Search results for "mutation."

showing 10 items of 2808 documents

Tetravalent single-chain avidin: from subunits to protein domains via circularly permuted avidins

2005

scAvd (single-chain avidin, where two dcAvd are joined in a single polypeptide chain), having four biotin-binding domains, was constructed by fusion of topologically modified avidin units. scAvd showed similar biotin binding and thermal stability properties as chicken avidin. The DNA construct encoding scAvd contains four circularly permuted avidin domains, plus short linkers connecting the four domains into a single polypeptide chain. In contrast with wild-type avidin, which contains four identical avidin monomers, scAvd enables each one of the four avidin domains to be independently modified by protein engineering. Therefore the scAvd scaffold can be used to construct spatially and stoich…

Models MolecularBiotin bindingProtein domainMolecular Sequence DataProtein EngineeringBiochemistrychemistry.chemical_compoundMoleculeAnimalsMolecular BiologyCells CulturedBinding SitesbiologyChemistryCell BiologyProtein engineeringCircular permutation in proteinsAvidinProtein Structure TertiaryCrystallographyProtein SubunitsMonomerBiophysicsbiology.proteinDNA constructChickensAvidinResearch ArticleProtein Binding
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Recurrent Mutations in the Basic Domain of TWIST2 Cause Ablepharon Macrostomia and Barber-Say Syndromes

2015

Contains fulltext : 153827.pdf (Publisher’s version ) (Open Access) Ablepharon macrostomia syndrome (AMS) and Barber-Say syndrome (BSS) are rare congenital ectodermal dysplasias characterized by similar clinical features. To establish the genetic basis of AMS and BSS, we performed extensive clinical phenotyping, whole exome and candidate gene sequencing, and functional validations. We identified a recurrent de novo mutation in TWIST2 in seven independent AMS-affected families, as well as another recurrent de novo mutation affecting the same amino acid in ten independent BSS-affected families. Moreover, a genotype-phenotype correlation was observed, because the two syndromes differed based s…

Models MolecularCandidate geneHirsutismProtein ConformationHeLa Cellmedicine.disease_causeTranscriptomeTwist transcription factorModelsGenetics(clinical)ExomeEye AbnormalitiesNon-U.S. Gov'tExomeGenetics (clinical)ZebrafishGeneticsMutationMicroscopyMacrostomiaSetleis syndromeHypertelorismResearch Support Non-U.S. Gov'tHypertrichosiEyelid DiseaseGENÉTICAPhenotypeEyelid DiseasesAbnormalitiesMultipleSequence AnalysisHumanChromatin ImmunoprecipitationMolecular Sequence DataMutation MissenseHypertrichosisAbnormalities; Multiple; Amino Acid Sequence; Animals; Base Sequence; Chromatin Immunoprecipitation; Exome; Eye Abnormalities; Eyelid Diseases; HeLa Cells; Hirsutism; Humans; Hypertelorism; Hypertrichosis; Macrostomia; Microscopy; Electron; Molecular Sequence Data; Mutation; Missense; Protein Conformation; Repressor Proteins; Sequence Analysis; DNA; Skin Abnormalities; Twist Transcription Factor; Zebrafish; Models; Molecular; Phenotype; Genetics; Genetics (clinical)Other Research Radboud Institute for Molecular Life Sciences [Radboudumc 0]BiologyResearch SupportElectronArticleFrameshift mutationGeneticAblepharon macrostomia syndromeSkin AbnormalitieGeneticsmedicineJournal ArticleAnimalsHumansAbnormalities MultipleAmino Acid SequenceNeurodevelopmental disorders Donders Center for Medical Neuroscience [Radboudumc 7]Base SequenceAnimalTwist-Related Protein 1MolecularSequence Analysis DNADNARepressor Proteinmedicine.diseaseRepressor ProteinsTwist Transcription FactorEye AbnormalitieMicroscopy ElectronMutationSkin Abnormalitiessense organsMissenseNanomedicine Radboud Institute for Molecular Life Sciences [Radboudumc 19]HeLa CellsAmerican journal of human genetics
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Asp333, Asp495, and His52.3 Form the Catalytic Triad of Rat Soluble Epoxide Hydrolase

1996

On the basis of the sequence similarity between mammalian epoxide hydrolases and bacterial haloalkane dehalogenase reported earlier (Arand, M., Grant, D. F., Beetham, J. K., Friedberg, T., Oesch, F., and Hammock, B. D. (1994) FEBS Lett. 338, 251-256; Beetham, J. K., Grant, D., Arand, M., Garbarino, J., Kiyosue, T., Pinot, F., Oesch, F., Belknap, W. R., Shinozaki, K., and hammock, B. D. (1995) DNA Cell. Biol. 14, 61-71) we selected candidate amino acid residues for the putative catalytic triad of the rat soluble epoxide hydrolase. The predicted amino acid residues were exchanged by site-directed mutagenesis of the epoxide hydrolase cDNA, followed by the expression of the respective mutant en…

Models MolecularEpoxide hydrolase 2StereochemistryMolecular Sequence DataRestriction MappingPolymerase Chain ReactionBiochemistryCatalysisProtein Structure SecondaryCatalytic triadEscherichia coliAnimalsHumansPoint MutationHistidineAmino Acid SequenceCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceDNA PrimersEpoxide Hydrolaseschemistry.chemical_classificationAspartic AcidBinding SitesSequence Homology Amino AcidChemistryCell BiologyRecombinant ProteinsRatsAmino acidEpoxide hydrolase activityKineticsBiochemistryEpoxide HydrolasesMutagenesis Site-DirectedHaloalkane dehalogenaseJournal of Biological Chemistry
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Molecular dynamics studies on HIV-1 protease: a comparison of the flap motions between wild type protease and the M46I/G51D double mutant

2007

The emergence of drug-resistant mutants of HIV-1 is a tragic effect associated with conventional long-treatment therapies against acquired immunodeficiency syndrome. These mutations frequently involve the aspartic protease encoded by the virus; knowledge of the molecular mechanisms underlying the conformational changes of HIV-1 protease mutants may be useful in developing more effective and longer lasting treatment regimes. The flap regions of the protease are the target of a particular type of mutations occurring far from the active site. These mutations modify the affinity for both substrate and ligands, thus conferring resistance. In this work, molecular dynamics simulations were perform…

Models MolecularGromacs 3.2Anti-HIV AgentsProtein Conformationmedicine.medical_treatmentflap motionMutantCatalysisVirusInorganic ChemistryProtein structureHIV ProteaseHIV-1 proteaseDrug Resistance ViralEnzyme StabilityHIV-1 proteasemedicineHumansComputer SimulationPhysical and Theoretical Chemistrychemistry.chemical_classificationProteasebiologyHIV-1 drug-resistant mutantOrganic ChemistryWild typeActive siteRecombinant ProteinsComputer Science ApplicationsCell biologyEnzymemolecular dynamics simulationAmino Acid SubstitutionComputational Theory and MathematicsBiochemistrychemistryMutationHIV-1biology.protein
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Identification of a novel activating mutation (Y842C) within the activation loop of FLT3 in patients with acute myeloid leukemia (AML).

2004

Fms-like tyrosine kinase 3 (FLT3) receptor mutations as internal tandem duplication (ITD) or within the kinase domain are detected in up to 35% of patients with acute myeloid leukemia (AML). N-benzoyl staurosporine (PKC412), a highly effective inhibitor of mutated FLT3 receptors, has significant antileukemic efficacy in patients with FLT3-mutated AML. Mutation screening of FLT3 exon 20 in AML patients (n = 110) revealed 2 patients with a novel mutation (Y842C) within the highly conserved activation loop of FLT3. FLT3-Y842C-transfected 32D cells showed constitutive FLT3 tyrosine phosphorylation and interleukin 3 (IL-3)-independent growth. Treatment with PKC412 led to inhibition of proliferat…

Models MolecularImmunologyBiologymedicine.disease_causeBiochemistryCell Linechemistry.chemical_compoundMicefluids and secretionshemic and lymphatic diseasesProto-Oncogene ProteinsmedicineSTAT5 Transcription FactorAnimalsHumansTyrosinePhosphotyrosineMutationCell CycleMyeloid leukemiaReceptor Protein-Tyrosine Kinaseshemic and immune systemsTyrosine phosphorylationCell BiologyHematologymedicine.diseaseMilk ProteinsProtein Structure TertiaryDNA-Binding ProteinsEnzyme ActivationLeukemiaLeukemia Myeloid AcutechemistryGene Expression Regulationfms-Like Tyrosine Kinase 3embryonic structuresFms-Like Tyrosine Kinase 3MutationCancer researchTrans-ActivatorsTyrosineSignal transductionTyrosine kinaseSignal TransductionBlood
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Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling.

2014

The type I interferon system is integral to human antiviral immunity. However, inappropriate stimulation or defective negative regulation of this system can lead to inflammatory disease. We sought to determine the molecular basis of genetically uncharacterized cases of the type I interferonopathy Aicardi-Goutières syndrome, and of other patients with undefined neurological and immunological phenotypes also demonstrating an upregulated type I interferon response. We found that heterozygous mutations in the cytosolic double-stranded RNA receptor gene IFIH1 (MDA5) cause a spectrum of neuro-immunological features consistently associated with an enhanced interferon state. Cellular and biochemica…

Models MolecularInterferon-Induced Helicase IFIH1Molecular Sequence DataHDE NEU PEDElectrophoretic Mobility Shift AssayBiologymedicine.disease_causeNervous System MalformationsReal-Time Polymerase Chain ReactionArticleDEAD-box RNA HelicasesImmune systemAutoimmune Diseases of the Nervous SystemDownregulation and upregulationAnalysis of Variance; Autoimmune Diseases of the Nervous System; Base Sequence; DEAD-box RNA Helicases; Electrophoretic Mobility Shift Assay; Exome; HEK293 Cells; Humans; Interferon Type I; Microsatellite Repeats; Molecular Sequence Data; Mutation; Nervous System Malformations; Real-Time Polymerase Chain Reaction; Sequence Analysis DNA; Signal Transduction; Spectrum Analysis; Models Molecular; Phenotype; GeneticsModelsInterferonGeneticsmedicineHumansExomeMutationAnalysis of VarianceBase SequenceSpectrum AnalysisMolecularRNAMDA5DNASequence Analysis DNAMolecular biology3. Good healthInterferon Tipo IHEK293 CellsPhenotypeInterferon Type IMutationCancer researchSignal transductionSequence AnalysisInterferon type Imedicine.drugMicrosatellite RepeatsSignal TransductionNature genetics
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Transient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome.

2020

Phytochromes are photosensory proteins in plants, fungi, and bacteria, which detect red- and far-red light. They undergo a transition between the resting (Pr) and photoactivated (Pfr) states. In bacterial phytochromes, the Pr-to-Pfr transition is facilitated by two intermediate states, called Lumi-R and Meta-R. The molecular structures of the protein in these states are not known and the molecular mechanism of photoconversion is not understood. Here, we apply transient infrared absorption spectroscopy to study the photocycle of the wild-type and Y263F mutant of the phytochrome from Deinococcus radiodurans (DrBphP) from nanoto milliseconds. We identify two sequentially forming Lumi-R states …

Models MolecularLight Signal TransductionSpectrophotometry InfraredspektroskopiaMutantGeneral Physics and AstronomyInfrared spectroscopy010402 general chemistry01 natural sciences03 medical and health scienceschemistry.chemical_compoundProtein structureBacterial ProteinsinfrapunasäteilyPhysical and Theoretical ChemistryTyrosineSpectroscopy030304 developmental biology0303 health sciencesBiliverdinPhytochromebiologyChemistryDeinococcus radioduransbiology.organism_classification0104 chemical sciencesProtein Structure TertiaryMutationBiophysicsproteiinitvalokemiaDeinococcusPhytochromePhysical chemistry chemical physics : PCCP
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Missense variants in DPYSL5 cause a neurodevelopmental disorder with corpus callosum agenesis and cerebellar abnormalities

2021

International audience; The collapsin response mediator protein (CRMP) family proteins are intracellular mediators of neurotrophic factors regulating neurite structure/spine formation and are essential for dendrite patterning and directional axonal pathfinding during brain developmental processes. Among this family, CRMP5/DPYSL5 plays a significant role in neuronal migration, axonal guidance, dendrite outgrowth, and synapse formation by interacting with microtubules. Here, we report the identification of missense mutations in DPYSL5 in nine individuals with brain malformations, including corpus callosum agenesis and/or posterior fossa abnormalities, associated with variable degrees of intel…

Models MolecularMale0301 basic medicineHydrolases[SDV]Life Sciences [q-bio]Hippocampal formationMedical and Health Sciences0302 clinical medicineNeurodevelopmental disorderTubulinModelsNeurotrophic factorsCerebellumIntellectual disability2.1 Biological and endogenous factorsMissense mutationAetiologyChilddendrite branchingGenetics (clinical)de novo missense variantsPediatricGenetics & HeredityDPYSL5Biological Sciences[SDV] Life Sciences [q-bio]corpus callosum agenesisMental HealthChild PreschoolNeurologicalFemaleMicrotubule-Associated ProteinsAdultNeuriteIntellectual and Developmental Disabilities (IDD)primary neuronal culturesMutation MissenseBiologyYoung Adult03 medical and health sciencesRare DiseasesMediatorReportIntellectual DisabilityGeneticsmedicineHumansPreschoolCorpus Callosum Agenesisbrain malformationNeurosciencesMolecularmedicine.diseaseneurodevelopmental disorderBrain Disorders030104 developmental biologyNeurodevelopmental DisordersMutationMissenseAgenesis of Corpus CallosumNeuroscience030217 neurology & neurosurgery
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Docking and multivariate methods to explore HIV-1 drug-resistance: a comparative analysis

2007

In this paper we describe a comparative analysis between multivariate and docking methods in the study of the drug resistance to the reverse transcriptase and the protease inhibitors. In our early papers we developed a simple but efficient method to evaluate the features of compounds that are less likely to trigger resistance or are effective against mutant HIV strains, using the multivariate statistical procedures PCA and DA. In the attempt to create a more solid background for the prediction of susceptibility or resistance, we carried out a comparative analysis between our previous multivariate approach and molecular docking study. The intent of this paper is not only to find further supp…

Models MolecularMultivariate statisticsMultivariate analysisAnti-HIV AgentsCombined useHuman immunodeficiency virus (HIV)Computational biologyDrug resistanceBiologyLigandsBioinformaticsmedicine.disease_causeHIV ProteaseMolecular descriptorDrug Resistance ViralDrug DiscoverymedicineHumansDOCKINGPhysical and Theoretical ChemistryBinding SitesHIV Protease InhibitorsSettore CHIM/08 - Chimica FarmaceuticaHIV Reverse TranscriptaseComputer Science ApplicationsDRUG RESISTANCEDocking (molecular)Drug DesignMultivariate AnalysisMutationHIV-1Computer-Aided DesignReverse Transcriptase InhibitorsMultivariate statisticalJournal of Computer-Aided Molecular Design
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Theoretical site-directed mutagenesis: Asp168Ala mutant of lactate dehydrogenase

2008

Molecular simulations based on the use of hybrid quantum mechanics/molecular mechanics methods are able to provide detailed information about the complex enzymatic reactions and the consequences of specific mutations on the activity of the enzyme. In this work, the reduction of pyruvate to lactate catalysed by wild-type and Asp168Ala mutant lactate dehydrogenase (LDH) has been studied by means of simulations using a very flexible molecular model consisting of the full tetramer of the enzyme, together with the cofactor NADH, the substrate and solvent water molecules. Our results indicate that the Asp168Ala mutation provokes a shift in the p K a value of Glu199 that becomes unprotonated at n…

Models MolecularMutantBiomedical EngineeringBiophysicsMutation MissenseBioengineeringBiochemistryMolecular mechanicsCofactorEnzyme catalysisBiomaterialschemistry.chemical_compoundLactate dehydrogenaseComputer SimulationSite-directed mutagenesisbiologyL-Lactate DehydrogenaseMolecular StructureWild typeSubstrate (chemistry)Computational BiologychemistryBiochemistrybiology.proteinBiophysicsMutagenesis Site-DirectedBiotechnologyResearch Article
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