Search results for "alignment"

showing 10 items of 627 documents

Molecular cloning and characterization of the cDNA encoding the rat liver gamma-butyrobetaine hydroxylase

1999

Carnitine biosynthesis from lysine and methionine involves five enzymatic reactions. gamma-butyrobetaine hydroxylase (BBH; EC 1.14. 11.1) is the last enzyme of this pathway. It catalyzes the reaction of hydroxylation of gamma-butyrobetaine to carnitine. The cDNA encoding this enzyme has been isolated and characterized. The cDNA contained an open reading frame of 1161 bp encoding a protein of 387 amino acids with a deduced molecular weight of 44.5 kDa. The sequence of the cDNA showed an important homology with the human cDNA recently isolated. Northern analysis showed gamma-butyrobetaine hydroxylase expression in the liver and in some extend in the testis and the epididymis. During this stud…

MaleDNA Complementarygamma-Butyrobetaine DioxygenaseMolecular Sequence DataBiologyMolecular cloningMixed Function Oxygenaseschemistry.chemical_compoundSequence Homology Nucleic AcidComplementary DNAmedicineAnimalsAmino Acid SequenceCarnitineCloning MolecularRats WistarMolecular Biologychemistry.chemical_classificationMessenger RNAMethionineBase SequenceSequence Homology Amino AcidGene Expression Regulation DevelopmentalCell BiologyMolecular biologyRatsAmino acidOpen reading frameLiverchemistryBiochemistryCarnitine biosynthesisSequence Alignmentmedicine.drugBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Mutations inWNT10Aare frequently involved in oligodontia associated with minor signs of ectodermal dysplasia

2012

Ectodermal dysplasias (ED) are a clinically and genetically heterogeneous group of hereditary disorders that have in common abnormal development of ectodermal derivatives. Hypohidrotic ectodermal dysplasia (HED) is characterized by abnormal development of eccrine sweat glands, hair, and teeth. The X-linked form of the disease, caused by mutations in the EDA gene, represents the majority of patients with the hypohidrotic form. Autosomal dominant and autosomal recessive forms are occasionally seen, and result from mutations in at least three genes (WNT10A, EDAR, or more rarely EDARADD). We have screened for mutations in EDAR (commonly involved in the hypohidrotic form) and WNT10A (involved in…

MaleEctodermal dysplasiaGenotypeMolecular Sequence Datamedicine.disease_causeCompound heterozygosityEctodermal DysplasiaGeneticsmedicineHumansAmino Acid SequenceHypohidrotic ectodermal dysplasiaGenetic Association StudiesGenetics (clinical)AnodontiaGeneticsMutationEDARADDEdar ReceptorGenetic heterogeneitybusiness.industrymedicine.diseaseWnt ProteinsHypodontiaPhenotypeMutationFemaleEctodysplasin AbusinessSequence AlignmentAmerican Journal of Medical Genetics Part A
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Visualization of a covalent intermediate between microsomal epoxide hydrolase, but not cholesterol epoxide hydrolase, and their substrates

1997

Mammalian soluble and microsomal epoxide hydrolases have been proposed to belong to the family of alpha/beta-hydrolase-fold enzymes. These enzymes hydrolyse their substrates by a catalytic triad, with the first step of the enzymatic reaction being the formation of a covalent enzyme-substrate ester. In the present paper, we describe the direct visualization of the ester formation between rat microsomal epoxide hydrolase and its substrate. Microsomal epoxide hydrolase was precipitated with acetone after brief incubation with [1-(14)C]epoxystearic acid. After denaturing SDS gel electrophoresis the protein-bound radioactivity was detected by fluorography. Pure epoxide hydrolase and crude micros…

MaleEpoxide hydrolase 21303 BiochemistryStereochemistryMolecular Sequence DataEpoxide10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiochemistryRats Sprague-Dawleychemistry.chemical_compoundCatalytic triadAnimalsAmino Acid SequenceEpoxide hydrolaseMolecular BiologyEpoxide Hydrolaseschemistry.chemical_classificationHydrolysisCell BiologyRatsKineticsCholesterolEnzymeModels ChemicalSolubilitychemistryBiochemistryMicrosomal epoxide hydrolaseEpoxide HydrolasesCarcinogensChromatography GelMicrosomes LiverMicrosomeEpoxy Compounds570 Life sciences; biologySequence AlignmentStearic Acids
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Echinostoma caproni: identification of enolase in excretory/secretory products, molecular cloning, and functional expression.

2007

In order to investigate molecules that could be involved in host-trematode relationships, we have analysed the excretory/secretory products (ESP) of Echinostoma caproni following a proteomic approach. Actin, Gluthathione S-transferase (GST) and enolase have been identified in the ESP. Enolase, observed to be one of the most abundant proteins, was further characterized. The molecular cloning and in vitro expression in Escherichia coli of E. caproni enolase allowed us to determine that the protein contains 431 amino acids and a theoretical MW of 46272 Da. E. caproni enolase shows high homology to other trematode enolases. The recombinant protein binds specifically to human plasminogen in vitr…

MaleImmunologyEnolaseBlotting WesternMolecular Sequence DataMolecular cloningBiologymedicine.disease_causeGene Expression Regulation Enzymologiclaw.inventionlawCricetinaeEchinostomamedicineAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularRats WistarEscherichia coliActinchemistry.chemical_classificationMesocricetusSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionPlasminogenGeneral MedicineMolecular biologyIn vitroRecombinant ProteinsAmino acidRatsInfectious DiseaseschemistryBiochemistryExcretory systemPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationRecombinant DNAParasitologyElectrophoresis Polyacrylamide GelSequence AlignmentExperimental parasitology
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Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion

1996

International audience; Friedreich's ataxia (FRDA) is an autosomal recessive, degenerative disease that involves the central and peripheral nervous systems and the heart. A gene, X25, was identified in the critical region for the FRDA locus on chromosome 9q13. This gene encodes a 210-amino acid protein, frataxin, that has homologs in distant species such as Caenorhabditis elegans and yeast. A few FRDA patients were found to have point mutations in X25, but the majority were homozygous for an unstable GAA trinucleotide expansion in the first X25 intron.

MaleIron-sulfur cluster assemblyPolymerase Chain Reaction0302 clinical medicineTrinucleotide RepeatsIron-Binding ProteinsGenetics0303 health sciencesMultidisciplinaryAutosomal recessive cerebellar ataxiaPedigree3. Good healthFemalemedicine.symptomChromosomes Human Pair 9HumanPair 9Heterozygotecongenital hereditary and neonatal diseases and abnormalitiesAtaxiaMolecular Sequence DataGenes RecessiveLocus (genetics)BiologyChromosomes03 medical and health sciencesGene mappingAlleles; Amino Acid Sequence; Base Sequence; Chromosomes Human Pair 9; DNA Primers; Female; Friedreich Ataxia; Genes Recessive; Heterozygote; Humans; Male; Molecular Sequence Data; Pedigree; Point Mutation; Polymerase Chain Reaction; Proteins; Sequence Alignment; Introns; Iron-Binding Proteins; Trinucleotide RepeatsmedicineRecessiveHumansPoint MutationAmino Acid SequenceAlleleAllelesDNA Primers030304 developmental biologyBase SequencePoint mutationProteins[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologymedicine.diseaseMolecular biologyIntronsGenes[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsFriedreich AtaxiaFrataxinbiology.proteinSequence Alignment030217 neurology & neurosurgeryScience
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Evolution of chromatin-remodeling complexes: comparative genomics reveals the ancient origin of "novel" compensasome genes.

2003

Dosage compensation in Drosophila is mediated by a complex, called compensasome, com- posed of at least five proteins and two noncoding RNAs. Genes encoding compensasome proteins have been collectively named male-specific lethals or msls. Recent work showed that three of the Drosophila msls (msl-3, mof, and mle) have an ancient origin. In this study, I describe likely orthologues of the two re- maining msls, msl-1 and msl-2, in several inverte- brates and vertebrates. The MSL-2 protein is the only one found in Drosophila and vertebrate genomes that contains both a RING finger and a peculiar type of CXC domain, related to the one present in Enhancer of Zeste proteins. MSL-1 also contains two…

MaleLeucine zipperAmino Acid MotifsMolecular Sequence DataBiologyGenomeChromatin remodelingEvolution MolecularDosage Compensation GeneticGeneticsRing fingermedicineAnimalsDrosophila ProteinsHumansAmino Acid SequenceEnhancerMolecular BiologyEcology Evolution Behavior and SystematicsCaenorhabditis elegansPhylogenyComparative genomicsGeneticsDosage compensationfungiNuclear ProteinsGenomicsbiology.organism_classificationChromatin Assembly and DisassemblyProtein Structure TertiaryDNA-Binding Proteinsmedicine.anatomical_structureVertebratesDrosophilaSequence AlignmentTranscription FactorsJournal of molecular evolution
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NOTCH, a new signaling pathway implicated in holoprosencephaly.

2011

International audience; Genetics of Holoprosencephaly (HPE), a congenital malformation of the developing human forebrain, is due to multiple genetic defects. Most genes that have been implicated in HPE belong to the sonic hedgehog signaling pathway. Here we describe a new candidate gene isolated from array comparative genomic hybridization redundant 6qter deletions, DELTA Like 1 (DLL1), which is a ligand of NOTCH. We show that DLL1 is co-expressed in the developing chick forebrain with Fgf8. By treating chick embryos with a pharmacological inhibitor, we demonstrate that DLL1 interacts with FGF signaling pathway. Moreover, a mutation analysis of DLL1 in HPE patients revealed a three-nucleoti…

MaleMESH: Signal TransductionCandidate gene[SDV.GEN] Life Sciences [q-bio]/GeneticsChick EmbryoMESH: Amino Acid SequenceMESH: Base SequenceHoloprosencephalyMESH: Animals[SDV.BDD]Life Sciences [q-bio]/Development BiologyGenetics (clinical)Sequence DeletionGenetics0303 health sciencesReceptors NotchMESH: Androstenediols030305 genetics & heredityMESH: Infant NewbornIntracellular Signaling Peptides and ProteinsGeneral MedicineMESH: Sequence DeletionMESH: Chick EmbryoCell biologyembryonic structuresFemale[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]MESH: Membrane ProteinsSignal transductionMESH: HoloprosencephalySignal TransductionAdultmusculoskeletal diseasesCell signalingcongenital hereditary and neonatal diseases and abnormalitiesanimal structuresMolecular Sequence DataNotch signaling pathwayMESH: Sequence AlignmentBiologyArticle03 medical and health sciencesFGF8[SDV.BDD] Life Sciences [q-bio]/Development BiologyHoloprosencephalyAndrostenediolsGeneticsmedicineAnimalsHumans[SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Amino Acid SequenceMolecular Biology030304 developmental biology[SDV.GEN]Life Sciences [q-bio]/GeneticsMESH: Molecular Sequence DataMESH: HumansBase SequenceInfant NewbornMembrane ProteinsMESH: Adultmedicine.diseaseMESH: MaleForebrainMutation testingMESH: Receptors NotchSequence AlignmentMESH: Female
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TBC1D24-TLDc-related epilepsy exercise-induced dystonia: rescue by antioxidants in a disease model

2019

Genetic mutations in TBC1D24 have been associated with multiple phenotypes, with epilepsy being the main clinical manifestation. The TBC1D24 protein consists of the unique association of a Tre2/Bub2/Cdc16 (TBC) domain and a TBC/lysin motif domain/catalytic (TLDc) domain. More than 50 missense and loss-of-function mutations have been described and are spread over the entire protein. Through whole genome/exome sequencing we identified compound heterozygous mutations, R360H and G501R, within the TLDc domain, in an index family with a Rolandic epilepsy exercise-induced dystonia phenotype (http://omim.org/entry/608105). A 20-year long clinical follow-up revealed that epilepsy was self-limited in…

MaleModels Molecular0301 basic medicineProtein ConformationAmino Acid Motifsalpha-TocopherolMutantCrystallography X-RayPHENOTYPECompound heterozygosityAntioxidantsAnimals Genetically ModifiedEpilepsy0302 clinical medicineCatalytic DomainDrosophila ProteinsMissense mutationoxidative stressChildTLDC DOMAINVITAMIN-EExome sequencingSequence DeletionNeuronsDystoniaGeneticsexercise-induced dystoniaTBC1D24GTPase-Activating ProteinsANNOTATIONSEpilepsy RolandicPhenotypeRecombinant ProteinsPedigree3. Good healthRolandic epilepsyDystoniaDrosophila melanogasterChild PreschoolFemaleSettore MED/26 - NeurologiaSynaptic VesiclesDrosophila melanogasterPROTEIN STABILITYLife Sciences & BiomedicineLocomotionAdolescentPhysical ExertionMutation MissenseClinical NeurologyPREDICTIONSBiology03 medical and health sciencesmedicineAnimalsHumansAmino Acid SequenceCOMPARTMENToxidative streScience & TechnologySequence Homology Amino AcidMUTATIONSNeurosciencesInfantBiological TransportDEGRADATIONmedicine.diseasebiology.organism_classificationAcetylcysteineDisease Models AnimalOxidative Stress030104 developmental biologyrab GTP-Binding ProteinsSEIZURESNeurosciences & NeurologyNeurology (clinical)Reactive Oxygen SpeciesSequence Alignment030217 neurology & neurosurgery
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Pseudodominant inheritance of goitrous congenital hypothyroidism caused by TPO mutations: molecular and in silico studies.

2007

CONTEXT AND OBJECTIVE: Most cases of goitrous congenital hypothyroidism (CH) from thyroid dyshormonogenesis 1) follow a recessive mode of inheritance and 2) are due to mutations in the thyroid peroxidase gene (TPO). We report the genetic mechanism underlying the apparently dominant inheritance of goitrous CH in a nonconsanguineous family of French Canadian origin. DESIGN, SETTING, AND PARTICIPANTS: Two brothers identified by newborn TSH screening had severe hypothyroidism and a goiter with increased (99m)Tc uptake. The mother was euthyroid, but the father and two paternal uncles had also been diagnosed with goitrous CH. After having excluded PAX8 gene mutations, we hypothesized that the und…

MaleModels Molecularendocrine systemmedicine.medical_specialtySurface PropertiesEndocrinology Diabetes and MetabolismClinical BiochemistryMolecular Sequence DataStatic ElectricityContext (language use)Gene mutationCompound heterozygosityBiochemistryIodide PeroxidasePolymerase Chain ReactionEndocrinologyThyroid dyshormonogenesisInternal medicineCongenital HypothyroidismMedicineMissense mutationHumansEuthyroidAmino Acid SequenceAlleleGeneticsBase Sequencebusiness.industryGoiterBiochemistry (medical)Infant NewbornDNAmedicine.diseaseCongenital hypothyroidismPedigreeEndocrinologyMutationFemalebusinessSequence AlignmentThe Journal of clinical endocrinology and metabolism
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In-Frame Mutations in Exon 1 of SKI Cause Dominant Shprintzen-Goldberg Syndrome

2012

International audience; Shprintzen-Goldberg syndrome (SGS) is characterized by severe marfanoid habitus, intellectual disability, camptodactyly, typical facial dysmorphism, and craniosynostosis. Using family-based exome sequencing, we identified a dominantly inherited heterozygous in-frame deletion in exon 1 of SKI. Direct sequencing of SKI further identified one overlapping heterozygous in-frame deletion and ten heterozygous missense mutations affecting recurrent residues in 18 of the 19 individuals screened for SGS; these individuals included one family affected by somatic mosaicism. All mutations were located in a restricted area of exon 1, within the R-SMAD binding domain of SKI. No mut…

MaleModels Molecularmedicine.disease_cause[SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMarfan SyndromeArachnodactylyExon0302 clinical medicineGene OrderMissense mutationGenetics(clinical)Child[ SDV.GEN.GH ] Life Sciences [q-bio]/Genetics/Human geneticsGenetics (clinical)Exome sequencingGenes DominantGenetics0303 health sciencesMutationShprintzen–Goldberg syndromeExonsPhenotypePedigreeDNA-Binding ProteinsPhenotypeChild PreschoolFemalemedicine.symptomAdultAdolescentMolecular Sequence Data[ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyBiology[SDV.GEN.GH] Life Sciences [q-bio]/Genetics/Human genetics03 medical and health sciencesCamptodactylyCraniosynostosesYoung Adultstomatognathic systemReportProto-Oncogene ProteinsmedicineGeneticsHumansAmino Acid Sequence030304 developmental biologyFacies[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologymedicine.diseaseMolecular biologyProtein Structure TertiaryArachnodactyly[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsMutationSequence Alignmenthuman activities030217 neurology & neurosurgery
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