Search results for "nonsense mutation"

showing 10 items of 86 documents

Minimum Free Energy Based Evaluation of mRNAs Secondary Structures Constructed by 18 Clinically Significant Exonic Single Nucleotide Polymorphisms (S…

2015

Clinically significant 18 Single Nucleotide Polymorphisms (SNPs) from exon regions of Retinoblastoma gene (RB1) were analyzed to find out the structural variations in mRNAs. Online bioinformatic tools i.e., Vienna RNA, RNAfold were used for secondary structure analysis of mRNAs. Predicted minimum Free Energy Change (MFE) was calculated for mRNAs structures. It has been observed that the average of predicted MFE value from 13 nonsense mutations was higher (0.76 kcal/mol) in comparison to 5 missense mutations. Presumably, 13 nonsense mutations are responsible for Nonsense Mediated mRNA Decay (NMD), therefore, excluded from haplotype analysis. From the statistical analysis all the thermodynami…

GeneticsExonNonsense mutationHaplotypeNonsense-mediated decaySNPRNAMissense mutationSingle-nucleotide polymorphismBiologyBiochemistryMolecular biologyBiotechnologyAmerican Journal of Biochemistry and Biotechnology
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Translational readthrough of ciliopathy genes BBS2 and ALMS1 restores protein, ciliogenesis and function in patient fibroblasts

2021

Abstract Background Ciliary dysfunction underlies a range of genetic disorders collectively termed ciliopathies, for which there are no treatments available. Bardet-Biedl syndrome (BBS) is characterised by multisystemic involvement, including rod-cone dystrophy and renal abnormalities. Together with Alstrom syndrome (AS), they are known as the ‘obesity ciliopathies’ due to their common phenotype. Nonsense mutations are responsible for approximately 11% and 40% of BBS and AS cases, respectively. Translational readthrough inducing drugs (TRIDs) can restore full-length protein bypassing in-frame premature termination codons, and are a potential therapeutic approach for nonsense-mediated ciliop…

BBS2AdultMaleMedicine (General)AdolescentNonsense mutationAminopyridinesCell Cycle ProteinsCiliopathiesGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundR5-920AtalurenCiliogenesismedicineHumansReceptors SomatostatinBardet-Biedl SyndromeAlstrom SyndromeCells CulturedOxadiazolesbusiness.industryTumor Suppressor ProteinsTranslational readthroughRProteinsGeneral MedicineFibroblastsmedicine.diseaseNonsense suppressionCiliopathiesAtalurenCiliopathyALMS1chemistryCodon NonsenseAmlexanoxCancer researchMedicineBBS2businessAlström syndromeResearch PaperEBioMedicine
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Genotype-phenotype correlations in nemaline myopathy caused by mutations in the genes for nebulin and skeletal muscle alpha-actin.

2003

We present comparisons of the clinical pictures in a series of 60 patients with nemaline myopathy in whom mutations had been identified in the genes for nebulin or skeletal muscle alpha-actin. In the patients with nebulin mutations, the typical form of nemaline myopathy predominated, while severe, mild or intermediate forms were less frequent. Autosomal recessive inheritance had been verified or appeared likely in all nebulin cases. In the patients with actin mutations, the severe form of nemaline myopathy was the most common, but some had the mild or typical form, and a few showed other associated features such as intranuclear rods or actin accumulation. Most cases were sporadic, but in ad…

AdultMalePathologymedicine.medical_specialtyAdolescentGenotypeNonsense mutationDNA Mutational AnalysisMuscle ProteinsBiologymedicine.disease_causeMyopathies Nemaline03 medical and health sciencesNebulin0302 clinical medicineNemaline myopathyGenotypemedicineHumansChildMuscle SkeletalGenetics (clinical)Actin030304 developmental biologyGenetics0303 health sciencesMutationInfantmedicine.diseaseCongenital myopathyPhenotypeActinsPhenotypeNeurologyChild PreschoolPediatrics Perinatology and Child HealthMutationbiology.proteinFemaleNeurology (clinical)030217 neurology & neurosurgeryNeuromuscular disorders : NMD
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Functional characterisation of alpha-galactosidase a mutations as a basis for a new classification system in fabry disease.

2013

Fabry disease (FD) is an X-linked hereditary defect of glycosphingolipid storage caused by mutations in the gene encoding the lysosomal hydrolase α-galactosidase A (GLA, α-gal A). To date, over 400 mutations causing amino acid substitutions have been described. Most of these mutations are related to the classical Fabry phenotype. Generally in lysosomal storage disorders a reliable genotype/phenotype correlation is difficult to achieve, especially in FD with its X-linked mode of inheritance. In order to predict the metabolic consequence of a given mutation, we combined in vitro enzyme activity with in vivo biomarker data. Furthermore, we used the pharmacological chaperone (PC) 1-deoxygalacto…

Cancer Research1-Deoxynojirimycinlcsh:QH426-470Nonsense mutationMutantBiologymedicine.disease_causeGeneticsmedicineHumansBiologyMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and SystematicsGeneticsSphingolipidsMutationAlpha-galactosidasePoint mutationmedicine.diseasePhenotypeFabry diseasePharmacological chaperoneProtein Transportlcsh:GeneticsPhenotypeAmino Acid Substitutionalpha-GalactosidaseMutationComputer Sciencebiology.proteinFabry DiseaseMedicineGlycolipidsResearch Articlemedicine.drugPLoS Genetics
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The G428A Nonsense Mutation in FUT2 Provides Strong but Not Absolute Protection against Symptomatic GII.4 Norovirus Infection

2009

In November 2004, 116 individuals in an elderly nursing home in El Grao de Castellón, Spain were symptomatically infected with genogroup II.4 (GII.4) norovirus. The global attack rate was 54.2%. Genotyping of 34 symptomatic individuals regarding the FUT2 gene revealed that one patient was, surprisingly, a non-secretor, hence indicating secretor-independent infection. Lewis genotyping revealed that Lewis-positive and negative individuals were susceptible to symptomatic norovirus infection indicating that Lewis status did not predict susceptibility. Saliva based ELISA assays were used to determine binding of the outbreak virus to saliva samples. Saliva from a secretor-negative individual boun…

Medicin och hälsovetenskapSalivaGenotypevirusesNonsense mutationPublic Health and Epidemiology/Infectious Diseaseslcsh:MedicineEnzyme-Linked Immunosorbent AssayBiologymedicine.disease_causeMedical and Health SciencesVirusABO Blood-Group SystemDisease OutbreaksLewis Blood Group Antigensfluids and secretionsVirologyGenotypemedicineHumansSalivalcsh:ScienceGenotypingPhylogenyCaliciviridae InfectionsMultidisciplinaryReverse Transcriptase Polymerase Chain ReactionNoroviruslcsh:Rvirus diseasesOutbreakFucosyltransferasesVirologyBiochemistry/Molecular EvolutionCodon NonsenseSpainViral evolutionNoroviruslcsh:QResearch ArticlePLoS ONE
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Nonsense codons suppression. An acute toxicity study of three optimized TRIDs in murine model, safety and tolerability evaluation.

2022

Stop mutations cause 11% of the genetic diseases, due to the introduction of a premature termination codon (PTC) in the mRNA, followed by the production of a truncated protein. A promising therapeutic approach is the suppression therapy by Translational Readthrough Inducing Drugs (TRIDs), restoring the expression of the protein. Recently, three new TRIDs (NV848, NV914, NV930) have been proposed, and validated by several in vitro assays, for the rescue of the CFTR protein, involved in Cystic Fibrosis disease. In this work, an acute toxicological study for the three TRIDs was conducted in vivo on mice, according to the OECD No.420 guidelines. Animals were divided into groups and treated with …

PharmacologyNonsense mutationCystic Fibrosis Transmembrane Conductance RegulatorGeneral MedicineOxadiazoleMiceDisease Models AnimalPremature termination codon (PTC)Pharmaceutical PreparationsCodon NonsenseProtein BiosynthesisAnimalsToxicity studyTranslational readthrough inducing drugs(TRIDs)Biomedicinepharmacotherapy = Biomedecinepharmacotherapie
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Heterozygous nonsense SCN5A mutation W822X explains a simultaneous sudden infant death syndrome.

2008

The sudden, unexpected, and unexplained death of both members of a set of healthy twins (simultaneous sudden infant death syndrome (SSIDS)) is defined as a case in which both infants meet the definition of sudden infant death syndrome individually. A search of the world medical literature resulted in only 42 reported cases of SSIDS. We report the case of a pair of identical, male, monozygotic twins, 138 days old, who suddenly died, meeting the full criteria of SSIDS and where a genetic screen was performed, resulting in a heterozygous nonsense SCN5A mutation (W822X) in both twins. Immunohistochemistry was performed on cardiac tissue samples utilizing polyclonal antibodies anti-Na+ CP type V…

MalePathologymedicine.medical_specialtyNav1.5 protein functionv1.5 protein functionmedia_common.quotation_subject2734Nonsense mutationNonsenseNa+ channel functionMuscle ProteinsSocio-culturaleBiology+Nav1.5 protein function; Na+ channel function; SCN5A gene mutation; Simultaneous sudden infant death syndrome; W822X mutation; Codon Nonsense; Diseases in Twins; Humans; Infant; Male; Muscle Proteins; NAV1.5 Voltage-Gated Sodium Channel; Sodium Channels; Sudden Infant Death; 2734Sudden deathSodium ChannelsNAV1.5 Voltage-Gated Sodium ChannelPathology and Forensic MedicinePathogenesisSCN5A gene mutationDiseases in TwinsmedicineHumansSimultaneous sudden infant death syndromeSCN5A gene mutationW822X mutationNa+ channel functionNav1.5 protein functionNaSimultaneous sudden infant death syndrome SCN5A gene mutation W822X mutation Na+ channel function Nav1.5 protein function CodonMolecular BiologyCellular localizationmedia_commonSimultaneous sudden infant death syndromeSettore BIO/16 - Anatomia UmanaSimultaneous sudden infant death syndrome SCN5A gene mutation W822X mutation Na+ channel function Nav1.5 protein functionW822X mutationInfantCell BiologyGeneral MedicineSudden infant death syndromeNonsenseTerminal deoxynucleotidyl transferaseCodon NonsenseImmunohistochemistryNa; v; 1.5 protein function; Na; +; channel function; SCN5A gene mutation; Simultaneous sudden infant death syndrome; W822X mutationchannel functionSudden Infant Death
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RESCUE OF LRBA GENE EXPRESSION IN PRIMARY HUMAN FIBROBLASTS CHARACTERISED BY NONSENSE MUTATION c. 5047 (C>T).

2021

Primary immunodeficiencies (PIDs) are rare genetic diseases characterized by susceptibility to infections, increased risk of autoimmunity, hypogammaglobulinemia, and lymphoproliferative syndromes. PIDs are associated to genetic alterations in about 400 known genes, among which, mutations of the LRBA gene. LRBA gene encodes a widely expressed multi-domain protein with highly conserved BEACH domain, involved in regulation of endosomal trafficking, particularly endocytosis of ligand-activated receptors. It was reported that stop mutations affect this gene leading to the loss of the protein expression. Recently, we identified three Translational Readthrough Inducing Drug (TRID), that showed hig…

translational readthroughNonsense mutationTRID
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A comparative evaluation of NB30, NB54 and PTC124 in translational read-through efficacy for treatment of an USH1C nonsense mutation

2012

Translational read-through-inducing drugs (TRIDs) promote read-through of nonsense mutations, placing them in the spotlight of current gene-based therapeutic research. Here, we compare for the first time the relative efficacies of new-generation aminoglycosides NB30, NB54 and the chemical compound PTC124 on retinal toxicity and read-through efficacy of a nonsense mutation in the USH1C gene, which encodes the scaffold protein harmonin. This mutation causes the human Usher syndrome, the most common form of inherited deaf-blindness. We quantify read-through efficacy of the TRIDs in cell culture and show the restoration of harmonin function. We do not observe significant differences in the read…

MaleRetinal DisorderUsher syndromemedia_common.quotation_subjectNonsenseNonsense mutationPeptide Chain Elongation TranslationalCell Cycle ProteinsIn Vitro TechniquesBiologyPharmacologymedicine.disease_causeRetinaCell LineMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRetinal DiseasesIn vivoretinitis pigmentosaRetinitis pigmentosaotorhinolaryngologic diseasesmedicineAnimalsHumansResearch ArticlesAdaptor Proteins Signal Transducingpharmacogenetics030304 developmental biologymedia_commonOxadiazoles0303 health sciencesMutationsensoneuronal degenerationRetinalmedicine.diseasedrug therapy3. Good healthMice Inbred C57BLCytoskeletal ProteinsAminoglycosideschemistryCodon NonsenseMolecular MedicineFemaleUsher syndrome030217 neurology & neurosurgeryEMBO Molecular Medicine
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Deciphering the Nonsense Readthrough Mechanism of Action of Ataluren: An in Silico Compared Study

2019

Ataluren was reported to suppress nonsense mutations by promoting the readthrough of premature stop codons, although its mechanism of action (MOA) is still debated. The likely interaction of Ataluren with CFTR-mRNA has been previously studied by molecular dynamics. In this work we extended the modeling of Ataluren's MOA by complementary computational approaches such as induced fit docking (IFD), quantum polarized ligand docking (QPLD), MM-GBSA free-energy calculations, and computational mutagenesis. In addition to CFTR-mRNA, this study considered other model targets implicated in the translation process, such as eukaryotic rRNA 18S, prokaryotic rRNA 16S, and eukaryotic Release Factor 1 (eRF…

In silicoNonsense mutationComputational biology01 natural sciencesRibosomeBiochemistrychemistry.chemical_compoundDrug DiscoveryQPLDcomputational mutagenesiMM-GBSA010405 organic chemistryChemistryDrug Discovery3003 Pharmaceutical ScienceOrganic Chemistrypremature termination codonSettore CHIM/06 - Chimica OrganicaSettore CHIM/08 - Chimica FarmaceuticaStop codon0104 chemical sciencesAtalurenInduced fit docking010404 medicinal & biomolecular chemistrySettore BIO/18 - GeneticaDocking (molecular)ProofreadingRelease factoroxadiazole
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