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Erratum(a).

Free radical biology & medicine

[No authors listed]
PMID: 11020670
Free Radic Biol Med. 2000 Sep 01;29(5):486.

No abstract available.

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Erratum(a). Free Radic Biol Med. 2000;29(5):486
(2000). Erratum(a). Free radical biology & medicine, 29(5), 486.
"Erratum(a)." Free radical biology & medicine vol. 29,5 (2000): 486.
Erratum(a). Free Radic Biol Med. 2000 Sep 01;29(5):486. PMID: 11020670.
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FORUM: oxidation and atherosclerosis.

Free radical biology & medicine

Pryor WA.
PMID: 10946208
Free Radic Biol Med. 2000 Jun 15;28(12):1681-2. doi: 10.1016/s0891-5849(00)00356-7.

No abstract available.

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Pryor WA. FORUM: oxidation and atherosclerosis. Free Radic Biol Med. 2000;28(12):1681-2doi: 10.1016/s0891-5849(00)00356-7.
Pryor, W. A. (2000). FORUM: oxidation and atherosclerosis. Free radical biology & medicine, 28(12), 1681-2. https://doi.org/10.1016/s0891-5849(00)00356-7
Pryor. "FORUM: oxidation and atherosclerosis." Free radical biology & medicine vol. 28,12 (2000): 1681-2. doi: https://doi.org/10.1016/s0891-5849(00)00356-7
Pryor WA. FORUM: oxidation and atherosclerosis. Free Radic Biol Med. 2000 Jun 15;28(12):1681-2. doi: 10.1016/s0891-5849(00)00356-7. PMID: 10946208.
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Oxidation and atherosclerosis.

Free radical biology & medicine

Hazen SL.
PMID: 10946209
Free Radic Biol Med. 2000 Jun 15;28(12):1683-4. doi: 10.1016/s0891-5849(00)00355-5.

No abstract available.

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Hazen SL. Oxidation and atherosclerosis. Free Radic Biol Med. 2000;28(12):1683-4doi: 10.1016/s0891-5849(00)00355-5.
Hazen, S. L. (2000). Oxidation and atherosclerosis. Free radical biology & medicine, 28(12), 1683-4. https://doi.org/10.1016/s0891-5849(00)00355-5
Hazen. "Oxidation and atherosclerosis." Free radical biology & medicine vol. 28,12 (2000): 1683-4. doi: https://doi.org/10.1016/s0891-5849(00)00355-5
Hazen SL. Oxidation and atherosclerosis. Free Radic Biol Med. 2000 Jun 15;28(12):1683-4. doi: 10.1016/s0891-5849(00)00355-5. PMID: 10946209.
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WITHDRAWN: Antioxidants-GRABbing new headlines.

Free radical biology & medicine

Jay Forman H, Traber M, Ursini F.
PMID: 24075892
Free Radic Biol Med. 2013 Sep 26; doi: 10.1016/j.freeradbiomed.2013.09.018. Epub 2013 Sep 26.

The Publisher regrets that this article is an accidental duplication of an article that has already been published, 10.1016/j.freeradbiomed.2013.09.018. The duplicate article has therefore been withdrawn.

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Jay Forman H, Traber M, Ursini F. WITHDRAWN: Antioxidants-GRABbing new headlines. Free Radic Biol Med. 2013;doi: 10.1016/j.freeradbiomed.2013.09.018.
Jay Forman, H., Traber, M., & Ursini, F. (2013). WITHDRAWN: Antioxidants-GRABbing new headlines. Free radical biology & medicine, . https://doi.org/10.1016/j.freeradbiomed.2013.09.018
Jay Forman, Henry, et al. "WITHDRAWN: Antioxidants-GRABbing new headlines." Free radical biology & medicine vol. (2013). doi: https://doi.org/10.1016/j.freeradbiomed.2013.09.018
Jay Forman H, Traber M, Ursini F. WITHDRAWN: Antioxidants-GRABbing new headlines. Free Radic Biol Med. 2013 Sep 26; doi: 10.1016/j.freeradbiomed.2013.09.018. Epub 2013 Sep 26. PMID: 24075892.
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Nrf2-mediated redox signalling in vascular health and disease.

Free radical biology & medicine

Mann GE.
PMID: 26461277
Free Radic Biol Med. 2014 Oct;75:S1. doi: 10.1016/j.freeradbiomed.2014.10.595. Epub 2014 Dec 10.

Cells have evolved endogenous defence mechanisms to counteract oxidative stress, and the redox sensitive transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2) plays a key role in the defence against oxidative stress via the induction of phase II...

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Mann GE. Nrf2-mediated redox signalling in vascular health and disease. Free Radic Biol Med. 2014;75:S1doi: 10.1016/j.freeradbiomed.2014.10.595.
Mann, G. E. (2014). Nrf2-mediated redox signalling in vascular health and disease. Free radical biology & medicine, 75S1. https://doi.org/10.1016/j.freeradbiomed.2014.10.595
Mann, Giovanni E. "Nrf2-mediated redox signalling in vascular health and disease." Free radical biology & medicine vol. 75 (2014): S1. doi: https://doi.org/10.1016/j.freeradbiomed.2014.10.595
Mann GE. Nrf2-mediated redox signalling in vascular health and disease. Free Radic Biol Med. 2014 Oct;75:S1. doi: 10.1016/j.freeradbiomed.2014.10.595. Epub 2014 Dec 10. PMID: 26461277.
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CD36 as a biomarker of atherosclerosis.

Free radical biology & medicine

Yazgan B, Ustunsoy S, Karademir B, Kartal-Ozer N.
PMID: 26461278
Free Radic Biol Med. 2014 Oct;75:S10. doi: 10.1016/j.freeradbiomed.2014.10.852. Epub 2014 Dec 10.

Atherosclerosis is a chronic inflammatory disorder occurs as a result of mononuclear lymphocyte infiltration to the arterial wall accompanied by smooth muscle cell proliferation and damage in the arterial wall caused by extracellular matrix accumulation. Besides several genetic and...

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Yazgan B, Ustunsoy S, Karademir B, et al. CD36 as a biomarker of atherosclerosis. Free Radic Biol Med. 2014;75:S10doi: 10.1016/j.freeradbiomed.2014.10.852.
Yazgan, B., Ustunsoy, S., Karademir, B., & Kartal-Ozer, N. (2014). CD36 as a biomarker of atherosclerosis. Free radical biology & medicine, 75S10. https://doi.org/10.1016/j.freeradbiomed.2014.10.852
Yazgan, Burak, et al. "CD36 as a biomarker of atherosclerosis." Free radical biology & medicine vol. 75 (2014): S10. doi: https://doi.org/10.1016/j.freeradbiomed.2014.10.852
Yazgan B, Ustunsoy S, Karademir B, Kartal-Ozer N. CD36 as a biomarker of atherosclerosis. Free Radic Biol Med. 2014 Oct;75:S10. doi: 10.1016/j.freeradbiomed.2014.10.852. Epub 2014 Dec 10. PMID: 26461278.
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Skin protection against dicarbonyl stress by the glyoxalase system.

Free radical biology & medicine

Sabrina R, Emmanuelle L, Sylvianne S, Carine N, Bertrand F, Isabelle P.
PMID: 26461301
Free Radic Biol Med. 2014 Oct;75:S19-20. doi: 10.1016/j.freeradbiomed.2014.10.635. Epub 2014 Dec 10.

Skin ageing is the result of intrinsic and photo-ageing, due to UV exposure, that both share important molecular features including alterations of proteins. Indeed, proteins can be modified by many molecular processes such as glycation. Glycation occurs when glucose...

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Sabrina R, Emmanuelle L, Sylvianne S, et al. Skin protection against dicarbonyl stress by the glyoxalase system. Free Radic Biol Med. 2014;75:S19-20doi: 10.1016/j.freeradbiomed.2014.10.635.
Sabrina, R., Emmanuelle, L., Sylvianne, S., Carine, N., Bertrand, F., & Isabelle, P. (2014). Skin protection against dicarbonyl stress by the glyoxalase system. Free radical biology & medicine, 75S19-20. https://doi.org/10.1016/j.freeradbiomed.2014.10.635
Sabrina, Radjei, et al. "Skin protection against dicarbonyl stress by the glyoxalase system." Free radical biology & medicine vol. 75 (2014): S19-20. doi: https://doi.org/10.1016/j.freeradbiomed.2014.10.635
Sabrina R, Emmanuelle L, Sylvianne S, Carine N, Bertrand F, Isabelle P. Skin protection against dicarbonyl stress by the glyoxalase system. Free Radic Biol Med. 2014 Oct;75:S19-20. doi: 10.1016/j.freeradbiomed.2014.10.635. Epub 2014 Dec 10. PMID: 26461301.
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Changes in glutathione-dependent redox status and mitochondrial energetic strategies are part of the adaptive response during the filamentation process in Candida albicans.

Free radical biology & medicine

Hala G, Rachel G, Arthur B, Océane V, Anne-Laure B, Jean-Michel C, Françoise A.
PMID: 26461308
Free Radic Biol Med. 2014 Oct;75:S22. doi: 10.1016/j.freeradbiomed.2014.10.736. Epub 2014 Dec 10.

Candia albicans is an opportunist pathogen responsible for a large spectrum of infections, from superficial mycosis to systemic diseases called candidiasis. Its ability to grow in various morphological forms, such as unicellular budding yeast, filamentous pseudohyphae and hyphae, contributes...

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Hala G, Rachel G, Arthur B, et al. Changes in glutathione-dependent redox status and mitochondrial energetic strategies are part of the adaptive response during the filamentation process in Candida albicans. Free Radic Biol Med. 2014;75:S22doi: 10.1016/j.freeradbiomed.2014.10.736.
Hala, G., Rachel, G., Arthur, B., Océane, V., Anne-Laure, B., Jean-Michel, C., & Françoise, A. (2014). Changes in glutathione-dependent redox status and mitochondrial energetic strategies are part of the adaptive response during the filamentation process in Candida albicans. Free radical biology & medicine, 75S22. https://doi.org/10.1016/j.freeradbiomed.2014.10.736
Hala, Guedouari, et al. "Changes in glutathione-dependent redox status and mitochondrial energetic strategies are part of the adaptive response during the filamentation process in Candida albicans." Free radical biology & medicine vol. 75 (2014): S22. doi: https://doi.org/10.1016/j.freeradbiomed.2014.10.736
Hala G, Rachel G, Arthur B, Océane V, Anne-Laure B, Jean-Michel C, Françoise A. Changes in glutathione-dependent redox status and mitochondrial energetic strategies are part of the adaptive response during the filamentation process in Candida albicans. Free Radic Biol Med. 2014 Oct;75:S22. doi: 10.1016/j.freeradbiomed.2014.10.736. Epub 2014 Dec 10. PMID: 26461308.
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Vismia cauliflora extracts: bioactive compounds and the in vitro scavenging capacity against reactive oxygen and nitrogen species.

Free radical biology & medicine

Chist RC, Ribeiro AB, Berto A, Freitas M, Visentainer JV, Fernandes E.
PMID: 26461320
Free Radic Biol Med. 2014 Oct;75:S26. doi: 10.1016/j.freeradbiomed.2014.10.748. Epub 2014 Dec 10.

Vismia cauliflora, a scientific unexploited plant from Amazonian forest, used by Amerindians to treat dermatosis and inflammatory processes in the skin may be considered an interesting source of bioactive compounds. Thus, we evaluated for the first time in literature,...

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Chist RC, Ribeiro AB, Berto A, et al. Vismia cauliflora extracts: bioactive compounds and the in vitro scavenging capacity against reactive oxygen and nitrogen species. Free Radic Biol Med. 2014;75:S26doi: 10.1016/j.freeradbiomed.2014.10.748.
Chist, R. C., Ribeiro, A. B., Berto, A., Freitas, M., Visentainer, J. V., & Fernandes, E. (2014). Vismia cauliflora extracts: bioactive compounds and the in vitro scavenging capacity against reactive oxygen and nitrogen species. Free radical biology & medicine, 75S26. https://doi.org/10.1016/j.freeradbiomed.2014.10.748
Chist, Renan Campos, et al. "Vismia cauliflora extracts: bioactive compounds and the in vitro scavenging capacity against reactive oxygen and nitrogen species." Free radical biology & medicine vol. 75 (2014): S26. doi: https://doi.org/10.1016/j.freeradbiomed.2014.10.748
Chist RC, Ribeiro AB, Berto A, Freitas M, Visentainer JV, Fernandes E. Vismia cauliflora extracts: bioactive compounds and the in vitro scavenging capacity against reactive oxygen and nitrogen species. Free Radic Biol Med. 2014 Oct;75:S26. doi: 10.1016/j.freeradbiomed.2014.10.748. Epub 2014 Dec 10. PMID: 26461320.
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Quantification of Carnosine-Aldehyde Adducts in Human Urine.

Free radical biology & medicine

da Silva Bispo V, Di Mascio P, Medeiros M.
PMID: 26461323
Free Radic Biol Med. 2014 Oct;75:S27. doi: 10.1016/j.freeradbiomed.2014.10.751. Epub 2014 Dec 10.

Lipid peroxidation generates several reactive carbonyl species, including 4-hydroxy-2-nonenal (HNE), acrolein (ACR), 4-hydroxy-2-hexenal (HHE) and malondialdehyde. One major pathwayof aldehydes detoxification is through conjugation with glutathione catalyzed by glutathione-S-transferases or, alternatively, by conjugation with endogenous histidine containing dipeptides, such...

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da Silva Bispo V, Di Mascio P, Medeiros M. Quantification of Carnosine-Aldehyde Adducts in Human Urine. Free Radic Biol Med. 2014;75:S27doi: 10.1016/j.freeradbiomed.2014.10.751.
da Silva Bispo, V., Di Mascio, P., & Medeiros, M. (2014). Quantification of Carnosine-Aldehyde Adducts in Human Urine. Free radical biology & medicine, 75S27. https://doi.org/10.1016/j.freeradbiomed.2014.10.751
da Silva Bispo, Vanderson, et al. "Quantification of Carnosine-Aldehyde Adducts in Human Urine." Free radical biology & medicine vol. 75 (2014): S27. doi: https://doi.org/10.1016/j.freeradbiomed.2014.10.751
da Silva Bispo V, Di Mascio P, Medeiros M. Quantification of Carnosine-Aldehyde Adducts in Human Urine. Free Radic Biol Med. 2014 Oct;75:S27. doi: 10.1016/j.freeradbiomed.2014.10.751. Epub 2014 Dec 10. PMID: 26461323.
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Disruption of the iron-sulfur cluster of aconitase by myeloperoxidase-derived oxidants.

Free radical biology & medicine

Talib J, Cook N, Pattison D, Davies M.
PMID: 26461324
Free Radic Biol Med. 2014 Oct;75:S27-8. doi: 10.1016/j.freeradbiomed.2014.10.752. Epub 2014 Dec 10.

Oxidative damage catalysed by the heme enzyme myeloperoxidase (MPO) has been linked with multiple inflammatory pathologies. The major oxidant species generated by MPO are hypochlorous (HOCl) and hypothiocyanous acids (HOSCN). The damage induced by HOCl is well characterized and...

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Talib J, Cook N, Pattison D, et al. Disruption of the iron-sulfur cluster of aconitase by myeloperoxidase-derived oxidants. Free Radic Biol Med. 2014;75:S27-8doi: 10.1016/j.freeradbiomed.2014.10.752.
Talib, J., Cook, N., Pattison, D., & Davies, M. (2014). Disruption of the iron-sulfur cluster of aconitase by myeloperoxidase-derived oxidants. Free radical biology & medicine, 75S27-8. https://doi.org/10.1016/j.freeradbiomed.2014.10.752
Talib, Jihan, et al. "Disruption of the iron-sulfur cluster of aconitase by myeloperoxidase-derived oxidants." Free radical biology & medicine vol. 75 (2014): S27-8. doi: https://doi.org/10.1016/j.freeradbiomed.2014.10.752
Talib J, Cook N, Pattison D, Davies M. Disruption of the iron-sulfur cluster of aconitase by myeloperoxidase-derived oxidants. Free Radic Biol Med. 2014 Oct;75:S27-8. doi: 10.1016/j.freeradbiomed.2014.10.752. Epub 2014 Dec 10. PMID: 26461324.
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Effect of novel 1-phenyl-3-methyl-4-acylpyrazolones on iron chelation and Fenton reaction.

Free radical biology & medicine

Filipský T, Mladenka P, Macáková K, Hrdina R, Saso L, Marchetti F, Pettinari C.
PMID: 26461329
Free Radic Biol Med. 2014 Oct;75:S29-30. doi: 10.1016/j.freeradbiomed.2014.10.758. Epub 2014 Dec 10.

Iron is an essential element in many physiological processes due to its ability to easily convert between two oxidation states Fe(III)/Fe(II). However, at a pathological state, unbound iron may promote the production of highly toxic hydroxyl radicals via Fenton...

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Filipský T, Mladenka P, Macáková K, et al. Effect of novel 1-phenyl-3-methyl-4-acylpyrazolones on iron chelation and Fenton reaction. Free Radic Biol Med. 2014;75:S29-30doi: 10.1016/j.freeradbiomed.2014.10.758.
Filipský, T., Mladenka, P., Macáková, K., Hrdina, R., Saso, L., Marchetti, F., & Pettinari, C. (2014). Effect of novel 1-phenyl-3-methyl-4-acylpyrazolones on iron chelation and Fenton reaction. Free radical biology & medicine, 75S29-30. https://doi.org/10.1016/j.freeradbiomed.2014.10.758
Filipský, Tomáš, et al. "Effect of novel 1-phenyl-3-methyl-4-acylpyrazolones on iron chelation and Fenton reaction." Free radical biology & medicine vol. 75 (2014): S29-30. doi: https://doi.org/10.1016/j.freeradbiomed.2014.10.758
Filipský T, Mladenka P, Macáková K, Hrdina R, Saso L, Marchetti F, Pettinari C. Effect of novel 1-phenyl-3-methyl-4-acylpyrazolones on iron chelation and Fenton reaction. Free Radic Biol Med. 2014 Oct;75:S29-30. doi: 10.1016/j.freeradbiomed.2014.10.758. Epub 2014 Dec 10. PMID: 26461329.
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Showing 1 to 12 of 883 entries