{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T05:07:19Z","timestamp":1789016839195,"version":"build-2803163510"},"reference-count":110,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T00:00:00Z","timestamp":1788307200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001700","name":"Coalition of Universities for Research Excellence (CURE) Program","doi-asserted-by":"publisher","award":["JPMXP1323015488"],"award-info":[{"award-number":["JPMXP1323015488"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]},{"name":"University of Tokyo, Japan"},{"id":[{"id":"https:\/\/ror.org\/057zh3y96","id-type":"ROR","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100010034","name":"Walailak University, Thailand","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100010034","id-type":"DOI","asserted-by":"crossref"}]},{"id":[{"id":"https:\/\/ror.org\/04b69g067","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Mitochondria are essential organelles for cellular energy production and the regulation of diverse biological processes, including apoptosis, redox homeostasis, and intracellular signaling. Although mitochondrial reactive oxygen species (mtROS) act as critical mediators of these functions, the molecular mechanisms underlying mtROS regulation remain poorly understood. This review summarizes current insights into the role of heat shock protein 47 (HSP47) in mitochondrial oxidative stress and mtROS-mediated cellular responses. In addition to its classical function as an endoplasmic reticulum (ER) chaperone, HSP47 translocates to the mitochondria under oxidative stress conditions. This mitochondrial localization promotes mtROS production, thereby triggering apoptotic pathways and redox-sensitive signal transduction. Furthermore, we examine the mechanistic insights linking HSP47 to mitochondrial function and oxidative stress, highlighting their implications for cellular homeostasis and disease pathogenesis. Overall, these findings establish HSP47 as a novel regulator of mtROS generation, suggesting that the HSP47\u2013mtROS axis represents a promising therapeutic target for oxidative stress-related disorders and a potential role for exploring virus-induced cellular responses in future research.<\/jats:p>","DOI":"10.3390\/cells15171601","type":"journal-article","created":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T14:35:29Z","timestamp":1788359729000},"page":"1601","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["HSP47 in Mitochondria: Roles in Apoptosis, Signal Transduction, and Protein and Virus Transportation"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9161-8567","authenticated-orcid":false,"given":"Sirirat","family":"Surinkaew","sequence":"first","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"},{"name":"Research Excellence Center for Innovation and Health Products (RECIHP), School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1418-0677","authenticated-orcid":false,"given":"Noriko","family":"Hosoya","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Radiology, Center for Disease Biology and Integrative Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo 113-8655, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiromu","family":"Ito","sequence":"additional","affiliation":[{"name":"Department of Oncology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, Japan"},{"name":"Quantum RedOx Chemistry Team, Quantum Life Spin Group, Institute for Quantum Life Science (iQLS), National Institutes for Quantum Science and Technology (QST), 4-9-1 Anagawa, Chiba 263-8555, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroshi","family":"Abe","sequence":"additional","affiliation":[{"name":"Department of Oncology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9204-0664","authenticated-orcid":false,"given":"Ikuo","family":"Nakanishi","sequence":"additional","affiliation":[{"name":"Quantum RedOx Chemistry Team, Quantum Life Spin Group, Institute for Quantum Life Science (iQLS), National Institutes for Quantum Science and Technology (QST), 4-9-1 Anagawa, Chiba 263-8555, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8151-4067","authenticated-orcid":false,"given":"Ken-ichiro","family":"Matsumoto","sequence":"additional","affiliation":[{"name":"Quantitative RedOx Sensing Group, Department of Radiation Regulatory Science Research, Institute for Radiological Science (NIRS), National Institutes for Quantum Science and Technology (QST), 4-9-1 Anagawa, Chiba 263-8555, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Motoki","family":"Imai","sequence":"additional","affiliation":[{"name":"Department of Molecular Diagnostics, School of Allied Health Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 252-0373, Japan"},{"name":"Department of Applied Tumor Pathology, Graduate School of Medical Sciences, Kitasato University, Sagamihara 252-0374, Japan"},{"name":"Regenerative Medicine and Cell Design Research Facility, School of Allied Health Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 252-0373, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8781-2516","authenticated-orcid":false,"given":"Fumitaka","family":"Kawakami","sequence":"additional","affiliation":[{"name":"Regenerative Medicine and Cell Design Research Facility, School of Allied Health Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 252-0373, Japan"},{"name":"Department of Regulation Biochemistry, Graduate School of Medical Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 252-0373, Japan"},{"name":"Department of Health Administration, School of Allied Health Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 252-0373, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8264-1343","authenticated-orcid":false,"given":"Makoto","family":"Kubo","sequence":"additional","affiliation":[{"name":"Regenerative Medicine and Cell Design Research Facility, School of Allied Health Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 252-0373, Japan"},{"name":"Department of Environmental Microbiology, Graduate School of Medical Sciences, Kitasato University, 1-15-1 Kitasato, Minami-ku, Sagamihara 252-0373, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takafumi","family":"Ichikawa","sequence":"additional","affiliation":[{"name":"Regenerative Medicine and Cell Design Research Facility, School of Allied Health Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 252-0373, Japan"},{"name":"Department of Regulation Biochemistry, Graduate School of Medical Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 252-0373, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4445-2928","authenticated-orcid":false,"given":"Hiroshi","family":"Ichikawa","sequence":"additional","affiliation":[{"name":"Department of Medical Life Systems, Graduate School of Life and Medical Sciences, Doshishia University, Kyoto 610-0394, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2682-752X","authenticated-orcid":false,"given":"Yoshikazu","family":"Yonei","sequence":"additional","affiliation":[{"name":"Anti-Aging Medical Research Center and Glycation Stress Research Center, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto 610-0394, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hisashi J.","family":"Beppu","sequence":"additional","affiliation":[{"name":"Dr. Beppu\u2019s Oral Health Care & Anti-Aging Clinic, Iwakami Building 3F, 3-2-6 Nihonbashi, Chuo-ku, Tokyo 103-0027, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Junko","family":"Suka","sequence":"additional","affiliation":[{"name":"Department of Medical Technology and Science, Faculty of Health Science, Kyoto Tachibana University, 34 Yamada-cho Otake, Yamashina-ku, Kyoto 607-8175, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9202-1594","authenticated-orcid":false,"given":"Rachasak","family":"Boonhok","sequence":"additional","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"},{"name":"Research Excellence Center for Innovation and Health Products (RECIHP), School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Moragot","family":"Chatatikun","sequence":"additional","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"},{"name":"Research Excellence Center for Innovation and Health Products (RECIHP), School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3789-926X","authenticated-orcid":false,"given":"Suriyan","family":"Sukati","sequence":"additional","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"},{"name":"Hematology and Transfusion Science Research Center (HTSRC), School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5469-4827","authenticated-orcid":false,"given":"Nitita","family":"Piya-amornphan","sequence":"additional","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3551-4039","authenticated-orcid":false,"given":"Chadapa","family":"Rungruangbaiyok","sequence":"additional","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charupa","family":"Lektip","sequence":"additional","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Voravuth","family":"Somsak","sequence":"additional","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"},{"name":"Research Excellence Center for Innovation and Health Products (RECIHP), School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7320-4117","authenticated-orcid":false,"given":"Luksana","family":"Chaiswing","sequence":"additional","affiliation":[{"name":"Department of Toxicology and Cancer Biology, 454 Bosomworth HSRB, University of Kentucky College of Medicine, Lexington, KY 40536, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pradoldej","family":"Sompol","sequence":"additional","affiliation":[{"name":"Sanders-Brown Center on Aging, University of Kentucky College of Medicine, Lexington, KY 40536, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jun","family":"Urano","sequence":"additional","affiliation":[{"name":"Cellibre, San Diego, CA 92121, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8103-6659","authenticated-orcid":false,"given":"Meng Ling","family":"Moi","sequence":"additional","affiliation":[{"name":"School of International Health, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroshi","family":"Takayanagi","sequence":"additional","affiliation":[{"name":"Department of Immunology, Graduate School of Medicine and Faculty of Medicine, The University of Tokyo, Tokyo 113-8655, Japan"},{"name":"Department of Microbiology and Immunology, Institute for Immunological Sciences, Department of Orthopaedics, University of Rochester Medical Center, 601 Elmwood Avenue, Rochester, NY 14642, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroko P.","family":"Indo","sequence":"additional","affiliation":[{"name":"Department of Oncology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, Japan"},{"name":"Amanogawa Galactic Astronomy Research Center (AGARC), Graduate School of Sciences and Engineering, Kagoshima University, 1-21-40 Korimoto, Kagoshima 890-0065, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2842-0467","authenticated-orcid":false,"given":"Hideyuki J.","family":"Majima","sequence":"additional","affiliation":[{"name":"School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"},{"name":"Research Excellence Center for Innovation and Health Products (RECIHP), School of Allied Health Sciences, Walailak University, Nakhon Si Thammarat 80160, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,2]]},"reference":[{"key":"ref_1","unstructured":"Rafferty, J.P. (2026, June 06). Hadean Eon: The Formation of Earth (4.6 to 4.0 Billion Years Ago). Available online: https:\/\/earthhow.com\/hadean-eon\/."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1038\/s41586-019-1436-4","article-title":"Challenges in evidencing the earliest traces of life","volume":"572","author":"Javaux","year":"2019","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"e00008-17","DOI":"10.1128\/MMBR.00008-17","article-title":"The Physiology of Phagocytosis in the Context of Mitochondrial Origin","volume":"81","author":"Martin","year":"2017","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1038\/nature16876","article-title":"Mitochondria in the second act","volume":"531","author":"Ettema","year":"2016","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/s41586-018-0059-5","article-title":"Deep mitochondrial origin outside the sampled alphaproteobacteria","volume":"557","author":"Martijn","year":"2018","journal-title":"Nature"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"8217","DOI":"10.1074\/jbc.273.14.8217","article-title":"Prevention of Mitochondrial Injury by Manganese Superoxide Dismutase Reveals a Primary Mechanism for Alkaline-induced Cell Death","volume":"273","author":"Majima","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Majima, H.J., Indo, H., Tomita, K., Suenaga, S., Motoori, S., Kato, H., Yen, H.-C., and Ozawa, T. (2006). Intracellular Oxidative Stress Caused by Ionizing Radiation. Oxidative Stress, Disease and Cancer, World Scientific Publishing.","DOI":"10.1142\/9781860948046_0002"},{"key":"ref_8","first-page":"5382","article-title":"Overexpression of mitochondrial manganese superoxide dismutase protects against radiation-induced cell death in the human hepatocellular carcinoma cell line HLE","volume":"61","author":"Motoori","year":"2001","journal-title":"Cancer Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3164\/jcbn.14-42","article-title":"A mitochondrial superoxide theory for oxidative stress diseases and aging","volume":"56","author":"Indo","year":"2015","journal-title":"J. Clin. Biochem. Nutr."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Indo, H.P., Chatatikun, M., Nakanishi, I., Matsumoto, K.-I., Imai, M., Kawakami, F., Kubo, M., Abe, H., Ichikawa, H., and Yonei, Y. (2024). The Roles of Mitochondria in Human Being\u2019s Life and Aging. Biomolecules, 14.","DOI":"10.3390\/biom14101317"},{"key":"ref_11","unstructured":"Tuttle, R.H. (2026, June 06). Human Evolution. Available online: https:\/\/www.britannica.com\/science\/human-evolution."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/bs.mcb.2019.11.006","article-title":"Studying protein import into mitochondria","volume":"155","author":"Priesnitz","year":"2020","journal-title":"Methods Cell Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1093\/embo-reports\/kve249","article-title":"High-level mitochondriology at high altitude","volume":"2","author":"Lightowlers","year":"2001","journal-title":"Embo Rep."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2656","DOI":"10.1056\/NEJMra022567","article-title":"Mitochondrial Respiratory-Chain Diseases","volume":"348","author":"DiMauro","year":"2003","journal-title":"New Engl. J. Med."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/S0022-2836(02)01440-7","article-title":"Insertion of Hydrophobic Membrane Proteins into the Inner Mitochondrial Membrane\u2014A Guided Tour","volume":"326","author":"Rehling","year":"2003","journal-title":"J. Mol. Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1016\/j.molcel.2023.02.020","article-title":"Mitochondrial protein transport: Versatility of translocases and mechanisms","volume":"83","author":"Busch","year":"2023","journal-title":"Mol. Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1146\/annurev-biochem-060815-014352","article-title":"Mitochondrial Machineries for Protein Import and Assembly","volume":"86","author":"Wiedemann","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1146\/annurev.biochem.66.1.863","article-title":"PROTEIN IMPORT INTO MITOCHONDRIA","volume":"66","author":"Neupert","year":"1997","journal-title":"Annu. Rev. Biochem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1038\/sj.embor.embor937","article-title":"Finding the right organelle","volume":"4","author":"Rapaport","year":"2003","journal-title":"Embo Rep."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/S1357-2725(97)00032-0","article-title":"The mitochondrial processing peptidase","volume":"29","author":"Braun","year":"1997","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0167-4889(02)00265-3","article-title":"Mitochondrial processing peptidases","volume":"1592","author":"Gakh","year":"2002","journal-title":"Biochim. et Biophys. Acta (BBA)-Mol. Cell Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2802","DOI":"10.1016\/j.febslet.2007.03.004","article-title":"A dynamic machinery for import of mitochondrial precursor proteins","volume":"581","author":"Bohnert","year":"2007","journal-title":"FEBS Lett."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Bayne, A.N., Dong, J., Amiri, S., Farhan, S.M.K., and Trempe, J.-F. (2023). MTSviewer: A database to visualize mitochondrial targeting sequences, cleavage sites, and mutations on protein structures. PLoS ONE, 18.","DOI":"10.1371\/journal.pone.0284541"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Tadokoro, T., Ikeda, M., Ide, T., Deguchi, H., Ikeda, S., Okabe, K., Ishikita, A., Matsushima, S., Koumura, T., and Yamada, K.-I. (2020). Mitochondria-dependent ferroptosis plays a pivotal role in doxorubicin cardiotoxicity. JCI Insight, 5.","DOI":"10.1172\/jci.insight.132747"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1006\/bbrc.1996.1525","article-title":"Import into Mitochondria of Phospholipid Hydroperoxide Glutathione Peroxidase Requires a Leader Sequence","volume":"227","author":"Araia","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1093\/jb\/118.5.1061","article-title":"Molecular Cloning and Functional Expression of a cDNA for Rat Phospholipid Hydroperoxide Glutathione Peroxidase: 3\u2019-Untranslated Region of the Gene Is Necessary for Functional Expression","volume":"118","author":"Imai","year":"1995","journal-title":"J. Biochem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"120140","DOI":"10.1016\/j.bbamcr.2026.120140","article-title":"Signal peptide-directed proteins generated in the endoplasmic reticulum are secreted or degraded via the autophagic pathway","volume":"1873","author":"Kim","year":"2026","journal-title":"Biochim. et Biophys. Acta (BBA) Mol. Cell Res."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1126\/science.abl6459","article-title":"Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting","volume":"375","author":"Jomaa","year":"2022","journal-title":"Science"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1126\/science.adp0787","article-title":"Identification of a factor that accelerates substrate release from the signal recognition particle","volume":"386","author":"Wang","year":"2024","journal-title":"Science"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"a040535","DOI":"10.1101\/cshperspect.a040535","article-title":"Glycolysis","volume":"13","author":"Chandel","year":"2021","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_31","unstructured":"Cox, J.D., Wagman, D.D., and Medvedev, V.A. (1989). CODATA Key Values for Thermodynamics, Hemisphere Publishing Corp."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/s41392-025-02141-x","article-title":"Energy metabolism in health and diseases","volume":"10","author":"Liu","year":"2025","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1042\/bj1340707","article-title":"The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen","volume":"134","author":"Boveris","year":"1973","journal-title":"Biochem. J."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1042\/bj1800129","article-title":"NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH\u2013ubiquinone reductase preparation","volume":"180","author":"Takeshige","year":"1979","journal-title":"Biochem. J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1139\/o92-061","article-title":"An analysis of the role of coenzyme Q in free radical generation and as an antioxidant","volume":"70","author":"Beyer","year":"1992","journal-title":"Biochem. Cell Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1038\/scientificamerican0897-40","article-title":"Mitochondrial DNA in Aging and Disease","volume":"277","author":"Wallace","year":"1997","journal-title":"Sci. Am."},{"key":"ref_37","unstructured":"Mathews, C.K., van Holde, K., and Appling, D. (2013). Biochemistry, Pearson. [4th ed.]."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.mito.2006.11.026","article-title":"Evidence of ROS generation by mitochondria in cells with impaired electron transport chain and mitochondrial DNA damage","volume":"7","author":"Indo","year":"2007","journal-title":"Mitochondrion"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"6049","DOI":"10.1016\/S0021-9258(18)63504-5","article-title":"Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)","volume":"244","author":"McCord","year":"1969","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"4793","DOI":"10.1016\/S0021-9258(19)43735-6","article-title":"Mitochondrial superoxide simutase. Site of synthesis and intramitochondrial localiza-tion","volume":"248","author":"Weisiger","year":"1973","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/0891-5849(88)90110-4","article-title":"Isolation and characterization of superoxide dismutase: A personal history and tribute to Joe McCord and Irwin Fridovich","volume":"5","author":"Bannister","year":"1988","journal-title":"Free. Radic. Biol. Med."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1084\/jem.182.2.367","article-title":"Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death","volume":"182","author":"Zamzami","year":"1995","journal-title":"J. Exp. Med."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0092-8674(00)80085-9","article-title":"Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c","volume":"86","author":"Liu","year":"1996","journal-title":"Cell"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1126\/science.275.5303.1129","article-title":"Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked","volume":"275","author":"Yang","year":"1997","journal-title":"Science"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"4924","DOI":"10.1074\/jbc.274.8.4924","article-title":"Mitochondrial Phospholipid Hydroperoxide Glutathione Peroxidase Plays a Major Role in Preventing Oxidative Injury to Cells","volume":"274","author":"Arai","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/17135","article-title":"Molecular characterization of mitochondrial apoptosis-inducing factor","volume":"397","author":"Susin","year":"1999","journal-title":"Nature"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1084\/jem.189.2.381","article-title":"Mitochondrial Release of Caspase-2 and -9 during the Apoptotic Process","volume":"189","author":"Susin","year":"1999","journal-title":"J. Exp. Med."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"3842","DOI":"10.1128\/MCB.19.5.3842","article-title":"Mitochondrial Regulation of Cell Death: Mitochondria Are Essential for Procaspase 3-p21 Complex Formation To Resist Fas-Mediated Cell Death","volume":"19","author":"Suzuki","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Masuda, D., Nakanishi, I., Ohkubo, K., Ito, H., Matsumoto, K.-I., Ichikawa, H., Chatatikun, M., Klangbud, W.K., Kotepui, M., and Imai, M. (2024). Mitochondria Play Essential Roles in Intracellular Protection against Oxidative Stress\u2014Which Molecules among the ROS Generated in the Mitochondria Can Escape the Mitochondria and Contribute to Signal Activation in Cytosol?. Biomolecules, 14.","DOI":"10.3390\/biom14010128"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2608","DOI":"10.1016\/j.bbamem.2011.06.010","article-title":"Effect of membrane tension on the electric field and dipole potential of lipid bilayer membrane","volume":"1808","author":"Warshaviak","year":"2011","journal-title":"Biochim. et Biophys. Acta (BBA)-Biomembr."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"7385","DOI":"10.1021\/acs.jpcb.4c01634","article-title":"Quantifying Induced Dipole Effects in Small Molecule Permeation in a Model Phospholipid Bilayer","volume":"128","author":"Montgomery","year":"2024","journal-title":"J. Phys. Chem. B"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/0005-2736(84)90409-7","article-title":"Permeability of bilayer lipid membranes for superoxide (O2\u2212) radicals","volume":"778","author":"Ivanov","year":"1984","journal-title":"Biochim. et Biophys. Acta (BBA)-Biomembr."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"343","DOI":"10.3109\/10715769609088032","article-title":"Permeability of Nitric Oxide through Lipid Bilayer Membranes","volume":"24","author":"Subczynski","year":"1996","journal-title":"Free. Radic. Res."},{"key":"ref_54","unstructured":"Cooper, G.M. (2026, June 06). Structure of the Plasma Membrane, The Cell: A Molecular Approach, Available online: https:\/\/www.ncbi.nlm.nih.gov\/books\/NBK9898\/."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1016\/S0891-5849(02)00850-X","article-title":"Kinetics of the reactions of nitrogen dioxide with glutathione, cysteine, and uric acid at physiological pH","volume":"32","author":"Ford","year":"2002","journal-title":"Free. Radic. Biol. Med."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1007\/s10072-009-0090-2","article-title":"Blood levels of homocysteine, cysteine, glutathione, folic acid, and vitamin B12 in the acute phase of atherothrombotic stroke","volume":"30","author":"Salemi","year":"2009","journal-title":"Neurol. Sci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1093\/clinchem\/42.1.64","article-title":"Blood glutathione concentrations in a large-scale human study","volume":"42","author":"Richie","year":"1996","journal-title":"Clin. Chem."},{"key":"ref_58","unstructured":"Ignarro, L.J. (2010). Chapter 1\u2014Determinants of nitric oxide chemistry: Impact of cell signaling processes. Nitric Oxide, Academic Press. [2nd ed.]."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1080\/15216540051081010","article-title":"Oxidative Stress, Antioxidant Defenses, and Damage Removal, Repair, and Replacement Systems","volume":"50","author":"Davies","year":"2000","journal-title":"IUBMB Life"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Indo, H.P., Masuda, D., Sriburee, S., Ito, H., Nakanishi, I., Matsumoto, K.-I., Mankhetkorn, S., Chatatikun, M., Surinkaew, S., and Udomwech, L. (2023). Evidence of Nrf2\/Keap1 Signaling Regulation by Mitochondria-Generated Reactive Oxygen Species in RGK1 Cells. Biomolecules, 13.","DOI":"10.3390\/biom13030445"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1007\/164_2016_117","article-title":"Role of Mitochondrial Reactive Oxygen Species in the Activation of Cellular Signals, Molecules, and Function","volume":"240","author":"Indo","year":"2017","journal-title":"Pharmacol. Mitochondria"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/83158","article-title":"A critical role for NF-\u03baB in Gata3 expression and TH2 differentiation in allergic airway inflammation","volume":"2","author":"Das","year":"2001","journal-title":"Nat. Immunol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/cr.2010.178","article-title":"Crosstalk of reactive oxygen species and NF-kappa\u03baB signaling","volume":"21","author":"Morgan","year":"2011","journal-title":"Cell Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1016\/j.cellsig.2007.01.020","article-title":"TNF-\u03b1-induced NF-\u03baB\/RelA Ser276 phosphorylation and enhanceosome formation is mediated by an ROS-dependent PKAc pathway","volume":"19","author":"Jamaluddin","year":"2007","journal-title":"Cell. Signal."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"3984","DOI":"10.1016\/j.molimm.2008.06.012","article-title":"DNA-binding activity of NF-\u03baB and phosphorylation of p65 are induced by N-acetylcysteine through phosphatidylinositol (PI) 3-kinase","volume":"45","author":"Liu","year":"2008","journal-title":"Mol. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1212","DOI":"10.1182\/blood.V82.4.1212.1212","article-title":"Reactive oxygen intermediates activate NF-\u03baB in a tyrosine kinase-dependent mechanism and in combination with vanadate activate the p56lck and p59fyn tyrosine kinases in human lymphocytes","volume":"82","author":"Schieven","year":"1993","journal-title":"Blood"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"14214","DOI":"10.1074\/jbc.270.23.14214","article-title":"Induction and Stabilization of I\u03baB\u03b1 by Nitric Oxide Mediates Inhibition of NF-\u03baB","volume":"270","author":"Peng","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1096\/fasebj.13.10.1137","article-title":"Is NF-\u03baB the sensor of oxidative stress?","volume":"13","author":"Li","year":"1999","journal-title":"FASEB J."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S0006-2952(99)00296-8","article-title":"Oxidative stress and nuclear factor-\u03baB activation","volume":"59","author":"Bowie","year":"2000","journal-title":"Biochem. Pharmacol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/S0014-5793(02)02712-6","article-title":"Hydrogen peroxide activates I\u03baB kinases through phosphorylation of serine residues in the activation loops","volume":"519","author":"Kamata","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1016\/S0006-2952(00)00371-3","article-title":"Oxidative stress interference with the nuclear factor- \u03baB activation pathways","volume":"60","author":"Schoonbroodt","year":"2000","journal-title":"Biochem. Pharmacol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"24233","DOI":"10.1074\/jbc.M212389200","article-title":"Hydrogen Peroxide Activates NF-\u03baB through Tyrosine Phosphorylation of I\u03baB\u03b1 and Serine Phosphorylation of p65: Evidence for the involvement of I&kappa;B\u03b1 kinase and Syk protein-tyrosine kinase","volume":"278","author":"Takada","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1016\/j.bcp.2006.04.011","article-title":"NF-\u03baB activation by reactive oxygen species: Fifteen years later","volume":"72","author":"Gloire","year":"2006","journal-title":"Biochem. Pharmacol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2209","DOI":"10.1089\/ars.2009.2463","article-title":"Redox Regulation of Nuclear Post-Translational Modifications During NF-\u03baB Activation","volume":"11","author":"Gloire","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.bbrc.2007.12.123","article-title":"Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347","volume":"367","author":"Herscovitch","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"2133","DOI":"10.1074\/jbc.TM118.002812","article-title":"Roles of the endoplasmic reticulum\u2013resident, collagen-specific molecular chaperone Hsp47 in vertebrate cells and human disease","volume":"294","author":"Ito","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.semcdb.2003.09.020","article-title":"HSP47 as a collagen-specific molecular chaperone: Function and expression in normal mouse development","volume":"14","author":"Nagata","year":"2003","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/0167-4781(92)90498-O","article-title":"Cloning of a human collagen-binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins","volume":"1129","author":"Clarke","year":"1992","journal-title":"Biochim. et Biophys. Acta (BBA)-Gene Struct. Expr."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"34523","DOI":"10.1074\/jbc.274.49.34523","article-title":"Substrate Recognition of Collagen-specific Molecular Chaperone HSP47","volume":"274","author":"Koide","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"6178","DOI":"10.1074\/jbc.M106497200","article-title":"Xaa-Arg-Gly Triplets in the Collagen Triple Helix Are Dominant Binding Sites for the Molecular Chaperone HSP47","volume":"277","author":"Koide","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"11177","DOI":"10.1074\/jbc.M601369200","article-title":"Specific Recognition of the Collagen Triple Helix by Chaperone HSP47","volume":"281","author":"Koide","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"3767","DOI":"10.1016\/j.bmc.2010.04.054","article-title":"A structure\u2013activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47","volume":"18","author":"Nishikawa","year":"2010","journal-title":"Bioorganic Med. Chem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"13243","DOI":"10.1073\/pnas.1208072109","article-title":"Molecular basis for the action of the collagen-specific chaperone Hsp47\/SERPINH1 and its structure-specific client recognition","volume":"109","author":"Widmer","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Cai, H., Sasikumar, P., Little, G., Bihan, D., Hamaia, S.W., Zhou, A., Gibbins, J.M., and Farndale, R.W. (2021). Identification of HSP47 Binding Site on Native Collagen and Its Implications for the Development of HSP47 Inhibitors. Biomolecules, 11.","DOI":"10.3390\/biom11070983"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"108853","DOI":"10.1016\/j.abb.2021.108853","article-title":"Translocation of HSP47 and generation of mitochondrial reactive oxygen species in human neuroblastoma SK-N-SH cells following electron and X-ray irradiation","volume":"703","author":"Indo","year":"2021","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1080\/15548627.2021.1990515","article-title":"Newcastle disease virus degrades SIRT3 via PINK1-PRKN-dependent mitophagy to reprogram energy metabolism in infected cells","volume":"18","author":"Gong","year":"2021","journal-title":"Autophagy"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1002\/rmv.611","article-title":"Access of viral proteins to mitochondria via mitochondria-associated membranes","volume":"19","author":"Williamson","year":"2009","journal-title":"Rev. Med. Virol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.mito.2010.08.006","article-title":"Mitochondria and viruses","volume":"11","author":"Ohta","year":"2011","journal-title":"Mitochondrion"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/B978-0-12-394315-6.00006-4","article-title":"The family Narnaviridae: Simplest of RNA viruses","volume":"86","author":"Hillman","year":"2013","journal-title":"Adv. Virus Res."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"2153","DOI":"10.1007\/s00705-014-2012-8","article-title":"Three mitovirus strains infecting a single isolate of Fusarium circinatum are the first putative members of the family Narnaviridae detected in a fungus of the genus Fusarium","volume":"159","author":"Vainio","year":"2014","journal-title":"Arch. Virol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1007\/s00705-014-1999-1","article-title":"A unique mitovirus from Glomeromycota, the phylum of arbuscular mycorrhizal fungi","volume":"159","author":"Kitahara","year":"2014","journal-title":"Arch. Virol."},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Namgaladze, D., Khodzhaeva, V., and Br\u00fcne, B. (2019). ER-Mitochondria Communication in Cells of the Innate Immune System. Cells, 8.","DOI":"10.3390\/cells8091088"},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Elesela, S., and Lukacs, N.W. (2021). Role of Mitochondria in Viral Infections. Life, 11.","DOI":"10.3390\/life11030232"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"e0209621","DOI":"10.1128\/mbio.02096-21","article-title":"Mitochondria and Viral Infection: Advances and Emerging Battlefronts","volume":"13","author":"Sorouri","year":"2022","journal-title":"mBio"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/j.tim.2021.12.011","article-title":"Mitochondria-mediated oxidative stress during viral infection","volume":"30","author":"Foo","year":"2022","journal-title":"Trends Microbiol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"121271","DOI":"10.1016\/j.lfs.2022.121271","article-title":"Modulation of mitochondria by viral proteins","volume":"313","author":"Saxena","year":"2022","journal-title":"Life Sci."},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Purandare, N., Ghosalkar, E., Grossman, L.I., and Aras, S. (2023). Mitochondrial Oxidative Phosphorylation in Viral Infections. Viruses, 15.","DOI":"10.3390\/v15122380"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1038\/s44298-024-00057-x","article-title":"Flaviviruses manipulate mitochondrial processes to evade the innate immune response","volume":"2","author":"Boytz","year":"2024","journal-title":"npj Viruses"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1007\/s10571-024-01503-3","article-title":"Viruses and Mitochondrial Dysfunction in Neurodegeneration and Cognition: An Evolutionary Perspective","volume":"44","author":"Stefano","year":"2024","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Duan, X., Liu, R., Lan, W., and Liu, S. (2025). The Essential Role of Mitochondrial Dynamics in Viral Infections. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26051955"},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Noonong, K., Chatatikun, M., Surinkaew, S., Kotepui, M., Hossain, R., Bunluepuech, K., Noothong, C., Tedasen, A., Klangbud, W.K., and Imai, M. (2023). Mitochondrial oxidative stress, mitochondrial ROS storms in long COVID pathogenesis. Front. Immunol., 14.","DOI":"10.3389\/fimmu.2023.1275001"},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Shoraka, S., Samarasinghe, A.E., Ghaemi, A., and Mohebbi, S.R. (2023). Host mitochondria: More than an organelle in SARS-CoV-2 infection. Front. Cell. Infect. Microbiol., 13.","DOI":"10.3389\/fcimb.2023.1228275"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/s41392-024-01836-x","article-title":"SARS-CoV-2 aberrantly elevates mitochondrial bioenergetics to induce robust virus propagation","volume":"9","author":"Shin","year":"2024","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"e29886","DOI":"10.1002\/jmv.29886","article-title":"Long-term persistence of mitochondrial dysfunctions after viral infections and antiviral therapies: A review of mechanisms involved","volume":"96","author":"Gay","year":"2024","journal-title":"J. Med. Virol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1007\/s44194-024-00032-x","article-title":"Mitochondrial homeostasis: Shaping health and disease","volume":"3","author":"Li","year":"2024","journal-title":"Curr. Med."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Stancheva, V.G., and Sanyal, S. (2024). Positive-strand RNA virus replication organelles at a glance. J. Cell Sci., 137.","DOI":"10.1242\/jcs.262164"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"e0003521","DOI":"10.1128\/MMBR.00035-21","article-title":"Endoplasmic Reticulum Chaperones in Viral Infection: Therapeutic Perspectives","volume":"85","author":"Kohli","year":"2021","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_108","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_109","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1038\/ni.3558","article-title":"Regulation and function of the cGAS\u2013STING pathway of cytosolic DNA sensing","volume":"17","author":"Chen","year":"2016","journal-title":"Nat. Immunol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.immuni.2020.05.013","article-title":"Structures and Mechanisms in the cGAS-STING Innate Immunity Pathway","volume":"53","author":"Zhang","year":"2020","journal-title":"Immunity"}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/15\/17\/1601\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T04:16:33Z","timestamp":1789013793000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/15\/17\/1601"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,2]]},"references-count":110,"journal-issue":{"issue":"17","published-online":{"date-parts":[[2026,9]]}},"alternative-id":["cells15171601"],"URL":"https:\/\/doi.org\/10.3390\/cells15171601","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,2]]}}}