Search results for " Missense"

showing 10 items of 168 documents

Ofd1, a Human Disease Gene, Regulates the Length and Distal Structure of Centrioles

2010

SUMMARYCentrosomes and their component centrioles represent the principal microtubule organizing centers of animal cells. Here we show that the gene underlying Orofaciodigital Syndrome 1, Ofd1, is a component of the distal centriole that controls centriole length. In the absence of Ofd1, distal regions of centrioles, but not procentrioles, elongate abnormally. These long centrioles are structurally similar to normal centrioles, but contain destabilized microtubules with abnormal post-translational modifications. Ofd1 is also important for centriole distal appendage formation and centriolar recruitment of the intraflagellar transport protein Ift88. To model OFD1 Syndrome in embryonic stem ce…

G2 PhaseCentrioleMicrotubule-associated proteinMutation MissenseHUMDISEASECell Cycle ProteinsBiologyMicrotubulesModels BiologicalArticleGeneral Biochemistry Genetics and Molecular BiologyCentriole elongationCell LineMiceIntraflagellar transportCiliogenesisAnimalsHumansBasal bodyMolecular BiologyEmbryonic Stem CellsCentriolesTumor Suppressor ProteinsProteinsCell BiologyOrofaciodigital SyndromesPhosphoproteinsRecombinant ProteinsCell biologyCentrosomeCELLBIOCentriolar satelliteMicrotubule-Associated ProteinsDevelopmental Biology
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Identification of Cysteine Residues in Human Cationic Amino Acid Transporter hCAT-2A That Are Targets for Inhibition by N-Ethylmaleimide

2013

In most cells, cationic amino acids such as l-arginine, l-lysine, and l-ornithine are transported by cationic (CAT) and y(+)L (y(+)LAT) amino acid transporters. In human erythrocytes, the cysteine-modifying agent N-ethylmaleimide (NEM) has been shown to inhibit system y(+) (most likely CAT-1), but not system y(+)L (Devés, R., Angelo, S., and Chávez, P. (1993) J. Physiol. 468, 753-766). We thus wondered if sensitivity to NEM distinguishes generally all CAT and y(+)LAT isoforms. Transport assays in Xenopus laevis oocytes established that indeed all human CATs (including the low affinity hCAT-2A), but neither y(+)LAT isoform, are inhibited by NEM. hCAT-2A inhibition was not due to reduced tran…

Gene isoformMutantMutation MissenseXenopusBiologyBiochemistryXenopus laevischemistry.chemical_compoundMembrane BiologyAnimalsHumansheterocyclic compoundsCysteineAmino acid transporterEnzyme InhibitorsMolecular Biologychemistry.chemical_classificationN-EthylmaleimideTransporterCell Biologybiology.organism_classificationMolecular biologyProtein Structure TertiaryAmino acidAmino Acid SubstitutionchemistryBiochemistryEthylmaleimideOocytesAmino Acid Transport Systems BasicCysteineJournal of Biological Chemistry
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Mutations in the β-tropomyosin (TPM2) gene – a rare cause of nemaline myopathy

2002

Nemaline myopathy is a clinically and genetically heterogeneous muscle disorder. In the nebulin gene we have detected a number of autosomal recessive mutations. Both autosomal dominant and recessive mutations have been detected in the genes for alpha -actin and alpha -tropomyosin 3. A recessive mutation causing nemaline myopathy among the Old Order Amish has recently been identified in the gene for slow skeletal muscle troponin T. As linkage studies had shown that at least one further gene exists for nemaline myopathy, we investigated another tropomyosin gene expressed in skeletal muscle, the beta -tropomyosin 2 gene. Screening 66 unrelated patients, using single strand conformation polymor…

Genetic MarkersMaleGenetic LinkageProtein ConformationBiopsyMolecular Sequence DataMutation MissenseTropomyosinmacromolecular substancesMuscle disorderMyopathies NemalineTPM203 medical and health sciencesNebulin0302 clinical medicineNemaline myopathymedicineAnimalsHumansAmino Acid SequenceMuscle SkeletalNemaline bodiesPolymorphism Single-Stranded ConformationalGenetics (clinical)DNA Primers030304 developmental biologyGenetics0303 health sciencesSequence Homology Amino AcidbiologyReverse Transcriptase Polymerase Chain Reactionmusculoskeletal systemmedicine.diseaseMolecular biologyTropomyosinCongenital myopathyPedigree3. Good healthHaplotypesNeurologyMutationPediatrics Perinatology and Child Healthbiology.proteinFemaleNeurology (clinical)Sequence Alignment030217 neurology & neurosurgeryCentral core diseaseNeuromuscular Disorders
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Mutations in SLC20A2 link familial idiopathic basal ganglia calcification with phosphate homeostasis.

2012

Familial idiopathic basal ganglia calcification (IBGC) is a genetic condition with a wide spectrum of neuropsychiatric symptoms, including parkinsonism and dementia. Here, we identified mutations in SLC20A2, encoding the type III sodium-dependent phosphate transporter 2 (PiT2), in IBGC-affected families of varied ancestry, and we observed significantly impaired phosphate transport activity for all assayed PiT2 mutants in Xenopus laevis oocytes. Our results implicate altered phosphate homeostasis in the etiology of IBGC.

Genetic Markersmedicine.medical_specialtyGenetic LinkageMolecular Sequence DataMutation MissenseXenopusBasal ganglia calcification610 Medicine & healthPhosphates10052 Institute of PhysiologyXenopus laevis03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAsian PeopleBasal Ganglia Diseases1311 GeneticsCalcinosisGenetic linkageInternal medicineGeneticsmedicineAnimalsHomeostasisHumansBasal ganglia disease030304 developmental biology0303 health sciencesBase SequencebiologySodium-Phosphate Cotransporter Proteins Type IIIParkinsonismCalcinosisSequence Analysis DNAmedicine.diseasePhosphatebiology.organism_classificationPedigreeEndocrinologychemistry10076 Center for Integrative Human PhysiologyOocytes570 Life sciences; biologyLod Score030217 neurology & neurosurgeryHomeostasisChromosomes Human Pair 8Nature genetics
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Sequence variants of the DFNB31 gene among Usher syndrome patients of diverse origin.

2010

Contains fulltext : 89306.pdf (Publisher’s version ) (Open Access) PURPOSE: It has been demonstrated that mutations in deafness, autosomal recessive 31 (DFNB31), the gene encoding whirlin, is responsible for nonsyndromic hearing loss (NSHL; DFNB31) and Usher syndrome type II (USH2D). We screened DFNB31 in a large cohort of patients with different clinical subtypes of Usher syndrome (USH) to determine the prevalence of DFNB31 mutations among USH patients. METHODS: DFNB31 was screened in 149 USH2, 29 USH1, six atypical USH, and 11 unclassified USH patients from diverse ethnic backgrounds. Mutation detection was performed by direct sequencing of all coding exons. RESULTS: We identified 38 diff…

Genetics and epigenetic pathways of disease [NCMLS 6]MutationMutation Missenseotorhinolaryngologic diseasesGenetic VariationHumansMembrane ProteinsFunctional Neurogenomics [DCN 2]Usher SyndromesIntronseye diseasesResearch Article
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Sequence characterization of the melanocortin 1 receptor (MC1R) gene in sheep with different coat colour and identification of the putative e allele …

2010

Abstract Sequence of the melanocortin 1 receptor (MC1R) gene (the Extension locus) was obtained from a panel of 73 animals belonging to 9 Italian sheep breeds or populations (Appenninica, Bergamasca, Comisana, Cornigliese-like, Delle Langhe, Massese, Merinizzata Italiana, Sarda and Valle del Belice) with different coat colours. Evaluation of the identified polymorphisms on this phenotype was reported with in silico predictions and comparative approaches within and across breeds and across species. Five novel single nucleotide polymorphisms (SNPs), organized in three haplotypes, were detected. Another haplotype, including the two missense mutations already described for the ED allele, was id…

GeneticsHaplotypeCoat colour; MC1R; Missense mutation; Ovine breedsSingle-nucleotide polymorphismLocus (genetics)BiologyOvine breedsSettore AGR/17 - Zootecnica Generale E Miglioramento GeneticoCOAT COLOURFood AnimalsSHEEPBREEDSMC1REpistasisAnimal Science and ZoologyMissense mutationAlleleGeneAllele frequencyPOLYMORPHISMSMelanocortin 1 receptor
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Genetic analysis of 2299delG and C759F mutations (USH2A) in patients with visual and/or auditory impairments

2004

The most common mutation in the USH2A gene (Usherin), 2299delG, causes both typical Usher (USH) syndrome type II and atypical USH syndrome, two autosomal recessive disorders, characterised by moderate to severe sensorineural hearing loss and retinitis pigmentosa (RP). Furthermore, the C759F mutation in the USH2A gene has been described in 4.5% of patients with nonsyndromic recessive RP. We have investigated the presence of the 2299delG and/or the C759F mutations in 191 unrelated Spanish patients with different syndromic and nonsyndromic retinal diseases, or with nonsyndromic hearing impairment. The 2299delG mutation was observed in patients with clinical signs of USHII or of atypical USH sy…

GenotypeHearing Loss SensorineuralEye diseaseDNA Mutational AnalysisMutation MissenseGenetic analysisGene FrequencyGenotypeRetinitis pigmentosaotorhinolaryngologic diseasesGeneticsmedicineHumansAlleleAllelesPolymorphism Single-Stranded ConformationalGenetics (clinical)Sequence DeletionGeneticsExtracellular Matrix Proteinsbusiness.industryDNAmedicine.diseasePhenotypePhenotypeSpainMutation (genetic algorithm)Sensorineural hearing lossbusinessRetinitis PigmentosaEuropean Journal of Human Genetics
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Yunis-Varón Syndrome Is Caused by Mutations in FIG4, Encoding a Phosphoinositide Phosphatase

2013

Yunis-Varón syndrome (YVS) is an autosomal-recessive disorder with cleidocranial dysplasia, digital anomalies, and severe neurological involvement. Enlarged vacuoles are found in neurons, muscle, and cartilage. By whole-exome sequencing, we identified frameshift and missense mutations of FIG4 in affected individuals from three unrelated families. FIG4 encodes a phosphoinositide phosphatase required for regulation of PI(3,5)P(2) levels, and thus endosomal trafficking and autophagy. In a functional assay, both missense substitutions failed to correct the vacuolar phenotype of Fig4-null mouse fibroblasts. Homozygous Fig4-null mice exhibit features of YVS, including neurodegeneration and enlarg…

GenotypePhosphataseMicrognathismMolecular Sequence DataLimb Deformities CongenitalMutation MissenseBiologyCompound heterozygositymedicine.disease_causeFrameshift mutation03 medical and health sciencesMice0302 clinical medicinePhosphatidylinositol PhosphatesEctodermal DysplasiaReportmedicineGeneticsMissense mutationAnimalsHumansExomeGenetic Predisposition to DiseaseGenetics(clinical)Yunis–Varon syndromeFrameshift MutationGenetics (clinical)030304 developmental biology0303 health sciencesMutationBone DevelopmentBase SequenceFlavoproteinsNeurodegenerationSequence Analysis DNAFibroblastsmedicine.diseaseMolecular biologyPhenotypePhosphoric Monoester HydrolasesCleidocranial Dysplasia030217 neurology & neurosurgeryThe American Journal of Human Genetics
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Mutations in DNA Binding and Transactivation Domains Affect the Dynamics of Parvovirus NS1 Protein

2013

ABSTRACT The multifunctional replication protein of autonomous parvoviruses, NS1, is vital for viral genome replication and for the control of viral protein production. Two DNA-interacting domains of NS1, the N-terminal and helicase domains, are necessary for these functions. In addition, the N and C termini of NS1 are required for activation of viral promoter P38. By comparison with the structural and biochemical data from other parvoviruses, we identified potential DNA-interacting amino acid residues from canine parvovirus NS1. The role of the identified amino acids in NS1 binding dynamics was studied by mutagenesis, fluorescence recovery after photobleaching, and computer simulations. Mu…

HMG-boxParvovirus CaninevirusesImmunologyDNA Mutational AnalysisMutation MissenseNS1 proteiiniViral Nonstructural ProteinsVirus ReplicationMicrobiologyNS1 proteinSingle-stranded binding proteinCell LineSeqA protein domainVirologyAnimalsDNA bindingReplication protein AbiologyTer proteinparvovirusvirus diseasesDNAn sitoutuminen [DNA]biochemical phenomena metabolism and nutritionMolecular biologyCell biologyVirus-Cell InteractionsProtein Structure TertiaryDNA binding siteDNA-Binding ProteinsInsect Sciencebiology.proteinMutant ProteinsViral genome replicationBinding domainProtein Binding
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Refined analysis of genetic variability parameters in hepatitis C virus and the ability to predict antiviral treatment response.

2008

Summary.  Hepatitis C virus (HCV) infects approximately 3% of the world population. The chronicity of hepatitis C seems to depend on the level of genetic variability. We have recently (Torres-Puente et al., J Viral Hepat, 2008; 15: 188) reported genetic variability estimates from a large-scale sequence analysis of 67 patients infected with HCV subtypes 1a (23 patients) and 1b (44 patients) and related them to response, or lack of, to alpha-interferon plus ribavirin treatment.. Two HCV genome regions were analysed in samples prior to antiviral therapy, one compressing the three hypervariable regions of the E2 glycoprotein and another one including the interferon sensitive determining region …

Hepatitis C virusMutation MissenseAlpha interferonHepacivirusBiologyViral Nonstructural Proteinsmedicine.disease_causeAntiviral AgentsNucleotide diversityViral Envelope ProteinsVirologyDrug Resistance ViralRibavirinmedicineHumansGenetic variabilityNS5AGeneticsHepatologyHaplotypeGenetic VariationHepatitis CHepatitis C Chronicmedicine.diseaseVirologyHypervariable regionInfectious DiseasesTreatment OutcomeHaplotypesInterferonsJournal of viral hepatitis
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