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[PMID]: 29524843
[Au] Autor:Sena FV; Sousa FM; Oliveira ASF; Soares CM; Catarino T; Pereira MM
[Ad] Address:Instituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Av. da Republica EAN, 2780-157 Oeiras, Portugal.
[Ti] Title:Regulation of the mechanism of Type-II NADH: Quinone oxidoreductase from S. aureus.
[So] Source:Redox Biol;16:209-214, 2018 Feb 17.
[Is] ISSN:2213-2317
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Type-II NADH:quinone oxidoreductases (NDH-2s) are membrane proteins involved in respiratory chains and the only enzymes with NADH:quinone oxidoreductase activity expressed in Staphylococcus aureus (S. aureus), one of the most common causes of clinical infections. NDH-2s are members of the two-Dinucleotide Binding Domains Flavoprotein (tDBDF) superfamily, having a flavin adenine dinucleotide, FAD, as prosthetic group and NAD(P)H as substrate. The establishment of a Charge-Transfer Complex (CTC) between the isoalloxazine ring of the reduced flavin and the nicotinamide ring of NAD+ in NDH-2 was described, and in this work we explored its role in the kinetic mechanism using different electron donors and electron acceptors. We observed that CTC slows down the rate of the second half reaction (quinone reduction) and determines the effect of HQNO, an inhibitor. Also, protonation equilibrium simulations clearly indicate that the protonation probability of an important residue for proton transfer to the active site (D302) is influenced by the presence of the CTC. We propose that CTC is critical for the overall mechanism of NDH-2 and possibly relevant to keep a low quinol/quinone ratio and avoid excessive ROS production in vivo.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  2 / 92416 MEDLINE  
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[PMID]: 29524414
[Au] Autor:Liu P; Feng T; Zuo X; Wang X; Luo J; Li N; Han X; Zhu N; Xu S; Xu Y; Jin ZG; Si S
[Ad] Address:Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China; Aab Cardiovascular Research Institute, Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY, USA.
[Ti] Title:A novel SIRT1 activator E6155 improves insulin sensitivity in type 2 diabetic KKA mice.
[So] Source:Biochem Biophys Res Commun;, 2018 Mar 07.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Sirtuin 1 (SIRT1) is an NAD -dependent protein deacetylase that plays a critical role in controlling energy metabolism, stress response and aging. Hence, enhancing SIRT1 activity could be a potential therapeutic strategy to treat metabolic diseases such as diabetes. However, pharmacological activators for SIRT1 are scarce to date. In this study, using the optimized high throughput screening, we identified E6155, a piperazine 1, 4- diamide compound, as a new small molecular activator of SIRT1. We further found that E6155 significantly upregulated glucose uptake in cultured mouse liver cells and skeletal muscle cells through increasing SIRT1 deacetylase activity. In type 2 diabetic KKA mice, E6155 treatment markedly decreased the level of fasting glucose. Moreover, E6155 improved oral glucose tolerance and insulin tolerance. Euglycemic clamp and the homeostasis model assessment of insulin resistance index showed that E6155 ameliorated the insulin resistance and increased insulin sensitivity in diabetic mice. Mechanistically, we observed that the antidiabetic effects of E6155 were involved in SIRT1 dependent activation of LKB1/AMPK and IRS1/AKT pathways. In conclusion, our findings identified E6155 as a novel SIRT1 activator and suggested that E6155 could be a promising drug candidate for treating insulin resistance and diabetes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  3 / 92416 MEDLINE  
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[PMID]: 29501752
[Au] Autor:Li J; Zhang Y; Hu K; Zhao Y; Lin R; Li Y; Huang Z; Zhang X; Geng X; Ding J
[Ad] Address:School of Life Sciences, Huaibei Normal University, Huaibei, Anhui, PR China.
[Ti] Title:Mitochondrial genome characteristics of two Sphingidae insects (Psilogramma increta and Macroglossum stellatarum) and implications for their phylogeny.
[So] Source:Int J Biol Macromol;113:592-600, 2018 Mar 06.
[Is] ISSN:1879-0003
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:In this study, complete mitogenomes of P. increta and M. stellatarum (Lepidoptera: Sphingidae) were sequenced and compared with other Sphingidae species. The mitogenomes containing 37 genes and a AT rich region are circular molecules with 15,252 and 15,290 base pairs in length respectively. Except cox1 all 13 protein-coding genes (PCGs) are initiated by ATN codons. Most of PCGs terminate with TAA except nad5 and cox1 in P. increta and nad5 and cox2 in M. stellatarum. Ile and Leu2 are the most frequently used codon families in both species and codons CGC, CCG, TCG and ACG are absent in P. increta while in M. stellatarum CGC, CCG, CTG, AGG are absent. All the tRNA genes could be folded into the typical cloverleaf secondary structure except the trnS1 of P. increta which lost dihydrouridine (DHU) stem. The AT-rich region of both insects includes the motif ATAGA followed by a 18-19bp polyT stretch and 2-3 short tandem repeats (STRs) of TA, and a poly-A element. Phylogenetic analyses showed that the phylogenetic relationships are (((Sphinx morio+Manduca sexta)+(P. increta+Notonagemia analis scribae))+(Agrius convolvuli)+(M. stellatarum+(Ampelophaga rubiginosa+Daphnis nerii)).
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  4 / 92416 MEDLINE  
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[PMID]: 29438734
[Au] Autor:Thomas M; Palombo P; Schuhmacher T; von Scheven G; Bazylianska V; Salzwedel J; Schäfer N; Bürkle A; Moreno-Villanueva M
[Ad] Address:Molecular Toxicology Group, Department of Biology, University of Konstanz, Universitaetsstrasse 10, 78457 Konstanz, Germany. Electronic address: mara_thomas@gmx.net.
[Ti] Title:Impaired PARP activity in response to the ß-adrenergic receptor agonist isoproterenol.
[So] Source:Toxicol In Vitro;50:29-39, 2018 Feb 10.
[Is] ISSN:1879-3177
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Psychological stress has been associated with DNA damage, thus increasing the risk of numerous diseases including cancer. Here, we investigate the effect of acute and chronic stress on poly(ADP-ribose) polymerase-1 (PARP-1), a sensor of DNA damage and DNA repair initiator. In order to mimic the chronic release of epinephrine, human peripheral blood mononuclear cells (PBMCs) were treated repeatedly with the sympathomimetic drug isoproterenol. We found significant induction of DNA strand breaks that remained unrepaired 24 h after ex vivo incubation. Isoproterenol-induced DNA strand breaks could be partially prevented by pre-treatment with the ß-adrenergic receptor antagonist propranolol. Furthermore, the level of PARP-1 protein and PARP activity decreased and the levels of the PARP substrate nicotinamide adenine dinucleotide (NAD ) and of adenosine triphosphate (ATP), necessary to replenish NAD pools, were lowered by isoproterenol treatment. In conclusion our data provide novel insights into the mechanisms of isoproterenol-induced genotoxicity linking ß-adrenergic stimulation and PARP-1.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  5 / 92416 MEDLINE  
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[PMID]: 28463821
[Au] Autor:Hoyt LR; Randall MJ; Ather JL; DePuccio DP; Landry CC; Qian X; Janssen-Heininger YM; van der Vliet A; Dixon AE; Amiel E; Poynter ME
[Ad] Address:Vermont Lung Center, University of Vermont, Burlington, VT 05405, USA; Division of Pulmonary Disease and Critical Care, Department of Medicine, University of Vermont, Burlington, VT 05405, USA.
[Ti] Title:Mitochondrial ROS induced by chronic ethanol exposure promote hyper-activation of the NLRP3 inflammasome.
[So] Source:Redox Biol;12:883-896, 2017 Aug.
[Is] ISSN:2213-2317
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Alcohol use disorders are common both in the United States and globally, and are associated with a variety of co-morbid, inflammation-linked diseases. The pathogenesis of many of these ailments are driven by the activation of the NLRP3 inflammasome, a multi-protein intracellular pattern recognition receptor complex that facilitates the cleavage and secretion of the pro-inflammatory cytokines IL-1ß and IL-18. We hypothesized that protracted exposure of leukocytes to ethanol would amplify inflammasome activation, which would help to implicate mechanisms involved in diseases associated with both alcoholism and aberrant NLRP3 inflammasome activation. Here we show that long-term ethanol exposure of human peripheral blood mononuclear cells and a mouse macrophage cell line (J774) amplifies IL-1ß secretion following stimulation with NLRP3 agonists, but not with AIM2 or NLRP1b agonists. The augmented NRLP3 activation was mediated by increases in iNOS expression and NO production, in conjunction with increases in mitochondrial membrane depolarization, oxygen consumption rate, and ROS generation in J774 cells chronically exposed to ethanol (CE cells), effects that could be inhibited by the iNOS inhibitor SEITU, the NO scavenger carboxy-PTIO, and the mitochondrial ROS scavenger MitoQ. Chronic ethanol exposure did not alter K efflux or Zn homeostasis in CE cells, although it did result in a lower intracellular concentration of NAD . Prolonged administration of acetaldehyde, the product of alcohol dehydrogenase (ADH) mediated metabolism of ethanol, mimicked chronic ethanol exposure, whereas ADH inhibition prevented ethanol-induced IL-1ß hypersecretion. Together, these results indicate that increases in iNOS and mitochondrial ROS production are critical for chronic ethanol-induced IL-1ß hypersecretion, and that protracted exposure to the products of ethanol metabolism are probable mediators of NLRP3 inflammasome hyperactivation.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1705
[Cu] Class update date: 180311
[Lr] Last revision date:180311
[St] Status:In-Process

  6 / 92416 MEDLINE  
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[PMID]: 29523164
[Au] Autor:Wu Y; Li L; Zhu G; Li W; Zhang N; Li S; Yao G; Tian W; Fu B; Yin H; Zhu X; Yan H; Jia W
[Ad] Address:State Key Laboratory of Veterinary Etiological Biology/Key Laboratory of Veterinary Parasitology of Gansu Province/Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, Gansu Province, People's Republic of China.
[Ti] Title:Mitochondrial genome data confirm that yaks can serve as the intermediate host of Echinococcus canadensis (G10) on the Tibetan Plateau.
[So] Source:Parasit Vectors;11(1):166, 2018 Mar 09.
[Is] ISSN:1756-3305
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Cervids used to be considered the only animal intermediate hosts of the G10 genotype of Echinococcus canadensis. Yaks are often herded in the Qinghai-Tibet Plateau, China, where echinococcosis remains prevalent. However, no E. canadensis G10 cases have been recorded in yaks until now. The aim of our study was to identify causative agents of echinococcosis in yaks in this region. METHODS: Total genomic DNA was extracted from the germinal layer of one hydatid using a Blood and Tissue Kit. Full-length mitochondrial (mt) cytochrome c oxidase subunit 1 (cox1) and NADH dehydrogenase subunit 1 (nad1) genes were amplified by PCR. All purified PCR products were directly sequenced in both directions. Then seven pairs of overlap primers were designed to amplify the entire mt genome sequence of a suspected E. canadensis G10 isolate. Phylogenetic analyses were performed based on concatenated nucleotides from the 12 protein-coding genes of mt genomes of Echinococcus species in a Bayesian framework using MrBayes v3.1 and implementing the GTR + I + G model. RESULTS: Hydatids were found in yaks (n = 129) when organs were inspected at the slaughterhouse in Maqu county, Gannan Tibetan Autonomous Prefecture, Gansu Province, China in October 2016. Of these, 33 (25.6%) harbored up to a dozen hydatid cysts. One cyst from each yak was characterized by sequencing its mitochondrial (mt) cox1 and nad1 genes. On the basis of these sequence data, 32 cysts were identified as Echinococcus granulosus (sensu stricto) (G1-G3) and the remaining one was identified as the G10 genotype of E. canadensis. Its mt genome was then fully sequenced and compared with that of the G10 genotype in GenBank (AB745463). Phylogenetic analysis using complete mt genomes confirmed the Chinese cyst as belonging to the G10 genotype. CONCLUSIONS: To our knowledge, this is the first report globally of E. canadensis (G10) from yaks in China, which suggests that the G10 genotype has a wider geographical distribution and broader host range than previously believed. This genotype has therefore potential risks to human health and animal husbandry.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:In-Data-Review
[do] DOI:10.1186/s13071-018-2684-0

  7 / 92416 MEDLINE  
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[PMID]: 29408361
[Au] Autor:Barinova K; Khomyakova E; Semenyuk P; Schmalhausen E; Muronetz V
[Ad] Address:Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119234, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119234, Russia.
[Ti] Title:Binding of alpha-synuclein to partially oxidized glyceraldehyde-3-phosphate dehydrogenase induces subsequent inactivation of the enzyme.
[So] Source:Arch Biochem Biophys;642:10-22, 2018 Mar 15.
[Is] ISSN:1096-0384
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:According to literature data, the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) co-localizes with alpha-synuclein in Lewy bodies in Parkinson's disease, which suggests the involvement of this protein in the development of synucleinopathies. The goal of the present work was to investigate the direct interaction between alpha-synuclein and GAPDH and to evaluate possible influence of this interaction on the catalytic properties of GAPDH. Molecular dynamic simulations predicted the binding of alpha-synuclein to the positively charged groove comprising NAD -binding pocket of GAPDH. The formation of the complex between alpha-synuclein and GAPDH in vitro was confirmed by different experimental approaches. The binding of alpha-synuclein to GAPDH with partially oxidized active site cysteines resulted in the subsequent inactivation of the enzyme, decreased its thermostability and increased its propensity for aggregation. At the same time, the formation of the complex between GAPDH and monomeric alpha-synuclein prevented amyloid transformation of alpha-synuclein. This work presents the first evidence for the fact that the initial oxidation of GAPDH induces the binding of alpha-synuclein to the enzyme, leading to further inactivation of GAPDH and, as a consequence, inhibition of glycolysis. The described mechanism may contribute to the metabolic disorders that are characteristic for synucleinopathies.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:In-Data-Review

  8 / 92416 MEDLINE  
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[PMID]: 29407039
[Au] Autor:Zuo C; Jolly AL; Nikolova AP; Satzer DI; Cao S; Sanchez JS; Ballou DP; Trimmer EE
[Ad] Address:Department of Chemistry, Grinnell College, Grinnell, IA 50112, USA.
[Ti] Title:A role for glutamine 183 in the folate oxidative half-reaction of methylenetetrahydrofolate reductase from Escherichia coli.
[So] Source:Arch Biochem Biophys;642:63-74, 2018 Mar 15.
[Is] ISSN:1096-0384
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The flavoprotein methylenetetrahydrofolate reductase (MTHFR) from Escherichia coli catalyzes a ping-pong reaction with NADH and 5,10-methylenetetrahydrofolate (CH -H folate) to produce NAD and 5-methyltetrahydrofolate (CH -H folate). This work focuses on the function of the invariant, active-site aminoacyl residue Gln183. X-ray structures of the enzyme complexes E (wild-type)•NADH and E (Glu28Gln)•CH -H folate indicate that Gln183 makes key hydrogen-bonding interactions with both NADH and folate in their respective half-reactions, suggesting roles in binding each substrate. We propose that the polarity of Gln183 may also aid in stabilizing the proposed 5-iminium cation intermediate during catalysis in the oxidative half-reaction with folate. We have prepared mutants Gln183Ala and Gln183Glu, which we hypothesize to have altered charge/polarity and hydrogen bonding properties. We have examined the enzymes by steady-state and stopped-flow kinetics and by measurement of the flavin redox potentials. In the reductive half-reaction, NADH binding affinity and the rate of flavin reduction have not been hindered by either mutation. By contrast, our results support a minor role for Gln183 in the oxidative half-reaction. The Gln183Ala variant exhibited a 6-10 fold lower rate of folate reduction and bound CH -H folate with 7-fold lower affinity, whereas the Gln183Glu mutant displayed catalytic constants within 3-fold of the wild-type enzyme.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:In-Data-Review

  9 / 92416 MEDLINE  
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[PMID]: 29366480
[Au] Autor:Zhang N; Zhang Y; Zhao S; Sun Y
[Ad] Address:Department of Cardiology, The First Hospital of China Medical University, 155 Nanjing North Street, Heping District, Shenyang, Liaoning 110001, PR China.
[Ti] Title:Septin4 as a novel binding partner of PARP1 contributes to oxidative stress induced human umbilical vein endothelial cells injure.
[So] Source:Biochem Biophys Res Commun;496(2):621-627, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Oxidative stress induced vascular endothelial cell injure is one of the key and initial event in the development of atherosclerosis. Septin4, as a member of GTP binding protein family, is widely expressed in the eukaryotic cells and considered to be an essential component of the cytoskeleton which is involved in many important physiological processes. However, whether Septin4 is involved in cardiovascular diseases, such as oxidative stress inducted endothelial cell injury still unclear. PARP1 as a DNA repair enzyme can be activated by identifying DNA damaged fragments, which consumes high levels of energy and leads to vascular endothelial cell apoptosis. Here, our results first found that Septin4 is involved in oxidative stress induced endothelial cell ROS production and apoptosis through knock-down and over-expression Septin4 approaches. Furthermore, to explore how Septin4 is involved in oxidative stress induced endothelial cells injure, we first identified that Septin4 is a novel PARP1 interacting protein and the interaction is enhanced under oxidative stress. In conclusions, our founding indicates that Septin4 is a novel essential factor involved in oxidative stress induced vascular endothelial cell injury by interacting with apoptosis-related protein PARP1.
[Mh] MeSH terms primary: Endothelial Cells/metabolism
Oxidative Stress
Poly (ADP-Ribose) Polymerase-1/metabolism
Protein Interaction Maps
Septins/metabolism
[Mh] MeSH terms secundary: Apoptosis
Endothelial Cells/cytology
Human Umbilical Vein Endothelial Cells
Humans
Protein Binding
Reactive Oxygen Species/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Reactive Oxygen Species); EC 2.4.2.30 (PARP1 protein, human); EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1); EC 3.6.1.- (SEPT4 protein, human); EC 3.6.1.- (Septins)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:180126
[St] Status:MEDLINE

  10 / 92416 MEDLINE  
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[PMID]: 29329317
[Au] Autor:Jeong BY; Lee HY; Park CG; Kang J; Yu SL; Choi DR; Han SY; Park MH; Cho S; Lee SY; Hwang WM; Yun SR; Ryu HM; Oh EJ; Park SH; Kim YL; Yoon SH
[Ad] Address:Department of Pharmacology, College of Medicine, Konyang University, Daejeon, Republic of Korea.
[Ti] Title:Oxidative stress caused by activation of NADPH oxidase 4 promotes contrast-induced acute kidney injury.
[So] Source:PLoS One;13(1):e0191034, 2018.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Contrast-induced acute kidney injury (CIAKI) is a leading cause of acute kidney injury following radiographic procedures. Intrarenal oxidative stress plays a critical role in CIAKI. Nicotinamide adenine dinucleotide 3-phosphate (NADPH) oxidases (Noxs) are important sources of reactive oxygen species (ROS). Among the various types of Noxs, Nox4 is expressed predominantly in the kidney in rodents. Here, we evaluated the role of Nox4 and benefit of Nox4 inhibition on CIAKI using in vivo and in vitro models. HK-2 cells were treated with iohexol, with or without Nox4 knockdown, or the most specific Nox1/4 inhibitor (GKT137831). Effects of Nox4 inhibition on CIAKI mice were examined. Expression of Nox4 in HK-2 cells was significantly increased following iohexol exposure. Silencing of Nox4 rescued the production of ROS, downregulated pro-inflammatory markers (particularly phospho-p38) implicated in CIAKI, and reduced Bax and caspase 3/7 activity, which resulted in increased cellular survival in iohexol-treated HK-2 cells. Pretreatment with GKT137831 replicated these effects by decreasing levels of phospho-p38. In a CIAKI mouse model, even though the improvement of plasma blood urea nitrogen was unclear, pretreatment with GKT137831 resulted in preserved structure, reduced expression of 8-hydroxy-2'-deoxyguanosine (8OHdG) and kidney injury molecule-1 (KIM-1), and reduced number of TUNEL (terminal deoxynucleotidyl transferase dUTP nick end labeling)-positive cells. These results suggest Nox4 as a key source of reactive oxygen species responsible for CIAKI and provide a novel potential option for prevention of CIAKI.
[Mh] MeSH terms primary: Acute Kidney Injury/metabolism
Contrast Media/adverse effects
NADPH Oxidase 4/metabolism
Oxidative Stress
[Mh] MeSH terms secundary: Acute Kidney Injury/chemically induced
Animals
Apoptosis/drug effects
Cell Line
Enzyme Activation
Gene Silencing
Humans
Iohexol/pharmacology
Kidney Tubules, Proximal/cytology
Kidney Tubules, Proximal/drug effects
Kidney Tubules, Proximal/metabolism
Male
Mice
Mice, Inbred C57BL
NADPH Oxidase 4/genetics
Reactive Oxygen Species/metabolism
Real-Time Polymerase Chain Reaction
Superoxides/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Contrast Media); 0 (Reactive Oxygen Species); 11062-77-4 (Superoxides); 4419T9MX03 (Iohexol); EC 1.6.3.- (NADPH Oxidase 4)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191034


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