev. Immunol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1158\/2326-6066.CIR-13-0081","article-title":"Innate Immune Cells in Inflammation and Cancer","volume":"1","author":"Nowarski","year":"2013","journal-title":"Cancer Immunol. Res."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Akbarzadeh, R., Humrich, J.Y., N\u00e9meth, T., and Amber, K.T. (2025). Editorial: Innate immune dysregulation: A driving force of autoimmunity and chronic inflammation. Front. Immunol., 16.","DOI":"10.3389\/fimmu.2025.1632416"},{"key":"ref_10","first-page":"33","article-title":"Post-transcriptional regulation of cytokine expression and signaling","volume":"19","author":"Guo","year":"2018","journal-title":"Curr. Trends Immunol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/s41590-017-0028-4","article-title":"RNA-binding proteins control gene expression and cell fate in the immune system","volume":"19","author":"Turner","year":"2018","journal-title":"Nat. Immunol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2937","DOI":"10.1007\/s00018-010-0383-x","article-title":"Post-transcriptional control during chronic inflammation and cancer: A focus on AU-rich elements","volume":"67","author":"Khabar","year":"2010","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Makita, S., Takatori, H., and Nakajima, H. (2021). Post-Transcriptional Regulation of Immune Responses and Inflammatory Diseases by RNA-Binding ZFP36 Family Proteins. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.711633"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1615\/CritRevEukaryotGeneExpr.2015013022","article-title":"Emerging Roles of CCCH-Type Zinc Finger Proteins in Destabilizing mRNA Encoding Inflammatory Factors and Regulating Immune Responses","volume":"25","author":"Yang","year":"2015","journal-title":"Crit. Rev. Eukaryot. Gene Expr."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1038\/ni.3724","article-title":"Maintenance of the marginal-zone B cell compartment specifically requires the RNA-binding protein ZFP36L1","volume":"18","author":"Newman","year":"2017","journal-title":"Nat. Immunol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"16229","DOI":"10.1038\/srep16229","article-title":"ZFP36L1 promotes monocyte\/macrophage differentiation by repressing CDK6","volume":"5","author":"Chen","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"e0166521","DOI":"10.1128\/JVI.01665-21","article-title":"Zinc Finger Protein ZFP36L1 Inhibits Flavivirus Infection by both 5\u2032-3\u2032 XRN1 and 3\u2032-5\u2032 RNA-Exosome RNA Decay Pathways","volume":"96","author":"Chiu","year":"2022","journal-title":"J. Virol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"110545","DOI":"10.1016\/j.jbc.2025.110545","article-title":"ZFP36L1 and L2 as novel antiviral factors for Crimean-Congo hemorrhagic fever virus via interaction with viral nucleoprotein","volume":"301","author":"Hirano","year":"2025","journal-title":"J. Biol. Chem."},{"key":"ref_19","first-page":"7371","article-title":"Zinc finger protein ZFP36L1 inhibits influenza A virus through translational repression by targeting HA, M and NS RNA transcripts","volume":"48","author":"Lin","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/nri2685","article-title":"Post-transcriptional regulons coordinate the initiation and resolution of inflammation","volume":"10","author":"Anderson","year":"2010","journal-title":"Nat. Rev. Immunol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.cell.2009.01.002","article-title":"MicroRNAs: Target recognition and regulatory functions","volume":"136","author":"Bartel","year":"2009","journal-title":"Cell"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.virusres.2015.08.019","article-title":"Long noncoding RNA: Novel links between gene expression and innate immunity","volume":"212","author":"Carpenter","year":"2016","journal-title":"Virus Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1097\/MS9.0000000000002761","article-title":"Circular RNAs: History, metabolism, mechanisms of function, and regulatory roles at a glance","volume":"87","author":"Karimi","year":"2025","journal-title":"Ann. Med. Surg."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.1016\/j.cell.2017.05.045","article-title":"Dynamic RNA Modifications in Gene Expression Regulation","volume":"169","author":"Roundtree","year":"2017","journal-title":"Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1007\/s44368-025-00015-6","article-title":"Cross-kingdom insights into the role of m6A RNA modifications in immune regulation","volume":"2","author":"Kuhlmann","year":"2025","journal-title":"Discov. Immun."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1038\/nrm3918","article-title":"In the right place at the right time: Visualizing and understanding mRNA localization","volume":"16","author":"Buxbaum","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Eberle, A.B., Stalder, L., Mathys, H., Orozco, R.Z., and M\u00fchlemann, O. (2008). Posttranscriptional gene regulation by spatial rearrangement of the 3\u2032 untranslated region. PLoS Biol., 6.","DOI":"10.1371\/journal.pbio.0060092"},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Otsuka, H., Fukao, A., Funakami, Y., Duncan, K.E., and Fujiwara, T. (2019). Emerging Evidence of Translational Control by AU-Rich Element-Binding Proteins. Front. Genet., 10.","DOI":"10.3389\/fgene.2019.00332"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1670","DOI":"10.1073\/pnas.83.6.1670","article-title":"Identification of a common nucleotide sequence in the 3\u2032-untranslated region of mRNA molecules specifying inflammatory mediators","volume":"83","author":"Caput","year":"1986","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1177\/0022034512437372","article-title":"Control of cytokine mRNA expression by RNA-binding proteins and microRNAs","volume":"91","author":"Palanisamy","year":"2012","journal-title":"J. Dent. Res."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1038\/s41576-019-0158-7","article-title":"The biogenesis, biology and characterization of circular RNAs","volume":"20","author":"Kristensen","year":"2019","journal-title":"Nat. Rev. Genet."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0076-6879(07)31005-7","article-title":"Mammalian stress granules and processing bodies","volume":"431","author":"Kedersha","year":"2007","journal-title":"Methods Enzymol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1038\/ni1584","article-title":"Post-transcriptional control of cytokine production","volume":"9","author":"Anderson","year":"2008","journal-title":"Nat. Immunol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1016\/j.bbagrm.2013.02.003","article-title":"Tristetraprolin (TTP): Interactions with mRNA and proteins, and current thoughts on mechanisms of action","volume":"1829","author":"Brooks","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"5735","DOI":"10.1007\/s11033-021-06556-x","article-title":"Zinc finger proteins: Insights into the transcriptional and post transcriptional regulation of immune response","volume":"48","author":"Rakhra","year":"2021","journal-title":"Mol. Biol. Rep."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"17827","DOI":"10.1074\/jbc.M001696200","article-title":"Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNA","volume":"275","author":"Lai","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1074\/jbc.M113.466326","article-title":"Mutational and structural analysis of the tandem zinc finger domain of tristetraprolin","volume":"289","author":"Lai","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1146\/annurev-biochem-010909-095056","article-title":"The discovery of zinc fingers and their applications in gene regulation and genome manipulation","volume":"79","author":"Klug","year":"2010","journal-title":"Annu. Rev. Biochem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1609","DOI":"10.1002\/j.1460-2075.1985.tb03825.x","article-title":"Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes","volume":"4","author":"Miller","year":"1985","journal-title":"EMBO J."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0014-5793(85)80723-7","article-title":"The primary structure of transcription factor TFIIIA has 12 consecutive repeats","volume":"186","author":"Brown","year":"1985","journal-title":"FEBS Lett."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"16556","DOI":"10.1016\/S0021-9258(17)46259-4","article-title":"Rapid insulin-stimulated accumulation of an mRNA encoding a proline-rich protein","volume":"265","author":"Lai","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1042\/bst0300945","article-title":"Tristetraprolin and other CCCH tandem zinc-finger proteins in the regulation of mRNA turnover","volume":"30","author":"Blackshear","year":"2002","journal-title":"Biochem. Soc. Trans."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.ymgme.2021.03.015","article-title":"Tristetraprolin: A cytosolic regulator of mRNA turnover moonlighting as transcriptional corepressor of gene expression","volume":"133","year":"2021","journal-title":"Mol. Genet. Metab."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"4717","DOI":"10.1021\/acs.jctc.6b00150","article-title":"Structural Basis of the Disorder in the Tandem Zinc Finger Domain of the RNA-Binding Protein Tristetraprolin","volume":"12","author":"Tavella","year":"2016","journal-title":"J. Chem. Theory Comput."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1038\/nsmb738","article-title":"Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d","volume":"11","author":"Hudson","year":"2004","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"14792","DOI":"10.1074\/jbc.M801234200","article-title":"A unique C-terminal repeat domain maintains the cytosolic localization of the placenta-specific tristetraprolin family member ZFP36L3","volume":"283","author":"Frederick","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1042\/BST20160166","article-title":"The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: A tale of two phosphatases","volume":"44","author":"Clark","year":"2016","journal-title":"Biochem. Soc. Trans."},{"key":"ref_48","unstructured":"Miah, I. (2021). Study of the Structure and Functionality of the Zinc Finger Protein ZFP36L1 and Its Role in Gene Regulation. [Master\u2019s Thesis, University of Essex]."},{"key":"ref_49","unstructured":"Shaikh Solaiman, N. (2021). The Role of the RNA-binding Protein ZFP36L1 in Suppression of Replication Stress-induced Genomic Instability. [Ph.D. Thesis, University of Westminster Life Sciences]."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2031","DOI":"10.1007\/s00018-012-1150-y","article-title":"Multiple functions of tristetraprolin\/TIS11 RNA-binding proteins in the regulation of mRNA biogenesis and degradation","volume":"70","author":"Ciais","year":"2013","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e1531","DOI":"10.1002\/wrna.1531","article-title":"The tandem zinc finger RNA binding domain of members of the tristetraprolin protein family","volume":"10","author":"Lai","year":"2019","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1089\/jir.2013.0150","article-title":"Phylogenetic distribution and evolution of the linked RNA-binding and NOT1-binding domains in the tristetraprolin family of tandem CCCH zinc finger proteins","volume":"34","author":"Blackshear","year":"2014","journal-title":"J. Interferon Cytokine Res."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"6445","DOI":"10.1128\/MCB.24.14.6445-6455.2004","article-title":"Chorioallantoic fusion defects and embryonic lethality resulting from disruption of Zfp36L1, a gene encoding a CCCH tandem zinc finger protein of the Tristetraprolin family","volume":"24","author":"Stumpo","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"3144","DOI":"10.1002\/dvdy.20949","article-title":"The RNA binding protein Zfp36l1 is required for normal vascularisation and post-transcriptionally regulates VEGF expression","volume":"235","author":"Bell","year":"2006","journal-title":"Dev. Dyn."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/ni.1901","article-title":"Deletion of the RNA-binding proteins ZFP36L1 and ZFP36L2 leads to perturbed thymic development and T lymphoblastic leukemia","volume":"11","author":"Hodson","year":"2010","journal-title":"Nat. Immunol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2673","DOI":"10.4049\/jimmunol.1600854","article-title":"The RNA-Binding Proteins Zfp36l1 and Zfp36l2 Enforce the Thymic \u03b2-Selection Checkpoint by Limiting DNA Damage Response Signaling and Cell Cycle Progression","volume":"197","author":"Vogel","year":"2016","journal-title":"J. Immunol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"11606","DOI":"10.1074\/jbc.M111457200","article-title":"Members of the tristetraprolin family of tandem CCCH zinc finger proteins exhibit CRM1-dependent nucleocytoplasmic shuttling","volume":"277","author":"Phillips","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2401","DOI":"10.1182\/blood-2009-04-214619","article-title":"Targeted disruption of Zfp36l2, encoding a CCCH tandem zinc finger RNA-binding protein, results in defective hematopoiesis","volume":"114","author":"Stumpo","year":"2009","journal-title":"Blood"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.1016\/S0006-291X(02)00363-7","article-title":"Identification of nuclear import and export signals within the structure of the zinc finger protein TIS11","volume":"293","author":"Murata","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"9497","DOI":"10.1128\/MCB.01099-06","article-title":"BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites","volume":"26","author":"Benjamin","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1126\/science.aad5978","article-title":"RNA-binding proteins ZFP36L1 and ZFP36L2 promote cell quiescence","volume":"352","author":"Galloway","year":"2016","journal-title":"Science"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S1074-7613(00)80411-2","article-title":"A pathogenetic role for TNF alpha in the syndrome of cachexia, arthritis, and autoimmunity resulting from tristetraprolin (TTP) deficiency","volume":"4","author":"Taylor","year":"1996","journal-title":"Immunity"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1126\/science.281.5379.1001","article-title":"Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin","volume":"281","author":"Carballo","year":"1998","journal-title":"Science"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2389","DOI":"10.1182\/blood.V98.8.2389","article-title":"Roles of tumor necrosis factor-alpha receptor subtypes in the pathogenesis of the tristetraprolin-deficiency syndrome","volume":"98","author":"Carballo","year":"2001","journal-title":"Blood"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"e00029-19","DOI":"10.1128\/MCB.00029-19","article-title":"Importance of the conserved carboxyl-terminal CNOT1 binding domain to tristetraprolin activity in vivo","volume":"39","author":"Lai","year":"2019","journal-title":"Mol. Cell. Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"446","DOI":"10.4062\/biomolther.2018.078","article-title":"ZFP36L1 and AUF1 Induction Contribute to the Suppression of Inflammatory Mediators Expression by Globular Adiponectin via Autophagy Induction in Macrophages","volume":"26","author":"Shrestha","year":"2018","journal-title":"Biomol. Ther."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Bhowmik, M., Momin, T., Newell, A., Janzow, M., Singh, N., Singh, A., Darweesh, M., and Rajput, M. (2026). ZFP36L1 negatively regulates autophagy and contributes to suppressing murine norovirus replication. Front. Virol., 6.","DOI":"10.3389\/fviro.2026.1752210"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1482","DOI":"10.1080\/15548627.2019.1687985","article-title":"RNA-binding protein ZFP36\/TTP protects against ferroptosis by regulating autophagy signaling pathway in hepatic stellate cells","volume":"16","author":"Zhang","year":"2020","journal-title":"Autophagy"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"199498","DOI":"10.1016\/j.virusres.2024.199498","article-title":"ZFP36 Facilitates Senecavirus A (SVA) replication by inhibiting the production of type I interferon","volume":"350","author":"Yin","year":"2024","journal-title":"Virus Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"4796","DOI":"10.1038\/s41467-026-71474-0","article-title":"ZFP36L2 is an interferon \u03b2-induced inhibitor that restricts the nuclear export of HIV-1 transcripts","volume":"17","author":"Pang","year":"2026","journal-title":"Nat. Commun."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"e33057","DOI":"10.7554\/eLife.33057","article-title":"ZFP36 RNA-binding proteins restrain T cell activation and anti-viral immunity","volume":"7","author":"Moore","year":"2018","journal-title":"eLife"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"e14776","DOI":"10.7717\/peerj.14776","article-title":"ZFP36 ring finger protein like 1 significantly suppresses human coronavirus OC43 replication","volume":"11","author":"Momin","year":"2023","journal-title":"PeerJ"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"e0111424","DOI":"10.1128\/jvi.01114-24","article-title":"Foot-and-mouth disease virus (FMDV) negatively regulates ZFP36 protein expression to alleviate its antiviral activity","volume":"98","author":"Yin","year":"2024","journal-title":"J. Virol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/j.abb.2007.04.011","article-title":"Comparative expression of tristetraprolin (TTP) family member transcripts in normal human tissues and cancer cell lines","volume":"462","author":"Carrick","year":"2007","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.ejcb.2016.04.007","article-title":"Functional analysis of ZFP36 proteins in keratinocytes","volume":"95","author":"Prenzler","year":"2016","journal-title":"Eur. J. Cell Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"20588","DOI":"10.18632\/oncotarget.15246","article-title":"Zinc finger protein ZFP36L1 promotes osteoblastic differentiation but represses adipogenic differentiation of mouse multipotent cells","volume":"8","author":"Tseng","year":"2017","journal-title":"Oncotarget"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"eabo0981","DOI":"10.1126\/sciimmunol.abo0981","article-title":"The ZFP36 family of RNA binding proteins regulates homeostatic and autoreactive T cell responses","volume":"7","author":"Cook","year":"2022","journal-title":"Sci. Immunol."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Wu, F., Kaczynski, T., Matheson, L.S., Liu, T., Wang, J., Turner, M., and Mu, X. (2020). Zfp36l1 and Zfp36l2 balances proliferation and differentiation in the developing retina. bioRxiv.","DOI":"10.1101\/2020.12.15.422926"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1038\/nature12215","article-title":"ZFP36L2 is required for self-renewal of early burst-forming unit erythroid progenitors","volume":"499","author":"Zhang","year":"2013","journal-title":"Nature"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1095\/biolreprod.105.040527","article-title":"Zfp36l3, a rodent X chromosome gene encoding a placenta-specific member of the Tristetraprolin family of CCCH tandem zinc finger proteins","volume":"73","author":"Blackshear","year":"2005","journal-title":"Biol. Reprod."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1093\/jb\/mvaa072","article-title":"Nuclear accumulation of ZFP36L1 is cell cycle-dependent and determined by a C-terminal serine-rich cluster","volume":"168","author":"Matsuura","year":"2020","journal-title":"J. Biochem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1038\/sj.emboj.7600163","article-title":"MK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decay","volume":"23","author":"Stoecklin","year":"2004","journal-title":"EMBO J."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"10176","DOI":"10.1074\/jbc.M310486200","article-title":"MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 binding","volume":"279","author":"Chrestensen","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"bio031575","DOI":"10.1242\/bio.031575","article-title":"ZFP36L2 is a cell cycle-regulated CCCH protein necessary for DNA lesion-induced S-phase arrest","volume":"7","author":"Noguchi","year":"2018","journal-title":"Biol. Open"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"868","DOI":"10.15252\/msb.20156628","article-title":"Tristetraprolin binding site atlas in the macrophage transcriptome reveals a switch for inflammation resolution","volume":"12","author":"Sedlyarov","year":"2016","journal-title":"Mol. Syst. Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"4311","DOI":"10.1128\/MCB.19.6.4311","article-title":"Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA","volume":"19","author":"Lai","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1089\/jir.2010.0154","article-title":"Tristetraprolin Regulates Interleukin-6 Expression Through p38 MAPK-Dependent Affinity Changes with mRNA 3\u2032 Untranslated Region","volume":"31","author":"Zhao","year":"2011","journal-title":"J. Interferon Cytokine Res."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"3922","DOI":"10.4049\/jimmunol.1300126","article-title":"Suppression of IL-12 production by tristetraprolin through blocking NF-kcyB nuclear translocation","volume":"191","author":"Gu","year":"2013","journal-title":"J. Immunol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1084\/jem.20120707","article-title":"Tristetraprolin regulation of interleukin 23 mRNA stability prevents a spontaneous inflammatory disease","volume":"210","author":"Molle","year":"2013","journal-title":"J. Exp. Med."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"e2350700","DOI":"10.1002\/eji.202350700","article-title":"Zfp36l1 establishes the high-affinity CD8 T-cell response by directly linking TCR affinity to cytokine sensing","volume":"54","author":"Petkau","year":"2024","journal-title":"Eur. J. Immunol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"e2451018","DOI":"10.1002\/eji.202451018","article-title":"Regulation of IFN-\u03b3 production by ZFP36L2 in T cells is time-dependent","volume":"54","author":"Zandhuis","year":"2024","journal-title":"Eur. J. Immunol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1161\/01.RES.0000222284.48288.28","article-title":"Atherosclerotic plaque macrophage transcriptional regulators are expressed in blood and modulated by tristetraprolin","volume":"98","author":"Patino","year":"2006","journal-title":"Circ. Res."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1038\/sj.cdd.4401850","article-title":"TLR signaling","volume":"13","author":"Kawai","year":"2006","journal-title":"Cell Death Differ."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"2195","DOI":"10.1101\/gad.1228704","article-title":"Signaling to NF-\u03baB","volume":"18","author":"Hayden","year":"2004","journal-title":"Genes Dev."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1933","DOI":"10.1016\/j.febslet.2009.04.039","article-title":"The p38 MAPK pathway inhibits tristetraprolin-directed decay of interleukin-10 and pro-inflammatory mediator mRNAs in murine macrophages","volume":"583","author":"Tudor","year":"2009","journal-title":"FEBS Lett."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1093\/nar\/gku652","article-title":"ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK-RSK pathway","volume":"42","author":"Adachi","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"7263","DOI":"10.4049\/jimmunol.172.12.7263","article-title":"The role of mRNA turnover in the regulation of tristetraprolin expression: Evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent, autoregulatory pathway","volume":"172","author":"Brooks","year":"2004","journal-title":"J. Immunol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"2408","DOI":"10.1128\/MCB.26.6.2408-2418.2006","article-title":"Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways","volume":"26","author":"Brook","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1842","DOI":"10.1073\/pnas.042575699","article-title":"Ubiquitin-dependent mechanism regulates rapid turnover of AU-rich cytokine mRNAs","volume":"99","author":"Laroia","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"e202451641","DOI":"10.1002\/eji.202451641","article-title":"Combined Deletion of ZFP36L1 and ZFP36L2 Drives Superior Cytokine Production in T Cells at the Cost of Cell Fitness","volume":"55","author":"Zandhuis","year":"2025","journal-title":"Eur. J. Immunol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"4192","DOI":"10.1038\/s41467-025-58993-y","article-title":"ZFP36-family RNA-binding proteins in regulatory T cells reinforce immune homeostasis","volume":"16","author":"Bell","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1038\/embor.2009.9","article-title":"miR-29a suppresses tristetraprolin, which is a regulator of epithelial polarity and metastasis","volume":"10","author":"Gebeshuber","year":"2009","journal-title":"EMBO Rep."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.cell.2004.12.038","article-title":"Involvement of MicroRNA in AU-Rich Element-Mediated mRNA Instability","volume":"120","author":"Jing","year":"2005","journal-title":"Cell"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1007\/PL00000854","article-title":"HuR and mRNA stability","volume":"58","author":"Brennan","year":"2001","journal-title":"Cell Mol. Life Sci."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"2089","DOI":"10.4049\/jimmunol.1201126","article-title":"Cutting edge: IL-10-mediated tristetraprolin induction is part of a feedback loop that controls macrophage STAT3 activation and cytokine production","volume":"189","author":"Gaba","year":"2012","journal-title":"J. Immunol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"3921","DOI":"10.1128\/MCB.00845-15","article-title":"Tristetraprolin Recruits Eukaryotic Initiation Factor 4E2 To Repress Translation of AU-Rich Element-Containing mRNAs","volume":"35","author":"Tao","year":"2015","journal-title":"Mol. Cell. Biol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1261\/rna.054833.115","article-title":"Recruitment of the 4EHP-GYF2 cap-binding complex to tetraproline motifs of tristetraprolin promotes repression and degradation of mRNAs with AU-rich elements","volume":"22","author":"Fu","year":"2016","journal-title":"RNA"},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Ma, J., Lin, Y., Xiong, W., Liu, X., Pan, M., Sun, J., Sun, Y., Li, Y., Guo, H., and Pang, G. (2024). The microRNA-29ab1\/Zfp36\/AR Axis in the Hypothalamus Regulates Male-Typical Behaviors in Mice. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms252313089"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"9838","DOI":"10.1093\/nar\/gkae555","article-title":"Structure and RNA-binding of the helically extended Roquin CCCH-type zinc finger","volume":"52","author":"Tants","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"3795","DOI":"10.1002\/ejic.202100402","article-title":"Targeting Zinc Finger Proteins with Exogenous Metals and Molecules: Lessons learned from Tristetraprolin, a CCCH type Zinc Finger","volume":"2021","author":"Ok","year":"2021","journal-title":"Eur. J. Inorg. Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"14120","DOI":"10.1016\/S0021-9258(17)43831-2","article-title":"Xenopus transcription factor A requires zinc for binding to the 5 S RNA gene","volume":"258","author":"Hanas","year":"1983","journal-title":"J. Biol. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"2219","DOI":"10.1128\/MCB.15.4.2219","article-title":"The nonamer UUAUUUAUU is the key AU-rich sequence motif that mediates mRNA degradation","volume":"15","author":"Zubiaga","year":"1995","journal-title":"Mol. Cell. Biol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"19947","DOI":"10.1074\/jbc.M301290200","article-title":"Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates","volume":"278","author":"Blackshear","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"2632","DOI":"10.1021\/acs.biochem.4c00259","article-title":"Structure and Dynamics of the CCCH-Type Tandem Zinc Finger Domain of POS-1 and Implications for RNA Binding Specificity","volume":"63","author":"Ertekin","year":"2024","journal-title":"Biochemistry"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1038\/nsmb.2572","article-title":"Structural basis for the recruitment of the human CCR4-NOT deadenylase complex by tristetraprolin","volume":"20","author":"Fabian","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1002\/jcb.21130","article-title":"Tristetraprolin recruits functional mRNA decay complexes to ARE sequences","volume":"100","author":"Hau","year":"2007","journal-title":"J. Cell. Biochem."},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Zhao, Q., Pavanello, L., Bartlam, M., and Winkler, G.S. (2023). Structure and function of molecular machines involved in deadenylation-dependent 5\u2032-3\u2032 mRNA degradation. Front. Genet., 14.","DOI":"10.3389\/fgene.2023.1233842"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"7528","DOI":"10.1038\/s41467-025-62741-7","article-title":"Multivalent interactions with CCR4\u2013NOT and PABPC1 determine mRNA repression efficiency by tristetraprolin","volume":"16","author":"Pekovic","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1189\/jlb.3A0214-106R","article-title":"Tristetraprolin (TTP) coordinately regulates primary and secondary cellular responses to proinflammatory stimuli","volume":"97","author":"Qiu","year":"2015","journal-title":"J. Leukoc. Biol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.4049\/jimmunol.180.4.2545","article-title":"Tristetraprolin regulates CXCL1 (KC) mRNA stability","volume":"180","author":"Datta","year":"2008","journal-title":"J. Immunol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"30166","DOI":"10.1074\/jbc.M502280200","article-title":"Functionally independent AU-rich sequence motifs regulate KC (CXCL1) mRNA","volume":"280","author":"Novotny","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1983","DOI":"10.1093\/carcin\/bgu080","article-title":"Posttranscriptional control of the chemokine receptor CXCR4 expression in cancer cells","volume":"35","author":"Khabar","year":"2014","journal-title":"Carcinogenesis"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"2051","DOI":"10.1172\/JCI80631","article-title":"The RNA-binding protein tristetraprolin schedules apoptosis of pathogen-engaged neutrophils during bacterial infection","volume":"127","author":"Ebner","year":"2017","journal-title":"J. Clin. Investig."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"2696","DOI":"10.4049\/jimmunol.1101149","article-title":"Zinc finger protein tristetraprolin interacts with CCL3 mRNA and regulates tissue inflammation","volume":"187","author":"Kang","year":"2011","journal-title":"J. Immunol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"2520","DOI":"10.1101\/gad.7.12b.2520","article-title":"Double-strand signal sequence breaks in V(D)J recombination are blunt, 5\u2032-phosphorylated, RAG-dependent, and cell cycle regulated","volume":"7","author":"Schlissel","year":"1993","journal-title":"Genes. Dev."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.molcel.2005.05.011","article-title":"Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle","volume":"18","author":"Jiang","year":"2005","journal-title":"Mol. Cell"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"6084","DOI":"10.4049\/jimmunol.1200368","article-title":"IL-7 functionally segregates the pro-B cell stage by regulating transcription of recombination mediators across cell cycle","volume":"188","author":"Johnson","year":"2012","journal-title":"J. Immunol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"e1419","DOI":"10.1002\/wrna.1419","article-title":"Cell cycle RNA regulons coordinating early lymphocyte development","volume":"8","author":"Galloway","year":"2017","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"eaau6085","DOI":"10.1126\/sciimmunol.aau6085","article-title":"Structure and function of the immune system in the spleen","volume":"4","author":"Lewis","year":"2019","journal-title":"Sci. Immunol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1038\/nri2656","article-title":"The follicular versus marginal zone B lymphocyte cell fate decision","volume":"9","author":"Pillai","year":"2009","journal-title":"Nat. Rev. Immunol."},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Wittner, J., and Schuh, W. (2021). Kr\u00fcppel-like Factor 2 (KLF2) in Immune Cell Migration. Vaccines, 9.","DOI":"10.3390\/vaccines9101171"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"4028","DOI":"10.1182\/blood-2008-01-129049","article-title":"IRF8 regulates B-cell lineage specification, commitment, and differentiation","volume":"112","author":"Wang","year":"2008","journal-title":"Blood"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"2274","DOI":"10.1038\/s41467-022-29979-x","article-title":"The timing of differentiation and potency of CD8 effector function is set by RNA binding proteins","volume":"13","author":"Petkau","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"e20200504","DOI":"10.1084\/jem.20200504","article-title":"Efficient homing of antibody-secreting cells to the bone marrow requires RNA-binding protein ZFP36L1","volume":"218","author":"Saveliev","year":"2021","journal-title":"J. Exp. Med."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"G\u00f3mez-Virgilio, L., Silva-Lucero, M.D., Flores-Morelos, D.S., Gallardo-Nieto, J., Lopez-Toledo, G., Abarca-Fernandez, A.M., Zacapala-G\u00f3mez, A.E., Luna-Mu\u00f1oz, J., Montiel-Sosa, F., and Soto-Rojas, L.O. (2022). Autophagy: A Key Regulator of Homeostasis and Disease: An Overview of Molecular Mechanisms and Modulators. Cells, 11.","DOI":"10.3390\/cells11152262"},{"key":"ref_136","doi-asserted-by":"crossref","unstructured":"Khandia, R., Dadar, M., Munjal, A., Dhama, K., Karthik, K., Tiwari, R., Yatoo, M.I., Iqbal, H.M.N., Singh, K.P., and Joshi, S.K. (2019). A Comprehensive Review of Autophagy and Its Various Roles in Infectious, Non-Infectious, and Lifestyle Diseases: Current Knowledge and Prospects for Disease Prevention, Novel Drug Design, and Therapy. Cells, 8.","DOI":"10.3390\/cells8070674"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1038\/nature09782","article-title":"Autophagy in immunity and inflammation","volume":"469","author":"Levine","year":"2011","journal-title":"Nature"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1007\/978-981-15-0602-4_27","article-title":"Autophagy and the Immune Response","volume":"1206","author":"Cui","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1111\/j.1365-2567.2010.03321.x","article-title":"Autophagy and adaptive immunity","volume":"131","author":"Crotzer","year":"2010","journal-title":"Immunology"},{"key":"ref_140","first-page":"313","article-title":"Tristetraprolin inhibits autophagy in cultured lung cancer cells via the nuclear factor-\u03baB pathway","volume":"39","author":"Deng","year":"2019","journal-title":"J. South. Med. Univ."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1038\/s41419-021-03873-8","article-title":"Stress granules, RNA-binding proteins and polyglutamine diseases: Too much aggregation?","volume":"12","author":"Marcelo","year":"2021","journal-title":"Cell Death Dis."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1261\/rna.078738.121","article-title":"The role of stress-activated RNA-protein granules in surviving adversity","volume":"27","author":"Escalante","year":"2021","journal-title":"RNA"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"a012286","DOI":"10.1101\/cshperspect.a012286","article-title":"P-bodies and stress granules: Possible roles in the control of translation and mRNA degradation","volume":"4","author":"Decker","year":"2012","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1934","DOI":"10.1080\/15548627.2022.2164427","article-title":"Stress granule homeostasis is modulated by TRIM21-mediated ubiquitination of G3BP1 and autophagy-dependent elimination of stress granules","volume":"19","author":"Yang","year":"2023","journal-title":"Autophagy"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1002\/1873-3468.14787","article-title":"The autophagy of stress granules","volume":"598","author":"Ryan","year":"2024","journal-title":"FEBS Lett."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1083\/jcb.200502088","article-title":"Stress granules and processing bodies are dynamically linked sites of mRNP remodeling","volume":"169","author":"Kedersha","year":"2005","journal-title":"J. Cell Biol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1128\/br.35.3.235-241.1971","article-title":"Expression of animal virus genomes","volume":"35","author":"Baltimore","year":"1971","journal-title":"Bacteriol. Rev."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"e1498","DOI":"10.1002\/wrna.1498","article-title":"Unconventional RNA-binding proteins step into the virus-host battlefront","volume":"9","author":"Castello","year":"2018","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"305","DOI":"10.4161\/rna.8.2.15391","article-title":"Diverse roles of host RNA binding proteins in RNA virus replication","volume":"8","author":"Li","year":"2011","journal-title":"RNA Biol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1186\/s12929-025-01122-0","article-title":"The zinc finger protein ZFP36L2 inhibits flavivirus infection via the 5\u2032-3\u2032 XRN1-mediated RNA decay pathway in the replication complexes","volume":"32","author":"Lin","year":"2025","journal-title":"J. Biomed. Sci."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/s41579-018-0003-6","article-title":"Autophagy during viral infection\u2014A double-edged sword","volume":"16","author":"Choi","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"107849","DOI":"10.1016\/j.jbc.2024.107849","article-title":"Lipoprotein receptors: A little grease for enveloped viruses to open the lock?","volume":"300","author":"Cosset","year":"2024","journal-title":"J. Biol. Chem."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"E416","DOI":"10.1152\/ajpendo.00091.2007","article-title":"Cell surface expression of LDL receptor in chronic hepatitis C: Correlation with viral load","volume":"293","author":"Petit","year":"2007","journal-title":"Am. J. Physiol.-Endocrinol. Metab."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"7306","DOI":"10.1073\/pnas.1214441110","article-title":"LDL receptor and its family members serve as the cellular receptors for vesicular stomatitis virus","volume":"110","author":"Finkelshtein","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Silva, M.J.A., Ribeiro, L.R., Gouveia, M.I.M., Marcelino, B.D.R., Santos, C.S.D., Lima, K.V.B., and Lima, L.N.G.C. (2023). Hyperinflammatory Response in COVID-19: A Systematic Review. Viruses, 15.","DOI":"10.3390\/v15020553"},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Gu, Y., Zuo, X., Zhang, S., Ouyang, Z., Jiang, S., Wang, F., and Wang, G. (2021). The Mechanism behind Influenza Virus Cytokine Storm. Viruses, 13.","DOI":"10.3390\/v13071362"},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Girija, A.S.S., Shankar, E.M., and Larsson, M. (2020). Could SARS-CoV-2-Induced Hyperinflammation Magnify the Severity of Coronavirus Disease (COVID-19) Leading to Acute Respiratory Distress Syndrome?. Front. Immunol., 11.","DOI":"10.3389\/fimmu.2020.01206"},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Choudhary, I., Vo, T., Bathula, C.S., Lamichhane, R., Lewis, B.W., Looper, J., Jeyaseelan, S., Blackshear, P.J., Saini, Y., and Patial, S. (2020). Tristetraprolin Overexpression in Non-hematopoietic Cells Protects Against Acute Lung Injury in Mice. Front. Immunol., 11.","DOI":"10.3389\/fimmu.2020.02164"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/j.celrep.2013.10.012","article-title":"Changes in cellular mRNA stability, splicing, and polyadenylation through HuR protein sequestration by a cytoplasmic RNA virus","volume":"5","author":"Barnhart","year":"2013","journal-title":"Cell Rep."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"920","DOI":"10.3390\/v3060920","article-title":"Pattern recognition receptors and the innate immune response to viral infection","volume":"3","author":"Thompson","year":"2011","journal-title":"Viruses"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"12223","DOI":"10.7150\/thno.50992","article-title":"Virus-induced p38 MAPK activation facilitates viral infection","volume":"10","author":"Cheng","year":"2020","journal-title":"Theranostics"}],"container-title":["Vaccines"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-393X\/14\/8\/656\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T04:24:50Z","timestamp":1785299090000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-393X\/14\/8\/656"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,27]]},"references-count":161,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2026,8]]}},"alternative-id":["vaccines14080656"],"URL":"https:\/\/doi.org\/10.3390\/vaccines14080656","relation":{},"ISSN":["2076-393X"],"issn-type":[{"value":"2076-393X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,27]]}}}