{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T23:09:37Z","timestamp":1792192177107,"version":"4.4.0"},"reference-count":239,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2024,10,16]],"date-time":"2024-10-16T00:00:00Z","timestamp":1729036800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["MOP-111012"],"award-info":[{"award-number":["MOP-111012"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["RGPIN436250-13"],"award-info":[{"award-number":["RGPIN436250-13"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["MOP-111012"],"award-info":[{"award-number":["MOP-111012"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN436250-13"],"award-info":[{"award-number":["RGPIN436250-13"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Neutrophil extracellular traps (NETs) are intricate, DNA-based, web-like structures adorned with cytotoxic proteins. They play a crucial role in antimicrobial defense but are also implicated in autoimmune diseases and tissue injury. The process of NET formation, known as NETosis, is a regulated cell death mechanism that involves the release of these structures and is unique to neutrophils. NETosis is heavily dependent on the production of reactive oxygen species (ROS), which can be generated either through NADPH oxidase (NOX) or mitochondrial pathways, leading to NOX-dependent or NOX-independent NETosis, respectively. Recent research has revealed an intricate interplay between ROS production, DNA repair, and NET formation in different contexts. UV radiation can trigger a combined process of NETosis and apoptosis, known as apoNETosis, driven by mitochondrial ROS and DNA repair. Similarly, in calcium ionophore-induced NETosis, both ROS and DNA repair are key components, but only play a partial role. In the case of bacterial infections, the early stages of DNA repair are pivotal. Interestingly, in serum-free conditions, spontaneous NETosis occurs through NOX-derived ROS, with early-stage DNA repair inhibition halting the process, while late-stage inhibition increases it. The intricate balance between DNA repair processes and ROS production appears to be a critical factor in regulating NET formation, with different pathways being activated depending on the nature of the stimulus. These findings not only deepen our understanding of the mechanisms behind NETosis but also suggest potential therapeutic targets for conditions where NETs contribute to disease pathology.<\/jats:p>","DOI":"10.3390\/biom14101307","type":"journal-article","created":{"date-parts":[[2024,10,18]],"date-time":"2024-10-18T09:14:48Z","timestamp":1729242888000},"page":"1307","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":114,"title":["How Do ROS Induce NETosis? Oxidative DNA Damage, DNA Repair, and Chromatin Decondensation"],"prefix":"10.3390","volume":"14","author":[{"given":"Dhia","family":"Azzouz","sequence":"first","affiliation":[{"name":"Translational Medicine, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2170-8548","authenticated-orcid":false,"given":"Nades","family":"Palaniyar","sequence":"additional","affiliation":[{"name":"Translational Medicine, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada"},{"name":"Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON M5S 1A8, Canada"},{"name":"Institute of Medical Sciences, Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,10,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1186\/s13223-018-0278-1","article-title":"An introduction to immunology and immunopathology","volume":"14","author":"Marshall","year":"2018","journal-title":"Allergy Asthma Clin. Immunol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1038\/ni1004-971","article-title":"The interface between innate and adaptive immunity","volume":"5","author":"Hoebe","year":"2004","journal-title":"Nat. Immunol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/j.cgh.2014.03.007","article-title":"Innate immunity in disease","volume":"12","author":"Elliott","year":"2014","journal-title":"Clin. Gastroenterol. Hepatol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1016\/j.cell.2021.01.007","article-title":"Adaptive immunity to SARS-CoV-2 and COVID-19","volume":"184","author":"Sette","year":"2021","journal-title":"Cell"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Holmes, E.C. (2004). Adaptation and immunity. PLoS Biol., 2.","DOI":"10.1371\/journal.pbio.0020307"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.imlet.2014.10.011","article-title":"The activation of the adaptive immune system: Cross-talk between antigen-presenting cells, T cells and B cells","volume":"162","author":"Arens","year":"2014","journal-title":"Immunol. Lett."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Fine, N., Tasevski, N., McCulloch, C.A., Tenenbaum, H.C., and Glogauer, M. (2020). The neutrophil: Constant defender and first responder. Front. Immunol., 11.","DOI":"10.3389\/fimmu.2020.571085"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1002\/jlb.59.2.229","article-title":"Rapid killing of human neutrophils by the potent activator phorbol 12-myristate 13-acetate (PMA) accompanied by changes different from typical apoptosis or necrosis","volume":"59","author":"Takei","year":"1996","journal-title":"J. Leukoc. Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1532","DOI":"10.1126\/science.1092385","article-title":"Neutrophil extracellular traps kill bacteria","volume":"303","author":"Brinkmann","year":"2004","journal-title":"Science"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.imlet.2012.01.013","article-title":"The role of neutrophils in autoimmune diseases","volume":"143","year":"2012","journal-title":"Immunol. Lett."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/nrneph.2016.71","article-title":"The role of neutrophils and NETosis in autoimmune and renal diseases","volume":"12","author":"Gupta","year":"2016","journal-title":"Nat. Rev. Nephrol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1016\/j.autrev.2017.09.012","article-title":"Neutrophil extracellular traps (NETs) in autoimmune diseases: A comprehensive review","volume":"16","author":"Lee","year":"2017","journal-title":"Autoimmun. Rev."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1186\/ar4325","article-title":"Role of neutrophils in systemic autoimmune diseases","volume":"15","author":"Kaplan","year":"2013","journal-title":"Arthritis Res. Ther."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1038\/nrc.2016.52","article-title":"Neutrophils in cancer: Neutral no more","volume":"16","author":"Coffelt","year":"2016","journal-title":"Nat. Rev. Cancer"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Khan, M.A., D\u2019Ovidio, A., Tran, H., and Palaniyar, N. (2019). Anthracyclines Suppress Both NADPH Oxidase-Dependent and-Independent NETosis in Human Neutrophils. Cancers, 11.","DOI":"10.3390\/cancers11091328"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.it.2019.05.001","article-title":"The healing power of neutrophils","volume":"40","author":"Phillipson","year":"2019","journal-title":"Trends Immunol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1258","DOI":"10.1038\/nm.4430","article-title":"Barrier-tissue macrophages: Functional adaptation to environmental challenges","volume":"23","author":"Mowat","year":"2017","journal-title":"Nat. Med."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.mib.2013.10.007","article-title":"Macrophages clean up: Efferocytosis and microbial control","volume":"17","author":"Martin","year":"2014","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/s41577-019-0167-y","article-title":"How macrophages deal with death","volume":"19","author":"Lemke","year":"2019","journal-title":"Nat. Rev. Immunol."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Ma, W.-T., Gao, F., Gu, K., and Chen, D.-K. (2019). The role of monocytes and macrophages in autoimmune diseases: A comprehensive review. Front. Immunol., 10.","DOI":"10.3389\/fimmu.2019.01140"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Cendrowicz, E., Sas, Z., Bremer, E., and Rygiel, T.P. (2021). The role of macrophages in cancer development and therapy. Cancers, 13.","DOI":"10.3390\/cancers13081946"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1186\/1478-811X-11-29","article-title":"Cell plasticity in wound healing: Paracrine factors of M1\/M2 polarized macrophages influence the phenotypical state of dermal fibroblasts","volume":"11","author":"Ploeger","year":"2013","journal-title":"Cell Commun. Signal."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1038\/sj.jid.5700001","article-title":"Cytotoxic T cells","volume":"126","author":"Andersen","year":"2006","journal-title":"J. Investig. Dermatol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1146\/annurev.immunol.18.1.423","article-title":"Regulatory T cells in autoimmmunity","volume":"18","author":"Shevach","year":"2000","journal-title":"Annu. Rev. Immunol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"232","DOI":"10.4049\/jimmunol.166.1.232","article-title":"IFN-\u03b3 production by Th1 cells generated from naive CD4+ T cells exposed to norepinephrine","volume":"166","author":"Swanson","year":"2001","journal-title":"J. Immunol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1081\/JAS-100107544","article-title":"Serum levels of interleukins (IL)-4, IL-5, IL-13, and interferon-\u03b3 in acute asthma","volume":"38","author":"Lee","year":"2001","journal-title":"J. Asthma"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.cyto.2007.11.022","article-title":"IL-23 and IL-17 in tuberculosis","volume":"41","author":"Khader","year":"2008","journal-title":"Cytokine"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2080","DOI":"10.1111\/cas.14069","article-title":"Regulatory T (Treg) cells in cancer: Can Treg cells be a new therapeutic target?","volume":"110","author":"Ohue","year":"2019","journal-title":"Cancer Sci."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/0167-5699(95)80132-4","article-title":"Psoriasis: A T-cell-mediated autoimmune disease induced by streptococcal superantigens?","volume":"16","author":"Valdimarsson","year":"1995","journal-title":"Immunol. Today"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"T\u00f6pfer, K., Kempe, S., M\u00fcller, N., Schmitz, M., Bachmann, M., Cartellieri, M., Schackert, G., and Temme, A. (2011). Tumor evasion from T cell surveillance. BioMed Res. Int., 2011.","DOI":"10.1155\/2011\/918471"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"5423","DOI":"10.4049\/jimmunol.0902733","article-title":"Epidermal T cells and wound healing","volume":"184","author":"Havran","year":"2010","journal-title":"J. Immunol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"137","DOI":"10.2215\/CJN.09430915","article-title":"B cells, antibodies, and more","volume":"11","author":"Hoffman","year":"2016","journal-title":"Clin. J. Am. Soc. Nephrol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.immuni.2015.04.005","article-title":"Regulatory B cells: Origin, phenotype, and function","volume":"42","author":"Rosser","year":"2015","journal-title":"Immunity"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.cyto.2015.02.007","article-title":"B cells responses and cytokine production are regulated by their immune microenvironment","volume":"74","author":"Vazquez","year":"2015","journal-title":"Cytokine"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/0092-8674(94)90338-7","article-title":"T and B memory cells","volume":"76","author":"Sprent","year":"1994","journal-title":"Cell"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1186\/ar2780","article-title":"B cells in autoimmunity","volume":"11","author":"Jacobi","year":"2009","journal-title":"Arthritis Res. Ther."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1111\/j.1600-065X.1999.tb01310.x","article-title":"The central and multiple roles of B cells in lupus pathogenesis","volume":"169","author":"Chan","year":"1999","journal-title":"Immunol. Rev."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1007\/s00262-016-1848-z","article-title":"Pro-and anti-tumour effects of B cells and antibodies in cancer: A comparison of clinical studies and preclinical models","volume":"65","author":"Guy","year":"2016","journal-title":"Cancer Immunol. Immunother."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1111\/wrr.12584","article-title":"Mature B cells accelerate wound healing after acute and chronic diabetic skin lesions","volume":"25","author":"Boehm","year":"2017","journal-title":"Wound Repair Regen."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.molimm.2018.02.019","article-title":"Relative antibacterial functions of complement and NETs: NETs trap and complement effectively kills bacteria","volume":"97","author":"Azzouz","year":"2018","journal-title":"Mol. Immunol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1165\/rcmb.2016-0193PS","article-title":"Evasion of neutrophil extracellular traps by respiratory pathogens","volume":"56","author":"Storisteanu","year":"2017","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.semcdb.2018.03.020","article-title":"Neutrophil extracellular traps in fungal infection","volume":"89","author":"Urban","year":"2019","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1189\/jlb.5BT0615-234R","article-title":"At the Bedside: Neutrophil extracellular traps (NETs) as targets for biomarkers and therapies in autoimmune diseases","volume":"99","author":"Barnado","year":"2016","journal-title":"J. Leucoc. Biol."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Fousert, E., Toes, R., and Desai, J. (2020). Neutrophil extracellular traps (NETs) take the central stage in driving autoimmune responses. Cells, 9.","DOI":"10.3390\/cells9040915"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"178ra40","DOI":"10.1126\/scitranslmed.3005580","article-title":"NETs are a source of citrullinated autoantigens and stimulate inflammatory responses in rheumatoid arthritis","volume":"5","author":"Khandpur","year":"2013","journal-title":"Sci. Transl. Med."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1038\/s41577-022-00787-0","article-title":"Neutrophil extracellular traps in systemic autoimmune and autoinflammatory diseases","volume":"23","author":"Wigerblad","year":"2023","journal-title":"Nat. Rev. Immunol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1097\/BOR.0b013e3283546703","article-title":"Lupus neutrophils: \u2018NET\u2019gain in understanding lupus pathogenesis","volume":"24","author":"Knight","year":"2012","journal-title":"Curr. Opin. Rheumatol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/nrrheum.2014.80","article-title":"The multifactorial role of neutrophils in rheumatoid arthritis","volume":"10","author":"Wright","year":"2014","journal-title":"Nat. Rev. Rheumatol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"14355","DOI":"10.1007\/s13277-016-5328-z","article-title":"NETs in cancer","volume":"37","author":"Garley","year":"2016","journal-title":"Tumor Biol."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Qi, H., Yang, S., and Zhang, L. (2017). Neutrophil extracellular traps and endothelial dysfunction in atherosclerosis and thrombosis. Front. Immunol., 8.","DOI":"10.3389\/fimmu.2017.00928"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Trivedi, A., Khan, M.A., Bade, G., and Talwar, A. (2021). Orchestration of neutrophil extracellular traps (Nets), a unique innate immune function during chronic obstructive pulmonary disease (COPD) development. Biomedicines, 9.","DOI":"10.3390\/biomedicines9010053"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1038\/nm.3887","article-title":"Diabetes primes neutrophils to undergo NETosis, which impairs wound healing","volume":"21","author":"Wong","year":"2015","journal-title":"Nat. Med."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"984","DOI":"10.1038\/s41419-021-04294-3","article-title":"The emerging roles of neutrophil extracellular traps in wound healing","volume":"12","author":"Zhu","year":"2021","journal-title":"Cell Death Dis."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1038\/s41418-017-0012-4","article-title":"Molecular mechanisms of cell death: Recommendations of the Nomenclature Committee on Cell Death 2018","volume":"25","author":"Galluzzi","year":"2018","journal-title":"Cell Death Differ."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1038\/s41418-018-0261-x","article-title":"To NET or not to NET: Current opinions and state of the science regarding the formation of neutrophil extracellular traps","volume":"26","author":"Boeltz","year":"2019","journal-title":"Cell Death Differ."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1182\/blood-2013-09-526707","article-title":"Akt is essential to induce NADPH-dependent NETosis and to switch the neutrophil death to apoptosis","volume":"123","author":"Douda","year":"2014","journal-title":"Blood"},{"key":"ref_57","first-page":"360","article-title":"Protein kinase C activation in human monocytes: Regulation of PKC isoforms","volume":"80","author":"Chang","year":"1993","journal-title":"Immunology"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Rastogi, R., Geng, X., Li, F., and Ding, Y. (2017). NOX activation by subunit interaction and underlying mechanisms in disease. Front. Cell. Neurosci., 10.","DOI":"10.3389\/fncel.2016.00301"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Khan, M.A., Farahvash, A., Douda, D.N., Licht, J.-C., Grasemann, H., Sweezey, N., and Palaniyar, N. (2017). JNK activation turns on LPS-and Gram-negative bacteria-induced NADPH oxidase-dependent suicidal NETosis. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-03257-z"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Paclet, M.-H., Laurans, S., and Dupr\u00e9-Crochet, S. (2022). Regulation of neutrophil NADPH oxidase, NOX2: A crucial effector in neutrophil phenotype and function. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.945749"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1038\/nchembio.496","article-title":"Activation of the Raf-MEK-ERK pathway is required for neutrophil extracellular trap formation","volume":"7","author":"Hakkim","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Fonseca, Z., D\u00edaz-God\u00ednez, C., Mora, N., Alem\u00e1n, O.R., Uribe-Querol, E., Carrero, J.C., and Rosales, C. (2018). Entamoeba histolytica induce signaling via Raf\/MEK\/ERK for neutrophil extracellular trap (NET) formation. Front. Cell. Infect. Microbiol., 8.","DOI":"10.3389\/fcimb.2018.00226"},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Khan, M.A., and Palaniyar, N. (2017). Transcriptional firing helps to drive NETosis. Sci. Rep., 7.","DOI":"10.1038\/srep41749"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1038\/s41420-018-0048-3","article-title":"Two-in-one: UV radiation simultaneously induces apoptosis and NETosis","volume":"4","author":"Azzouz","year":"2018","journal-title":"Cell Death Discov."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2817","DOI":"10.1073\/pnas.1414055112","article-title":"SK3 channel and mitochondrial ROS mediate NADPH oxidase-independent NETosis induced by calcium influx","volume":"112","author":"Douda","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1016\/j.bbrc.2013.12.007","article-title":"Uric acid induces NADPH oxidase-independent neutrophil extracellular trap formation","volume":"443","author":"Arai","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1136\/annrheumdis-2013-203844","article-title":"Citrullination of autoantigens implicates NETosis in the induction of autoimmunity","volume":"73","author":"Dwivedi","year":"2014","journal-title":"Ann. Rheum. Dis."},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Rohrbach, A.S., Slade, D.J., Thompson, P.R., and Mowen, K.A. (2012). Activation of PAD4 in NET formation. Front. Immunol., 3.","DOI":"10.3389\/fimmu.2012.00360"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2784","DOI":"10.1182\/blood-2013-04-457671","article-title":"NETosis: How vital is it?","volume":"122","author":"Yipp","year":"2013","journal-title":"Blood"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1083\/jcb.140.1.171","article-title":"Ultraviolet light induces apoptosis via direct activation of CD95 (Fas\/APO-1) independently of its ligand CD95L","volume":"140","author":"Aragane","year":"1998","journal-title":"J. Cell Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"8389","DOI":"10.1074\/jbc.273.14.8389","article-title":"p38 mitogen-activated protein kinase-dependent and-independent intracellular signal transduction pathways leading to apoptosis in human neutrophils","volume":"273","author":"Frasch","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1083\/jcb.201006052","article-title":"Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps","volume":"191","author":"Papayannopoulos","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"3503","DOI":"10.1182\/blood.V89.10.3503","article-title":"Granules of the human neutrophilic polymorphonuclear leukocyte","volume":"89","author":"Borregaard","year":"1997","journal-title":"Blood"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1038\/nm.4027","article-title":"Neutrophil extracellular traps enriched in oxidized mitochondrial DNA are interferogenic and contribute to lupus-like disease","volume":"22","author":"Lood","year":"2016","journal-title":"Nat. Med."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"e24437","DOI":"10.7554\/eLife.24437","article-title":"Diverse stimuli engage different neutrophil extracellular trap pathways","volume":"6","author":"Kenny","year":"2017","journal-title":"eLife"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Leshner, M., Wang, S., Lewis, C., Zheng, H., Chen, X.A., Santy, L., and Wang, Y. (2012). PAD4 mediated histone hypercitrullination induces heterochromatin decondensation and chromatin unfolding to form neutrophil extracellular trap-like structures. Front. Immunol., 3.","DOI":"10.3389\/fimmu.2012.00307"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1172\/JCI112962","article-title":"Calcium ionophore, phorbol ester, and chemotactic peptide-induced cytoskeleton reorganization in human neutrophils","volume":"79","author":"Howard","year":"1987","journal-title":"J. Clin. Investig."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/s41419-018-0846-9","article-title":"ApoNETosis: Discovery of a novel form of neutrophil death with concomitant apoptosis and NETosis","volume":"9","author":"Azzouz","year":"2018","journal-title":"Cell Death Dis."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"De Jager, T., Cockrell, A., and Du Plessis, S. (2017). Ultraviolet light induced generation of reactive oxygen species. Ultraviolet Light in Human Health, Diseases and Environment, Springer.","DOI":"10.1007\/978-3-319-56017-5_2"},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Arzumanyan, G., Mamatkulov, K., Arynbek, Y., Zakrytnaya, D., Jevremovi\u0107, A., and Vorobjeva, N. (2023). Radiation from UV-A to Red Light Induces ROS-Dependent Release of Neutrophil Extracellular Traps. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24065770"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"e48779","DOI":"10.15252\/embr.201948779","article-title":"Nuclear envelope rupture and NET formation is driven by PKC\u03b1-mediated lamin B disassembly","volume":"21","author":"Li","year":"2020","journal-title":"EMBO Rep."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Arroyo, R., Khan, M.A., Echaide, M., P\u00e9rez-Gil, J., and Palaniyar, N. (2019). SP-D attenuates LPS-induced formation of human neutrophil extracellular traps (NETs), protecting pulmonary surfactant inactivation by NETs. Commun. Biol., 2.","DOI":"10.1038\/s42003-019-0662-5"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Zawrotniak, M., Bartnicka, D., and Rapala-Kozik, M. (2019). UVA and UVB radiation induce the formation of neutrophil extracellular traps by human polymorphonuclear cells. J. Photochem. Photobiol. B Biol., 196.","DOI":"10.1016\/j.jphotobiol.2019.111511"},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Neubert, E., Bach, K.M., Busse, J., Bogeski, I., Sch\u00f6n, M.P., Kruss, S., and Erpenbeck, L. (2019). Blue and long-wave ultraviolet light induce in vitro Neutrophil Extracellular Trap (NET) formation. Front. Immunol., 10.","DOI":"10.3389\/fimmu.2019.02428"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1438","DOI":"10.1038\/cdd.2009.96","article-title":"Viable neutrophils release mitochondrial DNA to form neutrophil extracellular traps","volume":"16","author":"Yousefi","year":"2009","journal-title":"Cell Death Differ."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1038\/nm1565","article-title":"Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood","volume":"13","author":"Clark","year":"2007","journal-title":"Nat. Med."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"7413","DOI":"10.4049\/jimmunol.1000675","article-title":"A novel mechanism of rapid nuclear neutrophil extracellular trap formation in response to Staphylococcus aureus","volume":"185","author":"Pilsczek","year":"2010","journal-title":"J. Immunol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"4421","DOI":"10.1182\/blood-2011-12-401133","article-title":"Endocytosis of soluble immune complexes leads to their clearance by Fc\u03b3RIIIB but induces neutrophil extracellular traps via Fc\u03b3RIIA in vivo","volume":"120","author":"Chen","year":"2012","journal-title":"Blood"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2896380","DOI":"10.1155\/2017\/2896380","article-title":"Neutrophil Extracellular Traps and Microcrystals","volume":"2017","author":"Rada","year":"2017","journal-title":"J. Immunol. Res."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"P\u00e9rez-Figueroa, E., \u00c1lvarez-Carrasco, P., Ortega, E., and Maldonado-Bernal, C. (2021). Neutrophils: Many ways to die. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.631821"},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Poh, X.Y., Loh, F.K., Friedland, J.S., and Ong, C.W. (2022). Neutrophil-Mediated Immunopathology and Matrix Metalloproteinases in Central Nervous System\u2013Tuberculosis. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.788976"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2505","DOI":"10.1007\/s11011-023-01268-6","article-title":"Neutrophil extracellular traps in intracerebral hemorrhage: Implications for pathogenesis and therapeutic targets","volume":"38","author":"Liu","year":"2023","journal-title":"Metab. Brain Dis."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1111\/imr.13284","article-title":"A variety of death modes of neutrophils and their role in the etiology of autoimmune diseases","volume":"321","author":"Li","year":"2024","journal-title":"Immunol. Rev."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1111\/jmi.13252","article-title":"Structure-preserving fixation allows scanning electron microscopy to reveal biofilm microstructure and interactions with immune cells","volume":"293","author":"Wells","year":"2024","journal-title":"J. Microsc."},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Ramos-Mart\u00ednez, E., Hern\u00e1ndez-Gonz\u00e1lez, L., Ramos-Mart\u00ednez, I., P\u00e9rez-Campos Mayoral, L., L\u00f3pez-Cort\u00e9s, G.I., P\u00e9rez-Campos, E., Mayoral Andrade, G., Hern\u00e1ndez-Huerta, M.T., and Jos\u00e9, M.V. (2021). Multiple origins of extracellular DNA traps. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.621311"},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Na, J., Lee, C.-H., Chung, J.-K., and Youn, H. (2023). Overexpression of both human sodium iodide symporter (NIS) and BRG1-bromodomain synergistically enhances radioiodine sensitivity by stabilizing p53 through NPM1 Expression. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24032761"},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Monticolo, F., Palomba, E., and Chiusano, M.L. (2020). Identification of Novel Potential Genes Involved in Cancer by Integrated Comparative Analyses. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21249560"},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Andr\u00e9s, C.M.C., P\u00e9rez de la Lastra, J.M., Juan, C.A., Plou, F.J., and P\u00e9rez-Lebe\u00f1a, E. (2022). The role of reactive species on innate immunity. Vaccines, 10.","DOI":"10.3390\/vaccines10101735"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Niyonsaba, F. (2022). The role of neutrophils and its NETosis in autoimmunity and autoinflammation. Front. Immunol., 13.","DOI":"10.3389\/fimmu.2022.1035624"},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Radic, M., and Muller, S. (2022). LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis. Cells, 11.","DOI":"10.3390\/cells11152463"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1042\/BJ20140778","article-title":"The antimicrobial peptide LL-37 facilitates the formation of neutrophil extracellular traps","volume":"464","author":"Neumann","year":"2014","journal-title":"Biochem. J."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1189\/jlb.0704380","article-title":"Impact of LL-37 on anti-infective immunity","volume":"77","author":"Bowdish","year":"2005","journal-title":"J. Leukoc. Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1189\/jlb.0208086","article-title":"Neutrophil secondary necrosis is induced by LL-37 derived from cathelicidin","volume":"84","author":"Zhang","year":"2008","journal-title":"J. Leucoc. Biol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1083\/jcb.200606027","article-title":"Novel cell death program leads to neutrophil extracellular traps","volume":"176","author":"Fuchs","year":"2007","journal-title":"J. Cell Biol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/j.redox.2015.09.005","article-title":"Reactive oxygen species and mitochondria: A nexus of cellular homeostasis","volume":"6","author":"Dunn","year":"2015","journal-title":"Redox Biol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"8312","DOI":"10.1074\/jbc.M113.545301","article-title":"The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide\/hydrogen peroxide at much higher rates than complex I","volume":"289","author":"Quinlan","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Dexheimer, T.S. (2013). DNA repair pathways and mechanisms. DNA Repair Cancer Stem Cells, Springer.","DOI":"10.1007\/978-94-007-4590-2_2"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/nrmicro3391","article-title":"The BER necessities: The repair of DNA damage in human-adapted bacterial pathogens","volume":"13","author":"Tang","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Semenkov, V.F., Michalski, A.I., and Sapozhnikov, A.M. (2015). Heating and ultraviolet light activate anti-stress gene functions in humans. Front. Genet., 6.","DOI":"10.3389\/fgene.2015.00245"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Krokan, H.E., and Bj\u00f8r\u00e5s, M. (2013). Base excision repair. Cold Spring Harb. Perspect. Biol., 5.","DOI":"10.1101\/cshperspect.a012583"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1038\/s41420-021-00491-3","article-title":"ROS induces NETosis by oxidizing DNA and initiating DNA repair","volume":"7","author":"Azzouz","year":"2021","journal-title":"Cell Death Discov."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"3008","DOI":"10.1021\/acs.biochem.7b00295","article-title":"The nonbulky DNA lesions spiroiminodihydantoin and 5-guanidinohydantoin significantly block human RNA polymerase II elongation in vitro","volume":"56","author":"Kolbanovskiy","year":"2017","journal-title":"Biochemistry"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"6043","DOI":"10.1021\/bi0473657","article-title":"Spiroiminodihydantoin lesions derived from guanine oxidation: Structures, energetics, and functional implications","volume":"44","author":"Jia","year":"2005","journal-title":"Biochemistry"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1016\/j.dnarep.2013.04.026","article-title":"Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin","volume":"12","author":"Krokeide","year":"2013","journal-title":"DNA Repair"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1021\/ar2002182","article-title":"The formamidopyrimidines: Purine lesions formed in competition with 8-oxopurines from oxidative stress","volume":"45","author":"Greenberg","year":"2012","journal-title":"Acc. Chem. Res."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"4207","DOI":"10.1073\/pnas.1620932114","article-title":"NEIL1 protects against aflatoxin-induced hepatocellular carcinoma in mice","volume":"114","author":"Vartanian","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"114626","DOI":"10.18632\/oncotarget.22638","article-title":"Genetic variation in the NEIL2 DNA glycosylase gene is associated with oxidative DNA damage in BRCA2 mutation carriers","volume":"8","author":"Baquero","year":"2017","journal-title":"Oncotarget"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"40544","DOI":"10.1074\/jbc.M508772200","article-title":"Repair of formamidopyrimidines in DNA involves different glycosylases: Role of the OGG1, NTH1, and NEIL1 enzymes","volume":"280","author":"Hu","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"8935","DOI":"10.1038\/sj.onc.1205996","article-title":"Uracil in DNA\u2013occurrence, consequences and repair","volume":"21","author":"Krokan","year":"2002","journal-title":"Oncogene"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1034","DOI":"10.1096\/fasebj.9.11.7649402","article-title":"Hypermodified bases in DNA","volume":"9","author":"Borst","year":"1995","journal-title":"FASEB J."},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Bullard, W., Kieft, R., and Sabatini, R. (2017). A method for the efficient and selective identification of 5-hydroxymethyluracil in genomic DNA. Biol. Methods Protoc., 2.","DOI":"10.1093\/biomethods\/bpw006"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Choi, W.L., Mok, Y.G., and Huh, J.H. (2021). Application of 5-Methylcytosine DNA Glycosylase to the Quantitative Analysis of DNA Methylation. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22031072"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1016\/j.cell.2013.04.002","article-title":"Genome-wide analysis reveals TET-and TDG-dependent 5-methylcytosine oxidation dynamics","volume":"153","author":"Shen","year":"2013","journal-title":"Cell"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/1756-8935-6-10","article-title":"5-hydroxymethylcytosine and its potential roles in development and cancer","volume":"6","author":"Pfeifer","year":"2013","journal-title":"Epigenetics Chromatin"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.cell.2011.03.022","article-title":"Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain","volume":"145","author":"Guo","year":"2011","journal-title":"Cell"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"2688","DOI":"10.1021\/acs.chemrestox.0c00326","article-title":"1, N 6-Ethenoadenine: From Molecular to Biological Consequences","volume":"33","author":"Rioux","year":"2020","journal-title":"Chem. Res. Toxicol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1007\/s11010-008-9737-1","article-title":"Evidence of complete cellular repair of 1, N 6-ethenoadenine, a mutagenic and potential damage for human cancer, revealed by a novel method","volume":"313","author":"Choudhury","year":"2008","journal-title":"Mol. Cell. Biochem."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"4158","DOI":"10.1021\/bi0622569","article-title":"NEIL1 is the major DNA glycosylase that processes 5-hydroxyuracil in the proximity of a DNA single-strand break","volume":"46","author":"Parsons","year":"2007","journal-title":"Biochemistry"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/j.freeradbiomed.2018.12.010","article-title":"Defective repair capacity of variant proteins of the DNA glycosylase NTHL1 for 5-hydroxyuracil, an oxidation product of cytosine","volume":"131","author":"Shinmura","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.str.2020.12.011","article-title":"Breaking the rules: Protein sculpting in NEIL2 regulation","volume":"29","author":"Tsutakawa","year":"2021","journal-title":"Structure"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1038\/45843","article-title":"The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites","volume":"401","author":"Hendrich","year":"1999","journal-title":"Nature"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1186\/1897-4287-5-4-199","article-title":"Base excision repair and the role of MUTYH","volume":"5","author":"Kairupan","year":"2007","journal-title":"Hered. Cancer Clin. Pract."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"2763","DOI":"10.1093\/carcin\/bgu214","article-title":"Enzymatic MPG DNA repair assays for two different oxidative DNA lesions reveal associations with increased lung cancer risk","volume":"35","author":"Sevilya","year":"2014","journal-title":"Carcinogenesis"},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Lin, T., Zhang, L., Wu, M., Jiang, D., Li, Z., and Yang, Z. (2021). Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea. Front. Microbiol., 12.","DOI":"10.3389\/fmicb.2021.736915"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1080\/10409230802309905","article-title":"Base excision repair and its role in maintaining genome stability","volume":"43","author":"Baute","year":"2008","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"ref_136","doi-asserted-by":"crossref","unstructured":"Markkanen, E., Dorn, J., and H\u00fcbscher, U. (2013). MUTYH DNA glycosylase: The rationale for removing undamaged bases from the DNA. Front. Genet., 4.","DOI":"10.3389\/fgene.2013.00018"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"3","DOI":"10.2174\/1874467211205010003","article-title":"Overview of base excision repair biochemistry","volume":"5","author":"Kim","year":"2012","journal-title":"Curr. Mol. Pharmacol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"2183","DOI":"10.1016\/j.jmb.2014.03.014","article-title":"APE1 incision activity at abasic sites in tandem repeat sequences","volume":"426","author":"Li","year":"2014","journal-title":"J. Mol. Biol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S0921-8777(00)00028-8","article-title":"Abasic site recognition by two apurinic\/apyrimidinic endonuclease families in DNA base excision repair: The 3\u2032 ends justify the means","volume":"460","author":"Mol","year":"2000","journal-title":"Mutat. Res. DNA Repair"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1038\/35000249","article-title":"DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination","volume":"403","author":"Mol","year":"2000","journal-title":"Nature"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1158\/1541-7786.MCR-06-0329","article-title":"A dominant-negative form of the major human abasic endonuclease enhances cellular sensitivity to laboratory and clinical DNA-damaging agents","volume":"5","author":"McNeill","year":"2007","journal-title":"Mol. Cancer Res."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1038\/s41467-017-02175-y","article-title":"Molecular snapshots of APE1 proofreading mismatches and removing DNA damage","volume":"9","author":"Whitaker","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"36","DOI":"10.2174\/1874467211205010036","article-title":"APE1\/Ref-1role in redox signaling: Translational applications of targeting the redox function of the DNA repair\/redox protein APE1\/Ref-1","volume":"5","year":"2012","journal-title":"Curr. Mol. Pharmacol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1007\/s00018-009-8736-z","article-title":"DNA repair in mammalian cells","volume":"66","author":"Robertson","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1158\/1541-7786.MCR-09-0253","article-title":"FEN1 Functions in Long Patch Base Excision Repair Under Conditions of Oxidative Stress in Vertebrate CellsFEN1-Dependent DNA Metabolism","volume":"8","author":"Asagoshi","year":"2010","journal-title":"Mol. Cancer Res."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"3341","DOI":"10.1093\/emboj\/16.11.3341","article-title":"Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)","volume":"16","author":"Klungland","year":"1997","journal-title":"EMBO J."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/S0076-6879(06)08007-4","article-title":"Activities and mechanism of DNA polymerase \u03b2","volume":"408","author":"Beard","year":"2006","journal-title":"Methods Enzymol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1002\/em.20663","article-title":"XRCC1 coordinates disparate responses and multiprotein repair complexes depending on the nature and context of the DNA damage","volume":"52","author":"Sundheim","year":"2011","journal-title":"Environ. Mol. Mutagen."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1089\/ars.2010.3466","article-title":"Base excision repair and lesion-dependent subpathways for repair of oxidative DNA damage","volume":"14","author":"Svilar","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"3834","DOI":"10.1093\/emboj\/18.13.3834","article-title":"Post-replicative base excision repair in replication foci","volume":"18","author":"Otterlei","year":"1999","journal-title":"EMBO J."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"27028","DOI":"10.1074\/jbc.M802712200","article-title":"Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1","volume":"283","author":"Hegde","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"15230","DOI":"10.1074\/jbc.274.21.15230","article-title":"The type of DNA glycosylase determines the base excision repair pathway in mammalian cells","volume":"274","author":"Fortini","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1016\/j.dnarep.2006.10.008","article-title":"Base damage and single-strand break repair: Mechanisms and functional significance of short-and long-patch repair subpathways","volume":"6","author":"Fortini","year":"2007","journal-title":"DNA Repair"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1016\/S1568-7864(03)00117-4","article-title":"ATP-dependent selection between single nucleotide and long patch base excision repair","volume":"2","author":"Petermann","year":"2003","journal-title":"DNA Repair"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1016\/j.dnarep.2005.12.008","article-title":"Roles of DNA ligase III and XRCC1 in regulating the switch between short patch and long patch BER","volume":"5","author":"Petermann","year":"2006","journal-title":"DNA Repair"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"33696","DOI":"10.1074\/jbc.274.47.33696","article-title":"Long patch base excision repair with purified human proteins: DNA ligase I as patch size mediator for DNA polymerases \u03b4 and \u03b5","volume":"274","author":"Pascucci","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"4623","DOI":"10.1128\/MCB.05715-11","article-title":"Nucleosome disruption by DNA ligase III-XRCC1 promotes efficient base excision repair","volume":"31","author":"Odell","year":"2011","journal-title":"Mol. Cell. Biol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"103549","DOI":"10.1016\/j.dnarep.2023.103549","article-title":"Novel insights into bulky DNA damage formation and nucleotide excision repair from high-resolution genomics","volume":"130","author":"Cohen","year":"2023","journal-title":"DNA Repair"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1842","DOI":"10.1039\/c8pp00182k","article-title":"Solar UV damage to cellular DNA: From mechanisms to biological effects","volume":"17","author":"Mullenders","year":"2018","journal-title":"Photochem. Photobiol. Sci."},{"key":"ref_160","unstructured":"Geacintov, N.E., Naegeli, H., and Patel, D.J. (2005). Structural aspects of polycyclic aromatic carcinogen-damaged DNA and its recognition by NER proteins. DNA Damage Recognition, CRC Press."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.canlet.2005.11.018","article-title":"Aflatoxin B1-induced DNA damage and its repair","volume":"241","author":"Bedard","year":"2006","journal-title":"Cancer Lett."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"2409","DOI":"10.1089\/ars.2012.5036","article-title":"Oxidative DNA damage and nucleotide excision repair","volume":"18","author":"Melis","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1038\/nrm3822","article-title":"Understanding nucleotide excision repair and its roles in cancer and ageing","volume":"15","author":"Marteijn","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1016\/j.molcel.2009.09.035","article-title":"Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning","volume":"36","author":"Sugasawa","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.mad.2013.03.008","article-title":"The role of Cockayne syndrome group A (CSA) protein in transcription-coupled nucleotide excision repair","volume":"134","author":"Saijo","year":"2013","journal-title":"Mech. Ageing Dev."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1038\/cr.2008.6","article-title":"Transcription-coupled nucleotide excision repair in mammalian cells: Molecular mechanisms and biological effects","volume":"18","author":"Fousteri","year":"2008","journal-title":"Cell Res."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/j.dnarep.2011.04.028","article-title":"XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase","volume":"10","author":"Fuss","year":"2011","journal-title":"DNA Repair"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"2173","DOI":"10.1093\/nar\/gkz1231","article-title":"A key interaction with RPA orients XPA in NER complexes","volume":"48","author":"Sugitani","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1021\/bi002021b","article-title":"Novel functional interactions between nucleotide excision DNA repair proteins influencing the enzymatic activities of TFIIH, XPG, and ERCC1-XPF","volume":"40","author":"Winkler","year":"2001","journal-title":"Biochemistry"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/j.dnarep.2011.04.022","article-title":"Regulation of endonuclease activity in human nucleotide excision repair","volume":"10","author":"Fagbemi","year":"2011","journal-title":"DNA Repair"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1016\/j.molcel.2010.02.009","article-title":"Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells","volume":"37","author":"Ogi","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"3523","DOI":"10.1093\/nar\/gkl492","article-title":"Differential recruitment of DNA Ligase I and III to DNA repair sites","volume":"34","author":"Mortusewicz","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.3324\/haematol.11472","article-title":"Eosinophils, but not neutrophils, exhibit an efficient DNA repair machinery and high nucleolar activity","volume":"92","author":"Salati","year":"2007","journal-title":"Haematologica"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"2631","DOI":"10.1084\/jem.20092241","article-title":"Proliferating cell nuclear antigen acts as a cytoplasmic platform controlling human neutrophil survival","volume":"207","author":"Mocek","year":"2010","journal-title":"J. Exp. Med."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1096\/fasebj.28.1_supplement.902.5","article-title":"Role of PARP-1 in the modulation of neutrophil function: Relevance for inflammatory bowel disease (902.5)","volume":"28","author":"Larmonier","year":"2014","journal-title":"FASEB J."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"16975","DOI":"10.3390\/ijms150916975","article-title":"The role of 8-oxoguanine DNA glycosylase-1 in inflammation","volume":"15","author":"Ba","year":"2014","journal-title":"Int. J. Mol. Sci."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"R445","DOI":"10.1016\/j.cub.2014.03.060","article-title":"Polymerase stalling during replication, transcription and translation","volume":"24","author":"Edenberg","year":"2014","journal-title":"Curr. Biol."},{"key":"ref_178","first-page":"2842","article-title":"Neutrophil oxidative burst activates ATM to regulate cytokine production and apoptosis","volume":"126","author":"Harbort","year":"2015","journal-title":"Blood J. Am. Soc. Hematol."},{"key":"ref_179","first-page":"2773","article-title":"DNA damage signals inhibit neutrophil function","volume":"126","author":"Bednarski","year":"2015","journal-title":"Blood J. Am. Soc. Hematol."},{"key":"ref_180","doi-asserted-by":"crossref","unstructured":"Juan, C.A., P\u00e9rez de la Lastra, J.M., Plou, F.J., and P\u00e9rez-Lebe\u00f1a, E. (2021). The chemistry of reactive oxygen species (ROS) revisited: Outlining their role in biological macromolecules (DNA, lipids and proteins) and induced pathologies. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22094642"},{"key":"ref_181","doi-asserted-by":"crossref","unstructured":"Azzouz, D., and Palaniyar, N. (2023). Mitochondrial ROS and Base Excision Repair Steps Leading to DNA Nick Formation Drive Ultraviolet Induced-NETosis. Front. Immunol., 14.","DOI":"10.3389\/fimmu.2023.1198716"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1093\/aob\/mcq243","article-title":"Proliferating cell nuclear antigen (PCNA): A key factor in DNA replication and cell cycle regulation","volume":"107","author":"Strzalka","year":"2010","journal-title":"Ann. Bot."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"102921","DOI":"10.1016\/j.dnarep.2020.102921","article-title":"Mammalian DNA base excision repair: Dancing in the moonlight","volume":"93","author":"Caldecott","year":"2020","journal-title":"DNA Repair"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"e106","DOI":"10.1038\/emm.2014.42","article-title":"APE1\/Ref-1 as an emerging therapeutic target for various human diseases: Phytochemical modulation of its functions","volume":"46","author":"Thakur","year":"2014","journal-title":"Exp. Mol. Med."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"14","DOI":"10.2174\/1874467211205010014","article-title":"Small-molecule inhibitors of APE1 DNA repair function: An overview","volume":"5","author":"Odde","year":"2012","journal-title":"Curr. Mol. Pharmacol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1126\/science.8211165","article-title":"Transcription-coupled DNA repair","volume":"262","author":"Sweder","year":"1993","journal-title":"Science"},{"key":"ref_187","doi-asserted-by":"crossref","unstructured":"M\u00fcnzer, P., Negro, R., Fukui, S., Di Meglio, L., Aymonnier, K., Chu, L., Cherpokova, D., Gutch, S., Sorvillo, N., and Shi, L. (2021). NLRP3 inflammasome assembly in neutrophils is supported by PAD4 and promotes NETosis under sterile conditions. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.683803"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1895","DOI":"10.4049\/jimmunol.180.3.1895","article-title":"Histone deimination as a response to inflammatory stimuli in neutrophils","volume":"180","author":"Neeli","year":"2008","journal-title":"J. Immunol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"11727","DOI":"10.1021\/bi061180d","article-title":"Inhibitors and inactivators of protein arginine deiminase 4: Functional and structural characterization","volume":"45","author":"Luo","year":"2006","journal-title":"Biochemistry"},{"key":"ref_190","doi-asserted-by":"crossref","unstructured":"Zhang, X., Gamble, M.J., Stadler, S., Cherrington, B.D., Causey, C.P., Thompson, P.R., Roberson, M.S., Kraus, W.L., and Coonrod, S.A. (2011). Genome-wide analysis reveals PADI4 cooperates with Elk-1 to activate c-Fos expression in breast cancer cells. PLoS Genet., 7.","DOI":"10.1371\/journal.pgen.1002112"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"2840","DOI":"10.1096\/fj.13-247254","article-title":"Deimination of linker histones links neutrophil extracellular trap release with autoantibodies in systemic autoimmunity","volume":"28","author":"Dwivedi","year":"2014","journal-title":"FASEB J."},{"key":"ref_192","doi-asserted-by":"crossref","unstructured":"Hamam, H.J., Khan, M.A., and Palaniyar, N. (2019). Histone Acetylation Promotes Neutrophil Extracellular Trap Formation. Biomolecules, 9.","DOI":"10.3390\/biom9010032"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1186\/s12943-021-01373-z","article-title":"Histone citrullination: A new target for tumors","volume":"20","author":"Zhu","year":"2021","journal-title":"Mol. Cancer"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"4350965","DOI":"10.1155\/2016\/4350965","article-title":"ROS and ROS-mediated cellular signaling","volume":"2016","author":"Zhang","year":"2016","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1007\/s00281-008-0126-3","article-title":"Role of Nox2 in elimination of microorganisms","volume":"30","author":"Rada","year":"2008","journal-title":"Semin. Immunopathol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.immuni.2013.08.004","article-title":"Oxidative damage of DNA confers resistance to cytosolic nuclease TREX1 degradation and potentiates STING-dependent immune sensing","volume":"39","author":"Gehrke","year":"2013","journal-title":"Immunity"},{"key":"ref_197","doi-asserted-by":"crossref","unstructured":"Guo, Y., Gao, F., Wang, X., Pan, Z., Wang, Q., Xu, S., Pan, S., Li, L., Zhao, D., and Qian, J. (2021). Spontaneous formation of neutrophil extracellular traps is associated with autophagy. Sci. Rep., 11.","DOI":"10.1038\/s41598-021-03520-4"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.2337\/db15-0863","article-title":"NETosis delays diabetic wound healing in mice and humans","volume":"65","author":"Fadini","year":"2016","journal-title":"Diabetes"},{"key":"ref_199","doi-asserted-by":"crossref","unstructured":"Azzouz, D., and Palaniyar, N. (2022). ROS and DNA repair in spontaneous versus agonist-induced NETosis: Context matters. Front. Immunol., 13.","DOI":"10.3389\/fimmu.2022.1033815"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"271","DOI":"10.4239\/wjd.v7.i13.271","article-title":"Preliminary study on overproduction of reactive oxygen species by neutrophils in diabetes mellitus","volume":"7","author":"Ridzuan","year":"2016","journal-title":"World J. Diabetes"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1089\/ars.2021.0116","article-title":"Oxidative stress in neutrophils: Implications for diabetic cardiovascular complications","volume":"36","author":"Johnson","year":"2022","journal-title":"Antioxid. Redox Signal."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"5949","DOI":"10.1128\/MCB.00376-07","article-title":"ATP-dependent chromatin remodeling is required for base excision repair in conventional but not in variant H2A. Bbd nucleosomes","volume":"27","author":"Menoni","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1002\/2211-5463.12222","article-title":"Spontaneous formation of neutrophil extracellular traps in serum-free culture conditions","volume":"7","author":"Kamoshida","year":"2017","journal-title":"FEBS Open Bio"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"5116","DOI":"10.1038\/s41467-018-07550-x","article-title":"Plasma redox imbalance caused by albumin oxidation promotes lung-predominant NETosis and pulmonary cancer metastasis","volume":"9","author":"Inoue","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_205","doi-asserted-by":"crossref","unstructured":"Neubert, E., Senger-Sander, S.N., Manzke, V.S., Busse, J., Polo, E., Scheidmann, S.E., Sch\u00f6n, M.P., Kruss, S., and Erpenbeck, L. (2019). Serum and serum albumin inhibit in vitro formation of neutrophil extracellular traps (NETs). Front. Immunol., 10.","DOI":"10.3389\/fimmu.2019.00012"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1097\/BOR.0000000000000770","article-title":"Immunopathogenesis of skin injury in systemic lupus erythematosus","volume":"33","author":"Hile","year":"2021","journal-title":"Curr. Opin. Rheumatol."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/S0300-483X(03)00150-1","article-title":"UV-induced skin damage","volume":"189","author":"Ichihashi","year":"2003","journal-title":"Toxicology"},{"key":"ref_208","doi-asserted-by":"crossref","unstructured":"Clydesdale, G.J., Dandie, G.W., and Muller, H.K. (2001). Ultraviolet light induced injury: Immunological and inflammatory effects. Immunol. Cell Biol., 79.","DOI":"10.1046\/j.1440-1711.2001.01047.x"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1080\/000155502320624113","article-title":"Treatment of vitiligo vulgaris with narrow band UVB (311nm) for one year and the effect of addition of folic acid and vitamin B12","volume":"82","author":"Tjioe","year":"2002","journal-title":"Acta Derm.-Venereol."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1590\/abd1806-4841.20153694","article-title":"Evaluation of 25 years of phototherapy for treating psoriasis at a teaching hospital in southern Spain","volume":"90","year":"2015","journal-title":"An. Bras. Dermatol."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1080\/09546630701593465","article-title":"Targeted UV therapy in the treatment of psoriasis","volume":"19","author":"Stein","year":"2008","journal-title":"J. Dermatol. Treat."},{"key":"ref_212","doi-asserted-by":"crossref","unstructured":"Denning, N.-L., Aziz, M., Gurien, S.D., and Wang, P. (2019). DAMPs and NETs in sepsis. Front. Immunol., 10.","DOI":"10.3389\/fimmu.2019.02536"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1038\/nm.2053","article-title":"Extracellular histones are major mediators of death in sepsis","volume":"15","author":"Xu","year":"2009","journal-title":"Nat. Med."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12959-018-0190-4","article-title":"Circulating histone H3 levels in septic patients are associated with coagulopathy, multiple organ failure, and death: A single-center observational study","volume":"17","author":"Yokoyama","year":"2019","journal-title":"Thromb. J."},{"key":"ref_215","first-page":"33","article-title":"The Role of NETosis in Systemic Lupus Erythematosus","volume":"1","author":"Salemme","year":"2019","journal-title":"J. Cell. Immunol."},{"key":"ref_216","doi-asserted-by":"crossref","unstructured":"Chapman, E.A., Lyon, M., Simpson, D.M., Mason, D.N., Beynon, R.J., Moots, R.J., and Wright, H.L. (2019). Caught in a Trap? Proteomic analysis of neutrophil extracellular traps in rheumatoid arthritis and systemic lupus erythematosus. Front. Immunol., 10.","DOI":"10.3389\/fimmu.2019.00423"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/s41584-018-0039-z","article-title":"The role of neutrophil extracellular traps in rheumatic diseases","volume":"14","author":"Apel","year":"2018","journal-title":"Nat. Rev. Rheumatol."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.celrep.2013.12.017","article-title":"Mutation of POLB causes lupus in mice","volume":"6","author":"Senejani","year":"2014","journal-title":"Cell Rep."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1038\/cr.2007.115","article-title":"Mechanisms and functions of DNA mismatch repair","volume":"18","author":"Li","year":"2008","journal-title":"Cell Res."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1038\/bjc.1998.116","article-title":"The effect of different chemotherapeutic agents on the enrichment of DNA mismatch repair-deficient tumour cells","volume":"77","author":"Fink","year":"1998","journal-title":"Br. J. Cancer"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"2285","DOI":"10.1158\/0008-5472.CAN-14-2278","article-title":"Optimizing a lupus autoantibody for targeted cancer therapy","volume":"75","author":"Noble","year":"2015","journal-title":"Cancer Res."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"356","DOI":"10.4049\/immunohorizons.2100091","article-title":"Inhibition of NETosis by a nuclear-penetrating anti-DNA autoantibody","volume":"6","author":"Chen","year":"2022","journal-title":"Immunohorizons"},{"key":"ref_223","doi-asserted-by":"crossref","unstructured":"Farhan, A., Hassan, G., Ali, S.H.L., Yousaf, Z., Shafique, K., Faisal, A., Younis, B.B., and Mirza, S. (2023). Spontaneous NETosis in diabetes: A role of hyperglycemia mediated ROS and autophagy. Front. Med., 10.","DOI":"10.3389\/fmed.2023.1076690"},{"key":"ref_224","doi-asserted-by":"crossref","unstructured":"Seydi, H., Nouri, K., Rezaei, N., Tamimi, A., Hassan, M., Mirzaei, H., and Vosough, M. (2023). Autophagy orchestrates resistance in hepatocellular carcinoma cells. Biomed. Pharmacother., 161.","DOI":"10.1016\/j.biopha.2023.114487"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/leu.2010.6","article-title":"\u03b3H2AX: A sensitive molecular marker of DNA damage and repair","volume":"24","author":"Mah","year":"2010","journal-title":"Leukemia"},{"key":"ref_226","first-page":"146","article-title":"H2 inhibits the formation of neutrophil extracellular traps","volume":"7","author":"Shirakawa","year":"2022","journal-title":"Basic Transl. Sci."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/s41514-018-0028-0","article-title":"Clampdown of inflammation in aging and anticancer therapies by limiting upregulation and activation of GPCR, CXCR4","volume":"4","author":"Nair","year":"2018","journal-title":"Npj Aging Mech. Dis."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1111\/imr.13157","article-title":"The emerging role for metabolism in fueling neutrophilic inflammation","volume":"314","author":"Morrison","year":"2023","journal-title":"Immunol. Rev."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"22174","DOI":"10.1074\/jbc.M115.640094","article-title":"A metabolic shift toward pentose phosphate pathway is necessary for amyloid fibril-and phorbol 12-myristate 13-acetate-induced neutrophil extracellular trap (NET) formation","volume":"290","author":"Azevedo","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1093\/jleuko\/qiae025","article-title":"Metabolic regulation of neutrophil functions in homeostasis and diseases","volume":"116","author":"Leblanc","year":"2024","journal-title":"J. Leukoc. Biol."},{"key":"ref_231","doi-asserted-by":"crossref","unstructured":"Rashida, Z., and Laxman, S. (2021). The pentose phosphate pathway and organization of metabolic networks enabling growth programs. Curr. Opin. Syst. Biol., 28.","DOI":"10.1016\/j.coisb.2021.100390"},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.devcel.2017.10.013","article-title":"Cell-cycle proteins control production of neutrophil extracellular traps","volume":"43","author":"Amulic","year":"2017","journal-title":"Dev. Cell"},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.dnarep.2009.11.002","article-title":"DNA polymerase \u03b2-dependent long patch base excision repair in living cells","volume":"9","author":"Asagoshi","year":"2010","journal-title":"DNA Repair"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.dnarep.2010.09.005","article-title":"Efficiency and fidelity of human DNA polymerases \u03bb and \u03b2 during gap-filling DNA synthesis","volume":"10","author":"Brown","year":"2011","journal-title":"DNA Repair"},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1038\/sj.onc.1202001","article-title":"Mammalian base excision repair by DNA polymerases \u03b4 and \u03b5","volume":"17","author":"Stucki","year":"1998","journal-title":"Oncogene"},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"1717","DOI":"10.1016\/j.neurobiolaging.2012.12.016","article-title":"Modulation of DNA base excision repair during neuronal differentiation","volume":"34","author":"Sykora","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/S1383-5742(97)00041-0","article-title":"Adduct formation, mutagenesis and nucleotide excision repair of DNA damage produced by reactive oxygen species and lipid peroxidation product","volume":"410","author":"Wallin","year":"1998","journal-title":"Mutat. Res. Rev. Mutat. Res."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"12806","DOI":"10.1073\/pnas.1917196117","article-title":"The 6-4 photoproduct is the trigger of UV-induced replication blockage and ATR activation","volume":"117","author":"Hung","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"2868","DOI":"10.1016\/j.celrep.2017.02.066","article-title":"Major roles for pyrimidine dimers, nucleotide excision repair, and ATR in the alternative splicing response to UV irradiation","volume":"18","author":"Munoz","year":"2017","journal-title":"Cell Rep."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/14\/10\/1307\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:14:08Z","timestamp":1760112848000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/14\/10\/1307"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,10,16]]},"references-count":239,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2024,10]]}},"alternative-id":["biom14101307"],"URL":"https:\/\/doi.org\/10.3390\/biom14101307","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,10,16]]}}}