Reactive oxygen species (Apex, N.C.)最新文献

{"title":"Reactive Oxygen Species: Prospects in Plant Metabolism","authors":"","doi":"10.1007/978-981-19-9794-5","DOIUrl":"https://doi.org/10.1007/978-981-19-9794-5","url":null,"abstract":"","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":"60 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51125278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Conoidin A Abrogates Growth of Anchorage-Dependent and Anchorage-Independent SKOV3 Ovarian Cancer Cells","authors":"K. Borger, Kassidy M. Jungles, Marissa Z Powell, M. Sanchez, Calli A. Davison-Versagli","doi":"10.20455/ros.2022.r803","DOIUrl":"https://doi.org/10.20455/ros.2022.r803","url":null,"abstract":"Ovarian cancer is one of the leading causes of cancer death in the United States with only 49% of women surviving 5 years after initial diagnosis. Poor screening methods, chemoresistance, and its high metastatic capacity make this disease difficult to treat. Thus, improved treatment methodologies are necessary to improve survival rates and quality of life for ovarian cancer patients. Conoidin A is a water-soluble covalent inhibitor of peroxiredoxin 1 (PRDX1) and peroxiredoxin 2 (PRDX2). While its effects have been primarily studied on parasites, recent studies also begin to elucidate the impacts of conoidin A in other human health conditions, including anticancer effects. However, the anticancer effects and potential utility of conoidin A as a therapeutic, specifically in ovarian cancer, has yet to be investigated. Here, we report that conoidin A eliminates growth of anchorage-dependent and anchorage-independent SKOV3 cells. Furthermore, analyses of clinical samples show increased expression of PRDX1 and PRDX2 in ovarian cancerous tissue, which are the targets of conoidin A. These data identify conoidin A as a potential therapeutic for early and late-stage ovarian cancer and warrants further investigation.\u0000(First Online: December 31, 2022)","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44204706","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Is NADPH Critical to Maintain Redox Homeostasis in Hypoxia-Tolerant Naked Mole-Rat Brain?","authors":"Liam Eaton, M. Pamenter","doi":"10.20455/ros.2022.m801","DOIUrl":"https://doi.org/10.20455/ros.2022.m801","url":null,"abstract":"Nicotinamide adenine dinucleotide phosphate (NADPH) is a ubiquitous electron donor and a key reducing agent in numerous biochemical reactions. Among other important cellular roles, NADPH activity is central to the maintenance of redox homeostasis in eukaryotic cells. NADPH increases markedly during acute in vivo hypoxia in the brain of naked mole-rats, which are among the most hypoxia-tolerant mammals, and which do not exhibit imbalances in redox homeostasis or increased reactive oxygen species (ROS)-mediated damage during bouts of hypoxia-reoxygenation in brain. Conversely, NADPH does not increase in the brain of hypoxia-intolerant mice, which are prone to deleterious ROS bursts during perturbations in oxygen availability. Although the importance of NADPH in mediating ROS homeostasis has been demonstrated in the brain of other mammals, little is known about the source of NADPH changes in hypoxic naked mole-rat brain, nor about the mechanisms via which NADPH may provide neuroprotection in this species. Elucidating the underlying mechanisms that support the remarkably stable ROS profile in naked mole-rat brain may provide insight into novel mechanisms to ameliorate the deleterious impact of ROS bursts in the brains of hypoxia-intolerant mammals, such as occur during stroke and other diseases. In this review, we discuss what is known regarding the management of ROS and NADPH in naked mole-rat brain, examine potential cellular sources of NADPH that may underlie the large hypoxic increase in this molecule during acute hypoxic exposure, and propose experiments to advance our understanding of the role NADPH has in maintaining naked mole-rat brain redox balance.\u0000(First online: December 28, 2022)","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44800906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Do SNPs in Glutathione S-Transferase-Omega Allow Predictions of the Susceptibility of Vertebrates to SARS-CoV-2?","authors":"J. Hancock, D. Veal, T. Craig, Ros C. Rouse","doi":"10.20455/ros.2022.c805","DOIUrl":"https://doi.org/10.20455/ros.2022.c805","url":null,"abstract":"Infection with the SARS-Cov-2 virus causes COVID-19 in humans and is the cause of the pandemic around the world in 2020 and on. However, some animals have been found to be susceptible to the virus too. This has included the non-human primates, dogs, cats, and mustelids. Mink, and very recently hamsters and deer, have been shown to be able to contract the virus and pass it back to humans. However, which animals are susceptible to the virus has been very hard to predict. Many groups have looked at the sequence homology of the angiotensin converting enzyme 2 (ACE2), a receptor for the SARS-Cov-2 virus, across species, but this has had limited success. Similar work on other proteins such as transmembrane serine protease 2 (TMPRSS2), neuropilin-1, and furin have also been unfruitful. Recently, it has been suggested that single nucleotide polymorphisms (SNPs) in the glutathione S-transferase-omega (GSTO) genes of humans could alter viral susceptibility. Therefore, here, the presence of related sequences in vertebrates has been investigated. The SNPs in the GST-omega-1 (GSTO1) gene reported to increase COVID-19 in humans do not appear in the vertebrate species. However, the GST-omega-2 (GSTO2) SNP is represented in several vertebrate species known to have contracted the SAR-CoV-2 virus. Of course, animals may contain unknown SNPs at disruptive points in these genes too. In summary, GSTO1 genes are unlikely, at least at the moment, to be of value in predicting the susceptibility of an animal to the SARS-CoV-2 virus or disease progression, but a further study of the GST-omega-2 genes would be worthwhile. Therefore, more work on SARS-CoV-2 infections on vertebrates is recommended.\u0000(First Online: June 8, 2022)","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42459257","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Erythrocuprein, also Known as Superoxide Dismutase, Is a Hydroquinone Oxidase, and Imparts Resistance to Mitomycin C","authors":"P. Penketh","doi":"10.20455/ros.2022.c803","DOIUrl":"https://doi.org/10.20455/ros.2022.c803","url":null,"abstract":"The enzymatic function of superoxide dismutase (SOD) is proposed to be as a ubiquinol oxidase. The SOD activity of this protein is likely a consequence of the necessary dismutation of superoxide (O2˙ˉ), generated as an enzyme-bound intermediate during its normal activity. The relatively low specificity of this enzyme for hydroquinones allowed it to oxidize a wide range of hydroquinone substrates. The general hydroquinone oxidase activity of this enzyme would thus enable it to behave as a mammalian analogue to bacterial mitomycin C resistance protein (MCRA). This would account for its elevated activity in cells expressing resistance against mitomycin C, porfiromycin, and related analogues, since superoxide itself is relatively nontoxic.","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-05-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47263627","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Nrf2 Signaling in Viral Infections","authors":"E. Ros","doi":"10.20455/ros.2022.n.805","DOIUrl":"https://doi.org/10.20455/ros.2022.n.805","url":null,"abstract":"Nrf2 is a central regulator of cellular antioxidant and other cytoprotective genes. Several recent studies revealed a novel role for Nrf2 signaling in protecting against viral infections, including COVID-19. The findings from these studies pointed to a feasibility for treating viral infections, including COVID-19, via pharmacological activation of the Nrf2 signaling pathway.\u0000(First online: March 3, 2022)\u0000REFERENCES\u0000\u0000Itoh K, Chiba T, Takahashi S, Ishii T, Igarashi K, Katoh Y, et al. An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochem Biophys Res Commun 1997; 236(2):313–22. doi: https://dx.doi.org/10.1006/bbrc.1997.6943\u0000Yamamoto M, Kensler TW, Motohashi H. The KEAP1-NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis. Physiol Rev 2018; 98(3):1169–203. doi: https://dx.doi.org/10.1152/physrev.00023.2017\u0000Kobayashi EH, Suzuki T, Funayama R, Nagashima T, Hayashi M, Sekine H, et al. Nrf2 suppresses macrophage inflammatory response by blocking proinflammatory cytokine transcription. Nat Commun 2016; 7:11624. doi: https://dx.doi.org/10.1038/ncomms11624\u0000Rojo de la Vega M, Chapman E, Zhang DD. NRF2 and the hallmarks of cancer. Cancer Cell 2018; 34(1):21–43. doi: https://dx.doi.org/10.1016/j.ccell.2018.03.022\u0000Cho HY, Imani F, Miller-DeGraff L, Walters D, Melendi GA, Yamamoto M, et al. Antiviral activity of Nrf2 in a murine model of respiratory syncytial virus disease. Am J Respir Crit Care Med 2009; 179(2):138–50. doi: https://dx.doi.org/10.1164/rccm.200804-535OC\u0000Ferrari M, Zevini A, Palermo E, Muscolini M, Alexandridi M, Etna MP, et al. Dengue virus targets Nrf2 for NS2B3-mediated degradation leading to enhanced oxidative stress and viral replication. J Virol 2020; 94(24). doi: https://dx.doi.org/10.1128/JVI.01551-20\u0000Wyler E, Franke V, Menegatti J, Kocks C, Boltengagen A, Praktiknjo S, et al. Single-cell RNA-sequencing of herpes simplex virus 1-infected cells connects NRF2 activation to an antiviral program. Nat Commun 2019; 10(1):4878. doi: https://dx.doi.org/10.1038/s41467-019-12894-z\u0000Olagnier D, Farahani E, Thyrsted J, Blay-Cadanet J, Herengt A, Idorn M, et al. SARS-CoV2-mediated suppression of NRF2-signaling reveals potent antiviral and anti-inflammatory activity of 4-octyl-itaconate and dimethyl fumarate. Nat Commun 2020; 11(1):4938. doi: https://dx.doi.org/10.1038/s41467-020-18764-3\u0000","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44181483","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mitochondria as a Critical Target of COVID-19 Pathogenesis","authors":"E. Ros","doi":"10.20455/ros.2022.n.807","DOIUrl":"https://doi.org/10.20455/ros.2022.n.807","url":null,"abstract":"Over the past two years, findings from several research studies published in highly influential journals pointed to a critical involvement of mitochondria in the pathophysiology of SARS-CoV2 infections. Among the most exciting findings are the involvement of (i) the “mitochondrial ROS–HIF-1α –glycolysis” axis, (ii) the “cGAS–STING” signaling, and (iii) the “mitochondrial apoptotic cell death” pathway.\u0000(First online: March 3, 2022)\u0000REFERENCES                      \u0000\u0000Danial NN, Korsmeyer SJ. Cell death: critical control points. Cell 2004; 116(2):205–19. doi: https://dx.doi.org/10.1016/s0092-8674(04)00046-7\u0000Zorov DB, Juhaszova M, Sollott SJ. Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release. Physiol Rev 2014; 94(3):909–50. doi: https://dx.doi.org/10.1152/physrev.00026.2013\u0000Ros EO. Mitochondrial ROS take center stage in immune regulation. React Oxyg Species (Apex) 2021; 11:n9–n10. doi: https://dx.doi.org/10.20455/ros.2021.n.809\u0000Weinberg SE, Sena LA, Chandel NS. Mitochondria in the regulation of innate and adaptive immunity. Immunity 2015; 42(3):406–17. doi: https://dx.doi.org/10.1016/j.immuni.2015.02.002\u0000Codo AC, Davanzo GG, Monteiro LB, de Souza GF, Muraro SP, Virgilio-da-Silva JV, et al. Elevated glucose levels favor SARS-CoV-2 infection and monocyte response through a HIF-1alpha/glycolysis-dependent axis. Cell Metab 2020; 32(3):437–46 e5. doi: https://dx.doi.org/10.1016/j.cmet.2020.07.007\u0000Domizio JD, Gulen MF, Saidoune F, Thacker VV, Yatim A, Sharma K, et al. The cGAS-STING pathway drives type I IFN immunopathology in COVID-19. Nature 2022. doi: https://dx.doi.org/10.1038/s41586-022-04421-w\u0000Simpson DS, Pang J, Weir A, Kong IY, Fritsch M, Rashidi M, et al. Interferon-gamma primes macrophages for pathogen ligand-induced killing via a caspase-8 and mitochondrial cell death pathway. Immunity 2022. doi: https://dx.doi.org/10.1016/j.immuni.2022.01.003\u0000","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49400174","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ROS in 2022: New Focus, Same Mission","authors":"E. Ros","doi":"10.20455/ros.2022.e.801","DOIUrl":"https://doi.org/10.20455/ros.2022.e.801","url":null,"abstract":"This ROS Editorial brings to the reader’s attention a new focus of the Journal on disseminating cutting-edge research highlights and mini-review articles. The Journal also considers submissions on concise method protocols, insightful commentaries, and short-research communications.\u0000(First online: March 1, 2022)","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-03-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45073460","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Salt Promotes Inflammation: Mechanistic Insights","authors":"E. Ros","doi":"10.20455/ros.2022.n.801","DOIUrl":"https://doi.org/10.20455/ros.2022.n.801","url":null,"abstract":"It has been well established that high dietary salt intake promotes inflammation and contributes to the pathogenesis of many inflammatory disorders, especially cardiovascular diseases. Several recent studies published in prestigious journals have further elucidated the molecular pathways underlying high salt-induced inflammation, including identification of the involvement of mitochondrial electron transport chain and the Nrf2-SIRT3 signaling axis. These novel findings provide important mechanistic insights and offer potential opportunities for developing modalities for intervention of high salt-associated pathophysiological conditions.\u0000(First online: March 1, 2022)\u0000REFERENCES\u0000\u0000Thornton SN. Sodium intake, cardiovascular disease, and physiology. Nat Rev Cardiol 2018; 15(8):497. doi: https://dx.doi.org/10.1038/s41569-018-0047-3\u0000Cook NR, He FJ, MacGregor GA, Graudal N. Sodium and health-concordance and controversy. BMJ 2020; 369:m2440. doi: https://dx.doi.org/10.1136/bmj.m2440\u0000Wu C, Yosef N, Thalhamer T, Zhu C, Xiao S, Kishi Y, et al. Induction of pathogenic TH17 cells by inducible salt-sensing kinase SGK1. Nature 2013; 496(7446):513–7. doi: https://dx.doi.org/10.1038/nature11984\u0000Wilck N, Matus MG, Kearney SM, Olesen SW, Forslund K, Bartolomaeus H, et al. Salt-responsive gut commensal modulates TH17 axis and disease. Nature 2017; 551(7682):585–9. doi: https://dx.doi.org/10.1038/nature24628\u0000Zhang WC, Zheng XJ, Du LJ, Sun JY, Shen ZX, Shi C, et al. High salt primes a specific activation state of macrophages, M(Na). Cell Res 2015; 25(8):893–910. doi: https://dx.doi.org/10.1038/cr.2015.87\u0000Geisberger S, Bartolomaeus H, Neubert P, Willebrand R, Zasada C, Bartolomaeus T, et al. Salt Transiently inhibits mitochondrial energetics in mononuclear phagocytes. Circulation 2021; 144(2):144–58. doi: https://dx.doi.org/10.1161/CIRCULATIONAHA.120.052788\u0000Ros EO. Sodium ion regulates mitochondrial ROS. React Oxyg Species (Apex) 2021; 11:n5–n6. doi: https://dx.doi.org/10.20455/ros.2021.n.805.\u0000Shadel GS, Horvath TL. Mitochondrial ROS signaling in organismal homeostasis. Cell 2015; 163(3):560–9. doi: https://dx.doi.org/10.1016/j.cell.2015.10.001\u0000Lanaspa MA, Kuwabara M, Andres-Hernando A, Li N, Cicerchi C, Jensen T, et al. High salt intake causes leptin resistance and obesity in mice by stimulating endogenous fructose production and metabolism. Proc Natl Acad Sci USA 2018; 115(12):3138–43. doi: https://dx.doi.org/10.1073/pnas.1713837115\u0000Gao P, You M, Li L, Zhang Q, Fang X, Wei X, et al. Salt-Induced hepatic inflammatory memory contributes to cardiovascular damage through epigenetic modulation of SIRT3. Circulation 2022; 145(5):375–91. doi: https://dx.doi.org/10.1161/CIRCULATIONAHA.121.055600\u0000Dikalova AE, Pandey A, Xiao L, Arslanbaeva L, Sidorova T, Lopez MG, et al. Mitochondrial deacetylase Sirt3 reduces vascular dysfunction and hypertension while Sirt3 depletion in essential hypertension is linked to vascular inflammation and oxidative stress. Circ Res 2020; 126(4):439–5","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-03-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48904810","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Metformin Finds Its New Molecular Targets","authors":"E. Ros","doi":"10.20455/ros.2022.n.803","DOIUrl":"https://doi.org/10.20455/ros.2022.n.803","url":null,"abstract":"Metformin is a widely used antidiabetic drug. Studies over the past year have identified multiple novel molecular targets and pathways that metformin may act on to exert its beneficial effects in treating diabetes and potentially other disorders involving dysregulated inflammation. These newly found targets include mitochondrial complex I, Nrf2-SIRT3 signaling axis, PEN2, and lysosomal proton pump v-ATPase.\u0000(First online: March 1, 2022)\u0000REFERENCES\u0000\u0000Flory J, Lipska K. Metformin in 2019. JAMA 2019; 321(19):1926–7. doi: https://dx.doi.org/10.1001/jama.2019.3805\u0000Xian H, Liu Y, Rundberg Nilsson A, Gatchalian R, Crother TR, Tourtellotte WG, et al. Metformin inhibition of mitochondrial ATP and DNA synthesis abrogates NLRP3 inflammasome activation and pulmonary inflammation. Immunity 2021; 54(7):1463–77 e11. doi: https://dx.doi.org/10.1016/j.immuni.2021.05.004\u0000Madiraju AK, Erion DM, Rahimi Y, Zhang XM, Braddock DT, Albright RA, et al. Metformin suppresses gluconeogenesis by inhibiting mitochondrial glycerophosphate dehydrogenase. Nature 2014; 510(7506):542–6. doi: https://dx.doi.org/10.1038/nature13270\u0000Zhou G, Myers R, Li Y, Chen Y, Shen X, Fenyk-Melody J, et al. Role of AMP-activated protein kinase in mechanism of metformin action. J Clin Invest 2001; 108(8):1167–74. doi: https://dx.doi.org/10.1172/JCI13505\u0000Gao P, You M, Li L, Zhang Q, Fang X, Wei X, et al. Salt-Induced hepatic inflammatory memory contributes to cardiovascular damage through epigenetic modulation of SIRT3. Circulation 2022; 145(5):375–91. doi: https://dx.doi.org/10.1161/CIRCULATIONAHA.121.055600\u0000Ma T, Tian X, Zhang B, Li M, Wang Y, Yang C, et al. Low-dose metformin targets the lysosomal AMPK pathway through PEN2. Nature 2022. doi: https://dx.doi.org/10.1038/s41586-022-04431-8\u0000","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-03-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46107338","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}