Search results for "Mutant Protein"

showing 10 items of 42 documents

Recombinant NeutraLite Avidin: a non-glycosylated, acidic mutant of chicken avidin that exhibits high affinity for biotin and low non-specific bindin…

2000

AbstractA recombinant non-glycosylated and acidic form of avidin was designed and expressed in soluble form in baculovirus-infected insect cells. The mutations were based on the same principles that guided the design of the chemically and enzymatically modified avidin derivative, known as NeutraLite Avidin. In this novel recombinant avidin derivative, five out of the eight arginine residues were replaced with neutral amino acids, and two of the lysine residues were replaced by glutamic acid. In addition, the carbohydrate-bearing asparagine-17 residue was altered to an isoleucine, according to the known sequences of avidin-related genes. The resultant mutant protein, termed recombinant Neutr…

StreptavidinGlycosylationMolecular Sequence DataBiophysicsBiotinChick EmbryoNon-specific bindingBiochemistrylaw.inventionchemistry.chemical_compoundBiotinstomatognathic systemStructural BiologylawMutant proteinNon-glycosylated mutantGeneticsAnimalsHumansAmino Acid SequenceIsoelectric PointProtein Structure QuaternaryMolecular BiologyCells CulturedbiologyAvidin-biotin technologyDNACell BiologyProtein engineeringrespiratory systemAvidinRecombinant ProteinsKineticsAmino Acid SubstitutionchemistryBiochemistryBiotinylationMutationbiology.proteinRecombinant DNAThermodynamicsProtein engineeringEndopeptidase KIsoleucineBaculoviridaeProtein BindingAvidinFEBS Letters
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An overview on chemical structures as ΔF508-CFTR correctors

2019

Deletion of phenylalanine at position 508 (F508del) in the CFTR protein, is the most common mutation causing cystic fibrosis (CF). F508del causes misfolding and rapid degradation of CFTR protein a defect that can be targeted with pharmacological agents termed “correctors”. Correctors belong to various chemical classes but are generally small molecules based on nitrogen sulfur or oxygen heterocycles. The mechanism of action of correctors is generally unknown but there is experimental evidence that some of them can directly act on mutant CFTR improving folding and stability. Here we overview the characteristics of the various F508del correctors described so far to obtain indications on key ch…

Protein FoldingCystic FibrosisCFTR correctorMutantCystic Fibrosis Transmembrane Conductance RegulatorPyrimidinonesmedicine.disease_cause01 natural sciencesF508del-CFTR03 medical and health sciencesMutant proteinDrug DiscoverymedicineAnimalsHumansCFTR030304 developmental biologyPharmacology0303 health sciencesMutationCFTR correctorsbiology010405 organic chemistryChemistryOrganic ChemistryCFTR; CFTR correctors; Cystic fibrosis; Cystic fibrosis transmembrane conductance regulator; F508del-CFTR; Animals; Cystic Fibrosis; Cystic Fibrosis Transmembrane Conductance Regulator; Humans; Mutation; Protein Folding; Pyrimidinones; ThiazolesGeneral MedicineSettore CHIM/08 - Chimica FarmaceuticaSmall moleculeCystic fibrosis transmembrane conductance regulator0104 chemical sciencesCell biologyThiazolesMechanism of actionCystic fibrosiMutationbiology.proteinmedicine.symptomProtein Aδf508 cftrEuropean Journal of Medicinal Chemistry
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Inhibition of autophagy rescues muscle atrophy in a LGMDD2 Drosophila model

2021

Limb-girdle muscular dystrophy D2 (LGMDD2) is an ultrarare autosomal dominant myopathy caused by mutation of the normal stop codon of the TNPO3 nuclear importin. The mutant protein carries a 15 amino acid C-terminal extension associated with pathogenicity. Here we report the first animal model of the disease by expressing the human mutant TNPO3 gene in Drosophila musculature or motor neurons and concomitantly silencing the endogenous expression of the fly protein ortholog. A similar genotype expressing wildtype TNPO3 served as a control. Phenotypes characterization revealed that mutant TNPO3 expression targeted at muscles or motor neurons caused LGMDD2-like phenotypes such as muscle degener…

MaleMutantBiochemistryAnimals Genetically ModifiedMutant proteinAutophagyGeneticsmedicineAnimalsHumansGene silencingMuscular dystrophyMyopathyMolecular BiologyMotor NeuronsbiologyMusclesAutophagyChloroquinebeta Karyopherinsmedicine.diseasebiology.organism_classificationMuscle atrophyCell biologySurvival RateDisease Models AnimalMuscular AtrophyDrosophila melanogasterPhenotypeMuscular Dystrophies Limb-GirdleInsect HormonesFemalemedicine.symptomDrosophila melanogasterLocomotionBiotechnologyThe FASEB Journal
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Circadian System Functionality, Hippocampal Oxidative Stress, and Spatial Memory in the APPswe/PS1dE9 Transgenic Model of Alzheimer Disease: Effects …

2012

Alzheimer disease (AD) is a neurodegenerative disorder that primarily causes β-amyloid accumulation in the brain, resulting in cognitive and behavioral deficits. AD patients, however, also suffer from severe circadian rhythm disruptions, and the underlying causes are still not fully known. Patients with AD show reduced systemic melatonin levels. This may contribute to their symptoms, since melatonin is an effective chronobiotic and antioxidant with neuroprotective properties. Here, the authors critically assessed the effects of long-term melatonin treatment on circadian system function, hippocampal oxidative stress, and spatial memory performance in the APPswe/PS1 double transgenic (Tg) mou…

Malemedicine.medical_specialtyPhysiologyChronobioticRamelteonReceptors MelatoninHippocampusMice TransgenicMotor Activitymedicine.disease_causeHippocampusNeuroprotectionBody TemperatureMelatoninAmyloid beta-Protein PrecursorMiceAlzheimer DiseaseMemoryPhysiology (medical)Internal medicinePresenilin-1medicineAnimalsCircadian rhythmMelatoninmedicine.diseaseCircadian RhythmDisease Models AnimalOxidative StressEndocrinologyIndenesMutant ProteinsAlzheimer's diseasePsychologyNeuroscienceOxidative stressmedicine.drugChronobiology International
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Human apolipoprotein A-I natural variants: molecular mechanisms underlying amyloidogenic propensity

2012

Human apolipoprotein A-I (apoA-I)-derived amyloidosis can present with either wild-type (Wt) protein deposits in atherosclerotic plaques or as a hereditary form in which apoA-I variants deposit causing multiple organ failure. More than 15 single amino acid replacement amyloidogenic apoA-I variants have been described, but the molecular mechanisms involved in amyloid-associated pathology remain largely unknown. Here, we have investigated by fluorescence and biochemical approaches the stabilities and propensities to aggregate of two disease-associated apoA-I variants, apoA-IGly26Arg, associated with polyneuropathy and kidney dysfunction, and apoA-ILys107-0, implicated in amyloidosis in severe…

ProteomicsProtein Foldinglcsh:MedicineProtein aggregationpolymyxinsBiochemistryProtein Structure SecondaryMiceProtein structureneutrophilsMolecular Cell Biologypolycyclic compoundslcsh:ScienceCellular Stress ResponsesMultidisciplinaryProtein StabilityAmyloidosisCiencias QuímicasfluorescenseCell biologymacrophagesBiochemistryToxicityMedicineProtein foldinglipids (amino acids peptides and proteins)medicine.symptomPolyneuropathyResearch ArticleProtein StructureMedicinaLipoproteinsImmunologyBiophysicsInflammationAmyloidogenic ProteinsBiologyProtein ChemistryMicrobiologyCell Lineprotein aggregationmacrophage activationmedicineAnimalsHumansoligomersProtein InteractionsBiologyInflammationamyloidosisApolipoprotein A-IMacrophageslcsh:RImmunityProteinsnutritional and metabolic diseasesmedicine.diseaseApolipoproteinsAmino Acid SubstitutionCell cultureinflammationCiencias Médicaslcsh:QClinical ImmunologyMutant ProteinspolyneuropathyProtein Multimerization
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Respiratory behaviour of a Zymomonas mobilis adhB::kan(r) mutant supports the hypothesis of two alcohol dehydrogenase isoenzymes catalysing opposite …

2006

AbstractPerturbation of the aerobic steady-state in a chemostat culture of the ethanol-producing bacterium Zymomonas mobilis with a small pulse of ethanol causes a burst of ethanol oxidation, although the reactant ratio of the alcohol dehydrogenase (ADH) reaction ([NADH][acetaldehyde][H+])/([ethanol][NAD+]) remains above the Keq value. Simultaneous catalysis of ethanol synthesis and oxidation by the two ADH isoenzymes, residing in different redox microenvironments, has been proposed previously. In the present study, this hypothesis is verified by construction of an ADH-deficient strain and by demonstration that it lacks the oxidative burst in response to perturbation of its aerobic steady-s…

Kanamycin ResistanceBiophysicsMetabolic channellingChemostatBiochemistryRedoxZymomonas mobilisModels BiologicalCatalysischemistry.chemical_compoundContinuous cultureStructural BiologyGeneticsEthanol metabolismMolecular BiologyAlcohol dehydrogenaseZymomonasEthanolbiologyEthanolChemistryRespirationZymomonas mobilisAcetaldehydeAlcohol DehydrogenaseCell Biologybiology.organism_classificationAerobiosisIsoenzymesKineticsBiochemistrybiology.proteinMutant ProteinsNAD+ kinaseFEBS letters
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Crystal structures of bR(D85S) favor a model of bacteriorhodopsin as a hydroxyl-ion pump

2003

AbstractStructural features on the extracellular side of the D85S mutant of bacteriorhodopsin (bR) suggest that wild-type bR could be a hydroxyl-ion pump. A position between the protonated Schiff base and residue 85 serves as an anion-binding site in the mutant protein, and hydroxyl ions should have access to this site during the O-intermediate of the wild-type bR photocycle. The guanidinium group of R82 is proposed (1) to serve as a shuttle that eliminates the Born energy penalty for entry of an anion into this binding pocket, and conversely, (2) to block the exit of a proton or a related proton carrier.

Models MolecularProtein ConformationAnion Transport ProteinsBiophysicsBacteriorhodopsinProtonationCrystal structureCrystallography X-RayBiochemistryIon pumpIonchemistry.chemical_compoundResidue (chemistry)Structural BiologyMutant proteinHydroxidesGeneticsMolecular BiologyIon TransportSchiff basebiologyChemistryBacteriorhodopsinCell BiologyCrystallographyIon pumpBacteriorhodopsinsMutationbiology.proteinHydroxyl ionProtonsFEBS Letters
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Delayed lysis confers resistance to the nucleoside analogue 5-fluorouracil and alleviates mutation accumulation in the single-stranded DNA bacterioph…

2014

ABSTRACT Rates of spontaneous mutation determine viral fitness and adaptability. In RNA viruses, treatment with mutagenic nucleoside analogues selects for polymerase variants with increased fidelity, showing that viral mutation rates can be adjusted in response to imposed selective pressures. However, this type of resistance is not possible in viruses that do not encode their own polymerases, such as single-stranded DNA viruses. We previously showed that serial passaging of bacteriophage ϕX174 in the presence of the nucleoside analogue 5-fluorouracil (5-FU) favored substitutions in the lysis protein E (P. Domingo-Calap, M. Pereira-Gomez, and R. Sanjuán, J. Virol. 86: 9640–9646, 2012, doi:10…

Mutation rateImmunologyAdaptation BiologicalMutation MissenseDNA Single-Strandedmedicine.disease_causeMicrobiologyBacteriophage03 medical and health scienceschemistry.chemical_compoundViral ProteinsBacteriolysisMutation RateVirologymedicineBacteriophagesSelection GeneticPolymerase030304 developmental biologyGenetics0303 health sciencesMutationbiology030302 biochemistry & molecular biologyMutagenesisMutation AccumulationResistance mutationbiology.organism_classificationVirologychemistryGenetic Diversity and EvolutionInsect ScienceDNA Viralbiology.proteinMutant ProteinsFluorouracilDNAJournal of virology
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Hepatitis B Virus Large Envelope Protein Interacts with γ2-Adaptin, a Clathrin Adaptor-Related Protein

2001

ABSTRACT For the outcome of a hepatitis B virus (HBV) infection, the viral L envelope protein with its pre-S domain performs pivotal functions by mediating attachment of HBV to liver cells, envelopment of viral capsids, release of (sub)viral particles, regulation of supercoiled DNA amplification, and transcriptional transactivation. To assess its multiple functions and host-protein assistance involved, we initiated a two-hybrid screen using the L-specific pre-S1 domain as bait. With this approach, we have identified γ2-adaptin, a putative member of the clathrin adaptor proteins responsible for protein sorting and trafficking, as a specific binding partner of L protein. Evidence for a physic…

Hepatitis B virusVesicle-associated membrane protein 8ImmunoprecipitationImmunologyGolgi ApparatusTransfectionmedicine.disease_causeMicrobiologyClathrinChromatography AffinityCytosolViral Envelope ProteinsMutant proteinYeastsVirologyProtein targetingmedicineAnimalsBinding siteAdaptor Protein Complex gamma SubunitsBinding SitesbiologyMembrane ProteinsPrecipitin TestsClathrinTransmembrane proteinVirus-Cell InteractionsCell biologyInsect ScienceCOS CellsMutationbiology.proteinClathrin adaptor proteinsProtein BindingJournal of Virology
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Evaluation of Fused Pyrrolothiazole Systems as Correctors of Mutant CFTR Protein.

2021

Cystic fibrosis (CF) is a genetic disease caused by mutations that impair the function of the CFTR chloride channel. The most frequent mutation, F508del, causes misfolding and premature degradation of CFTR protein. This defect can be overcome with pharmacological agents named “correctors”. So far, at least three different classes of correctors have been identified based on the additive/synergistic effects that are obtained when compounds of different classes are combined together. The development of class 2 correctors has lagged behind that of compounds belonging to the other classes. It was shown that the efficacy of the prototypical class 2 corrector, the bithiazole corr-4a, could be impr…

Yellow fluorescent proteinProtein FoldingCystic FibrosisMutantPharmaceutical ScienceCystic Fibrosis Transmembrane Conductance RegulatorCarboxamidemedicine.disease_cause01 natural sciencesAnalytical Chemistrychemistry.chemical_compoundMutant ProteinDrug DiscoveryMoietyCFTR potentiatorCFTRchemistry.chemical_classification0303 health sciencesMutationbiologyChemistryChemistry (miscellaneous)Chloride channelMolecular MedicineHumanStereochemistrymedicine.drug_classCFTR correctorArticleF508del-CFTRlcsh:QD241-44103 medical and health scienceslcsh:Organic chemistrymedicineHumansBenzodioxolesPhysical and Theoretical ChemistryThiazoleCystic Fibrosi030304 developmental biology010405 organic chemistryOrganic ChemistryAminoimidazole Carboxamide0104 chemical sciencesThiazolesMutationbiology.proteinMutant ProteinsBenzodioxoleTricyclicMolecules (Basel, Switzerland)
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