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The role of peroxiredoxins in cancer.

Molecular and clinical oncology

Nicolussi A, D'Inzeo S, Capalbo C, Giannini G, Coppa A.
PMID: 28357082
Mol Clin Oncol. 2017 Feb;6(2):139-153. doi: 10.3892/mco.2017.1129. Epub 2017 Jan 10.

Peroxiredoxins (PRDXs) are a ubiquitously expressed family of small (22-27 kDa) non-seleno peroxidases that catalyze the peroxide reduction of H

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Nicolussi A, D'Inzeo S, Capalbo C, et al. The role of peroxiredoxins in cancer. Mol Clin Oncol. 2017;6(2):139-153doi: 10.3892/mco.2017.1129.
Nicolussi, A., D'Inzeo, S., Capalbo, C., Giannini, G., & Coppa, A. (2017). The role of peroxiredoxins in cancer. Molecular and clinical oncology, 6(2), 139-153. https://doi.org/10.3892/mco.2017.1129
Nicolussi, Arianna, et al. "The role of peroxiredoxins in cancer." Molecular and clinical oncology vol. 6,2 (2017): 139-153. doi: https://doi.org/10.3892/mco.2017.1129
Nicolussi A, D'Inzeo S, Capalbo C, Giannini G, Coppa A. The role of peroxiredoxins in cancer. Mol Clin Oncol. 2017 Feb;6(2):139-153. doi: 10.3892/mco.2017.1129. Epub 2017 Jan 10. PMID: 28357082; PMCID: PMC5351761.
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Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 Å resolution.

FEBS open bio

Singh RP, Singh A, Sirohi HV, Singh AK, Kaur P, Sharma S, Singh TP.
PMID: 27398304
FEBS Open Bio. 2016 Jun 14;6(7):640-50. doi: 10.1002/2211-5463.12051. eCollection 2016 Jul.

Lactoperoxidase (LPO, EC 1.11.1.7) is a member of the mammalian heme peroxidase family which also includes thyroid peroxidase (TPO). These two enzymes have a sequence homology of 76%. The structure of LPO is known but not that of TPO....

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Singh RP, Singh A, Sirohi HV, et al. Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 Å resolution. FEBS Open Bio. 2016;6(7):640-50doi: 10.1002/2211-5463.12051.
Singh, R. P., Singh, A., Sirohi, H. V., Singh, A. K., Kaur, P., Sharma, S., & Singh, T. P. (2016). Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 Å resolution. FEBS open bio, 6(7), 640-50. https://doi.org/10.1002/2211-5463.12051
Singh, Rashmi Prabha, et al. "Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 Å resolution." FEBS open bio vol. 6,7 (2016): 640-50. doi: https://doi.org/10.1002/2211-5463.12051
Singh RP, Singh A, Sirohi HV, Singh AK, Kaur P, Sharma S, Singh TP. Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 Å resolution. FEBS Open Bio. 2016 Jun 14;6(7):640-50. doi: 10.1002/2211-5463.12051. eCollection 2016 Jul. PMID: 27398304; PMCID: PMC4932444.
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Inhibition of growth and xylogenesis and promotion of vacuolation in prunus callus by the flavanone prunin.

Plant cell reports

Feucht W, Treutter D, Schmid P.
PMID: 24241596
Plant Cell Rep. 1988 May;7(3):189-92. doi: 10.1007/BF00269320.

Callus tissue of Prunus avium L. responded to supplied prunin (naringen in 7-glucoside) showing vaculoation and storage of oligomeric proanthocyanidins. In addition, prunin caused restricted callus initiation and/or less callus growth. When prunin was omitted from the medium numerous...

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Feucht W, Treutter D, Schmid P. Inhibition of growth and xylogenesis and promotion of vacuolation in prunus callus by the flavanone prunin. Plant Cell Rep. 1988;7(3):189-92doi: 10.1007/BF00269320.
Feucht, W., Treutter, D., & Schmid, P. (1988). Inhibition of growth and xylogenesis and promotion of vacuolation in prunus callus by the flavanone prunin. Plant cell reports, 7(3), 189-92. https://doi.org/10.1007/BF00269320
Feucht, W, et al. "Inhibition of growth and xylogenesis and promotion of vacuolation in prunus callus by the flavanone prunin." Plant cell reports vol. 7,3 (1988): 189-92. doi: https://doi.org/10.1007/BF00269320
Feucht W, Treutter D, Schmid P. Inhibition of growth and xylogenesis and promotion of vacuolation in prunus callus by the flavanone prunin. Plant Cell Rep. 1988 May;7(3):189-92. doi: 10.1007/BF00269320. PMID: 24241596.
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Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

van den Berg BM, Bianchi F, Wijsman HJ.
PMID: 24263194
Theor Appl Genet. 1983 Apr;65(1):1-8. doi: 10.1007/BF00276254.

In P. hybrida and the putative progenitor species P. axillaris s. l. and P. integrifolia s. l. five mobility alleles of the structural gene prxA were found. The five alleles show differential expression during development of tissue and plant,...

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van den Berg BM, Bianchi F, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles. Theor Appl Genet. 1983;65(1):1-8doi: 10.1007/BF00276254.
van den Berg, B. M., Bianchi, F., & Wijsman, H. J. (1983). Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 65(1), 1-8. https://doi.org/10.1007/BF00276254
van den Berg, B M, et al. "Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 65,1 (1983): 1-8. doi: https://doi.org/10.1007/BF00276254
van den Berg BM, Bianchi F, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : Part 5. Differential temporal expression of prxA alleles. Theor Appl Genet. 1983 Apr;65(1):1-8. doi: 10.1007/BF00276254. PMID: 24263194.
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Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

van den Berg BM, Bianchi F, Wijsman HJ.
PMID: 24258939
Theor Appl Genet. 1984 May;68(1):25-8. doi: 10.1007/BF00252306.

Two alleles of the structural gene prxA from Petunia, prxA6 and prxA7, could be identified by their differential temporal expression. The alleles prxA6 and prxA7 code for peroxidases with a similar electrophoretic mobility as the products of the previously...

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van den Berg BM, Bianchi F, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7. Theor Appl Genet. 1984;68(1):25-8doi: 10.1007/BF00252306.
van den Berg, B. M., Bianchi, F., & Wijsman, H. J. (1984). Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 68(1), 25-8. https://doi.org/10.1007/BF00252306
van den Berg, B M, et al. "Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 68,1 (1984): 25-8. doi: https://doi.org/10.1007/BF00252306
van den Berg BM, Bianchi F, Wijsman HJ. Genetics of the peroxidase isoenzymes in Petunia : 7. The alleles prxA6 and prxA7. Theor Appl Genet. 1984 May;68(1):25-8. doi: 10.1007/BF00252306. PMID: 24258939.
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Oxidative responses in soybean foliage to herbivory by bean leaf beetle and three-cornered alfalfa hopper.

Journal of chemical ecology

Felton GW, Summers CB, Mueller AJ.
PMID: 24242118
J Chem Ecol. 1994 Mar;20(3):639-50. doi: 10.1007/BF02059604.

Variation in induced responses in soybean is shown to be dependent, in part, upon herbivore species. Herbivory by the phloem-feeding three-cornered alfalfa hopper caused increases in the activities of several oxidative enzymes including lipoxygenases, peroxidases, ascorbate oxidase, and polyphenol...

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Felton GW, Summers CB, Mueller AJ. Oxidative responses in soybean foliage to herbivory by bean leaf beetle and three-cornered alfalfa hopper. J Chem Ecol. 1994;20(3):639-50doi: 10.1007/BF02059604.
Felton, G. W., Summers, C. B., & Mueller, A. J. (1994). Oxidative responses in soybean foliage to herbivory by bean leaf beetle and three-cornered alfalfa hopper. Journal of chemical ecology, 20(3), 639-50. https://doi.org/10.1007/BF02059604
Felton, G W, et al. "Oxidative responses in soybean foliage to herbivory by bean leaf beetle and three-cornered alfalfa hopper." Journal of chemical ecology vol. 20,3 (1994): 639-50. doi: https://doi.org/10.1007/BF02059604
Felton GW, Summers CB, Mueller AJ. Oxidative responses in soybean foliage to herbivory by bean leaf beetle and three-cornered alfalfa hopper. J Chem Ecol. 1994 Mar;20(3):639-50. doi: 10.1007/BF02059604. PMID: 24242118.
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A comparative study on variability and phylogeny of Triticum species : 1. Intraspecific variability.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Asins MJ, Carbonell EA.
PMID: 24248031
Theor Appl Genet. 1986 Jul;72(4):551-8. doi: 10.1007/BF00289540.

Intraspecific variability of A, S and D genome diploid species and AAGG and AABB allotetraploid species of the genus Triticum was examined in a comparative study using isoenzymatic characters (peroxidases of embryo plus scutellum, and endosperm; and alkaline phosphatases)...

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Asins MJ, Carbonell EA. A comparative study on variability and phylogeny of Triticum species : 1. Intraspecific variability. Theor Appl Genet. 1986;72(4):551-8doi: 10.1007/BF00289540.
Asins, M. J., & Carbonell, E. A. (1986). A comparative study on variability and phylogeny of Triticum species : 1. Intraspecific variability. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 72(4), 551-8. https://doi.org/10.1007/BF00289540
Asins, M J, and Carbonell, E A. "A comparative study on variability and phylogeny of Triticum species : 1. Intraspecific variability." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 72,4 (1986): 551-8. doi: https://doi.org/10.1007/BF00289540
Asins MJ, Carbonell EA. A comparative study on variability and phylogeny of Triticum species : 1. Intraspecific variability. Theor Appl Genet. 1986 Jul;72(4):551-8. doi: 10.1007/BF00289540. PMID: 24248031.
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Cellobiose dehydrogenase-an extracellular fungal flavocytochrome.

Enzyme and microbial technology

Cameron MD, Aust SD.
PMID: 11166803
Enzyme Microb Technol. 2001 Feb 01;28(2):129-138. doi: 10.1016/s0141-0229(00)00307-0.

Wood-degrading fungi, including white-rot and soft-rot fungi as well as at least one brown-rot fungus, produce cellobiose dehydrogenase (CDH). CDH has generated recent interest because of its ability to facilitate the formation of free radicals and because it makes...

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Cameron MD, Aust SD. Cellobiose dehydrogenase-an extracellular fungal flavocytochrome. Enzyme Microb Technol. 2001;28(2):129-138doi: 10.1016/s0141-0229(00)00307-0.
Cameron, M. D., & Aust, S. D. (2001). Cellobiose dehydrogenase-an extracellular fungal flavocytochrome. Enzyme and microbial technology, 28(2), 129-138. https://doi.org/10.1016/s0141-0229(00)00307-0
Cameron, M D., and Aust, S D.. "Cellobiose dehydrogenase-an extracellular fungal flavocytochrome." Enzyme and microbial technology vol. 28,2 (2001): 129-138. doi: https://doi.org/10.1016/s0141-0229(00)00307-0
Cameron MD, Aust SD. Cellobiose dehydrogenase-an extracellular fungal flavocytochrome. Enzyme Microb Technol. 2001 Feb 01;28(2):129-138. doi: 10.1016/s0141-0229(00)00307-0. PMID: 11166803.
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Purification and characterization of a novel bromoperoxidase-catalase isolated from bacteria found in recycled pulp white water.

Enzyme and microbial technology

Kuusk H, Björklund M, Rydström J.
PMID: 11339944
Enzyme Microb Technol. 2001 May 07;28(7):617-624. doi: 10.1016/s0141-0229(01)00305-2.

A bacterial strain, Pseudomonad EF group 70B, containing a high catalase-like activity was found in process water (white water) from pulp using recycled fibers. The enzyme was purified and characterized, and found to be a hydroperoxidase. The active enzyme...

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Kuusk H, Björklund M, Rydström J. Purification and characterization of a novel bromoperoxidase-catalase isolated from bacteria found in recycled pulp white water. Enzyme Microb Technol. 2001;28(7):617-624doi: 10.1016/s0141-0229(01)00305-2.
Kuusk, H., Björklund, M., & Rydström, J. (2001). Purification and characterization of a novel bromoperoxidase-catalase isolated from bacteria found in recycled pulp white water. Enzyme and microbial technology, 28(7), 617-624. https://doi.org/10.1016/s0141-0229(01)00305-2
Kuusk, H, et al. "Purification and characterization of a novel bromoperoxidase-catalase isolated from bacteria found in recycled pulp white water." Enzyme and microbial technology vol. 28,7 (2001): 617-624. doi: https://doi.org/10.1016/s0141-0229(01)00305-2
Kuusk H, Björklund M, Rydström J. Purification and characterization of a novel bromoperoxidase-catalase isolated from bacteria found in recycled pulp white water. Enzyme Microb Technol. 2001 May 07;28(7):617-624. doi: 10.1016/s0141-0229(01)00305-2. PMID: 11339944.
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Effect of interfering substances on current response of recombinant peroxidase and glucose oxidase-recombinant peroxidase modified graphite electrodes.

The Analyst

Dock E, Lindgren A, Ruzgas T, Gorton L.
PMID: 11763069
Analyst. 2001 Nov;126(11):1929-35. doi: 10.1039/b104815p.

Graphite electrodes have been modified with different forms of horseradish peroxidase (HRP). These included native HRP, wild-type recombinant HRP, and two single-point recombinant HRP mutants, N70V and N70D. The mediator-less response of these electrodes to H2O2 was studied indicating...

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Dock E, Lindgren A, Ruzgas T, et al. Effect of interfering substances on current response of recombinant peroxidase and glucose oxidase-recombinant peroxidase modified graphite electrodes. Analyst. 2001;126(11):1929-35doi: 10.1039/b104815p.
Dock, E., Lindgren, A., Ruzgas, T., & Gorton, L. (2001). Effect of interfering substances on current response of recombinant peroxidase and glucose oxidase-recombinant peroxidase modified graphite electrodes. The Analyst, 126(11), 1929-35. https://doi.org/10.1039/b104815p
Dock, E, et al. "Effect of interfering substances on current response of recombinant peroxidase and glucose oxidase-recombinant peroxidase modified graphite electrodes." The Analyst vol. 126,11 (2001): 1929-35. doi: https://doi.org/10.1039/b104815p
Dock E, Lindgren A, Ruzgas T, Gorton L. Effect of interfering substances on current response of recombinant peroxidase and glucose oxidase-recombinant peroxidase modified graphite electrodes. Analyst. 2001 Nov;126(11):1929-35. doi: 10.1039/b104815p. PMID: 11763069.
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Localization and Characterization of Peroxidases in the Mitochondria of Chilling-Acclimated Maize Seedlings.

Plant physiology

Prasad TK, Anderson MD, Stewart CR.
PMID: 12228565
Plant Physiol. 1995 Aug;108(4):1597-1605. doi: 10.1104/pp.108.4.1597.

We present evidence of two peroxidases in maize (Zea mays L.) mitochondria. One of these uses guaiacol and the other uses cytochrome c as the electron donor. Treatments of fresh mitochondria with protease(s) indicate that ascorbate and glutathione peroxidases...

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Prasad TK, Anderson MD, Stewart CR. Localization and Characterization of Peroxidases in the Mitochondria of Chilling-Acclimated Maize Seedlings. Plant Physiol. 1995;108(4):1597-1605doi: 10.1104/pp.108.4.1597.
Prasad, T. K., Anderson, M. D., & Stewart, C. R. (1995). Localization and Characterization of Peroxidases in the Mitochondria of Chilling-Acclimated Maize Seedlings. Plant physiology, 108(4), 1597-1605. https://doi.org/10.1104/pp.108.4.1597
Prasad, T. K., et al. "Localization and Characterization of Peroxidases in the Mitochondria of Chilling-Acclimated Maize Seedlings." Plant physiology vol. 108,4 (1995): 1597-1605. doi: https://doi.org/10.1104/pp.108.4.1597
Prasad TK, Anderson MD, Stewart CR. Localization and Characterization of Peroxidases in the Mitochondria of Chilling-Acclimated Maize Seedlings. Plant Physiol. 1995 Aug;108(4):1597-1605. doi: 10.1104/pp.108.4.1597. PMID: 12228565; PMCID: PMC157540.
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Changes in Dehydrodiferulic Acids and Peroxidase Activity against Ferulic Acid Associated with Cell Walls during Growth of Pinus pinaster Hypocotyl.

Plant physiology

Sanchez M, Pena MJ, Revilla G, Zarra I.
PMID: 12226339
Plant Physiol. 1996 Jul;111(3):941-946. doi: 10.1104/pp.111.3.941.

Hydroxycinnamic acids associated with hypocotyl cell walls of dark-grown seedlings of Pinus pinaster Aiton were extracted with 1 N NaOH and identified by gas chromatography-mass spectrometry. The main hydroxycinnamic acid found was ferulic acid. Diferulic acid dehydrodimers were also...

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Sanchez M, Pena MJ, Revilla G, et al. Changes in Dehydrodiferulic Acids and Peroxidase Activity against Ferulic Acid Associated with Cell Walls during Growth of Pinus pinaster Hypocotyl. Plant Physiol. 1996;111(3):941-946doi: 10.1104/pp.111.3.941.
Sanchez, M., Pena, M. J., Revilla, G., & Zarra, I. (1996). Changes in Dehydrodiferulic Acids and Peroxidase Activity against Ferulic Acid Associated with Cell Walls during Growth of Pinus pinaster Hypocotyl. Plant physiology, 111(3), 941-946. https://doi.org/10.1104/pp.111.3.941
Sanchez, M., et al. "Changes in Dehydrodiferulic Acids and Peroxidase Activity against Ferulic Acid Associated with Cell Walls during Growth of Pinus pinaster Hypocotyl." Plant physiology vol. 111,3 (1996): 941-946. doi: https://doi.org/10.1104/pp.111.3.941
Sanchez M, Pena MJ, Revilla G, Zarra I. Changes in Dehydrodiferulic Acids and Peroxidase Activity against Ferulic Acid Associated with Cell Walls during Growth of Pinus pinaster Hypocotyl. Plant Physiol. 1996 Jul;111(3):941-946. doi: 10.1104/pp.111.3.941. PMID: 12226339; PMCID: PMC157913.
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