Search results for "Conserved sequence"

showing 10 items of 103 documents

Identification of a Conserved HLA-A2-Restricted Decapeptide from the IE1 Protein (pUL123) of Human Cytomegalovirus

2002

Abstract Control of human cytomegalovirus (HCMV) infection is predominantly mediated by cytolytic CD8 + T lymphocytes (CTL). Among the roughly 200 HCMV-encoded polypeptides, the tegument protein pp65 (ppUL83) and the nonstructural IE1 protein are considered to be dominant CTL targets. Yet the importance of CTL against IE1 for protective immunity against HCMV reactivation and disease has remained elusive. Analyses have been difficult, as all MHC class I presented peptides of IE1 defined so far are located in parts of the protein that are variable between viral strains. In this study a conserved decameric peptide from IE1 (P6, IE1 354–363 ) that bound to HLA-A2 was identified. Using peptide-p…

Human cytomegalovirusherpesvirusesViral proteinvirusesMolecular Sequence DataIE1CytomegalovirusEpitopes T-Lymphocytecytotoxic T lymphocytesmedicine.disease_causeImmediate early proteinCell LineImmediate-Early ProteinsViral Proteinsconserved CTL epitopesVirologyHLA-A2 AntigenMHC class ImedicineHumansCytotoxic T cellAmino Acid SequenceConserved SequencebiologyELISPOTvirus diseasesHLA-A2biochemical phenomena metabolism and nutritionCytotoxicity Tests Immunologicmedicine.diseaseVirologyPeptide FragmentsVirus LatencyCTL*human cytomegalovirusCytomegalovirus InfectionsImmunologybiology.proteinPeptidesCD8T-Lymphocytes CytotoxicVirology
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A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase

2018

Scientific reports 8(1), 13104 (2018). doi:10.1038/s41598-018-31259-y

IsatinModels Molecular0301 basic medicineStereochemistryGlutaminelcsh:Medicine010402 general chemistry01 natural sciencesArticleAmidohydrolasesCatalysisEvolution Molecular03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsCatalytic DomainHydrolaseCatalytic triadAmino Acid SequenceRhodobacteraceaelcsh:ScienceConserved SequenceKynureninechemistry.chemical_classificationManganeseMultidisciplinarybiologyAmidohydrolaseHydrolysisIsatinlcsh:RActive site6000104 chemical sciencesZinc030104 developmental biologyEnzymechemistryBiocatalysisArylformamidaseBiocatalysisbiology.proteinQuantum Theorylcsh:QProtonsddc:600
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A conserved role for the mitochondrial citrate transporter Sea/SLC25A1 in the maintenance of chromosome integrity.

2009

Histone acetylation plays essential roles in cell cycle progression, DNA repair, gene expression and silencing. Although the knowledge regarding the roles of acetylation of histone lysine residues is rapidly growing, very little is known about the biochemical pathways providing the nucleus with metabolites necessary for physiological chromatin acetylation. Here, we show that mutations in the scheggia (sea)-encoded Sea protein, the Drosophila ortholog of the human mitochondrial citrate carrier Solute carrier 25 A1 (SLC25A1), impair citrate transport from mitochondria to the cytosol. Interestingly, inhibition of sea expression results in extensive chromosome breakage in mitotic cells and indu…

MaleAnion Transport ProteinsBlotting WesternMolecular Sequence DataOrganic Anion Transporterscitrate transporterSAP30BiologyModels BiologicalHistonesMitochondrial ProteinsHistone H2AGeneticsHistone codeAnimalsDrosophila ProteinsHumansAmino Acid SequenceCitratesSLC25A1Molecular BiologyGenetics (clinical)Cells CulturedConserved SequenceChromosome Aberrationsmetabolism epigenetics histone acetylation AcCoA Citrate carrierSequence Homology Amino AcidChromosome integrityhistone acetylationHDAC8AcetylationChromosome BreakageGeneral MedicineCitrate transportFibroblastsHDAC4mitochondriaHistoneBiochemistryAcetylationMutationcitrate transporter histone acetylationbiology.proteinFemaleRNA InterferenceCarrier ProteinsHuman molecular genetics
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The new gene DmX from Drosophila melanogaster encodes a novel WD-repeat protein

1998

DmX is a novel gene from Drosophila melanogaster located on the X chromosome in region 5D5/6-E1. The molecular analysis of the genomic and cDNA sequences of DmX shows that the gene spans appr. 16kb and displays a mosaic structure with 15 exons. The 12kb long DmX transcript is present in Drosophila embryos, larvae and adults of both sexes. The open reading frame of DmX encodes a novel WD-repeat protein, containing at least 30 WD-repeat units. WD-repeat proteins contain a conserved motif of approximately 40 amino acids (aa), usually ending with the dipeptide Trp-Asp (WD). Homologues of the DmX gene exist in other dipteran species, in Caenorhabditis elegans and human, revealing that DmX is an …

MaleDNA ComplementaryX ChromosomeTranscription GeneticMolecular Sequence DataGenes InsectOpen Reading FramesExonComplementary DNAGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequenceGeneConserved SequenceX chromosomeCaenorhabditis elegansRepetitive Sequences Nucleic AcidGeneticsAspartic AcidbiologyTryptophanChromosome MappingGene Expression Regulation DevelopmentalSequence Analysis DNAGeneral Medicinebiology.organism_classificationOpen reading frameDrosophila melanogasterInsect ProteinsFemaleDrosophila melanogasterSequence AlignmentGene
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Sequence variation in couch potato and its effects on life-history traits in a northern malt fly, Drosophila montana

2011

Abstract Couch potato ( cpo ) has previously been connected to reproductive diapause in several insect species including Drosophila melanogaster , where it has been suggested to provide a link between the insulin signalling pathway and the hormonal control of diapause. In the first part of the study we sequenced nearly 3.6 kb of this gene in a northern Drosophila species ( Drosophila montana ) with a robust photoperiodically determined diapause and found several types of polymorphisms along the sequenced area. We also found variation among five Drosophila virilis group species in the length of the 5th exon of cpo and in the site of the stop codon at the end of this exon. The second part of …

MalePhysiologyAmino Acid MotifsMolecular Sequence DataPopulationDiapauseExonSpecies SpecificityAnimalsDrosophila ProteinsAmino Acid SequenceeducationGeneConserved SequenceSequence DeletionGeneticseducation.field_of_studyPolymorphism GeneticSequence Homology Amino AcidbiologyWild typeNuclear ProteinsExonsSequence Analysis DNAbiology.organism_classificationIntronsStop codonDrosophila virilisPhenotypeInsect ScienceDrosophilaFemaleDrosophila melanogasterSequence AlignmentJournal of Insect Physiology
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A new heterozygous mutation (D196N) in the Gs alpha gene as a cause for pseudohypoparathyroidism type IA in a boy who had gallstones

2011

Background Pseudohypoparathyroidism (PHP) is characterized by hypocalcemia and hyperphosphatemia in association with an increased secretion of parathyroid hormone (PTH) due to decreased target tissue responsiveness to PTH. Patients with PHP type Ia are not only resistant to PTH, but also to other hormones that bind to receptors coupled to stimulatory G protein (Gsalpha). PHP Ia and Albright hereditary osteodystrophy (AHO) are caused by a reduced activity of the Gsalpha protein. Heterozygous inactivating Gs alpha (GNAS) gene mutations have been identified in these patients. Methods We studied a boy with PHP Ia. During follow-up the patient developed elevated liver enzyme serum levels and abd…

Malemusculoskeletal diseasesHeterozygotemedicine.medical_specialtyErythrocytesFoot Deformities CongenitalEndocrinology Diabetes and MetabolismMutation MissenseParathyroid hormoneGallstonesGene mutationHyperphosphatemiaEndocrinologyInternal medicineChromograninsGTP-Binding Protein alpha Subunits GsGNAS complex locusHumansMedicineMissense mutationnatural sciencesAmino Acid SequenceChildConserved SequencePseudohypoparathyroidismBase SequenceSequence Homology Amino Acidbiologybusiness.industryDNAExonsGallstonesmedicine.diseasePedigreeCholesterolEndocrinologyAmino Acid SubstitutionPseudohypoparathyroidismPediatrics Perinatology and Child Healthbiology.proteinbusinessHand Deformities CongenitalHormoneJournal of Pediatric Endocrinology and Metabolism
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Evolutionary conservation of the structural, pharmacological, and genomic characteristics of the melanocortin receptor subtypes

2005

We have cloned melanocortin receptors (MCRs) from several species of fish. The MC4R and MC5R subtypes arose early in vertebrate evolution and their primary structure is remarkably conserved. Expression and pharmacological characterization of the MCRs in fish has revealed that they bind and respond to melanocortin peptides with high potency. Detailed characterization of the binding properties of the different subtypes suggests that MCRs in early vertebrates had preference for adrenocorticotropic hormone (ACTH) peptides, while the high sensitivity for the shorter proopiomelanocortin (POMC) products, such as the alpha-, beta-, and gamma-melanocyte-stimulating hormone (MSH), has appeared later,…

Melanocyte-stimulating hormonePhysiologyMolecular Sequence DataBiochemistryConserved sequenceEvolution MolecularCellular and Molecular NeuroscienceEndocrinologyProopiomelanocortinMelanocortin receptorbiology.animalAnimalsHumansAmino Acid SequenceReceptorConserved SequenceG protein-coupled receptorGeneticsbiologyReceptors MelanocortinVertebrateGenomicsStructural Homology Proteinbiology.proteinMelanocortinhormones hormone substitutes and hormone antagonistsPeptides
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Characterization of the length polymorphism in the A + T-rich region of the Drosophila obscura group species

1993

In the twelve Drosophila obscura group species studied, belonging to the affinis, obscura, and pseudoobscura subgroups, the mitochondrial DNA length ranges from 15.8 to 17.2 kb. This length polymorphism is mainly due to insertions/deletions in the variable region of the A + T-rich region. In addition, one species (D. tristis) possess a tandem duplication of a 470-bp fragment that contains the replication origin. The same duplication has occurred at least twice in the Drosophila evolutionary history due to the fact that the repetition is analogous to repetitions found in the four species of the D. melanogaster complex. By comparing the nucleotide sequence of the conserved region in D. ambigu…

Mitochondrial DNAMolecular Sequence DataRestriction MappingDNA RecombinantDNA MitochondrialConserved sequenceSpecies SpecificityMolecular evolutionDrosophilidaeSequence Homology Nucleic AcidGene duplicationGeneticsAnimalsMolecular BiologyEcology Evolution Behavior and SystematicsGeneticsPolymorphism GeneticbiologyBase SequenceAdenineNucleic acid sequencebiology.organism_classificationNucleic Acid ConformationDrosophilaTandem exon duplicationDrosophila obscuraSequence AlignmentPlasmidsThymidine
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Maintenance of a Protein Structure in the Dynamic Evolution of TIMPs over 600 Million Years

2016

Deciphering the events leading to protein evolution represents a challenge, especially for protein families showing complex evolutionary history. Among them, TIMPs represent an ancient eukaryotic protein family widely distributed in the animal kingdom. They are known to control the turnover of the extracellular matrix and are considered to arise early during metazoan evolution, arguably tuning essential features of tissue and epithelial organization. To probe the structure and molecular evolution of TIMPs within metazoans, we report the mining and structural characterization of a large data set of TIMPs over approximately 600 Myr. The TIMPs repertoire was explored starting from the Cnidaria…

Models Molecular0301 basic medicineTIMPsProtein familyProtein Conformationhomology modelingSettore BIO/11 - Biologia MolecolareSequence alignmentBiologytranscriptome wide analysisConserved sequencecnidariansEvolution MolecularCnidaria03 medical and health sciences0302 clinical medicineProtein structurePhylogeneticsMolecular evolutionGeneticsAnimalsTIMPAmino Acid SequenceHomology modelingcnidarianConserved SequencePhylogenyEcology Evolution Behavior and SystematicsGeneticsmyrTissue Inhibitor of Metalloproteinases030104 developmental biologyEvolutionary biologyTIMPs; cnidarians; homology modeling; transcriptome wide analysisSequence Alignment030217 neurology & neurosurgeryResearch Article
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The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition.

2003

The PYRIN domain is a conserved sequence motif identified in more than 20 human proteins with putative functions in apoptotic and inflammatory signalling pathways. The three-dimensional structure of the PYRIN domain from human ASC was determined by NMR spectroscopy. The structure determination reveals close structural similarity to death domains, death effector domains, and caspase activation and recruitment domains, although the structural alignment with these other members of the death-domain superfamily differs from previously predicted amino acid sequence alignments. Two highly positively and negatively charged surfaces in the PYRIN domain of ASC result in a strong electrostatic dipole …

Models MolecularProtein FoldingMagnetic Resonance SpectroscopyCARD Signaling Adaptor ProteinsProtein ConformationProtein domainMolecular Sequence DataStatic ElectricityBiologyPyrin domainProtein Structure SecondaryConserved sequenceProtein structureStructural BiologyAnimalsHumansAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceZebrafishDeath domainGeneticsModels StatisticalSequence Homology Amino AcidProteinsPyrinZebrafish ProteinsCell biologyProtein Structure TertiaryCARD Signaling Adaptor ProteinsCytoskeletal ProteinsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProtein foldingProtein BindingSignal TransductionJournal of molecular biology
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