{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T03:38:33Z","timestamp":1778643513602,"version":"3.51.4"},"reference-count":283,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2024,1,9]],"date-time":"2024-01-09T00:00:00Z","timestamp":1704758400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Spanish Ministerio de Universidades\/NextGenerationEU\/Ayudas para la Recualificaci\u00f3n del Sistema Universitario Espa\u00f1ol"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>The COVID-19 pandemic has brought to the forefront the intricate relationship between SARS-CoV-2 and its impact on neurological complications, including potential links to neurodegenerative processes, characterized by a dysfunction of the protein quality control systems and ER stress. This review article explores the role of protein quality control systems, such as the Unfolded Protein Response (UPR), the Endoplasmic Reticulum-Associated Degradation (ERAD), the Ubiquitin\u2013Proteasome System (UPS), autophagy and the molecular chaperones, in SARS-CoV-2 infection. Our hypothesis suggests that SARS-CoV-2 produces ER stress and exploits the protein quality control systems, leading to a disruption in proteostasis that cannot be solved by the host cell. This disruption culminates in cell death and may represent a link between SARS-CoV-2 and neurodegeneration.<\/jats:p>","DOI":"10.3390\/cells13020123","type":"journal-article","created":{"date-parts":[[2024,1,9]],"date-time":"2024-01-09T10:48:06Z","timestamp":1704797286000},"page":"123","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Protein Quality Control Systems and ER Stress as Key Players in SARS-CoV-2-Induced Neurodegeneration"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8173-2638","authenticated-orcid":false,"given":"Elena","family":"Gavil\u00e1n","sequence":"first","affiliation":[{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de Farmacia, Universidad de Sevilla (US), 41012 Sevilla, Spain"},{"name":"Instituto de Biomedicina de Sevilla, IBIS, Hospital Universitario Virgen del Roc\u00edo, Junta de Andaluc\u00eda, CSIC, University of Seville (US), 41013 Sevilla, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1876-9961","authenticated-orcid":false,"given":"Rafael","family":"Medina-Guzman","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de Farmacia, Universidad de Sevilla (US), 41012 Sevilla, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8791-6710","authenticated-orcid":false,"given":"Bazhena","family":"Bahatyrevich-Kharitonik","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de Farmacia, Universidad de Sevilla (US), 41012 Sevilla, Spain"},{"name":"Instituto de Biomedicina de Sevilla, IBIS, Hospital Universitario Virgen del Roc\u00edo, Junta de Andaluc\u00eda, CSIC, University of Seville (US), 41013 Sevilla, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Diego","family":"Ruano","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de Farmacia, Universidad de Sevilla (US), 41012 Sevilla, Spain"},{"name":"Instituto de Biomedicina de Sevilla, IBIS, Hospital Universitario Virgen del Roc\u00edo, Junta de Andaluc\u00eda, CSIC, University of Seville (US), 41013 Sevilla, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2024,1,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1038\/s41580-021-00418-x","article-title":"Mechanisms of SARS-CoV-2 entry into cells","volume":"23","author":"Jackson","year":"2022","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1186\/s12964-023-01104-5","article-title":"Structural and non-structural proteins in SARS-CoV-2: Potential aspects to COVID-19 treatment or prevention of progression of related diseases","volume":"21","author":"Kakavandi","year":"2023","journal-title":"Cell Commun. Signal."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1038\/s41586-020-2772-0","article-title":"Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion","volume":"588","author":"Benton","year":"2020","journal-title":"Nature"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1038\/s41586-020-2852-1","article-title":"SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies","volume":"588","author":"Barnes","year":"2020","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1038\/s41579-021-00630-8","article-title":"Structural biology of SARS-CoV-2 and implications for therapeutic development","volume":"19","author":"Yang","year":"2021","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3059","DOI":"10.1007\/s00415-021-10406-y","article-title":"Neurological symptoms, manifestations, and complications associated with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and coronavirus disease 19 (COVID-19)","volume":"268","author":"Harapan","year":"2021","journal-title":"J. Neurol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"e13013","DOI":"10.1111\/bpa.13013","article-title":"SARS-CoV-2 and the brain: A review of the current knowledge on neuropathology in COVID-19","volume":"31","author":"Maiese","year":"2021","journal-title":"Brain Pathol."},{"key":"ref_8","first-page":"967","article-title":"Outcomes Among Patients Referred to Outpatient Rehabilitation Clinics After COVID-19 diagnosis\u2014United States, January 2020\u2013March 2021","volume":"70","author":"Wanga","year":"2021","journal-title":"MMWR Morb. Mortal. Wkly. Rep."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2192","DOI":"10.1007\/s12031-020-01767-6","article-title":"Evidence of Coronavirus (CoV) Pathogenesis and Emerging Pathogen SARS-CoV-2 in the Nervous System: A Review on Neurological Impairments and Manifestations","volume":"71","author":"Jha","year":"2021","journal-title":"J. Mol. Neurosci."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Villa, C., Rivellini, E., Lavitrano, M., and Combi, R. (2022). Can SARS-CoV-2 Infection Exacerbate Alzheimer\u2019s Disease? An Overview of Shared Risk Factors and Pathogenetic Mechanisms. J. Pers. Med., 12.","DOI":"10.3390\/jpm12010029"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Boura, I., Qamar, M.A., Daddoveri, F., Leta, V., Poplawska-Domaszewicz, K., Falup-Pecurariu, C., and Ray Chaudhuri, K. (2023). SARS-CoV-2 and Parkinson\u2019s Disease: A Review of Where We Are Now. Biomedicines, 11.","DOI":"10.3390\/biomedicines11092524"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1002\/jnr.25171","article-title":"SARS-CoV-2 infection and Parkinson\u2019s disease: Possible links and perspectives","volume":"101","author":"Kaushik","year":"2023","journal-title":"J. Neurosci. Res."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Ruano, D. (2021). Proteostasis Dysfunction in Aged Mammalian Cells. The Stressful Role of Inflammation. Front. Mol. Biosci., 8.","DOI":"10.3389\/fmolb.2021.658742"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Ghemrawi, R., and Khair, M. (2020). Endoplasmic Reticulum Stress and Unfolded Protein Response in Neurodegenerative Diseases. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21176127"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1038\/nrneurol.2017.99","article-title":"ER stress and the unfolded protein response in neurodegeneration","volume":"13","author":"Hetz","year":"2017","journal-title":"Nat. Rev. Neurol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"101417","DOI":"10.1016\/j.arr.2021.101417","article-title":"Exploring ER stress response in cellular aging and neuroinflammation in Alzheimer\u2019s disease","volume":"70","author":"Uddin","year":"2021","journal-title":"Ageing Res. Rev."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Cirone, M. (2021). ER Stress, UPR Activation and the Inflammatory Response to Viral Infection. Viruses, 13.","DOI":"10.3390\/v13050798"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1111\/j.1474-9726.2009.00519.x","article-title":"Dysfunction of the unfolded protein response increases neurodegeneration in aged rat hippocampus following proteasome inhibition","volume":"8","author":"Gavilan","year":"2009","journal-title":"Aging Cell"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1038\/s41419-022-05250-5","article-title":"Live and let die: Signaling AKTivation and UPRegulation dynamics in SARS-CoVs infection and cancer","volume":"13","author":"Suaya","year":"2022","journal-title":"Cell Death Dis."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1126\/science.1209038","article-title":"The unfolded protein response: From stress pathway to homeostatic regulation","volume":"334","author":"Walter","year":"2011","journal-title":"Science"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/nrm2199","article-title":"Signal integration in the endoplasmic reticulum unfolded protein response","volume":"8","author":"Ron","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1038\/nrm3270","article-title":"The unfolded protein response: Controlling cell fate decisions under ER stress and beyond","volume":"13","author":"Hetz","year":"2012","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/s41420-021-00518-9","article-title":"IRE1\u03b1 RIDD activity induced under ER stress drives neuronal death by the degradation of 14-3-3 \u03b8 mRNA in cortical neurons during glucose deprivation","volume":"7","author":"Massieu","year":"2021","journal-title":"Cell Death Discov."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"24217","DOI":"10.1038\/srep24217","article-title":"Novel mechanism of enhancing IRE1\u03b1-XBP1 signalling via the PERK-ATF4 pathway","volume":"6","author":"Tsuru","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1126\/science.1123480","article-title":"Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1\u03b1","volume":"312","author":"Hetz","year":"2006","journal-title":"Science"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Inoue, T., and Tsai, B. (2013). How viruses use the endoplasmic reticulum for entry, replication, and assembly. Cold Spring Harb. Perspect. Biol., 5.","DOI":"10.1101\/cshperspect.a013250"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"3147","DOI":"10.3389\/fimmu.2019.03147","article-title":"Insights into the Role of Endoplasmic Reticulum Stress in Infectious Diseases","volume":"10","author":"Choi","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"150","DOI":"10.3109\/1040841X.2013.813899","article-title":"The expanding roles of endoplasmic reticulum stress in virus replication and pathogenesis","volume":"41","author":"Li","year":"2015","journal-title":"Crit. Rev. Microbiol."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Prasad, V., and Greber, U.F. (2021). The endoplasmic reticulum unfolded protein response\u2014Homeostasis, cell death and evolution in virus infections. FEMS Microbiol. Rev., 45.","DOI":"10.1093\/femsre\/fuab016"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.1007\/s00415-020-10197-8","article-title":"Why do SARS-CoV-2 NSPs rush to the ER?","volume":"268","author":"Santerre","year":"2021","journal-title":"J. Neurol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"197820","DOI":"10.1016\/j.virusres.2019.197820","article-title":"Induction of the unfolded protein response (UPR) suppresses porcine reproductive and respiratory syndrome virus (PRRSV) replication","volume":"276","author":"Catanzaro","year":"2020","journal-title":"Virus Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"293","DOI":"10.3389\/fpls.2012.00293","article-title":"Virus-induced ER stress and the unfolded protein response","volume":"3","author":"Zhang","year":"2012","journal-title":"Front. Plant Sci."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Rios-Ocampo, W.A., Navas, M.C., Buist-Homan, M., Faber, K.N., Daemen, T., and Moshage, H. (2020). Hepatitis C Virus Proteins Core and NS5A Are Highly Sensitive to Oxidative Stress-Induced Degradation after eIF2\u03b1\/ATF4 Pathway Activation. Viruses, 12.","DOI":"10.3390\/v12040425"},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Kolpikova, E.P., Tronco, A.R., Hartigh, A.B.D., Jackson, K.J., Iwawaki, T., and Fink, S.L. (2020). IRE1\u03b1 Promotes Zika Virus Infection via XBP1. Viruses, 12.","DOI":"10.3390\/v12030278"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Johnston, B.P., and McCormick, C. (2019). Herpesviruses and the Unfolded Protein Response. Viruses, 12.","DOI":"10.20944\/preprints201912.0040.v1"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Fang, P., Tian, L., Zhang, H., Xia, S., Ding, T., Zhu, X., Zhang, J., Ren, J., Fang, L., and Xiao, S. (2022). Induction and modulation of the unfolded protein response during porcine deltacoronavirus infection. Vet. Microbiol., 271.","DOI":"10.1016\/j.vetmic.2022.109494"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"117842","DOI":"10.1016\/j.lfs.2020.117842","article-title":"Crosstalk between endoplasmic reticulum stress and anti-viral activities: A novel therapeutic target for COVID-19","volume":"255","author":"Banerjee","year":"2020","journal-title":"Life Sci."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Yiang, G.T., Wu, C.C., Lu, C.L., Hu, W.C., Tsai, Y.J., Huang, Y.M., Su, W.L., and Lu, K.C. (2023). Endoplasmic Reticulum Stress in Elderly Patients with COVID-19: Potential of Melatonin Treatment. Viruses, 15.","DOI":"10.3390\/v15010156"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"e0001123","DOI":"10.1128\/jvi.00011-23","article-title":"SARS-CoV-2 ORF8 Protein Induces Endoplasmic Reticulum Stress-like Responses and Facilitates Virus Replication by Triggering Calnexin: An Unbiased Study","volume":"97","author":"Wang","year":"2023","journal-title":"J. Virol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/j.omtn.2021.12.034","article-title":"SARS-CoV-2 causes a significant stress response mediated by small RNAs in the blood of COVID-19 patients","volume":"27","author":"Liu","year":"2022","journal-title":"Mol. Ther. Nucleic Acids"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/iub.2537","article-title":"Endoplasmic reticulum stress and NF-kB activation in SARS-CoV-2 infected cells and their response to antiviral therapy","volume":"74","author":"Bartolini","year":"2022","journal-title":"IUBMB Life"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Chaudhry, Z.L., Gamal, M., Ferhati, I., Warda, M., and Ahmed, B.Y. (2022). ER Stress in COVID-19 and Parkinson\u2019s Disease: In Vitro and In Silico Evidences. Brain Sci., 12.","DOI":"10.3390\/brainsci12040507"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Echavarria-Consuegra, L., Cook, G.M., Busnadiego, I., Lefevre, C., Keep, S., Brown, K., Doyle, N., Dowgier, G., Franaszek, K., and Moore, N.A. (2021). Manipulation of the unfolded protein response: A pharmacological strategy against coronavirus infection. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009644"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"198350","DOI":"10.1016\/j.virusres.2021.198350","article-title":"The ORF8 protein of SARS-CoV-2 induced endoplasmic reticulum stress and mediated immune evasion by antagonizing production of interferon beta","volume":"296","author":"Rashid","year":"2021","journal-title":"Virus Res."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Su, W.Q., Yu, X.J., and Zhou, C.M. (2021). SARS-CoV-2 ORF3a Induces Incomplete Autophagy via the Unfolded Protein Response. Viruses, 13.","DOI":"10.3390\/v13122467"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Xue, M., and Feng, L. (2021). The Role of Unfolded Protein Response in Coronavirus Infection and Its Implications for Drug Design. Front. Microbiol., 12.","DOI":"10.3389\/fmicb.2021.808593"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Rozpedek-Kaminska, W., Siwecka, N., Wawrzynkiewicz, A., Wojtczak, R., Pytel, D., Diehl, J.A., and Majsterek, I. (2020). The PERK-Dependent Molecular Mechanisms as a Novel Therapeutic Target for Neurodegenerative Diseases. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21062108"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"5536","DOI":"10.1038\/s41467-021-25551-1","article-title":"Multi-level inhibition of coronavirus replication by chemical ER stress","volume":"12","author":"Shaban","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1038\/nrm2546","article-title":"One step at a time: Endoplasmic reticulum-associated degradation","volume":"9","author":"Vembar","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"3658","DOI":"10.1016\/j.febslet.2007.04.070","article-title":"Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins","volume":"581","author":"Olivari","year":"2007","journal-title":"FEBS Lett."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/j.molcel.2015.06.010","article-title":"Pathogenic Hijacking of ER-Associated Degradation: Is ERAD Flexible?","volume":"59","author":"Morito","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1038\/s12276-023-00945-x","article-title":"ERdj5 protects goblet cells from endoplasmic reticulum stress-mediated apoptosis under inflammatory conditions","volume":"55","author":"Jeong","year":"2023","journal-title":"Exp. Mol. Med."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Lopata, A., Kniss, A., Lohr, F., Rogov, V.V., and Dotsch, V. (2020). Ubiquitination in the ERAD Process. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21155369"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.molcel.2016.09.014","article-title":"The K48-K63 Branched Ubiquitin Chain Regulates NF-\u03baB Signaling","volume":"64","author":"Ohtake","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1016\/j.cell.2017.04.023","article-title":"The Logic of the 26S Proteasome","volume":"169","author":"Collins","year":"2017","journal-title":"Cell"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2736","DOI":"10.1038\/s41467-022-30376-7","article-title":"Deubiquitinating enzymes and the proteasome regulate preferential sets of ubiquitin substrates","volume":"13","author":"Trulsson","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/j.neurobiolaging.2005.05.010","article-title":"Cellular environment facilitates protein accumulation in aged rat hippocampus","volume":"27","author":"Vela","year":"2006","journal-title":"Neurobiol. Aging"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.2217\/fmb-2021-0044","article-title":"Coronaviruses construct an interconnection way with ERAD and autophagy","volume":"16","author":"Movaqar","year":"2021","journal-title":"Future Microbiol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"10272","DOI":"10.1128\/JVI.00801-14","article-title":"How viruses hijack the ERAD tuning machinery","volume":"88","author":"Noack","year":"2014","journal-title":"J. Virol."},{"key":"ref_60","first-page":"187","article-title":"Ubiquitin-Proteasome System in Neurodegenerative Disorders","volume":"6","author":"Rao","year":"2015","journal-title":"J. Drug Metab. Toxicol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"70","DOI":"10.3389\/fnmol.2014.00070","article-title":"The ubiquitin-proteasome system in neurodegenerative diseases: Precipitating factor, yet part of the solution","volume":"7","author":"Dantuma","year":"2014","journal-title":"Front. Mol. Neurosci."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1038\/s41418-020-00706-7","article-title":"Ubiquitin signalling in neurodegeneration: Mechanisms and therapeutic opportunities","volume":"28","author":"Schmidt","year":"2021","journal-title":"Cell Death Differ."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"van Vliet, V.J.E., Huynh, N., Pala, J., Patel, A., Singer, A., Slater, C., Chung, J., van Huizen, M., Teyra, J., and Miersch, S. (2022). Ubiquitin variants potently inhibit SARS-CoV-2 PLpro and viral replication via a novel site distal to the protease active site. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1011065"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"3142","DOI":"10.1105\/tpc.109.072090","article-title":"The ubiquitin-proteasome system regulates the accumulation of Turnip yellow mosaic virus RNA-dependent RNA polymerase during viral infection","volume":"22","author":"Camborde","year":"2010","journal-title":"Plant Cell"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"3410","DOI":"10.1016\/j.cell.2021.04.047","article-title":"TRIM7 inhibits enterovirus replication and promotes emergence of a viral variant with increased pathogenicity","volume":"184","author":"Fan","year":"2021","journal-title":"Cell"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.lfs.2018.06.014","article-title":"Pleiotropic roles of the ubiquitin-proteasome system during viral propagation","volume":"207","author":"Tang","year":"2018","journal-title":"Life Sci."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1186\/s12985-019-1183-z","article-title":"The interaction of hepatitis B virus with the ubiquitin proteasome system in viral replication and associated pathogenesis","volume":"16","author":"Kong","year":"2019","journal-title":"Virol. J."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1002\/rmv.1725","article-title":"The ubiquitin-proteasome system in positive-strand RNA virus infection","volume":"23","author":"Choi","year":"2013","journal-title":"Rev. Med. Virol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1038\/s41392-023-01335-5","article-title":"The E3 ligase RNF5 restricts SARS-CoV-2 replication by targeting its envelope protein for degradation","volume":"8","author":"Li","year":"2023","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"199191","DOI":"10.1016\/j.virusres.2023.199191","article-title":"Ubiquitin-protein ligase E3A (UBE3A) mediation of viral infection and human diseases","volume":"335","author":"Chaudhary","year":"2023","journal-title":"Virus Res."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Rojas, V.K., and Park, I.W. (2019). Role of the Ubiquitin Proteasome System (UPS) in the HIV-1 Life Cycle. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20122984"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Voss, M., Braun, V., Bredow, C., Kloetzel, P.M., and Beling, A. (2021). Coxsackievirus B3 Exploits the Ubiquitin-Proteasome System to Facilitate Viral Replication. Viruses, 13.","DOI":"10.3390\/v13071360"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Zhao, M., Zhang, M., Yang, Z., Zhou, Z., Huang, J., and Zhao, B. (2023). Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection. Front. Cell. Infect. Microbiol., 13.","DOI":"10.3389\/fcimb.2023.1217383"},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Zu, S., Li, C., Li, L., Deng, Y.Q., Chen, X., Luo, D., Ye, Q., Huang, Y.J., Li, X.F., and Zhang, R.R. (2022). TRIM22 suppresses Zika virus replication by targeting NS1 and NS3 for proteasomal degradation. Cell Biosci., 12.","DOI":"10.1186\/s13578-022-00872-w"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"197938","DOI":"10.1016\/j.virusres.2020.197938","article-title":"Ub to no good: How cytomegaloviruses exploit the ubiquitin proteasome system","volume":"281","author":"Trilling","year":"2020","journal-title":"Virus Res."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1016\/j.micpath.2019.04.044","article-title":"The ubiquitin-proteasome system is necessary for the replication of duck Tembusu virus","volume":"132","author":"Han","year":"2019","journal-title":"Microb. Pathog."},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Pang, Y., Li, M., Zhou, Y., Liu, W., Tao, R., Zhang, H., Xiao, S., and Fang, L. (2021). The ubiquitin proteasome system is necessary for efficient proliferation of porcine reproductive and respiratory syndrome virus. Vet. Microbiol., 253.","DOI":"10.1016\/j.vetmic.2020.108947"},{"key":"ref_78","first-page":"6698069","article-title":"The Role of Ubiquitin-Proteasome System in the Pathogenesis of Severe Acute Respiratory Syndrome Coronavirus-2 Disease","volume":"2023","year":"2023","journal-title":"Int. J. Inflam."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Gao, W., Wang, L., Ju, X., Zhao, S., Li, Z., Su, M., Xu, J., Wang, P., Ding, Q., and Lv, G. (2022). The Deubiquitinase USP29 Promotes SARS-CoV-2 Virulence by Preventing Proteasome Degradation of ORF9b. mBio, 13.","DOI":"10.1128\/mbio.01300-22"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1080\/15548627.2021.2002101","article-title":"Inhibition of USP14 influences alphaherpesvirus proliferation by degrading viral VP16 protein via ER stress-triggered selective autophagy","volume":"18","author":"Ming","year":"2022","journal-title":"Autophagy"},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Schneider, S.M., Lee, B.H., and Nicola, A.V. (2021). Viral entry and the ubiquitin-proteasome system. Cell Microbiol., 23.","DOI":"10.1111\/cmi.13276"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.coviro.2015.09.005","article-title":"Interplay between the virus and the ubiquitin-proteasome system: Molecular mechanism of viral pathogenesis","volume":"17","author":"Luo","year":"2016","journal-title":"Curr. Opin. Virol."},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Dubiella, U., and Serrano, I. (2021). The Ubiquitin Proteasome System as a Double Agent in Plant-Virus Interactions. Plants, 10.","DOI":"10.3390\/plants10050928"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1104\/pp.112.201905","article-title":"Ubiquitin and plant viruses, let\u2019s play together!","volume":"160","author":"Jupin","year":"2012","journal-title":"Plant Physiol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1139\/y05-144","article-title":"The ubiquitin-proteasome pathway in viral infections","volume":"84","author":"Gao","year":"2006","journal-title":"Can. J. Physiol. Pharmacol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/j.chom.2009.05.012","article-title":"Ubiquitination, ubiquitin-like modifiers, and deubiquitination in viral infection","volume":"5","author":"Isaacson","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"McCarthy, M.K., and Weinberg, J.B. (2015). The immunoproteasome and viral infection: A complex regulator of inflammation. Front. Microbiol., 6.","DOI":"10.3389\/fmicb.2015.00021"},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Cetin, G., Klafack, S., Studencka-Turski, M., Kruger, E., and Ebstein, F. (2021). The Ubiquitin-Proteasome System in Immune Cells. Biomolecules, 11.","DOI":"10.3390\/biom11010060"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"102310","DOI":"10.1016\/j.coph.2022.102310","article-title":"Ubiquitin proteasome system in immune regulation and therapeutics","volume":"67","author":"Bhat","year":"2022","journal-title":"Curr. Opin. Pharmacol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1038\/nri888","article-title":"Viruses and interferon: A fight for supremacy","volume":"2","author":"Katze","year":"2002","journal-title":"Nat. Rev. Immunol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"e112907","DOI":"10.15252\/embj.2022112907","article-title":"Viral recognition and the antiviral interferon response","volume":"42","author":"Dalskov","year":"2023","journal-title":"EMBO J."},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Zou, L., Wang, X., Zhao, F., Wu, K., Li, X., Li, Z., Li, Y., Chen, W., Zeng, S., and Liu, X. (2022). Viruses Hijack ERAD to Regulate Their Replication and Propagation. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23169398"},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Magadan, J.G., Perez-Victoria, F.J., Sougrat, R., Ye, Y., Strebel, K., and Bonifacino, J.S. (2010). Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000869"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.molimm.2015.07.005","article-title":"Identifying the ERAD ubiquitin E3 ligases for viral and cellular targeting of MHC class I","volume":"68","author":"Lehner","year":"2015","journal-title":"Mol. Immunol."},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Lazar, C., Macovei, A., Petrescu, S., and Branza-Nichita, N. (2012). Activation of ERAD pathway by human hepatitis B virus modulates viral and subviral particle production. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0034169"},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Park, E.S., Dezhbord, M., Lee, A.R., and Kim, K.H. (2022). The Roles of Ubiquitination in Pathogenesis of Influenza Virus Infection. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23094593"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1016\/j.bpj.2016.02.006","article-title":"How Viruses Invade Cells","volume":"110","author":"Cohen","year":"2016","journal-title":"Biophys. J."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1038\/s41564-020-0750-9","article-title":"Adenovirus-mediated ubiquitination alters protein-RNA binding and aids viral RNA processing","volume":"5","author":"Herrmann","year":"2020","journal-title":"Nat. Microbiol."},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Cai, D., Liu, L., Tian, B., Fu, X., Yang, Q., Chen, J., Zhang, Y., Fang, J., Shen, L., and Wang, Y. (2022). Dual-Role Ubiquitination Regulation Shuttling the Entire Life Cycle of the Flaviviridae. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.835344"},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Valerdi, K.M., Hage, A., van Tol, S., Rajsbaum, R., and Giraldo, M.I. (2021). The Role of the Host Ubiquitin System in Promoting Replication of Emergent Viruses. Viruses, 13.","DOI":"10.3390\/v13030369"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1007\/s13365-021-00995-9","article-title":"Viruses, SUMO, and immunity: The interplay between viruses and the host SUMOylation system","volume":"27","author":"Imbert","year":"2021","journal-title":"J. Neurovirol."},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Zhang, Q., Jia, Q., Gao, W., and Zhang, W. (2022). The Role of Deubiquitinases in Virus Replication and Host Innate Immune Response. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.839624"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"3441","DOI":"10.1016\/j.jmb.2017.06.010","article-title":"Structure and Function of Viral Deubiquitinating Enzymes","volume":"429","author":"Knaap","year":"2017","journal-title":"J. Mol. Biol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"7869","DOI":"10.1128\/JVI.00485-10","article-title":"The ubiquitin-proteasome system plays an important role during various stages of the coronavirus infection cycle","volume":"84","author":"Raaben","year":"2010","journal-title":"J. Virol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"e1103","DOI":"10.1002\/ctm2.1103","article-title":"Elevated ubiquitination contributes to protective immunity against severe SARS-CoV-2 infection","volume":"12","author":"Che","year":"2022","journal-title":"Clin. Transl. Med."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"9802969","DOI":"10.34133\/2022\/9802969","article-title":"Heat Treatment Promotes Ubiquitin-Mediated Proteolysis of SARS-CoV-2 RNA Polymerase and Decreases Viral Load","volume":"2022","author":"Maimaitiyiming","year":"2022","journal-title":"Research"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1089\/vim.2022.0112","article-title":"New Avenues to Explore in SARS-CoV-2 Infection: Both TRIM25 and TRIM56 Positively Correlate with VEGF, GAS6, and sAXL in COVID-19 Patients","volume":"35","author":"Baskol","year":"2022","journal-title":"Viral Immunol."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Zhu, Y., Afolabi, L.O., Wan, X., Shim, J.S., and Chen, L. (2022). TRIM family proteins: Roles in proteostasis and neurodegenerative diseases. Open Biol., 12.","DOI":"10.1098\/rsob.220098"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"100134","DOI":"10.1016\/j.mcpro.2021.100134","article-title":"Proteomic Signature of Host Response to SARS-CoV-2 Infection in the Nasopharynx","volume":"20","author":"Vanderboom","year":"2021","journal-title":"Mol. Cell. Proteom."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1038\/s41392-022-01156-y","article-title":"Multiomics approach reveals the ubiquitination-specific processes hijacked by SARS-CoV-2","volume":"7","author":"Xu","year":"2022","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Longhitano, L., Tibullo, D., Giallongo, C., Lazzarino, G., Tartaglia, N., Galimberti, S., Li Volti, G., Palumbo, G.A., and Liso, A. (2020). Proteasome Inhibitors as a Possible Therapy for SARS-CoV-2. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21103622"},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Grosse, M., Setz, C., Rauch, P., Auth, J., Morokutti-Kurz, M., Temchura, V., and Schubert, U. (2022). Inhibitors of Deubiquitinating Enzymes Interfere with the SARS-CoV-2 Papain-like Protease and Block Virus Replication In Vitro. Viruses, 14.","DOI":"10.3390\/v14071404"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"100031","DOI":"10.1016\/j.cellin.2022.100031","article-title":"Endomembrane remodeling in SARS-CoV-2 infection","volume":"1","author":"Chen","year":"2022","journal-title":"Cell Insight"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Clemente, V., D\u2019Arcy, P., and Bazzaro, M. (2020). Deubiquitinating Enzymes in Coronaviruses and Possible Therapeutic Opportunities for COVID-19. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21103492"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.1021\/acsinfecdis.0c00168","article-title":"Characterization and Noncovalent Inhibition of the Deubiquitinase and deISGylase Activity of SARS-CoV-2 Papain-Like Protease","volume":"6","author":"Freitas","year":"2020","journal-title":"ACS Infect. Dis."},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Narayanan, A., Narwal, M., Majowicz, S.A., Varricchio, C., Toner, S.A., Ballatore, C., Brancale, A., Murakami, K.S., and Jose, J. (2022). Identification of SARS-CoV-2 inhibitors targeting Mpro and PLpro using in-cell-protease assay. Commun. Biol., 5.","DOI":"10.1038\/s42003-022-03090-9"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1038\/ncb0910-823","article-title":"Autophagy in mammalian development and differentiation","volume":"12","author":"Mizushima","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1089\/ars.2013.5371","article-title":"An overview of autophagy: Morphology, mechanism, and regulation","volume":"20","author":"Parzych","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"162.e1","DOI":"10.1016\/j.cell.2007.12.026","article-title":"SnapShot: Macroautophagy","volume":"132","author":"Levine","year":"2008","journal-title":"Cell"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1007\/s00018-011-0865-5","article-title":"Microautophagy: Lesser-known self-eating","volume":"69","author":"Li","year":"2012","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1513\/pats.200909-102JS","article-title":"Chaperone-mediated autophagy","volume":"7","author":"Bejarano","year":"2010","journal-title":"Proc. Am. Thorac. Soc."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/cr.2013.168","article-title":"The machinery of macroautophagy","volume":"24","author":"Feng","year":"2014","journal-title":"Cell Res."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/s41580-022-00529-z","article-title":"The emerging mechanisms and functions of microautophagy","volume":"24","author":"Wang","year":"2023","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/s41580-018-0001-6","article-title":"The coming of age of chaperone-mediated autophagy","volume":"19","author":"Kaushik","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1016\/j.neurobiolaging.2015.02.025","article-title":"Age-related dysfunctions of the autophagy lysosomal pathway in hippocampal pyramidal neurons under proteasome stress","volume":"36","author":"Gavilan","year":"2015","journal-title":"Neurobiol. Aging"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1021\/cb600182h","article-title":"Autophagy and neurodegeneration","volume":"1","author":"He","year":"2006","journal-title":"ACS Chem. Biol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1038\/s43587-021-00098-4","article-title":"Autophagy in healthy aging and disease","volume":"1","author":"Aman","year":"2021","journal-title":"Nat. Aging"},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Chen, T., Tu, S., Ding, L., Jin, M., Chen, H., and Zhou, H. (2023). The role of autophagy in viral infections. J. Biomed. Sci., 30.","DOI":"10.1186\/s12929-023-00899-2"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/978-981-15-0606-2_5","article-title":"Autophagy and Viral Infection","volume":"1209","author":"Mao","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_130","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_131","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1038\/nrd3802","article-title":"Autophagy modulation as a potential therapeutic target for diverse diseases","volume":"11","author":"Rubinsztein","year":"2012","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Liang, S., Wu, Y.S., Li, D.Y., Tang, J.X., and Liu, H.F. (2021). Autophagy in Viral Infection and Pathogenesis. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.766142"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.chom.2010.01.007","article-title":"Autophagy protects against Sindbis virus infection of the central nervous system","volume":"7","author":"Orvedahl","year":"2010","journal-title":"Cell Host Microbe"},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Wu, Y., Zhou, T., Hu, J., Liu, Y., Jin, S., Wu, J., Guan, X., and Cui, J. (2022). Autophagy Activation Induces p62-Dependent Autophagic Degradation of Dengue Virus Capsid Protein During Infection. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.889693"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1038\/nature21032","article-title":"PLA2G16 represents a switch between entry and clearance of Picornaviridae","volume":"541","author":"Staring","year":"2017","journal-title":"Nature"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/15548627.2018.1539585","article-title":"Inflammatory-dependent Sting activation induces antiviral autophagy to limit zika virus in the Drosophila brain","volume":"15","author":"Klionsky","year":"2019","journal-title":"Autophagy"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"e12978","DOI":"10.1111\/sji.12978","article-title":"Involvement of autophagy in MHC class I antigen presentation","volume":"92","author":"Oynebraten","year":"2020","journal-title":"Scand. J. Immunol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1016\/j.it.2016.08.017","article-title":"Autophagy Beyond Intracellular MHC Class II Antigen Presentation","volume":"37","author":"Munz","year":"2016","journal-title":"Trends Immunol."},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Tian, Y., Wang, M.L., and Zhao, J. (2019). Crosstalk between Autophagy and Type I Interferon Responses in Innate Antiviral Immunity. Viruses, 11.","DOI":"10.3390\/v11020132"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"153","DOI":"10.3390\/immuno2010012","article-title":"Autophagy in Virus Infection: A Race between Host Immune Response and Viral Antagonism","volume":"2","author":"Chawla","year":"2022","journal-title":"Immuno"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/j.chom.2009.09.006","article-title":"Autophagy induction by the pathogen receptor CD46","volume":"6","author":"Joubert","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Gregoire, I.P., Richetta, C., Meyniel-Schicklin, L., Borel, S., Pradezynski, F., Diaz, O., Deloire, A., Azocar, O., Baguet, J., and Le Breton, M. (2011). IRGM is a common target of RNA viruses that subvert the autophagy network. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002422"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.chom.2006.12.001","article-title":"HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein","volume":"1","author":"Orvedahl","year":"2007","journal-title":"Cell Host Microbe"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1080\/15548627.2015.1125071","article-title":"Analysis of the role of autophagy inhibition by two complementary human cytomegalovirus BECN1\/Beclin 1-binding proteins","volume":"12","author":"Mouna","year":"2016","journal-title":"Autophagy"},{"key":"ref_145","first-page":"401","article-title":"AKTivation of PI3K\/AKT\/mTOR signaling pathway by KSHV","volume":"3","author":"Bhatt","year":"2012","journal-title":"Front. Immunol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"10136","DOI":"10.1074\/jbc.M306124200","article-title":"Coronavirus replication complex formation utilizes components of cellular autophagy","volume":"279","author":"Prentice","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1128\/JVI.01890-17","article-title":"Glycine Zipper Motifs in Hepatitis C Virus Nonstructural Protein 4B Are Required for the Establishment of Viral Replication Organelles","volume":"92","author":"Paul","year":"2018","journal-title":"J. Virol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.chom.2009.09.005","article-title":"Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes","volume":"6","author":"Gannage","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/j.chom.2014.04.004","article-title":"Phosphoprotein of human parainfluenza virus type 3 blocks autophagosome-lysosome fusion to increase virus production","volume":"15","author":"Ding","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"32243","DOI":"10.1038\/srep32243","article-title":"Autophagy-associated dengue vesicles promote viral transmission avoiding antibody neutralization","volume":"6","author":"Wu","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/j.cell.2015.01.032","article-title":"Phosphatidylserine vesicles enable efficient en bloc transmission of enteroviruses","volume":"160","author":"Chen","year":"2015","journal-title":"Cell"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"5204","DOI":"10.1038\/s41467-022-32957-y","article-title":"Suppression of ACE2 SUMOylation protects against SARS-CoV-2 infection through TOLLIP-mediated selective autophagy","volume":"13","author":"Jin","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Li, F., Li, J., Wang, P.H., Yang, N., Huang, J., Ou, J., Xu, T., Zhao, X., Liu, T., and Huang, X. (2021). SARS-CoV-2 spike promotes inflammation and apoptosis through autophagy by ROS-suppressed PI3K\/AKT\/mTOR signaling. Biochim. Biophys. Acta Mol. Basis Dis., 1867.","DOI":"10.1016\/j.bbadis.2021.166260"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"110984","DOI":"10.1016\/j.mehy.2022.110984","article-title":"Autophagy: A self-guard against SARS-CoV-2","volume":"169","author":"Silva","year":"2022","journal-title":"Med. Hypotheses"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"3818","DOI":"10.1038\/s41467-021-24007-w","article-title":"SARS-CoV-2-mediated dysregulation of metabolism and autophagy uncovers host-targeting antivirals","volume":"12","author":"Gassen","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Rayner, J.O., Roberts, R.A., Kim, J., Poklepovic, A., Roberts, J.L., Booth, L., and Dent, P. (2020). AR12 (OSU-03012) suppresses GRP78 expression and inhibits SARS-CoV-2 replication. Biochem. Pharmacol., 182.","DOI":"10.1016\/j.bcp.2020.114227"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"eabi9007","DOI":"10.1126\/sciimmunol.abi9007","article-title":"Pharmacological activation of STING blocks SARS-CoV-2 infection","volume":"6","author":"Li","year":"2021","journal-title":"Sci. Immunol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"614599","DOI":"10.3389\/fimmu.2021.614599","article-title":"Reduced Expression of Autophagy Markers and Expansion of Myeloid-Derived Suppressor Cells Correlate with Poor T Cell Response in Severe COVID-19 Patients","volume":"12","author":"Tomic","year":"2021","journal-title":"Front. Immunol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"e0153721","DOI":"10.1128\/JVI.01537-21","article-title":"Inhibition of Autophagy Suppresses SARS-CoV-2 Replication and Ameliorates Pneumonia in hACE2 Transgenic Mice and Xenografted Human Lung Tissues","volume":"95","author":"Shang","year":"2021","journal-title":"J. Virol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"e0064321","DOI":"10.1128\/mSystems.00643-21","article-title":"RNA-Protein Interaction Analysis of SARS-CoV-2 5\u2019 and 3\u2019 Untranslated Regions Reveals a Role of Lysosome-Associated Membrane Protein-2a during Viral Infection","volume":"6","author":"Verma","year":"2021","journal-title":"mSystems"},{"key":"ref_161","doi-asserted-by":"crossref","unstructured":"Zhou, H., Hu, Z., and Castro-Gonzalez, S. (2023). Bidirectional interplay between SARS-CoV-2 and autophagy. mBio, 14.","DOI":"10.1128\/mbio.01020-23"},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Ivanova, T., Mariienko, Y., Mehterov, N., Kazakova, M., Sbirkov, Y., Todorova, K., Hayrabedyan, S., and Sarafian, V. (2023). Autophagy and SARS-CoV-2-Old Players in New Games. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24097734"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"112286","DOI":"10.1016\/j.celrep.2023.112286","article-title":"Coronavirus subverts ER-phagy by hijacking FAM134B and ATL3 into p62 condensates to facilitate viral replication","volume":"42","author":"Tan","year":"2023","journal-title":"Cell Rep."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1728","DOI":"10.1080\/15548627.2021.1989150","article-title":"The role of autophagy in the pathogenesis of SARS-CoV-2 infection in different cell types","volume":"18","author":"Samimi","year":"2022","journal-title":"Autophagy"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1038\/s41421-021-00268-z","article-title":"The SARS-CoV-2 protein ORF3a inhibits fusion of autophagosomes with lysosomes","volume":"7","author":"Zhang","year":"2021","journal-title":"Cell Discov."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"e2024202118","DOI":"10.1073\/pnas.2024202118","article-title":"The ORF8 protein of SARS-CoV-2 mediates immune evasion through down-regulating MHC-Iota","volume":"118","author":"Zhang","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1002\/cbin.11609","article-title":"The role of autophagy in controlling SARS-CoV-2 infection: An overview on virophagy-mediated molecular drug targets","volume":"45","author":"Sargazi","year":"2021","journal-title":"Cell Biol. Int."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"109126","DOI":"10.1016\/j.celrep.2021.109126","article-title":"Systematic functional analysis of SARS-CoV-2 proteins uncovers viral innate immune antagonists and remaining vulnerabilities","volume":"35","author":"Hayn","year":"2021","journal-title":"Cell Rep."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.vetmic.2019.07.005","article-title":"Porcine epidemic diarrhea virus ORF3 protein causes endoplasmic reticulum stress to facilitate autophagy","volume":"235","author":"Zou","year":"2019","journal-title":"Vet. Microbiol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.bbrc.2020.12.091","article-title":"The papain-like protease of coronaviruses cleaves ULK1 to disrupt host autophagy","volume":"540","author":"Mohamud","year":"2021","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"e24","DOI":"10.1016\/j.jinf.2020.03.058","article-title":"Evolutionary analysis of SARS-CoV-2: How mutation of Non-Structural Protein 6 (NSP6) could affect viral autophagy","volume":"81","author":"Benvenuto","year":"2020","journal-title":"J. Infect."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"1724","DOI":"10.7150\/ijbs.45498","article-title":"Targeting the Endocytic Pathway and Autophagy Process as a Novel Therapeutic Strategy in COVID-19","volume":"16","author":"Yang","year":"2020","journal-title":"Int. J. Biol. Sci."},{"key":"ref_173","doi-asserted-by":"crossref","unstructured":"Liang, H., Luo, D., Liao, H., and Li, S. (2022). Coronavirus Usurps the Autophagy-Lysosome Pathway and Induces Membranes Rearrangement for Infection and Pathogenesis. Front. Microbiol., 13.","DOI":"10.3389\/fmicb.2022.846543"},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Qu, Y., Wang, X., Zhu, Y., Wang, W., Wang, Y., Hu, G., Liu, C., Li, J., Ren, S., and Xiao, M.Z.X. (2021). ORF3a-Mediated Incomplete Autophagy Facilitates Severe Acute Respiratory Syndrome Coronavirus-2 Replication. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.716208"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"2659","DOI":"10.1080\/15548627.2021.1953847","article-title":"Manipulation of autophagy by SARS-CoV-2 proteins","volume":"17","author":"Koepke","year":"2021","journal-title":"Autophagy"},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Wu, W., Luo, X., and Ren, M. (2021). Clearance or Hijack: Universal Interplay Mechanisms Between Viruses and Host Autophagy from Plants to Animals. Front. Cell. Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.786348"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1080\/15548627.2022.2084686","article-title":"The ORF7a protein of SARS-CoV-2 initiates autophagy and limits autophagosome-lysosome fusion via degradation of SNAP29 to promote virus replication","volume":"19","author":"Hou","year":"2023","journal-title":"Autophagy"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1038\/s41423-021-00807-4","article-title":"SARS-CoV-2 ORF10 suppresses the antiviral innate immune response by degrading MAVS through mitophagy","volume":"19","author":"Li","year":"2022","journal-title":"Cell. Mol. Immunol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"110161","DOI":"10.1016\/j.mehy.2020.110161","article-title":"Mitochondrial-targeted ubiquinone: A potential treatment for COVID-19","volume":"144","author":"Ouyang","year":"2020","journal-title":"Med. Hypotheses"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1038\/s41586-022-04421-w","article-title":"The cGAS-STING pathway drives type I IFN immunopathology in COVID-19","volume":"603","author":"Domizio","year":"2022","journal-title":"Nature"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"e28175","DOI":"10.1002\/jmv.28175","article-title":"SARS-CoV-2 ORF3a inhibits cGAS-STING-mediated autophagy flux and antiviral function","volume":"95","author":"Su","year":"2023","journal-title":"J. Med. Virol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"5174","DOI":"10.1002\/jmv.27965","article-title":"SARS-CoV-2 ORF10 antagonizes STING-dependent interferon activation and autophagy","volume":"94","author":"Han","year":"2022","journal-title":"J. Med. Virol."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.it.2021.12.005","article-title":"K63 ubiquitination in immune signaling","volume":"43","author":"Madiraju","year":"2022","journal-title":"Trends Immunol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1038\/s41392-021-00515-5","article-title":"Unique and complementary suppression of cGAS-STING and RNA sensing- triggered innate immune responses by SARS-CoV-2 proteins","volume":"6","author":"Rui","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1038\/nature10317","article-title":"Molecular chaperones in protein folding and proteostasis","volume":"475","author":"Hartl","year":"2011","journal-title":"Nature"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/s41556-022-01074-9","article-title":"Small heat shock proteins operate as molecular chaperones in the mitochondrial intermembrane space","volume":"25","author":"Adriaenssens","year":"2023","journal-title":"Nat. Cell Biol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/978-3-319-57379-3_20","article-title":"Molecular Chaperones in Neurodegenerative Diseases: A Short Review","volume":"987","author":"Bobori","year":"2017","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1101\/gad.1657108","article-title":"Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging","volume":"22","author":"Morimoto","year":"2008","journal-title":"Genes. Dev."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1007\/s12035-012-8325-2","article-title":"Molecular chaperones, alpha-synuclein, and neurodegeneration","volume":"47","author":"Witt","year":"2013","journal-title":"Mol. Neurobiol."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1080\/02656730500069955","article-title":"The role of heat shock proteins Hsp70 and Hsp27 in cellular protection of the central nervous system","volume":"21","author":"Franklin","year":"2005","journal-title":"Int. J. Hyperth."},{"key":"ref_191","doi-asserted-by":"crossref","unstructured":"Bohush, A., Bieganowski, P., and Filipek, A. (2019). Hsp90 and Its Co-Chaperones in Neurodegenerative Diseases. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20204976"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1007\/s12192-012-0352-4","article-title":"Loss of stress response as a consequence of viral infection: Implications for disease and therapy","volume":"17","author":"Hooper","year":"2012","journal-title":"Cell Stress Chaperones"},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Paladino, L., Vitale, A.M., Caruso Bavisotto, C., Conway de Macario, E., Cappello, F., Macario, A.J.L., and Gammazza, A.M. (2020). The Role of Molecular Chaperones in Virus Infection and Implications for Understanding and Treating COVID-19. J. Clin. Med., 9.","DOI":"10.3390\/jcm9113518"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1128\/JVI.00540-07","article-title":"Hsp40 facilitates nuclear import of the human immunodeficiency virus type 2 Vpx-mediated preintegration complex","volume":"82","author":"Cheng","year":"2008","journal-title":"J. Virol."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1089\/088282402760312296","article-title":"Role for heat shock proteins in the immune response to measles virus infection","volume":"15","author":"Oglesbee","year":"2002","journal-title":"Viral Immunol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/j.bbrc.2004.04.046","article-title":"Interaction of the hepatitis B virus X protein (HBx) with heat shock protein 60 enhances HBx-mediated apoptosis","volume":"318","author":"Tanaka","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.canlet.2009.02.003","article-title":"Interaction of hepatitis C virus core protein with Hsp60 triggers the production of reactive oxygen species and enhances TNF-\u03b1-mediated apoptosis","volume":"279","author":"Kang","year":"2009","journal-title":"Cancer Lett."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"947789","DOI":"10.3389\/fimmu.2022.947789","article-title":"Heat shock proteins and viral infection","volume":"13","author":"Zhang","year":"2022","journal-title":"Front. Immunol."},{"key":"ref_199","doi-asserted-by":"crossref","unstructured":"Wang, Z., Li, Y., Yang, X., Zhao, J., Cheng, Y., and Wang, J. (2020). Mechanism and Complex Roles of HSC70 in Viral Infections. Front. Microbiol., 11.","DOI":"10.3389\/fmicb.2020.01577"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1038\/sj.gt.3302160","article-title":"Secretory heat-shock protein as a dendritic cell-targeting molecule: A new strategy to enhance the potency of genetic vaccines","volume":"11","author":"Hauser","year":"2004","journal-title":"Gene Ther."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1159\/000480740","article-title":"DNAJB1\/HSP40 Suppresses Melanoma Differentiation-Associated Gene 5-Mitochondrial Antiviral Signaling Protein Function in Conjunction with HSP70","volume":"10","author":"Takashima","year":"2018","journal-title":"J. Innate Immun."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.vetmic.2017.04.031","article-title":"Down-regulating heat shock protein 27 is involved in porcine epidemic diarrhea virus escaping from host antiviral mechanism","volume":"205","author":"Sun","year":"2017","journal-title":"Vet. Microbiol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.fsi.2017.08.032","article-title":"The antiviral role of heat shock protein 27 against red spotted grouper nervous necrosis virus infection in sea perch","volume":"70","author":"Le","year":"2017","journal-title":"Fish. Shellfish. Immunol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1016\/j.jmb.2011.04.005","article-title":"Reciprocal regulation of human immunodeficiency virus-1 gene expression and replication by heat shock proteins 40 and 70","volume":"410","author":"Kumar","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"19063","DOI":"10.1038\/srep19063","article-title":"Human Heat shock protein 40 (Hsp40\/DnaJB1) promotes influenza A virus replication by assisting nuclear import of viral ribonucleoproteins","volume":"6","author":"Batra","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"39851","DOI":"10.1074\/jbc.M301618200","article-title":"Antisense oligodeoxynucleotides targeted against molecular chaperonin Hsp60 block human hepatitis B virus replication","volume":"278","author":"Park","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/s41392-020-00233-4","article-title":"Stress proteins: The biological functions in virus infection, present and challenges for target-based antiviral drug development","volume":"5","author":"Wan","year":"2020","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"4557","DOI":"10.1128\/JVI.79.8.4557-4567.2005","article-title":"Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells","volume":"79","author":"Medina","year":"2005","journal-title":"J. Virol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1002\/jmv.23248","article-title":"Characterization of putative Japanese encephalitis virus receptor molecules on microglial cells","volume":"84","author":"Thongtan","year":"2012","journal-title":"J. Med. Virol."},{"key":"ref_210","doi-asserted-by":"crossref","unstructured":"Lubkowska, A., Pluta, W., Stronska, A., and Lalko, A. (2021). Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22179366"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"5015","DOI":"10.1038\/sj.emboj.7601367","article-title":"Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90","volume":"25","author":"Okamoto","year":"2006","journal-title":"EMBO J."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/j.virol.2008.04.040","article-title":"Hsp90 inhibitors reduce influenza virus replication in cell culture","volume":"377","author":"Chase","year":"2008","journal-title":"Virology"},{"key":"ref_213","doi-asserted-by":"crossref","unstructured":"Aviner, R., and Frydman, J. (2020). Proteostasis in Viral Infection: Unfolding the Complex Virus-Chaperone Interplay. Cold Spring Harb. Perspect. Biol., 12.","DOI":"10.1101\/cshperspect.a034090"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"40041","DOI":"10.1074\/jbc.M508904200","article-title":"Heat shock protein 40 is necessary for human immunodeficiency virus-1 Nef-mediated enhancement of viral gene expression and replication","volume":"280","author":"Kumar","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1128\/JVI.05720-11","article-title":"Secretion modification region-derived peptide disrupts HIV-1 Nef\u2019s interaction with mortalin and blocks virus and Nef exosome release","volume":"86","author":"Shelton","year":"2012","journal-title":"J. Virol."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1038\/ncb2339","article-title":"BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol","volume":"13","author":"Geiger","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1038\/s41598-020-79803-z","article-title":"A functional interaction between GRP78 and Zika virus E protein","volume":"11","author":"Khongwichit","year":"2021","journal-title":"Sci. Rep."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"11709","DOI":"10.1074\/jbc.RA118.001897","article-title":"Middle East respiratory syndrome coronavirus and bat coronavirus HKU9 both can utilize GRP78 for attachment onto host cells","volume":"293","author":"Chu","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"411","DOI":"10.2217\/fvl-2022-0192","article-title":"Cs-GRP78 recognition site on dengue virus envelope protein: In silico perspective","volume":"18","author":"Elfiky","year":"2023","journal-title":"Future Virol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1128\/JVI.01881-07","article-title":"Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP\/GRP78, which is required for virion assembly","volume":"82","author":"Buchkovich","year":"2008","journal-title":"J. Virol."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"5368","DOI":"10.1128\/JVI.02751-07","article-title":"Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles","volume":"82","author":"Lopez","year":"2008","journal-title":"J. Virol."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"8691","DOI":"10.1128\/JVI.00813-10","article-title":"Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT","volume":"84","author":"Fislova","year":"2010","journal-title":"J. Virol."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1111\/1348-0421.12186","article-title":"The chaperonin CCT\u03b1 is required for efficient transcription and replication of rabies virus","volume":"58","author":"Zhang","year":"2014","journal-title":"Microbiol. Immunol."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1038\/s41564-018-0122-x","article-title":"The TRiC chaperonin controls reovirus replication through outer-capsid folding","volume":"3","author":"Knowlton","year":"2018","journal-title":"Nat. Microbiol."},{"key":"ref_225","doi-asserted-by":"crossref","unstructured":"Tahmaz, I., Shahmoradi Ghahe, S., and Topf, U. (2022). Prefoldin Function in Cellular Protein Homeostasis and Human Diseases. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.816214"},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"e2018127118","DOI":"10.1073\/pnas.2018127118","article-title":"Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC\/CCT chaperone network","volume":"118","author":"Knowlton","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.bbrc.2006.07.062","article-title":"Interaction of hepatitis C virus F protein with prefoldin 2 perturbs tubulin cytoskeleton organization","volume":"348","author":"Tsao","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.ymeth.2009.02.002","article-title":"Yeast two-hybrid detection of integrase-host factor interactions","volume":"47","author":"Rain","year":"2009","journal-title":"Methods"},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"2663","DOI":"10.1080\/22221751.2020.1850183","article-title":"Human coronavirus dependency on host heat shock protein 90 reveals an antiviral target","volume":"9","author":"Li","year":"2020","journal-title":"Emerg. Microbes Infect."},{"key":"ref_230","doi-asserted-by":"crossref","unstructured":"Zhao, Z., Xu, L.D., Zhang, F., Liang, Q.Z., Jiao, Y., Shi, F.S., He, B., Xu, P., and Huang, Y.W. (2023). Heat shock protein 90 facilitates SARS-CoV-2 structural protein-mediated virion assembly and promotes virus-induced pyroptosis. J. Biol. Chem., 299.","DOI":"10.1016\/j.jbc.2023.104668"},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"102151","DOI":"10.1016\/j.isci.2021.102151","article-title":"Transcriptomic profiling of SARS-CoV-2 infected human cell lines identifies HSP90 as target for COVID-19 therapy","volume":"24","author":"Wyler","year":"2021","journal-title":"iScience"},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"118781","DOI":"10.1016\/j.lfs.2020.118781","article-title":"High GRP78 levels in COVID-19 infection: A case-control study","volume":"265","author":"Sabirli","year":"2021","journal-title":"Life Sci."},{"key":"ref_233","doi-asserted-by":"crossref","unstructured":"Shin, J., Toyoda, S., Fukuhara, A., and Shimomura, I. (2022). GRP78, a Novel Host Factor for SARS-CoV-2: The Emerging Roles in COVID-19 Related to Metabolic Risk Factors. Biomedicines, 10.","DOI":"10.3390\/biomedicines10081995"},{"key":"ref_234","doi-asserted-by":"crossref","unstructured":"Carlos, A.J., Ha, D.P., Yeh, D.W., Van Krieken, R., Tseng, C.C., Zhang, P., Gill, P., Machida, K., and Lee, A.S. (2021). The chaperone GRP78 is a host auxiliary factor for SARS-CoV-2 and GRP78 depleting antibody blocks viral entry and infection. J. Biol. Chem., 296.","DOI":"10.1016\/j.jbc.2021.100759"},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"6551","DOI":"10.1038\/s41467-022-34065-3","article-title":"The stress-inducible ER chaperone GRP78\/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein","volume":"13","author":"Shin","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_236","doi-asserted-by":"crossref","unstructured":"Ha, D.P., Shin, W.J., Hernandez, J.C., Neamati, N., Dubeau, L., Machida, K., and Lee, A.S. (2023). GRP78 Inhibitor YUM70 Suppresses SARS-CoV-2 Viral Entry, Spike Protein Production and Ameliorates Lung Damage. Viruses, 15.","DOI":"10.3390\/v15051118"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1038\/s41392-021-00719-9","article-title":"SARS-CoV-2 crosses the blood-brain barrier accompanied with basement membrane disruption without tight junctions alteration","volume":"6","author":"Zhang","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1007\/s00401-021-02314-2","article-title":"The olfactory nerve is not a likely route to brain infection in COVID-19: A critical review of data from humans and animal models","volume":"141","author":"Butowt","year":"2021","journal-title":"Acta Neuropathol."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1038\/s41593-022-01242-y","article-title":"Full protection from SARS-CoV-2 brain infection and damage in susceptible transgenic mice conferred by MVA-CoV2-S vaccine candidate","volume":"26","author":"Villadiego","year":"2023","journal-title":"Nat. Neurosci."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"3704","DOI":"10.1021\/acschemneuro.0c00676","article-title":"Seeding Brain Protein Aggregation by SARS-CoV-2 as a Possible Long-Term Complication of COVID-19 Infection","volume":"11","author":"Tavassoly","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/s13024-022-00529-9","article-title":"The route of SARS-CoV-2 to brain infection: Have we been barking up the wrong tree?","volume":"17","author":"Butowt","year":"2022","journal-title":"Mol. Neurodegener."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1038\/s41392-022-01072-1","article-title":"SARS-CoV-2 infection and the brain: Direct evidence for brain changes in milder cases","volume":"7","author":"Sollmann","year":"2022","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"220","DOI":"10.3389\/fnins.2017.00220","article-title":"Endoplasmic Reticulum Malfunction in the Nervous System","volume":"11","author":"Jung","year":"2017","journal-title":"Front. Neurosci."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.1038\/s41467-020-15119-w","article-title":"Microglia clear neuron-released \u03b1-synuclein via selective autophagy and prevent neurodegeneration","volume":"11","author":"Choi","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"3566","DOI":"10.1080\/15548627.2021.1883880","article-title":"ATG5 in microglia does not contribute vitally to autoimmune neuroinflammation in mice","volume":"17","author":"Kotur","year":"2021","journal-title":"Autophagy"},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"13285","DOI":"10.1523\/JNEUROSCI.4393-08.2008","article-title":"Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons","volume":"28","author":"Tydlacka","year":"2008","journal-title":"J. Neurosci."},{"key":"ref_247","first-page":"695","article-title":"Selective Neuronal Death in Neurodegenerative Diseases: The Ongoing Mystery","volume":"92","author":"Subramaniam","year":"2019","journal-title":"Yale J. Biol. Med."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"8189","DOI":"10.1523\/JNEUROSCI.2218-08.2008","article-title":"Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies","volume":"28","author":"Bedford","year":"2008","journal-title":"J. Neurosci."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"315","DOI":"10.4161\/auto.2974","article-title":"Autophagy and neurodegeneration","volume":"2","author":"Komatsu","year":"2006","journal-title":"Autophagy"},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1038\/nature04724","article-title":"Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice","volume":"441","author":"Hara","year":"2006","journal-title":"Nature"},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1126\/science.abj8222","article-title":"Longitudinal analysis reveals high prevalence of Epstein-Barr virus associated with multiple sclerosis","volume":"375","author":"Bjornevik","year":"2022","journal-title":"Science"},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1007\/s13365-019-00732-3","article-title":"Does HIV infection contribute to increased beta-amyloid synthesis and plaque formation leading to neurodegeneration and Alzheimer\u2019s disease?","volume":"25","author":"Fulop","year":"2019","journal-title":"J. Neurovirol"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1007\/s12035-012-8320-7","article-title":"Infectious agents and neurodegeneration","volume":"46","author":"Marcocci","year":"2012","journal-title":"Mol. Neurobiol."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"2737","DOI":"10.1016\/j.neurobiolaging.2015.06.014","article-title":"Herpes simplex virus type 2 infection induces AD-like neurodegeneration markers in human neuroblastoma cells","volume":"36","author":"Kristen","year":"2015","journal-title":"Neurobiol. Aging"},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1186\/s13195-019-0552-6","article-title":"HHV-6A infection induces amyloid-beta expression and activation of microglial cells","volume":"11","author":"Bortolotti","year":"2019","journal-title":"Alzheimers Res. Ther."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1016\/j.neuron.2022.12.029","article-title":"Virus exposure and neurodegenerative disease risk across national biobanks","volume":"111","author":"Levine","year":"2023","journal-title":"Neuron"},{"key":"ref_257","doi-asserted-by":"crossref","unstructured":"Leblanc, P., and Vorberg, I.M. (2022). Viruses in neurodegenerative diseases: More than just suspects in crimes. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1010670"},{"key":"ref_258","doi-asserted-by":"crossref","unstructured":"Romeo, M.A., Gilardini Montani, M.S., Gaeta, A., D\u2019Orazi, G., Faggioni, A., and Cirone, M. (2020). HHV-6A infection dysregulates autophagy\/UPR interplay increasing beta amyloid production and tau phosphorylation in astrocytoma cells as well as in primary neurons, possible molecular mechanisms linking viral infection to Alzheimer\u2019s disease. Biochim. Biophys. Acta Mol. Basis Dis., 1866.","DOI":"10.1016\/j.bbadis.2019.165647"},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"6741","DOI":"10.1073\/pnas.1906466117","article-title":"Disruption of cellular proteostasis by H1N1 influenza A virus causes \u03b1-synuclein aggregation","volume":"117","author":"Marreiros","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"1553","DOI":"10.1007\/s12640-022-00542-2","article-title":"A Review of In Silico Research, SARS-CoV-2, and Neurodegeneration: Focus on Papain-Like Protease","volume":"40","author":"Rieder","year":"2022","journal-title":"Neurotox. Res."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"1105247","DOI":"10.3389\/fncel.2023.1105247","article-title":"The neuroprotective effects of targeting key factors of neuronal cell death in neurodegenerative diseases: The role of ER stress, oxidative stress, and neuroinflammation","volume":"17","author":"Karvandi","year":"2023","journal-title":"Front. Cell. Neurosci."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"2331","DOI":"10.1007\/s00415-020-10251-5","article-title":"Neurologic manifestations in 1760 COVID-19 patients admitted to Papa Giovanni XXIII Hospital, Bergamo, Italy","volume":"268","author":"Rifino","year":"2021","journal-title":"J Neurol"},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"1764","DOI":"10.1111\/ene.14277","article-title":"Does SARS-CoV-2 invade the brain? Translational lessons from animal models","volume":"27","author":"Natoli","year":"2020","journal-title":"Eur. J. Neurol."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"399","DOI":"10.3233\/JAD-220105","article-title":"COVID-19 and Neurodegenerative Diseases: Prion-Like Spread and Long-Term Consequences","volume":"88","author":"Baazaoui","year":"2022","journal-title":"J. Alzheimers Dis."},{"key":"ref_265","doi-asserted-by":"crossref","unstructured":"Krey, L., Huber, M.K., Hoglinger, G.U., and Wegner, F. (2021). Can SARS-CoV-2 Infection Lead to Neurodegeneration and Parkinson\u2019s Disease?. Brain Sci., 11.","DOI":"10.3390\/brainsci11121654"},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.bbrc.2021.03.100","article-title":"SARS-CoV-2 spike protein interactions with amyloidogenic proteins: Potential clues to neurodegeneration","volume":"554","author":"Idrees","year":"2021","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.3724\/abbs.2023085","article-title":"Oxidative stress and COVID-19-associated neuronal dysfunction: Mechanisms and therapeutic implications","volume":"55","author":"Bowen","year":"2023","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1007\/s00702-022-02500-w","article-title":"SARS-CoV-2 and neurodegenerative diseases: What we know and what we don\u2019t","volume":"129","author":"Lingor","year":"2022","journal-title":"J. Neural Transm."},{"key":"ref_269","doi-asserted-by":"crossref","unstructured":"Tonges, L., and Klebe, S. (2022). SARS-CoV-2, COVID-19 and Neurodegeneration. Brain Sci., 12.","DOI":"10.3390\/brainsci12070897"},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1111\/jnc.15736","article-title":"SARS-CoV-2, aging, and Post-COVID-19 neurodegeneration","volume":"165","author":"Strong","year":"2023","journal-title":"J. Neurochem."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"e04433","DOI":"10.1002\/ccr3.4433","article-title":"Can COVID-19 accelerate neurodegeneration?","volume":"9","author":"Salari","year":"2021","journal-title":"Clin. Case Rep."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"e106230","DOI":"10.15252\/embj.2020106230","article-title":"SARS-CoV-2 targets neurons of 3D human brain organoids","volume":"39","author":"Ramani","year":"2020","journal-title":"EMBO J."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"1875","DOI":"10.1007\/s12035-020-02266-w","article-title":"Brain Disease Network Analysis to Elucidate the Neurological Manifestations of COVID-19","volume":"58","author":"Prasad","year":"2021","journal-title":"Mol. Neurobiol."},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1002\/jmv.25915","article-title":"Central nervous system involvement by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2)","volume":"92","author":"Bryce","year":"2020","journal-title":"J. Med. Virol."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"378","DOI":"10.3389\/fnagi.2018.00378","article-title":"A Critical Role of Autophagy in Regulating Microglia Polarization in Neurodegeneration","volume":"10","author":"Jin","year":"2018","journal-title":"Front. Aging Neurosci."},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/B978-0-12-385114-7.00004-0","article-title":"Measuring ER stress and the unfolded protein response using mammalian tissue culture system","volume":"490","author":"Oslowski","year":"2011","journal-title":"Methods Enzymol."},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/1040841X.2023.2274840","article-title":"Modulation of endoplasmic reticulum stress response pathways by respiratory viruses","volume":"7","author":"Macauslane","year":"2023","journal-title":"Crit. Rev. Microbiol."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/s41419-023-06102-6","article-title":"Immune landscape and redox imbalance during neurological disorders in COVID-19","volume":"14","author":"Thakur","year":"2023","journal-title":"Cell Death Dis."},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.mito.2020.06.008","article-title":"Mitochondria and microbiota dysfunction in COVID-19 pathogenesis","volume":"54","author":"Saleh","year":"2020","journal-title":"Mitochondrion"},{"key":"ref_280","first-page":"e123302","article-title":"Oxidative Stress Derived from COVID-19 and Its Possible Association with the Development of Neurodegenerative Diseases","volume":"9","year":"2022","journal-title":"Arch. Neurosci."},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"5497046","DOI":"10.1155\/2020\/5497046","article-title":"Proteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative Stress","volume":"2020","author":"Hohn","year":"2020","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"1003721","DOI":"10.3389\/fnagi.2022.1003721","article-title":"Redox signaling and metabolism in Alzheimer\u2019s disease","volume":"14","author":"Holubiec","year":"2022","journal-title":"Front. Aging Neurosci."},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"108502","DOI":"10.1016\/j.intimp.2021.108502","article-title":"Oxidative stress and inflammatory markers in patients with COVID-19: Potential role of RAGE, HMGB1, GFAP and COX-2 in disease severity","volume":"104","author":"Passos","year":"2022","journal-title":"Int. Immunopharmacol."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/13\/2\/123\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T13:43:14Z","timestamp":1760103794000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/13\/2\/123"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,1,9]]},"references-count":283,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2024,1]]}},"alternative-id":["cells13020123"],"URL":"https:\/\/doi.org\/10.3390\/cells13020123","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,1,9]]}}}