Search results for "point mutation"

showing 10 items of 199 documents

STAG1 mutations cause a novel cohesinopathy characterised by unspecific syndromic intellectual disability

2017

Item does not contain fulltext BACKGROUND: Cohesinopathies are rare neurodevelopmental disorders arising from a dysfunction in the cohesin pathway, which enables chromosome segregation and regulates gene transcription. So far, eight genes from this pathway have been reported in human disease. STAG1 belongs to the STAG subunit of the core cohesin complex, along with five other subunits. This work aimed to identify the phenotype ascribed to STAG1 mutations. METHODS: Among patients referred for intellectual disability (ID) in genetics departments worldwide, array-comparative genomic hybridisation (CGH), gene panel, whole-exome sequencing or whole-genome sequencing were performed following the …

0301 basic medicineGeneticsMutationCohesin complexPoint mutationBiologymedicine.diseasemedicine.disease_causeBioinformaticsFrameshift mutation03 medical and health sciences030104 developmental biology0302 clinical medicineIntellectual disabilityGeneticsmedicineJournal ArticleMissense mutationGene030217 neurology & neurosurgeryGenetics (clinical)Exome sequencingRare cancers Radboud Institute for Health Sciences [Radboudumc 9]Journal of Medical Genetics
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Biallelic variants in LARS2 and KARS cause deafness and (ovario)leukodystrophy

2019

Supplemental Digital Content is available in the text.

0301 basic medicineLysine-tRNA LigaseMalePathologyMagnetic Resonance SpectroscopyMedizinmembrane proteins030204 cardiovascular system & hematologyMitochondrionDeafnessmedicine.disease_causeCompound heterozygosityCorrectionsLeukoencephalopathyMyelin0302 clinical medicineCytosolLeukoencephalopathies030212 general & internal medicineOvarian DiseasesTransfer RNA AminoacylationChildZebrafishMUTATIONExome sequencing10012MutationBrainMetabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6]General MedicineMiddle AgedDisorders of movement Donders Center for Medical Neuroscience [Radboudumc 3]Magnetic Resonance ImagingMitochondriaProtein Transportendoplasmic reticulummedicine.anatomical_structureChild PreschoolTransfer RNAComputingMethodologies_DOCUMENTANDTEXTPROCESSING/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Biological AssayFemaleWRBRare cancers Radboud Institute for Health Sciences [Radboudumc 9]Adultcardiomyopathiesmedicine.medical_specialtyMitochondrial diseaseAminoacylationMuscle disorderBiologyArticleMEDIATES INSERTIONAmino Acyl-tRNA Synthetases03 medical and health sciencesSDG 3 - Good Health and Well-beingmedicineAnimalsPoint MutationHumansAmino Acid SequenceAlleleAllelesCOMPLEXGenetic heterogeneitybusiness.industryArsenite Transporting ATPasesLeukodystrophyGenetic Variation10090Original ArticlesZebrafish Proteinsbiology.organism_classificationDILATED CARDIOMYOPATHYmedicine.diseasezebrafishGENEMolecular biologyDisease Models Animal030104 developmental biologyMembrane protein[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics10084Neurology (clinical)Transfer RNA AminoacylationMEMBRANEbusinessSequence Alignment030217 neurology & neurosurgeryexomeNeurology
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Exome-wide somatic mutation characterization of small bowel adenocarcinoma

2018

Small bowel adenocarcinoma (SBA) is an aggressive disease with limited treatment options. Despite previous studies, its molecular genetic background has remained somewhat elusive. To comprehensively characterize the mutational landscape of this tumor type, and to identify possible targets of treatment, we conducted the first large exome sequencing study on a population-based set of SBA samples from all three small bowel segments. Archival tissue from 106 primary tumors with appropriate clinical information were available for exome sequencing from a patient series consisting of a majority of confirmed SBA cases diagnosed in Finland between the years 2003–2011. Paired-end exome sequencing was…

0301 basic medicineMaleCancer ResearchMICROSATELLITE INSTABILITYColorectal canceroncogenesReceptor ErbB-2medicine.disease_causeCOLORECTAL-CANCERACTIVATIONCohort Studies0302 clinical medicineAnimal CellsAdenocarcinomasMedicine and Health SciencesExomeFrameshift MutationExomeGenetics (clinical)Exome sequencingAged 80 and overSMALL-INTESTINEeducation.field_of_study1184 Genetics developmental biology physiologyCELIAC-DISEASENonsense MutationMiddle Aged3. Good healthsyöpägeenitOncology030220 oncology & carcinogenesissyöpätauditFemaleSIGNALING PATHWAYKRASCellular TypesResearch ArticleAdultProto-Oncogene Proteins B-raflcsh:QH426-470SEQUENCING DATAImmune CellsNonsense mutationPopulationImmunologyAntigen-Presenting CellsComputational biologysuolistosyövätBiologyAdenocarcinomata3111CarcinomasFrameshift mutation03 medical and health sciencesGermline mutationQUALITY-CONTROLGenetiikka kehitysbiologia fysiologia - Genetics developmental biology physiologySyöpätaudit - CancersIntestinal NeoplasmsmedicineGeneticsPoint MutationHumanseducationMolecular BiologyEcology Evolution Behavior and SystematicsAgedColorectal CancerBiology and Life SciencesCancers and Neoplasmscancerous diseasesCell Biologymedicine.diseaseta3122mutationsCOMPREHENSIVE MOLECULAR CHARACTERIZATIONlcsh:Genetics030104 developmental biologyMutationSomatic Mutationbowel cancer3111 BiomedicinemutaatiotHIGH-RESOLUTIONPLoS Genetics
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Am J Hum Genet

2019

ZMIZ1 is a coactivator of several transcription factors, including p53, the androgen receptor, and NOTCH1. Here, we report 19 subjects with intellectual disability and developmental delay carrying variants in ZMIZ1. The associated features include growth failure, feeding difficulties, microcephaly, facial dysmorphism, and various other congenital malformations. Of these 19, 14 unrelated subjects carried de novo heterozygous single-nucleotide variants (SNVs) or single-base insertions/deletions, 3 siblings harbored a heterozygous single-base insertion, and 2 subjects had a balanced translocation disrupting ZMIZ1 or involving a regulatory region of ZMIZ1. In total, we identified 13 point mutat…

0301 basic medicineMaleMicrocephaly[SDV]Life Sciences [q-bio]Developmental DisabilitiesAucunBiology030226 pharmacology & pharmacyTransactivation03 medical and health sciencesMiceNeurodevelopmental disorder0302 clinical medicineReportIntellectual DisabilityCoactivatormedicineGeneticsAnimalsHumansPoint MutationAlleleChildExomeGenetics (clinical)Alleles030304 developmental biologyGenetics0303 health sciencesPoint mutationCorrectionInfantSyndromemedicine.diseaseAndrogen receptor030104 developmental biologyChild PreschoolFemale030217 neurology & neurosurgeryTranscription Factors
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Lamivudine/Adefovir Treatment Increases the Rate of Spontaneous Mutation of Hepatitis B Virus in Patients.

2016

The high levels of genetic diversity shown by hepatitis B virus (HBV) are commonly attributed to the low fidelity of its polymerase. However, the rate of spontaneous mutation of human HBV in vivo is currently unknown. Here, based on the evolutionary principle that the population frequency of lethal mutations equals the rate at which they are produced, we have estimated the mutation rate of HBV in vivo by scoring premature stop codons in 621 publicly available, full-length, molecular clone sequences derived from patients. This yielded an estimate of 8.7 × 10-5 spontaneous mutations per nucleotide per cell infection in untreated patients, which should be taken as an upper limit estimate becau…

0301 basic medicineMaleRNA virusesMutation ratelcsh:Medicinemedicine.disease_causeBiochemistryPolymerasesAdefovirFrameshift Mutationlcsh:SciencePathology and laboratory medicineeducation.field_of_studyMultidisciplinaryMicrobial MutationLamivudineMedical microbiologyResistance mutation3. Good healthLamivudineVirusesFemalePathogensSequence AnalysisImmunosuppressive Agentsmedicine.drugResearch ArticleHepatitis B virusSubstitution MutationPopulationOrganophosphonatesBiologyResearch and Analysis MethodsPolymorphism Single NucleotideMicrobiologyFrameshift mutation03 medical and health sciencesHepatitis B ChronicDrug Resistance ViralDNA-binding proteinsmedicineGeneticsHumanseducationMolecular Biology TechniquesSequencing TechniquesMolecular BiologyHepatitis B virusMedicine and health sciencesPoint mutationAdeninelcsh:RViral pathogensOrganismsBiology and Life SciencesProteinsVirologyMolecular biologyHepatitis virusesMicrobial pathogens030104 developmental biologyMutationlcsh:QCloningPLoS ONE
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Mutations in SKI in Shprintzen-Goldberg syndrome lead to attenuated TGF-β responses through SKI stabilization.

2020

ABSTRACTShprintzen-Goldberg syndrome (SGS) is a multisystemic connective tissue disorder, with considerable clinical overlap with Marfan and Loeys-Dietz syndromes. These syndromes have commonly been associated with enhanced TGF-β signaling. In SGS patients, heterozygous point mutations have been mapped to the transcriptional corepressor SKI, which is a negative regulator of TGF-β signaling that is rapidly degraded upon ligand stimulation. The molecular consequences of these mutations, however, are not understood. Here we use a combination of structural biology, genome editing and biochemistry to show that SGS mutations in SKI abolish its binding to phosphorylated SMAD2 and SMAD3. This resul…

0301 basic medicineMaleSMADmedicine.disease_causeMarfan SyndromeActivin0302 clinical medicineGenome editingTransforming Growth Factor betaGene expressionBiology (General)MutationShprintzen-Goldberg syndromeGeneral NeuroscienceQRShprintzen–Goldberg syndromeGeneral MedicineLigand (biochemistry)Chromosomes and Gene ExpressionCell biologyDNA-Binding ProteinsMedicinePhosphorylationFemaleSignal TransductionResearch ArticleHumanTGF-βQH301-705.5ScienceBiologyGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesCraniosynostosesstomatognathic systemBiochemistry and Chemical BiologyProto-Oncogene ProteinsmedicineHumansGeneral Immunology and MicrobiologyPoint mutationmedicine.diseaseSKIArachnodactyly030104 developmental biologyStructural biologyMutation030217 neurology & neurosurgerySMADTransforming growth factoreLife
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Sequential cleavage of the proteins encoded by HNOT/ALG3, the human counterpart of the Drosophila NOT and yeast ALG3 gene, results in products acting…

2017

This study provides first insights into the biosynthesis, structure, biochemistry and complex processing of the proteins encoded by hNOT/ALG3, the human counterpart of the Drosophila Neighbour of TID (NOT) and the yeast asparagine linked glycosylation 3 gene (ALG3), which encodes a mannosyltransferase. Unambiguous evidence that both the fly and human proteins act as mannosyltransferases has not been provided yet. Previously, we showed that hNOT/ALG3 encodes two alternatively spliced main transcripts, hNOT-1/ALG3-1 and hNOT-4/ALG3-4, and their 15 truncated derivatives that lack diverse sets of exons and/or carry point mutations that result in premature termination codons. Here we show that t…

0301 basic medicineMannosyltransferaseGlycosylationSaccharomyces cerevisiae ProteinsGlycosylationProtein ConformationRNA SplicingSaccharomyces cerevisiaeBiologyMannosyltransferases03 medical and health scienceschemistry.chemical_compoundExonNuclear Receptor Subfamily 4 Group A Member 2GeneticsAnimalsHumansAmino Acid SequenceAsparagineMolecular BiologyGeneGenetics (clinical)Cellular compartmentPoint mutationComputational BiologyMembrane ProteinsExonsGeneral MedicineCell biologyAlternative Splicing030104 developmental biologychemistryCodon NonsenseDrosophilaCytokinesisHuman Molecular Genetics
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Comprehensive evaluation of coding region point mutations in microsatellite-unstable colorectal cancer

2018

Microsatellite instability (MSI) leads to accumulation of an excessive number of mutations in the genome, mostly small insertions and deletions. MSI colorectal cancers (CRCs), however, also contain more point mutations than microsatellite-stable (MSS) tumors, yet they have not been as comprehensively studied. To identify candidate driver genes affected by point mutations in MSI CRC, we ranked genes based on mutation significance while correcting for replication timing and gene expression utilizing an algorithm, MutSigCV. Somatic point mutation data from the exome kit-targeted area from 24 exome-sequenced sporadic MSI CRCs and respective normals, and 12 whole-genome-sequenced sporadic MSI CR…

0301 basic medicineMedicine (General)Candidate geneclinical evaluationgenetic identificationgenetic analysisQH426-470medicine.disease_causeChromatin Epigenetics Genomics & Functional Genomicswhole exome sequencingddc:590mutator genesingle nucleotide polymorphismddc:576.5Gene Regulatory NetworksExomeExome sequencingCancercancer cellGeneticsMutation1184 Genetics developmental biology physiology3. Good healthgenetic codesyöpägeenitpriority journalMolecular Medicinewild typepoint mutationSystems MedicineColorectal Neoplasmscongenital hereditary and neonatal diseases and abnormalitiesddc:025.063/5703122 Cancerscancer geneticsSingle-nucleotide polymorphismcolorectal cancerBiologygene frequencyta3111mikrosatelliititcolony formationR105W geneArticle03 medical and health sciencesR5-920Gene interactionReportGeneticsmedicineHumanscontrolled studyhumanneoplasmspaksusuolisyöpäPoint mutationgene interactionhuman celltumor-related geneMicrosatellite instabilityMolecular Sequence AnnotationSequence Analysis DNAmedicine.diseaseta3122digestive system diseaseshuman tissueSTK38L gene030104 developmental biologyvalidation processgene expressionSMARCB1 genemicrosatellite instability3111 Biomedicinegene replicationReports
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Different rates of spontaneous mutation of chloroplastic and nuclear viroids as determined by high-fidelity ultra-deep sequencing

2017

[EN] Mutation rates vary by orders of magnitude across biological systems, being higher for simpler genomes. The simplest known genomes correspond to viroids, subviral plant replicons constituted by circular non-coding RNAs of few hundred bases. Previous work has revealed an extremely high mutation rate for chrysanthemum chlorotic mottle viroid, a chloroplastreplicating viroid. However, whether this is a general feature of viroids remains unclear. Here, we have used high-fidelity ultra-deep sequencing to determine the mutation rate in a common host (eggplant) of two viroids, each representative of one family: the chloroplastic eggplant latent viroid (ELVd, Avsunviroidae) and the nuclear pot…

0301 basic medicineMutation rateChloroplastsViroidvirusesPospiviroidaeArtificial Gene Amplification and ExtensionPlant ScienceSelf-CleavageVirus ReplicationBiochemistryPolymerase Chain ReactionGenomeDatabase and Informatics MethodsSequencing techniquesRibozymeNucleic AcidsRibozymesBiology (General)GeneticsHigh-Throughput Nucleotide Sequencingfood and beveragesRNA sequencingViroidsEnzymesAvsunviroidaeDeletion MutationVirusesPhysical SciencesRNA ViralIn-VivoSequence AnalysisResearch ArticleSubstitution MutationHammerhead RibozymesQH301-705.5Materials by StructureBioinformaticsEvolutionMaterials ScienceImmunologyPlant PathogensGenerationReplicationBiologyMicrobiology03 medical and health sciencesSequence Motif AnalysisVirologyGeneticsSolanum melongenaRNA-PolymeraseMolecular BiologyPotato spindle tuber viroidPlant DiseasesMatter030102 biochemistry & molecular biologyPoint mutationOrganismsBiology and Life SciencesProteinsRNAReverse Transcriptase-Polymerase Chain ReactionRC581-607Plant Pathologybiology.organism_classificationVirologyResearch and analysis methodsMolecular biology techniques030104 developmental biologyMutagenesisOligomersMutationEnzymologyRNAMotifParasitologyImmunologic diseases. AllergyPLOS Pathogens
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Differential subcellular expression of P525LFUS as a putative biomarker for ALS phenoconversion

2020

P525LFused-in-Sarcoma ( FUS ) mutation is associated with a specific amyotrophic lateral sclerosis (ALS) phenotype characterized by a juvenile-onset and a severe course.1 This harmful point mutation is located in the nuclear localization signal (NLS) domain at the protein C-terminal.2 Although wild-type FUS protein is expressed almost exclusively in the nucleus, the P525L FUS mutation leads to a protein mislocalization into the cytoplasm3,4 because of its loss of capacity to bind its transporter karyopherin-2 and to be transferred back to the nucleus.3

0301 basic medicineMutationPoint mutationTransporterALS FUS fibroblastsBiologymedicine.disease_causemedicine.diseasePhenotypeCell biology03 medical and health sciences030104 developmental biology0302 clinical medicinemedicine.anatomical_structuremedicineNLSSettore MED/26 - NeurologiaNeurology (clinical)Amyotrophic lateral sclerosisNucleus030217 neurology & neurosurgeryGenetics (clinical)Nuclear localization sequence
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