91 resultados para Allergic rhinitis
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Aim: To determine the potential aetiological factors related to molar-incisor hypomineralisation (MIH) in Brazilian children. Methods: A total of 1,151 children aged 7-12 years (mean 8.86 ± 1.28), born and living in the urban area of Araraquara, Brazil, were examined by two examiners evaluating the presence of MIH according to criteria suggested by the European Academy of Paediatric Dentistry (2003). Their mothers completed a structured questionnaire about medical history, from pregnancy to the first 3 years of the children's life. Descriptive analyses of data and odds ratios (OR) with 95 % test-based confidence intervals (CI) were estimated. Chi-square test was used to evaluate the differences between groups. Results: The prevalence of MIH in the children was 12.3 %. The interviewing response rate was 90.4 %. The prevalence of miscarriage history (25 vs. 15.4 %; OR = 1.21; 95 % CI 0.30-4.92) and occurrence of anaemia (23 vs. 12.4 %; OR = 2.07; 95 % CI 0.50-8.63) were higher in mothers from MIH group than those from non-MIH group. However, these associations were not statically significant. In the children's medical history, rhinitis, bronchitis (56.5 vs. 52.5 %; OR = 1.17; 95 % CI 0.82-1.68), and high fever (20.4 vs. 18.2 %; OR = 1.14; 0.73-1.76) were more prevalent in MIH group, but there were no significant differences between the groups (p > 0.05). Conclusions: No possible aetiological factor investigated was associated with MIH. Prospective studies are needed to define the aetiological factors involved with MIH. © 2013 European Academy of Paediatric Dentistry.
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Honey bee venom toxins trigger immunological, physiological, and neurological responses within victims. The high occurrence of bee attacks involving potentially fatal toxic and allergic reactions in humans and the prospect of developing novel pharmaceuticals make honey bee venom an attractive target for proteomic studies. Using label-free quantification, we compared the proteome and phosphoproteome of the venom of Africanized honeybees with that of two European subspecies, namely Apis mellifera ligustica and A. m. carnica. From the total of 51 proteins, 42 were common to all three subspecies. Remarkably, the toxins melittin and icarapin were phosphorylated. In all venoms, icarapin was phosphorylated at the 205Ser residue, which is located in close proximity to its known antigenic site. Melittin, the major toxin of honeybee venoms, was phosphorylated in all venoms at the 10Thr and 18Ser residues. 18Ser phosphorylated melittin-the major of its two phosphorylated forms-was less toxic compared to the native peptide. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Pós-graduação em Ciências Biológicas (Biologia Celular e Molecular) - IBRC
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Pós-graduação em Biociências e Biotecnologia Aplicadas à Farmácia - FCFAR
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Pós-graduação em Psicologia - FCLAS
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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Pós-graduação em Ciências Biológicas (Biologia Celular e Molecular) - IBRC
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Pós-graduação em Biologia Geral e Aplicada - IBB
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Pós-graduação em Pediatria - FMB