{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPeroxiredoxin‐II (commonly referred to as PRDX2) is a thiol‐specific peroxidase that plays a central role in cellular redox regulation by detoxifying hydrogen peroxide and other reactive oxygen species. Its enzymatic activity not only protects cells from oxidative damage but also modulates signal transduction cascades – for example, by locally regulating growth factor–mediated pathways such as those triggered by platelet‐derived growth factor. In several cell types, the inducible expression and post‐translational modifications of PRDX2 enable it to maintain redox homeostasis under both physiological and stress conditions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn red blood cells, PRDX2 is one of the most abundant cytosolic proteins, serving a critical role in neutralizing endogenous hydrogen peroxide produced during oxygen transport. By protecting hemoglobin from oxidative modification and aggregation, PRDX2 minimizes cellular damage and hemolysis. Its regulation—through mechanisms such as glutathionylation and interaction with reducing systems—ensures that erythrocytes cope with oxidative challenges, a function whose disruption leads to pathologies like hemolytic anemia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical antioxidant function, PRDX2 participates in the modulation of cell signaling pathways that control cellular proliferation, differentiation, and senescence. In various models, its deficiency has been linked to accelerated cellular aging via upregulation of Ras–ERK cascades, while maintenance of its activity is associated with suppression of pro‐inflammatory responses. Moreover, in the context of hematological malignancies, such as acute myeloid leukemia, modulating PRDX2 activity has been shown to influence differentiation outcomes, suggesting that its redox-regulatory function can impact oncogenic processes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA protective role for PRDX2 has also been documented in diverse tissues. In cardiovascular cells, diminished PRDX2 levels correlate with increased oxidative stress and cell death under ischemic conditions, while in neuronal and podocyte cells its activity sustains mitochondrial integrity and cell survival. Similarly, in reproductive tissues, PRDX2 modulates oocyte maturation and cumulus expansion, underscoring its importance in normal development. These findings illustrate that PRDX2 not only functions as an antioxidant but also as a crucial regulator of cell fate in tissues that are highly vulnerable to oxidative injury."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nEmerging evidence further reveals that PRDX2 has multifaceted roles in metabolic and developmental processes. In models of diet‐induced fatty liver and obesity, alterations in redox balance mediated by PRDX2 affect mitochondrial function and insulin sensitivity. In reproductive immunology, its regulated expression in uterine natural killer cells appears to contribute to maternal–fetal tolerance, whereas its dynamic post‐translational modifications (such as nitrosylation) influence stem cell differentiation and tissue remodeling. Moreover, reduced PRDX2 levels in vascular and skeletal tissues have been associated with pathological remodeling in atherosclerosis and impaired osteoblast differentiation, highlighting its relevance as a therapeutic target in conditions characterized by chronic oxidative stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "A Bast, G Wolf, I Oberbäumer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetologia (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00125-002-0846-1"}], "href": "https://doi.org/10.1007/s00125-002-0846-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12107731"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12107731"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Tae-Hoon Lee, Sun-Uk Kim, Seong-Lan Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2002-08-2548"}], "href": "https://doi.org/10.1182/blood-2002-08-2548"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12586629"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12586629"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Min Hee Choi, In Kyung Lee, Gyung Whan Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature03587"}], "href": "https://doi.org/10.1038/nature03587"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15902258"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15902258"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Robert M Johnson, Ye-Shih Ho, Dae-Yeul Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Free Radic Biol Med (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.freeradbiomed.2009.11.021"}], "href": "https://doi.org/10.1016/j.freeradbiomed.2009.11.021"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19969073"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19969073"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Alessandro Matte, Philip S Low, Franco Turrini, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Peroxiredoxin-2 expression is increased in beta-thalassemic mouse red cells but is displaced from the membrane as a marker of oxidative stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Free Radic Biol Med (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.freeradbiomed.2010.05.003"}], "href": "https://doi.org/10.1016/j.freeradbiomed.2010.05.003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20488244"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20488244"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Ying-Hao Han, Sun-Uk Kim, Tae-Ho Kwon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Peroxiredoxin II is essential for preventing hemolytic anemia from oxidative stress through maintaining hemoglobin stability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2012.08.113"}], "href": "https://doi.org/10.1016/j.bbrc.2012.08.113"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22960070"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22960070"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Alexander V Peskin, Paul E Pace, Jessica B Behring, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Glutathionylation of the Active Site Cysteines of Peroxiredoxin 2 and Recycling by Glutaredoxin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M115.692798"}], "href": "https://doi.org/10.1074/jbc.M115.692798"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26601956"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26601956"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Ying-Hao Han, Hyun-Sun Kim, Jin-Man Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibitory role of peroxiredoxin II (Prx II) on cellular senescence."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2005.07.049"}], "href": "https://doi.org/10.1016/j.febslet.2005.07.049"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16109412"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16109412"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Min-Hyuk Yoo, Xue-Ming Xu, Bradley A Carlson, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenicity of lung carcinoma cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.C600012200"}], "href": "https://doi.org/10.1074/jbc.C600012200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16565519"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16565519"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Ying-Hao Han, Jeong-Hoon Kwon, Dae-Yeul Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibitory effect of peroxiredoxin II (Prx II) on Ras-ERK-NFkappaB pathway in mouse embryonic fibroblast (MEF) senescence."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Free Radic Res (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/10715760600868552"}], "href": "https://doi.org/10.1080/10715760600868552"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17050172"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17050172"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Chul-Su Yang, Dong-Seok Lee, Chang-Hwa Song, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Roles of peroxiredoxin II in the regulation of proinflammatory responses to LPS and protection against endotoxin-induced lethal shock."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Exp Med (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1084/jem.20061849"}], "href": "https://doi.org/10.1084/jem.20061849"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17325201"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17325201"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Meidan Ying, Xuejing Shao, Hui Jing, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ubiquitin-dependent degradation of CDK2 drives the therapeutic differentiation of AML by targeting PRDX2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2017-10-813139"}], "href": "https://doi.org/10.1182/blood-2017-10-813139"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29720484"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29720484"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Joshua P Gray, Diane E Heck, Vladimir Mishin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Paraquat increases cyanide-insensitive respiration in murine lung epithelial cells by activating an NAD(P)H:paraquat oxidoreductase: identification of the enzyme as thioredoxin reductase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M611817200"}], "href": "https://doi.org/10.1074/jbc.M611817200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17229725"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17229725"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Michael Reinartz, Zhaoping Ding, Ulrich Flögel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nitrosative stress leads to protein glutathiolation, increased s-nitrosation, and up-regulation of peroxiredoxins in the heart."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M800126200"}], "href": "https://doi.org/10.1074/jbc.M800126200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18426799"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18426799"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Wen Zhao, Guo-Chang Fan, Zhi-Guo Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protection of peroxiredoxin II on oxidative stress-induced cardiomyocyte death and apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Basic Res Cardiol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00395-008-0764-6"}], "href": "https://doi.org/10.1007/s00395-008-0764-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19030911"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19030911"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Sun-Uk Kim, Mei-Hua Jin, Yoon Sik Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Peroxiredoxin II preserves cognitive function against age-linked hippocampal oxidative damage."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neurobiol Aging (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neurobiolaging.2009.05.017"}], "href": "https://doi.org/10.1016/j.neurobiolaging.2009.05.017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19577336"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19577336"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Hsiang-Hao Hsu, Sigrid Hoffmann, Giovana S Di Marco, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Downregulation of the antioxidant protein peroxiredoxin 2 contributes to angiotensin II-mediated podocyte apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Kidney Int (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ki.2011.250"}], "href": "https://doi.org/10.1038/ki.2011.250"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21814176"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21814176"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "E Nagababu, J G Mohanty, J S Friedman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of peroxiredoxin-2 in protecting RBCs from hydrogen peroxide-induced oxidative stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Free Radic Res (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3109/10715762.2012.756138"}], "href": "https://doi.org/10.3109/10715762.2012.756138"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23215741"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23215741"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Hee Yeon Won, Eun Jung Jang, Kihyun Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ablation of peroxiredoxin II attenuates experimental colitis by increasing FoxO1-induced Foxp3+ regulatory T cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.1203247"}], "href": "https://doi.org/10.4049/jimmunol.1203247"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24048895"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24048895"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Enrica Federti, Alessandro Matté, Alessandra Ghigo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Peroxiredoxin-2 plays a pivotal role as multimodal cytoprotector in the early phase of pulmonary hypertension."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Free Radic Biol Med (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.freeradbiomed.2017.08.004"}], "href": "https://doi.org/10.1016/j.freeradbiomed.2017.08.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28801243"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28801243"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "You-Jee Jang, Jin-Seon Kim, Pu-Reum Yun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Involvement of peroxiredoxin 2 in cumulus expansion and oocyte maturation in mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Reprod Fertil Dev (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1071/RD19310"}], "href": "https://doi.org/10.1071/RD19310"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32389179"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32389179"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "M Chiba, M Kubo, T Miura, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Localization of sense and antisense transcripts of Prdx2 gene in mouse tissues."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cytogenet Genome Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1159/000138889"}], "href": "https://doi.org/10.1159/000138889"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18758163"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18758163"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Sachin S Kunde, James R Roede, Miriam B Vos, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hepatic oxidative stress in fructose-induced fatty liver is not caused by sulfur amino acid insufficiency."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nutrients (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/nu3110987"}], "href": "https://doi.org/10.3390/nu3110987"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22254090"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22254090"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Tae-Ho Kwon, Ying-Hao Han, So Gun Hong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Reactive oxygen species mediated DNA damage is essential for abnormal erythropoiesis in peroxiredoxin II(-/-) mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2012.06.113"}], "href": "https://doi.org/10.1016/j.bbrc.2012.06.113"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22749995"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22749995"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Sun-Uk Kim, Young-Ho Park, Jin-Man Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dominant role of peroxiredoxin/JNK axis in stemness regulation during neurogenesis from embryonic stem cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Stem Cells (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/stem.1593"}], "href": "https://doi.org/10.1002/stem.1593"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24715692"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24715692"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Marc Pirson, Bernard Knoops "}, {"type": "b", "children": [{"type": "t", "text": "Expression of peroxiredoxins and thioredoxins in the mouse spinal cord during embryonic development."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Comp Neurol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/cne.23807"}], "href": "https://doi.org/10.1002/cne.23807"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25975898"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25975898"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Kohtaro Morita, Mikiko Tokoro, Yuki Hatanaka, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Peroxiredoxin as a functional endogenous antioxidant enzyme in pronuclei of mouse zygotes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Reprod Dev (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1262/jrd.2018-005"}], "href": "https://doi.org/10.1262/jrd.2018-005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29503398"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29503398"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Rina Kato, Masataka Hayashi, Toshihiro Aiuchi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Temporal and spatial changes of peroxiredoxin 2 levels in aortic media at very early stages of atherosclerotic lesion formation in apoE-knockout mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Free Radic Biol Med (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.freeradbiomed.2018.10.458"}], "href": "https://doi.org/10.1016/j.freeradbiomed.2018.10.458"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30395970"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30395970"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Mi Hye Kim, Jae Yeop Kim, Jung-Hak Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Peroxiredoxin 2 deficiency reduces white adipogenesis due to the excessive ROS generation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Biol Int (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/cbin.11417"}], "href": "https://doi.org/10.1002/cbin.11417"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32639620"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32639620"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Se-Jin Jeong, Min Ji Cho, Na Young Ko, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deficiency of peroxiredoxin 2 exacerbates angiotensin II-induced abdominal aortic aneurysm."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Mol Med (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s12276-020-00498-3"}], "href": "https://doi.org/10.1038/s12276-020-00498-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32929220"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32929220"}]}, {"type": "r", "ref": 31, "children": [{"type": "t", "text": "Gulzhakhan Sadvakassova, Kerstin Tiedemann, Kieran J D Steer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Active hematopoiesis triggers exosomal release of PRDX2 that promotes osteoclast formation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Physiol Rep (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.14814/phy2.14745"}], "href": "https://doi.org/10.14814/phy2.14745"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33587325"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33587325"}]}, {"type": "r", "ref": 32, "children": [{"type": "t", "text": "Tomokazu Nunoue, Satoshi Yamaguchi, Sanae Teshigawara, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Lgals9 deficiency ameliorates obesity by modulating redox state of PRDX2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-021-85080-1"}], "href": "https://doi.org/10.1038/s41598-021-85080-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33727589"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33727589"}]}, {"type": "r", "ref": 33, "children": [{"type": "t", "text": "Mei-Hua Jin, Nan-Nan Yu, Ying-Hua Jin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Peroxiredoxin II with dermal mesenchymal stem cells accelerates wound healing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Aging (Albany NY) (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/aging.202990"}], "href": "https://doi.org/10.18632/aging.202990"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34030134"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34030134"}]}, {"type": "r", "ref": 34, "children": [{"type": "t", "text": "Guo-Lin Xu, Xiao-Lin Ye, Manoj Kumar Vashisth, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Correlation between PRDX2 and spermatogenesis under oxidative stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2023.03.050"}], "href": "https://doi.org/10.1016/j.bbrc.2023.03.050"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36963350"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36963350"}]}, {"type": "r", "ref": 35, "children": [{"type": "t", "text": "Yang Du, Jinjin Wang, Jia Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Intracerebral hemorrhage-induced brain injury in mice: The role of peroxiredoxin 2-Toll-like receptor 4 inflammatory axis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "CNS Neurosci Ther (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/cns.14681"}], "href": "https://doi.org/10.1111/cns.14681"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38516845"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38516845"}]}]}]}