Search results for "SD"

showing 10 items of 20459 documents

Anatomical and functional macular changes after rhegmatogenous retinal detachment with macula off

2011

International audience; Purpose: To evaluate the correlation between morphologic changes in the outer retina and visual function after successful repair of rhegmatogenous retinal detachment with macula off. Methods: Thirty patients (30 eyes) with successful repair of rhegmatogenous retinal detachment (RD) after macula off and a minimum 6-month follow-up after the surgery were examined. Preoperative characteristics of the RD (visual acuity and duration) were collected. Postoperative visual acuity measurement with ETDRS scale and fundus autofluorescence (FAF) were performed. Spectral-Domain Optical Coherence Tomography (HRA OCT) of outer retina was performed to analyse the number of disrupted…

retinal detachment[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologygenetic structures[SDV.MHEP.OS] Life Sciences [q-bio]/Human health and pathology/Sensory Organsimaging/image analysissense organs[SDV.MHEP.OS]Life Sciences [q-bio]/Human health and pathology/Sensory Organsvitreoretinal surgeryeye diseasesclinical[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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Plasmalogens and cell-cell communication between retinal glial cells

2016

This is an abstract that was submitted for the 2016 ARVO Annual Meeting, held in Seattle, Wash., May 1-5, 2016.; Purpose: Plasmalogens (or ether-lipids) are a particular class of glycerophospholipids characterized by the presence of a vinyl-ether bond at the sn-1 position of the glycerol backbone and by the preferential esterification of polyunsaturated fatty acids (PUFAs) at the sn-2 position. Plasmalogens are found at high concentrations in retinal macroglial cells such as Müller cells and astrocytes. Müller cells and astrocytes are known to communicate by the way of intracellular calcium waves and gap junctions. Connexin 43 is the major protein of these communicating junctions. The aim o…

retinal glial cells[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyOrganes des sens[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionrétineSensory Organsglial cell[ SDV.MHEP.OS ] Life Sciences [q-bio]/Human health and pathology/Sensory Organs[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyAlimentation et NutritionFood and Nutritionophtalmologycellule gliale[SDV.MHEP.OS]Life Sciences [q-bio]/Human health and pathology/Sensory Organs[SDV.AEN]Life Sciences [q-bio]/Food and NutritionComputingMilieux_MISCELLANEOUS[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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The success of Agronomy for Sustainable Development: from IF 0.566 rank 29/53 to IF 2.9 rank 4/75

2012

Scientific journals are facing an increasing competition directly impacting publishers and editorial boards. In addition, access to scientific information and reading patterns have deeply changed. From 2003 the journal Agronomy for Sustainable Development (ASD) has adapted its editorial policy to this highly competitive and moving environment in order to stand out and improve its impact (1). The scope, language and title of the journal were modified. A preselection step was introduced, several calls for reviews were made and spin-off books were published (2). Particular attention was given to abstracts, titles, colour figures and photos. A sister book series named Sustainable Agriculture Re…

reviews[SDV] Life Sciences [q-bio][SDE] Environmental Sciences[SDV]Life Sciences [q-bio]editingEASEsocial media[SDE]Environmental Sciences[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal Biologyimpact factorAgronomySCImago
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Procédé de réduction du gaz à effet de serre N2O en N2 par des couples symbiotiques légumineus-rghizobia, sélectionnés conjointement pour application…

2009

rghizobia[SDV] Life Sciences [q-bio][SDE] Environmental SciencesN2Ocouple symbiotiqueN2légumineusgaz à effet de serre
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Rho GTPases Are Involved in the Regulation of NF-κB by Genotoxic Stress

2001

A common cellular response to genotoxic agents and inflammatory cytokines is the activation of NF-kappaB. Here, we addressed the question of whether small GTPases of the Rho family are involved in the stimulation of NF-kappaB signaling by genotoxic agents or TNFalpha in HeLa cells. Inhibition of isoprenylation of Rho proteins by use of the HMG-CoA reductase inhibitor lovastatin attenuated UV-, doxorubicin-, and TNFalpha-induced degradation of IkappaBalpha as well as drug-stimulated DNA binding activity of NF-kappaB. Furthermore, NF-kappaB-regulated gene expression stimulated by either UV irradiation or treatment with TNFalpha was abrogated by lovastatin pretreatment. This indicates that iso…

rho GTP-Binding ProteinsBacterial ToxinsClostridium difficile toxin BGenotoxic StressGTPaseBiologyProinflammatory cytokinechemistry.chemical_compoundBacterial ProteinsNF-KappaB Inhibitor alphamedicineHumansLovastatinTumor Necrosis Factor-alphaNF-kappa BNF-kappa B p50 SubunitNF-κBCell BiologyCell biologyDNA-Binding ProteinsIκBαchemistryDoxorubicinI-kappa B ProteinsTumor necrosis factor alphaLovastatinHeLa CellsSignal Transductionmedicine.drugExperimental Cell Research
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Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin s…

1994

Cytotoxic necrotizing factor type 2 (CNF2) produced by Escherichia coli strains isolated from intestinal and extraintestinal infections is a dermonecrotic toxin of 110 kDa. We cloned the CNF2 gene from a large plasmid carried by an Escherichia coli strain isolated from a lamb with septicemia. Hydropathy analysis of the deduced amino acid sequence revealed a largely hydrophilic protein with two potential hydrophobic transmembrane domains. The N-terminal half of CNF2 showed striking homology (27% identity and 80% conserved residues) to the N-terminal portion of Pasteurella multocida toxin. Methylamine protection experiments and immunofluorescence studies suggested that CNF2 enters the cytosol…

rho GTP-Binding ProteinsBacterial ToxinsMolecular Sequence DataRestriction Mapping[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyIn Vitro TechniquesSEQUENCE GENIQUEmedicine.disease_causeCell LineGTP-binding protein regulatorsGTP-Binding ProteinsmedicineEscherichia coliHumansCloning MolecularCytoskeletonEscherichia coliPeptide sequence[SDV.BC] Life Sciences [q-bio]/Cellular BiologyActinAdenosine Diphosphate RiboseMultidisciplinaryBase SequenceSequence Homology Amino AcidCytotoxinsBinding proteinEscherichia coli ProteinsMolecular biologyActinsCytosolTransmembrane domainActin CytoskeletonBiochemistryGenes BacterialFACTEUR CYTOTOXIQUE NECROSANTSequence AlignmentResearch Article
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Targeting the mevalonate pathway for improved anticancer therapy.

2009

The mevalonate pathway is important for the generation of isoprene moieties thereby providing the basis for the biosynthesis of molecules required for maintaining membrane integrity, steroid production and cell respiration. Additionally, isoprene precursors are indispensable for the prenylation of regulatory proteins such as Ras and Ras-homologous (Rho) GTPases. These low molecular GTP-binding proteins play key roles in numerous signal transduction pathways stimulated upon activation of cell surface receptors by ligand binding. Thus, Ras/Rho proteins eventually regulate cell proliferation, tumor progression and cell death induced by anticancer therapeutics. Lipid modification of Ras/Rho pro…

rho GTP-Binding ProteinsCancer Researchmedicine.medical_treatmentProtein PrenylationMevalonic AcidAntineoplastic AgentsGTPaseModels BiologicalSteroidDrug Delivery SystemsPrenylationCell surface receptorNeoplasmsDrug DiscoverymedicineAnimalsHumansPharmacologyCell DeathDiphosphonatesChemistryCell growthMembrane ProteinsDimethylallyltranstransferaseCell biologyOncologyras ProteinsMevalonate pathwayLipid modificationSignal transductionHydroxymethylglutaryl-CoA Reductase InhibitorsSignal TransductionCurrent cancer drug targets
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Late Activation of Stress-activated Protein Kinases/c-Jun N-terminal Kinases Triggered by Cisplatin-induced DNA Damage in Repair-defective Cells

2011

Although stress-activated protein kinases/c-Jun N-terminal kinases (SAPK/JNK) are rapidly activated by genotoxins, the role of DNA damage in this response is not well defined. Here we show that the SEK1/MKK4-mediated dual phosphorylation of SAPK/JNK (Thr-183/Tyr-185) correlates with the level of cisplatin-DNA adducts at late times (16–24 h) after drug treatment in both human and mouse cells. Transfection of platinated plasmid DNA also caused SAPK/JNK activation. A defect in transcription-coupled nucleotide excision repair resting on a mutation in Cockayne syndrome group B protein promoted the late SAPK/JNK activation following cisplatin exposure. Signaling to SAPK/JNK was accompanied by act…

rho GTP-Binding ProteinsDNA RepairMAP Kinase Kinase 4DNA repairDNA damageDNA damage response; DNA repair; cisplatin-DNA adducts; SAPK/JNKp38 mitogen-activated protein kinasesAntineoplastic AgentsCell Cycle ProteinsAtaxia Telangiectasia Mutated ProteinsProtein Serine-Threonine KinasesDNA and ChromosomesBiologyBiochemistryAtaxia Telangiectasia Mutated ProteinsDNA AdductsMiceRadiation IonizingAnimalsHumansDNA Breaks Double-StrandedMolecular BiologyReplication protein ACells CulturedMice KnockoutKinaseTumor Suppressor ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyMolecular biologyDNA-Binding ProteinsEnzyme Activationc-Jun N-terminal kinasesbiology.proteinCisplatinSignal TransductionNucleotide excision repairJournal of Biological Chemistry
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Inhibition of small G proteins of the Rho family by statins orClostridium difficiletoxin B enhances cytokine-mediated induction of NO synthase II

2000

In order to investigate the involvement of Ras and/or Rho proteins in the induction of the inducible isoform of nitric oxide synthase (NOS II) we used HMG-CoA reductase inhibitors (statins) and Clostridium difficile toxin B (TcdB) as pharmacological tools. Statins indirectly inhibit small G proteins by preventing their essential farnesylation (Ras) and/or geranylgeranylation (Rho). In contrast, TcdB is a glucosyltransferase and inactivates Rho-proteins directly. Human A549/8- and DLD-1 cells as well as murine 3T3 fibroblasts were preincubated for 18 h with statins (1–100 μM) or TcdB (0.01–10 ng ml−1). Then NOS II expression was induced by cytokines. NOS II mRNA was measured after 4–8 h by R…

rho GTP-Binding ProteinsG proteinBacterial ToxinsMevalonic AcidNitric Oxide Synthase Type IISmall G ProteinClostridium difficile toxin BBiologyGene Expression Regulation EnzymologicMiceGeranylgeranylationBacterial ProteinsPolyisoprenyl PhosphatesPrenylationGTP-Binding ProteinsGene expressionAtorvastatinTumor Cells CulturedAnimalsHumansDrug InteractionsPyrrolesLovastatinPromoter Regions GeneticPharmacology3T3 CellsTransfectionMolecular biologyHeptanoic AcidsEnzyme InductionPapersCytokinesHydroxymethylglutaryl-CoA Reductase InhibitorsNitric Oxide SynthaseSignal transductionBritish Journal of Pharmacology
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Mtlinteracts with members of Egfr signaling and cell adhesion genes in the Drosophila eye

2011

Mtl is a member of the Rho family of small GTPases in Drosophila. It was shown that Mtl is involved in planar cell polarity (PCP) establishment, together with other members of the same family like Cdc42, Rac1, Rac2 and RhoA. However, while Rac1, Rac2 and RhoA function downstream of Dsh in Fz/PCP signaling and upstream of a JNK cassette, Mtl and Cdc42 do not. To determine the functional context of Mtl during PCP establishment in the Drosophila eye, we performed a loss-of-function screen to search for dominant modifiers of a sev>Mtl rough eye phenotype. In addition, genetic interaction assays with candidate genes were also carried out. Our results show that Mtl interacts genetically with memb…

rho GTP-Binding ProteinsGeneticsOmmatidial rotationRHOAbiologyCytoskeleton organizationCell PolarityCDC42Cell biologyErbB ReceptorsPhenotypeInsect ScienceCell polarityCell Adhesionbiology.proteinAnimalsDrosophila ProteinsImmunoglobulin superfamilyDrosophilaCompound Eye ArthropodReceptors Invertebrate PeptideCell adhesionpsychological phenomena and processesDrosophila ProteinSignal TransductionFly
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