S Nitrosoglutathione Reductase
Mostrando 1-8 de 8 artigos, teses e dissertações.
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1. Modulação da atividade mitocondrial pela S-nitrosoglutationa redutase em resposta ao estresse nutricional em suspensões celulares de Arabidopsis thaliana / Modulation of mitochondrial activity by S-nitrosoglutathione reductase in response to nutritional stress in Arabidopsis thaliana cell suspensions
Embora o radical óxido nítrico (NO) seja um importante sinalizador em plantas, pouco se conhece sobre os mecanismos que controlam sua homeostase na célula. Acreditase que a enzima S-nitrosoglutationa redutase (GSNOR) tenha um papel relevante no metabolismo de S-nitrosotióis (SNO), e consequentemente na homeostase do NO, através do catabolismo da S-nitro
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 07/07/2011
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2. S-Nitrosoglutathione Reductase: An Important Regulator in Human Asthma
Rationale: Nitric oxide bioactivity, mediated through the formation of S-nitrosothiols (SNOs), has a significant effect on bronchomotor tone. S-Nitrosoglutathione is an endogenous bronchodilator that is decreased in children with asthmatic respiratory failure and in adults with asthma undergoing segmental airway challenge. Recently we showed that S-nitrosogl
American Thoracic Society.
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3. Kinetic and Cellular Characterization of Novel Inhibitors of S-Nitrosoglutathione Reductase*
S-Nitrosoglutathione reductase (GSNOR) is an alcohol dehydrogenase involved in the regulation of S-nitrosothiols (SNOs) in vivo. Knock-out studies in mice have shown that GSNOR regulates the smooth muscle tone in airways and the function of β-adrenergic receptors in lungs and heart. GSNOR has emerged as a target for the development of therapeutic approaches
American Society for Biochemistry and Molecular Biology.
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4. Nitric oxide reacts with intracellular glutathione and activates the hexose monophosphate shunt in human neutrophils: evidence for S-nitrosoglutathione as a bioactive intermediary.
We performed experiments to determine whether nitric oxide promoted the formation of intracellular S-nitrosothiol adducts in human neutrophils. At concentrations sufficient to inhibit chemoattractant-induced superoxide anion production, nitric oxide caused a depletion of measurable intracellular glutathione as determined by both the monobromobimane HPLC meth
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5. Glutathionylation of human thioredoxin: A possible crosstalk between the glutathione and thioredoxin systems
To identify proteins undergoing glutathionylation (formation of protein-glutathione mixed disulfides) in human T cell blasts, we radiolabeled the glutathione pool with 35S, exposed cells to the oxidant diamide, and analyzed cellular proteins by two-dimensional electrophoresis. One of the proteins undergoing glutathionylation was identified by molecular weigh
The National Academy of Sciences.
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6. Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
Inducible nitric oxide synthase (iNOS) plays an important role in host defense. Macrophages expressing iNOS release the reactive nitrogen intermediates (RNI) nitrite and S-nitrosoglutathione (GSNO), which are bactericidal in vitro at a pH characteristic of the phagosome of activated macrophages. We sought to characterize the active intrabacterial forms
National Academy of Sciences.
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7. Role of an Inducible Single-Domain Hemoglobin in Mediating Resistance to Nitric Oxide and Nitrosative Stress in Campylobacter jejuni and Campylobacter coli
Campylobacter jejuni expresses two hemoglobins, each of which exhibits a heme pocket and structural signatures in common with vertebrate and plant globins. One of these, designated Cgb, is homologous to Vgb from Vitreoscilla stercoraria and does not possess the reductase domain seen in the flavohemoglobins. A Cgb-deficient mutant of C. jejuni was hypersensit
American Society for Microbiology.
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8. Exogenous Glutathione Completes the Defense against Oxidative Stress in Haemophilus influenzae
Since they are equipped with several strategies by which they evade the antimicrobial defense of host macrophages, it is surprising that members of the genus Haemophilus appear to be deficient in common antioxidant systems that are well established to protect prokaryotes against oxidative stress. Among others, no genetic evidence for glutathione (γ-Glu-Cys-
American Society for Microbiology.