Relevant bibliographies by topics / Peroxidasin

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Peroxidasin'

Author: Grafiati
Published: 2 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Peroxidasin"

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Bathish, Boushra, Martina Paumann-Page, Louise N. Paton, Anthony J. Kettle, and Christine C. Winterbourn. "Peroxidasin mediates bromination of tyrosine residues in the extracellular matrix." Journal of Biological Chemistry 295, no. 36 (2020): 12697–705. http://dx.doi.org/10.1074/jbc.ra120.014504.

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Peroxidasin is a heme peroxidase that oxidizes bromide to hypobromous acid (HOBr), a powerful oxidant that promotes the formation of the sulfilimine crosslink in collagen IV in basement membranes. We investigated whether HOBr released by peroxidasin leads to other oxidative modifications of proteins, particularly bromination of tyrosine residues, in peroxidasin-expressing PFHR9 cells. Using stable isotope dilution LC-MS/MS, we detected the formation of 3-bromotyrosine, a specific biomarker of HOBr-mediated protein modification. The level of 3-bromotyrosine in extracellular matrix proteins from
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McCall, A. Scott, Gautam Bhave, Vadim Pedchenko, et al. "Inhibitory Anti-Peroxidasin Antibodies in Pulmonary-Renal Syndromes." Journal of the American Society of Nephrology 29, no. 11 (2018): 2619–25. http://dx.doi.org/10.1681/asn.2018050519.

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BackgroundGoodpasture syndrome (GP) is a pulmonary-renal syndrome characterized by autoantibodies directed against the NC1 domains of collagen IV in the glomerular and alveolar basement membranes. Exposure of the cryptic epitope is thought to occur via disruption of sulfilimine crosslinks in the NC1 domain that are formed by peroxidasin-dependent production of hypobromous acid. Peroxidasin, a heme peroxidase, has significant structural overlap with myeloperoxidase (MPO), and MPO-ANCA is present both before and at GP diagnosis in some patients. We determined whether autoantibodies directed agai
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He, Cuiwen, Wenxin Song, Thomas A. Weston, et al. "Peroxidasin-mediated bromine enrichment of basement membranes." Proceedings of the National Academy of Sciences 117, no. 27 (2020): 15827–36. http://dx.doi.org/10.1073/pnas.2007749117.

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Bromine and peroxidasin (an extracellular peroxidase) are essential for generating sulfilimine cross-links between a methionine and a hydroxylysine within collagen IV, a basement membrane protein. The sulfilimine cross-links increase the structural integrity of basement membranes. The formation of sulfilimine cross-links depends on the ability of peroxidasin to use bromide and hydrogen peroxide substrates to produce hypobromous acid (HOBr). Once a sulfilimine cross-link is created, bromide is released into the extracellular space and becomes available for reutilization. Whether the HOBr genera
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Kovács, Hajnal A., Enikő Lázár, György Várady, Gábor Sirokmány, and Miklós Geiszt. "Characterization of the Proprotein Convertase-Mediated Processing of Peroxidasin and Peroxidasin-like Protein." Antioxidants 10, no. 10 (2021): 1565. http://dx.doi.org/10.3390/antiox10101565.

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Peroxidasin (PXDN) and peroxidasin-like protein (PXDNL) are members of the peroxidase-cyclooxygenase superfamily. PXDN functions in basement membrane synthesis by forming collagen IV crosslinks, while the function of PXDNL remains practically unknown. In this work, we characterized the post-translational proteolytic processing of PXDN and PXDNL. Using a novel knock-in mouse model, we demonstrate that the proteolytic cleavage of PXDN occurs in vivo. With the help of furin-specific siRNA we also demonstrate that the proprotein-convertase, furin participates in the proteolytic processing of PXDN.
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Paumann-Page, Martina, Christian Obinger, Christine C. Winterbourn, and Paul G. Furtmüller. "Peroxidasin Inhibition by Phloroglucinol and Other Peroxidase Inhibitors." Antioxidants 13, no. 1 (2023): 23. http://dx.doi.org/10.3390/antiox13010023.

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Human peroxidasin (PXDN) is a ubiquitous peroxidase enzyme expressed in most tissues in the body. PXDN represents an interesting therapeutic target for inhibition, as it plays a role in numerous pathologies, including cardiovascular disease, cancer and fibrosis. Like other peroxidases, PXDN generates hypohalous acids and free radical species, thereby facilitating oxidative modifications of numerous biomolecules. We have studied the inhibition of PXDN halogenation and peroxidase activity by phloroglucinol and 14 other peroxidase inhibitors. Although a number of compounds on their own potently i
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Arnhold, Jürgen, and Ernst Malle. "Halogenation Activity of Mammalian Heme Peroxidases." Antioxidants 11, no. 5 (2022): 890. http://dx.doi.org/10.3390/antiox11050890.

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Mammalian heme peroxidases are fascinating due to their unique peculiarity of oxidizing (pseudo)halides under physiologically relevant conditions. These proteins are able either to incorporate oxidized halides into substrates adjacent to the active site or to generate different oxidized (pseudo)halogenated species, which can take part in multiple (pseudo)halogenation and oxidation reactions with cell and tissue constituents. The present article reviews basic biochemical and redox mechanisms of (pseudo)halogenation activity as well as the physiological role of heme peroxidases. Thyroid peroxida
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Colon, Selene, Haiyan Luan, Yan Liu, Cameron Meyer, Leslie Gewin, and Gautam Bhave. "Peroxidasin and eosinophil peroxidase, but not myeloperoxidase, contribute to renal fibrosis in the murine unilateral ureteral obstruction model." American Journal of Physiology-Renal Physiology 316, no. 2 (2019): F360—F371. http://dx.doi.org/10.1152/ajprenal.00291.2018.

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Renal fibrosis is the pathological hallmark of chronic kidney disease (CKD) and manifests as glomerulosclerosis and tubulointerstitial fibrosis. Reactive oxygen species contribute significantly to renal inflammation and fibrosis, but most research has focused on superoxide and hydrogen peroxide (H2O2). The animal heme peroxidases myeloperoxidase (MPO), eosinophil peroxidase (EPX), and peroxidasin (PXDN) uniquely metabolize H2O2 into highly reactive and destructive hypohalous acids, such as hypobromous and hypochlorous acid. However, the role of these peroxidases and their downstream hypohalous
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Péterfi, Zalán, Zsuzsanna E. Tóth, Hajnal A. Kovács, et al. "Peroxidasin-like protein: a novel peroxidase homologue in the human heart." Cardiovascular Research 101, no. 3 (2013): 393–99. http://dx.doi.org/10.1093/cvr/cvt256.

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Brandes, R. P. "Vascular peroxidase 1/peroxidasin: a complex protein with a simple function?" Cardiovascular Research 91, no. 1 (2011): 1–2. http://dx.doi.org/10.1093/cvr/cvr120.

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Dempsey, Bianca, Litiele Cezar Cruz, Marcela Franco Mineiro, Railmara Pereira da Silva, and Flavia Carla Meotti. "Uric Acid Reacts with Peroxidasin, Decreases Collagen IV Crosslink, Impairs Human Endothelial Cell Migration and Adhesion." Antioxidants 11, no. 6 (2022): 1117. http://dx.doi.org/10.3390/antiox11061117.

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Uric acid is considered the main substrate for peroxidases in plasma. The oxidation of uric acid by human peroxidases generates urate free radical and urate hydroperoxide, which might affect endothelial function and explain, at least in part, the harmful effects of uric acid on the vascular system. Peroxidasin (PXDN), the most recent heme-peroxidase described in humans, catalyzes the formation of hypobromous acid, which mediates collagen IV crosslinks in the extracellular matrix. This enzyme has gained increasing scientific interest since it is associated with cardiovascular disease, cancer, a
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Dissertations / Theses on the topic "Peroxidasin"

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Gotenstein, Jennifer Rose. "PXN-2, a C. elegans homolog of the extracellular matrix peroxidase peroxidasin, is important for embryonic morphogenesis." Diss., [La Jolla] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p1469240.

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Thesis (M.S.)--University of California, San Diego, 2009.<br>Title from first page of PDF file (viewed Oct. 6, 2009). Available via ProQuest Digital Dissertations. Includes bibliographical references (p. 85-90).
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Yan, Xiaohe. "The role of peroxidasin and Bpr1b in eye development and diseases." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-173917.

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Yan, Xiaohe [Verfasser], and Anselm [Akademischer Betreuer] Kampik. "The role of peroxidasin and Bpr1b in eye development and diseases / Xiaohe Yan. Betreuer: Anselm Kampik." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2014. http://d-nb.info/1058322915/34.

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Lazzarotto, Fernanda. "Caracterização de um novo membro da superfamília de peroxidases não animais : ascorbato peroxidase-relacionada." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2015. http://hdl.handle.net/10183/131943.

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Peroxidases atuam catalisando a redução do peróxido de hidrogênio à água a fim de minimizar o dano celular e modular, direta ou indiretamente, respostas celulares dependentes da sinalização operada por esta espécie reativa de oxigênio. Análises prévias, feitas em bancos de dados de sequências genômicas, permitiram a identificação de uma nova heme peroxidase não-animal (ascorbato peroxidase-relacionada ou APx-R), a qual foi descrita pela primeira vez em 2011 em um estudo publicado pelo nosso grupo de pesquisa. O trabalho detalhado nos próximos capítulos desta tese teve como objetivo caracteriza
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Bartonek-Roxå, Eva. "Recombinant peroxidases and xylanases I. Cloning and production of a peroxidase from horseradish : II. Characterisation of functional domains of thermostable xylanases from Rhodothermus marinus /." Lund : Lund University, 1998. http://catalog.hathitrust.org/api/volumes/oclc/68945038.html.

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Sato, Shin. "Degradation of cis-1,4-polyisoprene rubbers by white rot fungi and manganese peroxidase-catalyzed lipid peroxidation." Kyoto University, 2005. http://hdl.handle.net/2433/78163.

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Kyoto University (京都大学)<br>0048<br>新制・課程博士<br>博士(農学)<br>甲第11635号<br>農博第1491号<br>新制||農||908(附属図書館)<br>学位論文||H17||N4028(農学部図書室)<br>UT51-2005-D384<br>京都大学大学院農学研究科応用生命科学専攻<br>(主査)教授 渡邊 隆司, 教授 島田 幹夫, 教授 東 順一<br>学位規則第4条第1項該当
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Cunha, Gina Gabriela Seabra. "Atividade peroxidativa de extratos enzimáticos obtidos a partir de cultivos de Ceriporiopsis subvermispora e sua relação com a degradação de lignina." Universidade de São Paulo, 2008. http://www.teses.usp.br/teses/disponiveis/97/97131/tde-20082013-164851/.

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Os fungos de decomposição branca são organismos capazes de degradar os materiais lignocelulósicos de maneira eficiente através de reações catalisadas por enzimas hidrolíticas e oxidativas ou ainda por meio de metabólitos de baixa massa molar que iniciam o processo degradativo. Ceriporiopsis subvermispora é um fungo de decomposição branca que se destaca como um dos mais seletivos na degradação da lignina, possuindo grande potencial de aplicação tecnológica. Este fungo é capaz de iniciar reações de peroxidação de lipídeos a partir da formação de íons Mn3+ oriundos da ação da enzima manganês pero
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Seidel, Julian [Verfasser], and Oliver [Akademischer Betreuer] Einsle. "Crystallographic and mutational studies of bacterial cytochrome c peroxidases = Kristallografische und Mutagenese-Studien an bakteriellen Cytochrom c Peroxidasesn." Freiburg : Universität, 2011. http://d-nb.info/1123468109/34.

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Ellis, Katie E. "Electron transfer and catalysis in bacterial diheme cytochrome c peroxidases and peroxidase paralogues: developing a structure function relationship." Thesis, Boston University, 2013. https://hdl.handle.net/2144/12754.

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Thesis (Ph.D.)--Boston University PLEASE NOTE: Boston University Libraries did not receive an Authorization To Manage form for this thesis or dissertation. It is therefore not openly accessible, though it may be available by request. If you are the author or principal advisor of this work and would like to request open access for it, please contact us at open-help@bu.edu. Thank you.<br>The major source of energy within aerobic orgamsms results from the direct reduction of molecular oxygen. This four-electron four-proton coupled reaction produces toxic intermediates before producing the beni
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Acebes, Serrano Sandra. "Rational enzyme engineering of heme peroxidases through biophysical and biochemical modeling." Doctoral thesis, Universitat de Barcelona, 2016. http://hdl.handle.net/10803/399735.

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Enzymes are proteins that catalyze biochemical reactions and their use report multiple advantages, as they can be very selective, low polluting (biodegradable), cheap and allow working in mild conditions compared with traditional non enzymatic processes. Despite their enormous benefits, their applications at the industrial level are still limited, mainly due to low productivity, low substrate tolerance (too specifics) and poor resistance to the industrial conditions, and for this reason, developing enhanced enzymes by means of enzyme engineering is a central research field nowadays. Notably, t
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Books on the topic "Peroxidasin"

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Johannes, Everse, Everse Kathleen E, and Grisham Matthew B, eds. Peroxidasesin chemistry and biology. CRC Press, 1991.

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Johannes, Everse, Everse Kathleen E, and Grisham Matthew B, eds. Peroxidases in chemistry and biology. CRC Press, 1991.

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Brian, Dunford H., and Dunford H. Brian, eds. Peroxidases and catalases: Biochemistry, biophysics, biotechnology, and physiology. 2nd ed. John Wiley & Sons, 2010.

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1933-, Pruitt Kenneth M., and Tenovuo Jorma O. 1949-, eds. The Lactoperoxidase system: Chemistry and biological significance. Dekker, 1985.

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Raven, Emma, and Brian Dunford, eds. Heme Peroxidases. Royal Society of Chemistry, 2015. http://dx.doi.org/10.1039/9781782622628.

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H, Esterbauer, and Cheeseman Kevin H, eds. Liquid peroxidation. Elsevier Scientific Publishers Ireland, 1987.

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Dunford, H. Brian. Heme peroxidases. John Wiley, 1999.

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Hawkins, Clare L., and William M. Nauseef. Mammalian Heme Peroxidases. CRC Press, 2021. http://dx.doi.org/10.1201/9781003212287.

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Torres, Eduardo, and Marcela Ayala, eds. Biocatalysis Based on Heme Peroxidases. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-12627-7.

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Nigam, Santosh K., David C. H. McBrien, and Trevor F. Slater, eds. Eicosanoids, Lipid Peroxidation and Cancer. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73424-3.

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Book chapters on the topic "Peroxidasin"

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Sirokmány, Gábor, Hajnal A. Kovács, and Miklós Geiszt. "Peroxidasin: Structure and Function." In Mammalian Heme Peroxidases. CRC Press, 2021. http://dx.doi.org/10.1201/9781003212287-4.

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Bhave, Gautam. "Role of Peroxidasin in Disease." In Mammalian Heme Peroxidases. CRC Press, 2021. http://dx.doi.org/10.1201/9781003212287-21.

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Dosoretz, Carlos G., and Gary Ward. "Peroxidases." In Enzyme Technology. Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-35141-4_21.

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Stohs, S. J., Z. F. Al-Bayati, M. Q. Hassan, W. J. Murray, and H. A. Mohammadpour. "Glutathione Peroxidase and Reactive Oxygen Species in TCDD-Induced Lipid Peroxidation." In Biological Reactive Intermediates III. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5134-4_33.

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Schomburg, D., M. Salzmann, and D. Stephan. "Peroxidase." In Enzyme Handbook 7. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_142.

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Stellmach, Bruno. "Peroxidase." In Bestimmungsmethoden Enzyme. Steinkopff, 1988. http://dx.doi.org/10.1007/978-3-642-93668-5_28.

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Pike, Daniel P., and David A. Ford. "Reactivity of Peroxidase Oxidants with Lipids: The Generation of Biologically Important Modified Lipids." In Mammalian Heme Peroxidases. CRC Press, 2021. http://dx.doi.org/10.1201/9781003212287-8.

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Furtmüller, Paul G., Marcel Zámocký, Stefan Hofbauer, and Christian Obinger. "Evolution, Structure and Biochemistry of Human Peroxidases." In Mammalian Heme Peroxidases. CRC Press, 2021. http://dx.doi.org/10.1201/9781003212287-2.

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Mehrkens, Dennis, Simon Geißen, Stephan Baldus, and Volker Rudolph. "Myeloperoxidase in Ischemic Heart Disease." In Mammalian Heme Peroxidases. CRC Press, 2021. http://dx.doi.org/10.1201/9781003212287-18.

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Reynolds, Wanda F., and Richard A. Maki. "The Role of Myeloperoxidase in Neurodegenerative Disease." In Mammalian Heme Peroxidases. CRC Press, 2021. http://dx.doi.org/10.1201/9781003212287-19.

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Conference papers on the topic "Peroxidasin"

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Cheng, G., Z. Cao, G. Liu, and W. E. Swords. "Peroxidasin Deficiency and Exaggerated Inflammatory Response in the Lung." In American Thoracic Society 2022 International Conference, May 13-18, 2022 - San Francisco, CA. American Thoracic Society, 2022. http://dx.doi.org/10.1164/ajrccm-conference.2022.205.1_meetingabstracts.a2622.

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Woods, Keith. "Abstract 3011: The role of peroxidasin in human prostate cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3011.

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Maya, Anka, and Seregina Inga Ivanovna. "Peroxidase isoform activity in spring wheat grain under the influence of growth regulators." In III All-Russian Scientific Conference with International Participation "Science, technology, society: Environmental engineering for sustainable development of territories". Krasnoyarsk Science and Technology City Hall, 2022. http://dx.doi.org/10.47813/nto.3.2022.6.318-324.

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In laboratory experiments, the effect of various growth biological preparations on the activity of peroxidase isoforms in dormant seeds and during their germination was studied. In the experiment, at pH = 5.5, 7.0, 8.0, the activity of enzyme isoforms was determined using a phosphate-buffer system (1/15 M). The activity of isoforms of the peroxidase enzyme (by a method based on tyrosine peroxidation) was determined on dormant wheat grains (after ripening after harvesting) and germinated on the 3rd, 5th, and 7th days of germination. According to the research results, different effects of the bi
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Caus, Maria, Alexandru Dascaliuc, and Pantelimon Borozan. "Activitatea catalazei, peroxidazei și peroxidării lipidelor în rădăcinile porumbului sub influența șocului termic și a reglalgului." In Scientific International Symposium "Plant Protection – Achievements and Perspectives". Institute of Genetics, Physiology and Plant Protection, Republic of Moldova, 2023. http://dx.doi.org/10.53040/ppap2023.44.

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In recent years, due to the climate changes, the growth and development of corn is affected by heat stress, especially at an early stage of ontogeny. Influence of biostimulant Reglalg, used for seed pretreatment of maize hybrids Por. 310 and Por. 374 before exposure to heat shock (HS) at 50°C for 30 min, on catalase (CAT), peroxidase (PO), and lipid peroxidation (LPO) of root seedlings was studied. Compared to the Reglalg variants, root growth of control seedlings was more strongly affected by HS, since the activity levels of CAT, PO and MDA content in the roots were higher. This demonstrates
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Schaffer, W. M., and T. V. Bronnikova. "Modeling Peroxidase-Oxidase Interactions." In ASME 2011 Dynamic Systems and Control Conference and Bath/ASME Symposium on Fluid Power and Motion Control. ASMEDC, 2011. http://dx.doi.org/10.1115/dscc2011-5946.

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Reactive oxygen species (ROS) and peroxidase-oxidase (PO) reactions are Janus-faced contributors to cellular metabolism. At low concentrations, reactive oxygen species serve as signaling molecules; at high concentrations, as destroyers of proteins, lipids and DNA. Correspondingly, PO reactions are both sources and consumers of ROS. In the present paper, we study a well-tested model of the PO reaction based on horseradish peroxidase chemistry. Our principal predictions are these: 1. Under hypoxia, the PO reaction can emit pulses of hydrogen peroxide at apparently arbitrarily long intervals. 2.
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Schneider, Claus. "Epoxide Formation During Lipid Peroxidation." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists’ Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.346.

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Sitter, Andrew J., Catherine M. Reczek, and James Terner. "Resonance Raman Spectroscopy Of Peroxidase Intermediates." In OE/LASE '89, edited by Fran Adar, James E. Griffiths, and Jeremy M. Lerner. SPIE, 1989. http://dx.doi.org/10.1117/12.951598.

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Gaidamauskaite, E., and R. Baronas. "Modelling A Peroxidase-Based Fluorescent Biosensor." In 22nd Conference on Modelling and Simulation. ECMS, 2008. http://dx.doi.org/10.7148/2008-0152.

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Chang-Cheng Gao, Xian-Feng Zou, Qiong Wu, Xing Chen, Li-Hong Zhang, and Li-Na Chen. "A novel micromolecule glutathione peroxidase mimic." In 2011 International Symposium on Information Technology in Medicine and Education (ITME 2011). IEEE, 2011. http://dx.doi.org/10.1109/itime.2011.6132096.

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Leksin, I. Yu, C. C. Gorina, and F. V. Minibaeva. "Lichen peroxidase genes: cloning, sequencing, analysis activity." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-260.

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Reports on the topic "Peroxidasin"

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Kanner, Joseph, Dennis Miller, Ido Bartov, John Kinsella, and Stella Harel. The Effect of Dietary Iron Level on Lipid Peroxidation of Muscle Food. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7604282.bard.

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Biological oxidations are almost exclusively metal ion-promoted reactions and in ths respect iron, being the most abundant, is the commonly involved. The effect of dietary iron levels on pork, turkey and chick muscle lipid peroxidation and various other related compounds were evaluated. Crossbred feeder pigs were fed to market weight on corn-soy rations containing either 62, 131 or 209 ppm iron. After slaughter, the muscles were dissected, cooked and stored at 4°C. Heavily fortifying swine rations with iron (&gt;200 ppm) increase nn-heme iron (NHI), thiobarbituric acid reactive substances (TBA
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Author, Not Given. (Characterization of lignin peroxidases from Phanerochaete). Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/6015628.

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Leibovitz, Brian. Ascorbic acid, lipid peroxidation, and aging. Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.2896.

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Arnold, Frances H. Expression and Directed Evolution of Peroxidase Enzymes. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada378502.

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Lagrimini, L. (Molecular characteristics of the lignin forming peroxidase). Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/7138283.

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Lagrimini, L. M. The molecular characterization of the lignin-forming peroxidase. Office of Scientific and Technical Information (OSTI), 1992. http://dx.doi.org/10.2172/5445343.

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Lagrimini, L. The molecular characterization of the lignin-forming peroxidase. Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/6367020.

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8

Handa, Avtar K., Yuval Eshdat, Avichai Perl, Bruce A. Watkins, Doron Holland, and David Levy. Enhancing Quality Attributes of Potato and Tomato by Modifying and Controlling their Oxidative Stress Outcome. United States Department of Agriculture, 2004. http://dx.doi.org/10.32747/2004.7586532.bard.

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Abstract:
General The final goal and overall objective of the current research has been to modify lipid hydroperoxidation in order to create desirable phenotypes in two important crops, potato and tomato, which normally are exposed to abiotic stress associated with such oxidation. The specific original objectives were: (i) the roles of lipoxygenase (LOX) and phospholipids hydroperoxide glutathione peroxidase (PHGPx) in regulating endogenous levels of lipid peroxidation in plant tissues; (ii) the effect of modified lipid peroxidation on fruit ripening, tuber quality, crop productivity and abiotic stress
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9

Stoyanova, Tsveta, Daniela Ivanova, Albena Alexandrova, and Stanislav Yanev. Interaction and Metabolism of N-Octylxanthate by Horseradish Peroxidase. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, 2019. http://dx.doi.org/10.7546/crabs.2019.04.06.

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10

Hodgson, K. M., and T. R. Lunsford. Testing of a Peroxidation Systems, Inc. perox-pure SSB-30. Office of Scientific and Technical Information (OSTI), 1994. http://dx.doi.org/10.2172/10173126.

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