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Presence of epidermal allantoin further supports oxidative stress in vitiligo.
- Published in:
- Experimental Dermatology, 2008, v. 17, n. 9, p. 761, doi. 10.1111/j.1600-0625.2008.00697.x
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- Article
Computer simulation of heterogeneous single nucleotide polymorphisms in the catalase gene indicates structural changes in the enzyme active site, NADPH-binding and tetramerization domains: a genetic predisposition for an altered catalase in patients with vitiligo?
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- Experimental Dermatology, 2008, v. 17, n. 4, p. 366, doi. 10.1111/j.1600-0625.2008.00699.x
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- Article
Structural and functional alterations in the β2-adrenoceptor are caused by a point mutation in patients with atopic eczema.
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- Experimental Dermatology, 2007, v. 16, n. 10, p. 807, doi. 10.1111/j.1600-0625.2007.00600.x
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- Article
Enhanced DNA binding capacity on up-regulated epidermal wild-type p53 in vitiligo by H<sub>2</sub>O<sub>2</sub>-mediated oxidation: a possible repair mechanism for DNA damage.
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- FASEB Journal, 2009, v. 23, n. 11, p. 3790, doi. 10.1096/fj.09-132621
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- Article
Methionine Sulfoxide Reductases A and B Are Deactivated by Hydrogen Peroxide (H<sub>2</sub>O<sub>2</sub>) in the Epidermis of Patients with Vitiligo.
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- Journal of Investigative Dermatology, 2008, v. 128, n. 4, p. 808, doi. 10.1038/sj.jid.5701100
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- Article
Oxidative Stress Via Hydrogen Peroxide Affects Proopiomelanocortin Peptides Directly in the Epidermis of Patients with Vitiligo.
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- Journal of Investigative Dermatology, 2007, v. 127, n. 2, p. 411, doi. 10.1038/sj.jid.5700538
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- Article
Computer Simulation of Native Epidermal Enzyme Structures in the Presence and Absence of Hydrogen Peroxide (H<sub>2</sub>O<sub>2</sub>): Potential and Pitfalls.
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- Journal of Investigative Dermatology, 2006, v. 126, n. 12, p. 2576, doi. 10.1038/sj.jid.5700612
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- Article
ORIGINAL ARTICLE Perturbed 6-Tetrahydrobiopterin Recycling via Decreased Dihydropteridine Reductase in Vitiligo: More Evidence for H<sub>2</sub>O<sub>2</sub> Stress.
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- Journal of Investigative Dermatology, 2004, v. 122, n. 2, p. 307, doi. 10.1046/j.0022-202X.2004.22230.x
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- Article