Search results for "Exon"

showing 10 items of 437 documents

Role of adjuvant imatinib dose in radically resected GIST harboring KIT exon 9 mutations

2020

11533 Background: Gastrointestinal stromal tumors (GIST) with a driver mutation in KIT exon 9 (Ex9) represent about 10% of all newly diagnosed cases. In the metastatic setting, Ex9-mutated GIST patients benefit from higher doses of imatinib (800 mg/day vs standard 400 mg/day). The additional therapeutic benefit from a higher dose of imatinib in the adjuvant setting in this molecular subgroup has not been confirmed. Methods: We retrospectively identified 105 patients (pts) with resected Ex9-mutated GIST treated with adjuvant imatinib (800 mg/day or 400 mg/day) in 15 different European centers. Disease-Free Survival (DFS) and Imatinib Failure-Free Survival (IFFS) were calculated and analyzed…

Cancer ResearchStromal cellGiSTbusiness.industrymedicine.medical_treatmentMedizinImatinibNewly diagnosed3. Good health03 medical and health sciencesExon0302 clinical medicineOncology030220 oncology & carcinogenesisMutation (genetic algorithm)medicineCancer research10. No inequalitybusinessAdjuvant030215 immunologymedicine.drug
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The FHIT gene is alternatively spliced in normal kidney and renal cell carcinoma.

1997

FHIT (Fragile Histidine Triad), a putative tumor suppressor gene, was cloned from fetal brain and colon cDNA libraries. Portions of this gene are deleted in esophageal, colon, lung and breast tumors, but this gene has not been found altered in sporadic renal cell carcinomas. We report here an alternatively spliced form of this gene cloned from a kidney cDNA library. This cDNA is 1189 bp in length, and contains an additional 94 bp exon, designated exon 2a (E2a). This novel sequence is located between exon 2 and exon 3 of the FHIT gene's untranslated region and exon 2a is present in all normal kidney tissues and cell lines. Analyses performed on sporadic renal cell carcinoma (RCC) tissues and…

Cancer ResearchTumor suppressor geneMolecular Sequence DataBiologymedicine.disease_causeKidneyPolymerase Chain ReactionExonFHITComplementary DNAGene expressionGeneticsmedicineHumansGenes Tumor SuppressorAmino Acid SequenceCloning MolecularneoplasmsMolecular BiologyCarcinoma Renal CellBase SequencecDNA libraryAlternative splicingProteinsBlotting NorthernKidney NeoplasmsAcid Anhydride HydrolasesNeoplasm ProteinsAlternative SplicingCancer researchCarcinogenesisOncogene
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Divergently Transcribed Overlapping Genes Expressed in Liver and Kidney and Located in the 11p15.5 Imprinted Domain

1998

Human chromosomal band 11p15.5 has been shown to contain genes involved in the development of several pediatric and adult tumors and in Beckwith-Wiedemann syndrome (BWS). Overlapping P1 artificial chromosome clones from this region have been used as templates for genomic sequencing in an effort to identify candidate genes for these disorders. PowerBLAST identified several matches with expressed sequence tags (ESTs) from fetal brain and liver cDNA libraries. Northern blot analysis indicated that two of the genes identified by these ESTs encode transcripts of 1-1.5 kb with predominant expression in fetal and adult liver and kidney. With RT-PCR and RACE, full-length transcripts were isolated f…

Candidate geneBeckwith-Wiedemann SyndromeDNA ComplementaryTranscription GeneticDNA Mutational AnalysisMolecular Sequence DataBiologyKidneyWilms TumorGenomic ImprintingMiceExonGene mappingGene expressionGenes OverlappingGeneticsAnimalsHumansAmino Acid SequenceGeneGeneticsExpressed sequence tagBase SequencecDNA libraryChromosomes Human Pair 11Membrane ProteinsMolecular biologyLiverCarrier ProteinsGenomic imprintingGenomics
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FOXP2 gene and language impairment in schizophrenia: association and epigenetic studies

2010

Abstract Background Schizophrenia is considered a language related human specific disease. Previous studies have reported evidence of positive selection for schizophrenia-associated genes specific to the human lineage. FOXP2 shows two important features as a convincing candidate gene for schizophrenia vulnerability: FOXP2 is the first gene related to a language disorder, and it has been subject to positive selection in the human lineage. Methods Twenty-seven SNPs of FOXP2 were genotyped in a cohort of 293 patients with schizophrenia and 340 controls. We analyzed in particular the association with the poverty of speech and the intensity of auditory hallucinations. Potential expansion of thre…

Candidate genelcsh:Internal medicineGenotypeHallucinationslcsh:QH426-470Epigenetics of schizophreniaSingle-nucleotide polymorphismBiologyPolymorphism Single NucleotideEpigenesis GeneticCohort StudiesmedicineGeneticsHumansLanguage disorderGenetics(clinical)lcsh:RC31-1245Genetics (clinical)GeneticsPsychiatric Status Rating ScalesLanguage DisordersFOXP2 GeneFOXP2Forkhead Transcription FactorsExonsDNA Methylationmedicine.diseaselcsh:GeneticsSchizophreniaDNA methylationSchizophreniaParahippocampal GyrusCpG IslandsResearch Article
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Silicateins, the major biosilica forming enzymes present in demosponges: protein analysis and phylogenetic relationship.

2007

Silicateins are enzymes, which are restricted to sponges (phylum Porifera), that mediate the catalytic formation of biosilica from monomeric silicon compounds. The silicatein protein is compartmented in the sponges in the axial filaments which reside in the axial canals of the siliceous spicules. In the present study silicatein has been isolated from the freshwater sponge Lubomirskia baicalensis where it occurs in isoforms with sizes of 23 kDa, 24 kDa and 26 kDa. Since the larger protein is glycosylated we posit that it is a processed form of one of the smaller size forms. The silicatein isoforms are post-translationally modified by phosphorylation; at least four isoforms exist with pI's of…

Cathepsin LMolecular Sequence DataCathepsin LDemospongeCatalytic triadGeneticsAnimalsAmino Acid SequenceGenePeptide sequencePhylogenyCathepsinbiologySequence Homology Amino AcidGeneral MedicineExonsbiology.organism_classificationSilicon DioxideCathepsinsIntronsPoriferaSuberites domunculaSpongeCysteine EndopeptidasesMicroscopy ElectronBiochemistrybiology.proteinGene
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Cloning of a rat-specific long PCP4/PEP19 isoform

2007

We report the identification of a cDNA that encodes a putative protein of 94 amino acids and expected molecular weight of 10.7 kDa, the C-terminal half of which is identical to that of PEP19, a small, brain-specific protein involved in Ca++/calmodulin signaling. The novel rat-specific protein, tentatively named long PEP19 isoform (LPI), is the product of alternative splicing of the rat PCP4 gene encoding PEP19. We found that antibodies raised against the first 13 N-terminal amino acids of LPI, not present in PEP19, recognize a protein enriched in the developing rat brain.

Cell ExtractsGene isoformProtein isoformDNA ComplementaryCalmodulinMolecular Sequence DataNerve Tissue ProteinsAntibodiesRats Sprague-DawleyMiceExonComplementary DNAGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequencechemistry.chemical_classificationBase SequencebiologyGene Expression ProfilingAlternative splicingBrainGene Expression Regulation DevelopmentalRNA-Binding ProteinsExonsGeneral MedicineMolecular biologyIntronsRatsAmino acidchemistryBiochemistrybiology.proteinCalmodulin-Binding ProteinsPeptidesInternational Journal of Molecular Medicine
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Two Enhancers Control Transcription of Drosophila muscleblind in the Embryonic Somatic Musculature and in the Central Nervous System

2014

The phylogenetically conserved family of Muscleblind proteins are RNA-binding factors involved in a variety of gene expression processes including alternative splicing regulation, RNA stability and subcellular localization, and miRNA biogenesis, which typically contribute to cell-type specific differentiation. In humans, sequestration of Muscleblind-like proteins MBNL1 and MBNL2 has been implicated in degenerative disorders, particularly expansion diseases such as myotonic dystrophy type 1 and 2. Drosophila muscleblind was previously shown to be expressed in embryonic somatic and visceral muscle subtypes, and in the central nervous system, and to depend on Mef2 for transcriptional activatio…

Central Nervous SystemTranscription Geneticlcsh:MedicineEnhancer RNAsMechanical Treatment of SpecimensExonGenes ReporterMolecular Cell BiologyMorphogenesisPattern Formationlcsh:SciencePromoter Regions GeneticConserved SequenceGeneticsRegulation of gene expressionMultidisciplinaryMusclesDrosophila MelanogasterGene Expression Regulation DevelopmentalRNA-Binding ProteinsCell DifferentiationGenomicsAnimal ModelsInsectsEnhancer Elements GeneticElectroporationSpecimen DisruptionOrgan SpecificityRegulatory sequenceDrosophilaResearch ArticleMef2ArthropodaMolecular Sequence DataDNA transcriptionBiologyResearch and Analysis MethodsGenètica molecularModel OrganismsGeneticsAnimalsHumansEnhancerTranscription factorBase SequenceBiology and life scienceslcsh:ROrganismsPromoterCell BiologyInvertebratesSpecimen Preparation and Treatmentlcsh:QGene expressionAnimal GeneticsDevelopmental BiologyNeurosciencePLoS ONE
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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An exon junction complex‐independent function of Barentsz in neuromuscular synapse growth

2021

The exon junction complex controls the translation, degradation, and localization of spliced mRNAs, and three of its core subunits also play a role in splicing. Here, we show that a fourth subunit, Barentsz, has distinct functions within and separate from the exon junction complex in Drosophila neuromuscular development. The distribution of mitochondria in larval muscles requires Barentsz as well as other exon junction complex subunits and is not rescued by a Barentsz transgene in which residues required for binding to the core subunit eIF4AIII are mutated. In contrast, interactions with the exon junction complex are not required for Barentsz to promote the growth of neuromuscular synapses.…

ChemistryTransgeneProtein subunitMutantRNA-Binding ProteinsTranslation (biology)ExonsBiochemistryNeuromuscular junctionCell biologySynapsemedicine.anatomical_structureRNA splicingEukaryotic Initiation Factor-4ASynapsesGeneticsmedicineExon junction complexAnimalsDrosophila ProteinsDrosophilaMolecular BiologyReports
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Clinical Course and Significance of the Novel FLT3-Y842C Mutation in a Patient with AML Treated with PKC412 Monotherapy.

2004

Abstract We recently identified a novel mutation (Y842C) within the tyrosine kinase domain of FLT3 in a patient treated with PKC410 monotherapy (ASH 2003, # 4681). Here, we present follow up studies including the clinical course of the patient and frequency analysis in 110 patients with AML. In addition, we characterized the novel mutation using overexpression of FLT3-Y842C in 32D cells. AML M2 was diagnosed in a 63 year old, male patient in 1993. After having experienced his second relapse upon standard therapy the patient was refractory to alemtuzumab treatment. Due to reduced performance status the patient was not eligible to standard chemotherapy and was enrolled into a phase II trial i…

ChemotherapyPerformance statusbusiness.industryPoint mutationmedicine.medical_treatmentImmunologyhemic and immune systemsCell BiologyHematologyBioinformaticsBiochemistryExonfluids and secretionshemic and lymphatic diseasesembryonic structuresCancer researchmedicineAlemtuzumabClinical significancebusinessTyrosine kinaseEx vivomedicine.drugBlood
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