Search results for "MUTATION"

showing 10 items of 2830 documents

Algebraic (2, 2)-transformation groups

2009

This paper contains the more significant part of the article with the same title that will appear in the Volume 12 of Journal of Group Theory (2009). In this paper we determine all algebraic transformation groups $G$, defined over an algebraically closed field $\sf k$, which operate transitively, but not primitively, on a variety $\Omega$, provided the following conditions are fulfilled. We ask that the (non-effective) action of $G$ on the variety of blocks is sharply 2-transitive, as well as the action on a block $\Delta$ of the normalizer $G_\Delta$. Also we require sharp transitivity on pairs $(X,Y)$ of independent points of $\Omega$, i.e. points contained in different blocks.

Transitive relationAlgebra and Number TheoryNaturwissenschaftliche Fakultät -ohne weitere Spezifikation-14L30permutation groupsBlock (permutation group theory)-Group Theory (math.GR)Permutation groupCentralizer and normalizerAction (physics)CombinatoricsFOS: Mathematicsddc:510Variety (universal algebra)Algebraically closed fieldAlgebraic numberMathematics - Group TheoryMathematicsJournal of Group Theory
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Fertility and Polarized Cell Growth Depends on eIF5A for Translation of Polyproline-Rich Formins in Saccharomyces cerevisiae

2014

eIF5A is an essential and evolutionary conserved translation elongation factor, which has recently been proposed to be required for the translation of proteins with consecutive prolines. The binding of eIF5A to ribosomes occurs upon its activation by hypusination, a modification that requires spermidine, an essential factor for mammalian fertility that also promotes yeast mating. We show that in response to pheromone, hypusinated eIF5A is required for shmoo formation, localization of polarisome components, induction of cell fusion proteins, and actin assembly in yeast. We also show that eIF5A is required for the translation of Bni1, a proline-rich formin involved in polarized growth during …

TranslationSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalForminsRNA-binding proteinSaccharomyces cerevisiaeInvestigationsPeptide Initiation FactorsMorphogenesisGeneticsQc-SNARE ProteinsPolyproline helixPolarisomeGeneticsMatingbiologyMicrofilament ProteinsMembrane ProteinsRNA-Binding ProteinsTranslation (biology)Polarized growthbiology.organism_classificationActinsProtein Structure TertiaryCell biologyCytoskeletal ProteinsMating of yeastForminsMutationbiology.proteinEIF5APeptidesRibosomesEIF5A
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Retrotransposon silencing and telomere integrity in somatic cells of Drosophila depends on the cytosine-5 methyltransferase DNMT2

2009

Here we show that the cytosine-5 methyltransferase DNMT2 controls retrotransposon silencing in Drosophila somatic cells. In Drosophila, significant DNMT2-dependent DNA methylation occurs during early embryogenesis. Suppression of white gene silencing by Mt2 (Dnmt2) null mutations in variegated P[w(+)] element insertions identified functional targets of DNMT2. The enzyme controls DNA methylation at retrotransposons in early embryos and initiates histone H4K20 trimethylation catalyzed by the SUV4-20 methyltransferase. In somatic cells, loss of DNMT2 eliminates H4K20 trimethylation at retrotransposons and impairs maintenance of retrotransposon silencing. In Dnmt2 and Suv4-20 null genotypes, re…

Transposable elementDNA-Cytosine MethylasesEmbryo NonmammalianMethyltransferaseRetroelementsSomatic cellRetrotransposonGene Knockout TechniquesDrosophilidaeGeneticsAnimalsDrosophila ProteinsGene silencingDNA (Cytosine-5-)-MethyltransferasesGene SilencingCrosses GeneticIn Situ Hybridization FluorescenceGeneticsbiologyfungifood and beveragesHistone-Lysine N-MethyltransferaseDNA MethylationTelomerebiology.organism_classificationTelomereMutationDrosophilaDrosophila melanogasterNature Genetics
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Functional genomics of Lactobacillus casei establishment in the gut

2014

International audience; Although the composition of the gut microbiota and its symbiotic contribution to key host physiological functions are well established, little is known as yet about the bacterial factors that account for this symbiosis. We selected Lactobacillus casei as a model microorganism to proceed to genomewide identification of the functions required for a symbiont to establish colonization in the gut. As a result of our recent development of a transposon-mutagenesis tool that overcomes the barrier that had prevented L. casei random mutagenesis, we developed a signature-tagged mutagenesis approach combining whole-genome reverse genetics using a set of tagged transposons and in…

Transposable elementLactobacillus caseiMESH: MutationMutagenesis (molecular biology technique)MESH: RabbitsGenomicsBiologyMESH: Genome BacterialGenomedigestive system03 medical and health sciencesIleumLactic acid bacteriaAnimalsMESH: AnimalsGene030304 developmental biologyMESH: MutagenesisGenetics0303 health sciencesMultidisciplinaryMESH: Lactobacillus casei030306 microbiologyMESH: Genomicsdigestive oral and skin physiologyfood and beveragesGenomicsbiology.organism_classificationReverse geneticsCommensalismLacticaseibacillus caseiPNAS PlusMutagenesisMESH: IleumMutationMESH: Genome-Wide Association StudybacteriaRabbitsFunctional genomics[SDV.AEN]Life Sciences [q-bio]/Food and NutritionGenome BacterialGenome-Wide Association Study
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Predicting 19F NMR Chemical Shifts: A Combined Computational and Experimental Study of a Trypanosomal Oxidoreductase–Inhibitor Complex

2020

Abstract The absence of fluorine from most biomolecules renders it an excellent probe for NMR spectroscopy to monitor inhibitor–protein interactions. However, predicting the binding mode of a fluorinated ligand from a chemical shift (or vice versa) has been challenging due to the high electron density of the fluorine atom. Nonetheless, reliable 19F chemical‐shift predictions to deduce ligand‐binding modes hold great potential for in silico drug design. Herein, we present a systematic QM/MM study to predict the 19F NMR chemical shifts of a covalently bound fluorinated inhibitor to the essential oxidoreductase tryparedoxin (Tpx) from African trypanosomes, the causative agent of African sleepi…

Trypanosoma brucei bruceiProtozoan ProteinsContext (language use)PyrimidinonesThiophenes010402 general chemistry01 natural sciencesCatalysisquantum chemistryThioredoxinsNMR spectroscopyComputational chemistryOxidoreductasestructural biologyEnzyme InhibitorsNuclear Magnetic Resonance Biomolecularchemistry.chemical_classificationAfrican sleeping sickness010405 organic chemistryChemistryChemical shiftCommunicationGeneral ChemistryNuclear magnetic resonance spectroscopyFluorineOxidoreductase inhibitorLigand (biochemistry)Trypanocidal AgentsCommunications0104 chemical sciencesStructural biologyCovalent bondddc:540Mutationcovalent inhibitorsProtein BindingAngewandte Chemie (International Ed. in English)
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Structure-based engineering of strictosidine synthase: auxiliary for alkaloid libraries.

2007

SummaryThe highly substrate-specific strictosidine synthase (EC 4.3.3.2) catalyzes the biological Pictet-Spengler condensation between tryptamine and secologanin, leading to the synthesis of about 2000 monoterpenoid indole alkaloids in higher plants. The crystal structure of Rauvolfia serpentina strictosidine synthase (STR1) in complex with strictosidine has been elucidated here, allowing the rational site-directed mutation of the active center of STR1 and resulting in modulation of its substrate acceptance. Here, we report on the rational redesign of STR1 by generation of a Val208Ala mutant, further describing the influence on substrate acceptance and the enzyme-catalyzed synthesis of 10-m…

TryptamineCHEMBIOLStrictosidine synthaseMICROBIOStereochemistryProtein ConformationClinical BiochemistryMutantDrug Evaluation PreclinicalMutation MissenseCrystallography X-RayProtein EngineeringBiochemistryIndole AlkaloidsSubstrate Specificitychemistry.chemical_compoundRauvolfia serpentinaDrug DiscoveryCatharanthusCarbon-Nitrogen LyasesMolecular BiologyVinca AlkaloidsPlant ProteinsPharmacologybiologyMolecular StructureGeneral Medicinebiology.organism_classificationLyaseBiochemistrychemistryStrictosidinebiology.proteinMutagenesis Site-DirectedMolecular MedicineSecologaninProtein BindingChemistrybiology
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Spectrum of pncA Mutations in Multidrug-Resistant Mycobacterium tuberculosis Isolates Obtained in Latvia

2004

Pyrazinamide (PZA) is an effective antituberculous agent ([1][1]) that becomes active when bacterial pyrazinamidase converts it to pyrazinoic acid, which is toxic to mycobacteria ([4][2]). In Mycobacerium tuberculosis , PZA resistance is associated with the loss of pyrazinamidase activity, mainly

TuberculosisAntitubercular AgentsAmidohydrolasesMicrobiologyMycobacterium tuberculosischemistry.chemical_compoundPyrazinoic acidDrug Resistance Multiple BacterialmedicineHumansTuberculosisPharmacology (medical)Multidrug-Resistant Mycobacterium tuberculosisCodonLetters to the EditorPharmacologybiologyReverse Transcriptase Polymerase Chain ReactionMycobacterium tuberculosisPyrazinamidebiology.organism_classificationmedicine.diseaseLatviaPyrazinamideVirologyInfectious DiseaseschemistryMutationPncAmedicine.drugAntimicrobial Agents and Chemotherapy
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Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases

2005

The tumor suppressor phosphatase PTEN is a key regulator of cell growth and apoptosis that interacts with PDZ domains from regulatory proteins, including MAGI-1/2/3, hDlg, and MAST205. Here we identified novel PTEN-binding PDZ domains within the MAST205-related proteins, syntrophin-associated serine/threonine kinase and MAST3, characterized the regions of PTEN involved in its interaction with distinctive PDZ domains, and analyzed the functional consequences on PTEN of PDZ domain binding. Using a panel of PTEN mutations, as well as PTEN chimeras containing distinct domains of the related protein TPTE, we found that the PTP and C2 domains of PTEN do not affect PDZ domain binding and that the …

Tumor Suppressor Proteins/chemistry/ metabolismTime FactorsAmino Acid MotifsPlasma protein bindingBiochemistryMicrotubulesSerineDiscs Large Homolog 1 ProteinProtein structureSaccharomyces cerevisiae/metabolismPhosphorylationGlutathione Transferaseddc:616Nucleoside-Phosphate Kinase/metabolismbiologyChemistryDystrophin-Associated Proteins/ chemistrySignal transducing adaptor proteinProtein-Serine-Threonine Kinases/metabolismRecombinant Fusion Proteins/chemistryGuanylate KinaseCell biologyCOS CellsMicrotubule-Associated Proteins/metabolismPhosphorylationProteins/metabolismGlutathione Transferase/metabolismMicrotubule-Associated ProteinsMicrotubules/ metabolismPlasmidsProtein BindingCèl·lulesRecombinant Fusion ProteinsPDZ domainSaccharomyces cerevisiaeProtein Serine-Threonine KinasesTransfectionModels BiologicalTwo-Hybrid System TechniquesDiscs Large Homolog 1 ProteinPTENAnimalsHumansImmunoprecipitationProteïnes supressores de tumorsMolecular BiologyAdaptor Proteins Signal TransducingTumor Suppressor ProteinsPTEN PhosphohydrolaseProteinsMembrane ProteinsCell BiologyPlasmids/metabolismPhosphoric Monoester HydrolasesProtein Structure TertiaryDystrophin-Associated ProteinsMutationCancer researchbiology.proteinNucleoside-Phosphate KinaseCarrier ProteinsGuanylate KinasesPhosphoric Monoester Hydrolases/chemistry/ metabolism
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Analysis of p53 and mdm2 proteins in malignant fibrous histiocytoma in absence of gene alteration: prognostic significance.

2000

TP53 and MDM2 genes and their protein expression were evaluated in frozen and paraffin-embedded tissue from 27 patients with malignant fibrous histiocytoma to elucidate the relationship between them, their implication in tumor progression mechanisms and their possible diagnostic-prognostic value in malignant fibrous histiocytoma. Single-strand conformation polymorphism analysis and direct sequencing of polymerase chain reaction-amplified DNA were used to establish two TP53 mutations (7.4%): a point mutation and a 63-bp duplication. Amplification of the MDM2 gene was observed in two tumors (7.4%) by means of Southern-blot analysis, one of them also carrying the TP53 point mutation. Immunohis…

Tumor suppressor geneBlotting WesternSoft Tissue NeoplasmsBiologyPolymerase Chain ReactionPathology and Forensic MedicineImmunoenzyme TechniquesMiceProto-Oncogene ProteinsGene duplicationGene expressionAnimalsHumansneoplasmsMolecular BiologyGeneTP53 Gene MutationPolymorphism Single-Stranded ConformationalCell NucleusMice Inbred BALB CHistiocytoma Benign FibrousPoint mutationNuclear ProteinsSingle-strand conformation polymorphismProto-Oncogene Proteins c-mdm2Cell BiologyGeneral MedicineDNA NeoplasmMolecular biologyNeoplasm ProteinsSurvival RateBlotting SouthernTumor progressionMutationCancer researchNeoplasm Recurrence LocalTumor Suppressor Protein p53Virchows Archiv : an international journal of pathology
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Analysis of the p53 and MDM-2 gene in acute myeloid leukemia

1996

The MDM-2 (murine double minute 2) gene codes for a cellular protein that can bind to the p53 tumor suppressor gene product, thereby functioning as a negative regulator of p53. In order to define the role of the MDM-2 gene in the pathogenesis of human acute myeloid leukemia, the expression and the sequence of the MDM-2 gene were examined in samples of bone marrow and/or peripheral mononuclear cells of 38 patients by using immunostaining, polymerase chain reaction (PCR), single strand conformation polymorphism, and sequencing. Immunohistochemical staining detected a weak accumulation of the MDM-2 protein in AML patients of FAB classification M4 and M5. RT-PCR analysis revealed a heterogeneou…

Tumor suppressor geneGene ExpressionBiologyPolymerase Chain ReactionExonBone MarrowProto-Oncogene ProteinsGene expressionmedicineHumansMissense mutationRNA MessengerGenePolymorphism Single-Stranded ConformationalBase SequenceNuclear ProteinsMyeloid leukemiaProto-Oncogene Proteins c-mdm2Single-strand conformation polymorphismExonsSequence Analysis DNAHematologyGeneral MedicineGenes p53medicine.diseaseImmunohistochemistryMolecular biologyLeukemiaLeukemia MyeloidAcute DiseaseLeukocytes MononuclearCancer researchEuropean Journal of Haematology
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