Search results for "homology"

showing 10 items of 770 documents

Identification of proteins and developmental expression of RNAs encoded by the 65A cuticle protein gene cluster in Drosophila melanogaster

1998

0965-1748 (Print) Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.; Proteins of the third instar larval cuticle of Drosophila melanogaster, LCP5-LCP9, were purified and their N-terminal sequences determined. Three of these proteins (LCP5, 6, and 8) were found to be encoded by two multicopy genes previously mapped to the gene cluster at 65A 5-6 on the left arm of the third chromosome. The analysis of the patterns of developmental expression of the 8 distinct genes at this site showed that all but two were expressed during larval life. The patterns fell into three groups: one where expression was all through larval life, one where expression was primar…

Drosophila melanogaster/*genetics/growth & developmentCuticleMolecular Sequence DataInsect Proteins/*genetics/isolation & purificationSequence HomologyGenes InsectLarva/genetics/growth & developmentBiochemistryGene clusterAnimalsDevelopmentalAmino Acid SequenceMolecular BiologyGeneGeneticsRegulation of gene expressionSequence Homology Amino AcidbiologyfungiGene Expression Regulation DevelopmentalChromosome Mappingbiology.organism_classificationAmino AcidDrosophila melanogasterGene Expression RegulationGenesLarvaMultigene FamilyInsect ScienceEcdysisRNA/*geneticsInsect ProteinsRNAInstarDrosophila melanogasterInsectOverlapping geneInsect Biochemistry and Molecular Biology
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A high-quality homology model for the human dopamine transporter validated for drug design purposes.

2018

The human dopamine transporter (hDAT) plays many vital functions within the central nervous system and is thus targeted by many pharmaceutical agents. Dopamine-related therapies are in current development for individuals with dopamine-related disorders including depression, Parkinson's disease, and psychostimulant addictions such as cocaine abuse. Yet, most efforts to develop new dopamine therapies are within costly structure-activity relationship studies. Through structure-based drug design techniques, the binding site of hDAT can be utilized to develop novel selective and potent dopamine therapies at reduced costs. However, no structural models of hDAT specifically validated for rational …

DrugComputer sciencemedia_common.quotation_subjectDrug designComputational biologyNortriptyline01 natural sciencesBiochemistryInhibitory Concentration 50DopamineDrug DiscoverymedicineAnimalsDrosophila ProteinsHumansHomology modelingmedia_commonDopamine transporterPharmacologyDopamine Plasma Membrane Transport ProteinsBinding Sitesbiology010405 organic chemistryAddictionOrganic Chemistry0104 chemical sciencesProtein Structure TertiaryMolecular Docking Simulation010404 medicinal & biomolecular chemistryDrug Designbiology.proteinMolecular MedicineDrosophilaCocaine abusemedicine.drugChemical biologydrug design
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CYP3 phylogenomics: evidence for positive selection of CYP3A4 and CYP3A7.

2008

CYP3A metabolizes 50% of currently prescribed drugs and is frequently involved in clinically relevant drug interactions. The understanding of roles and regulations of the individual CYP3A genes in pharmacology and physiology is incomplete.Using genomic sequences from 16 species we investigated the evolution of CYP3 genomic loci over a period of 450 million years.CYP3A genes in amniota evolved from two ancestral CYP3A genes. Upon the emergence of eutherian mammals, one of them was lost, whereas, the other acquired a novel genomic environment owing to translocation. In primates, CYP3A underwent rapid evolutionary changes involving multiple gene duplications, deletions, pseudogenizations, and …

DrugDNA Complementarymedia_common.quotation_subjectMolecular Sequence DataGenomicsBiologyCatalysisCytochrome P-450 Enzyme SystemSpecies SpecificityPhylogenomicsSequence Homology Nucleic AcidGeneticsAnimalsHumansGeneral Pharmacology Toxicology and PharmaceuticsMolecular BiologyGeneGenetics (clinical)CYP3A7media_commonComparative genomicsGeneticsCYP3A4Base SequenceGenomicsIsoenzymesMolecular MedicinePharmacogeneticsPharmacogenetics and genomics
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Identification of protein IT of the intestinal cytoskeleton as a novel type I cytokeratin with unusual properties and expression patterns.

1990

A major cytoskeletal polypeptide (Mr approximately 46,000; protein IT) of human intestinal epithelium was characterized by biochemical and immunological methods. The polypeptide, which was identified as a specific and genuine mRNA product by translation in vitro, reacted, in immunoblotting after SDS-PAGE, only with one of numerous cytokeratin (CK) antisera tested but with none of many monoclonal CK antibodies. In vitro, it formed heterotypic complexes with the type II CK 8, as shown by blot binding assays and gel electrophoresis in 4 M urea, and these complexes assembled into intermediate filaments (IFs) under appropriate conditions. A chymotrypsin-resistant Mr approximately 38,000 core fra…

DuodenumImmunoblottingMolecular Sequence DataBiologyPeptide MappingEpitheliumCytokeratinIntestinal mucosaSequence Homology Nucleic AcidKeratinProtein biosynthesisAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceRNA MessengerIntestinal MucosaIntermediate filamentCytoskeletonPeptide sequenceCytoskeletonchemistry.chemical_classificationArticlesCell BiologyMolecular biologyRatsBlotCytoskeletal ProteinsMicroscopy ElectronBiochemistrychemistryProtein BiosynthesisKeratinsJournal of Cell Biology
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Reciprocal regulation of the human sterol regulatory element binding protein (SREBP)-1a promoter by Sp1 and EGR-1 transcription factors.

2007

AbstractSterol regulatory element binding protein (SREBP)-1a is a transcription factor that is highly expressed in actively growing cells, and is involved in the biosynthesis of cholesterol, fatty acids and phospholipids. We have mapped the minimal human SREBP-1a promoter region to 75bp upstream of the translation start site where we discovered a functional role for the 3 GC-boxes containing overlapping sites for the Sp1 and EGR-1 transcription factors. Intact SP1-binding sites are essential for promoter activity, whereas EGR-1 suppresses the transcription of the human SREBP-1a promoter. These results reveal a novel physiologically relevant transcriptional mechanism for the reciprocal regul…

Egr-1Chromatin ImmunoprecipitationSp1 Transcription FactorSREBP-1aResponse elementMolecular Sequence DataBiophysicsElectrophoretic Mobility Shift AssayBiologyBiochemistrySp1Cell LineUpstream activating sequenceStructural BiologyTranscription (biology)Sequence Homology Nucleic AcidGene expressionGeneticsHumansPromoter Regions GeneticMolecular BiologyTranscription factorGeneral transcription factorBase SequenceReverse Transcriptase Polymerase Chain ReactionPromoterPromoterCell BiologySterol regulatory element-binding proteinBiochemistryEarly Growth Response Transcription Factorslipids (amino acids peptides and proteins)Gene expressionSterol Regulatory Element Binding Protein 1FEBS letters
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Novel molluskan biomineralization proteins retrieved from proteomics: a case study with upsalin.

2012

12 pages; International audience; The formation of the molluskan shell is regulated by an array of extracellular proteins secreted by the calcifying epithelial cells of the mantle. These proteins remain occluded within the recently formed biominerals. To date, many shell proteins have been retrieved, but only a few of them, such as nacreins, have clearly identified functions. In this particular case, by combining molecular biology and biochemical approaches, we performed the molecular characterization of a novel protein that we named Upsalin, associated with the nacreous shell of the freshwater mussel Unio pictorum. The full sequence of the upsalin transcript was obtained by RT-PCR and 5'/3…

ElectrophoresisMolecular Sequence DataBiologyProteomicsBioinformaticsBiochemistryHomology (biology)03 medical and health sciencesproteomicsGene silencingAnimalsAmino Acid Sequence[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyPeptide sequence030304 developmental biology0303 health sciencesMineralsBase Sequence030302 biochemistry & molecular biologyOrganic ChemistrymollusksImmunogold labelling[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsbiomineralizationIn vitroproteinsfreshwater bivalvesBiochemistryMolluscaMicroscopy Electron ScanningMolecular MedicineTarget proteinBiomineralization
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Gene within gene configuration and expression of the Drosophila melanogaster genes lethal(2) neighbour of tid [l(2)not] and lethal(2) relative of tid…

1997

In this paper, we describe the structure and temporal expression pattern of the Drosophila melanogaster genes l(2)not and l(2)rot located at locus 59F5 vis a vis the tumor suppressor gene l(2)tid described previously and exhibiting a gene within gene configuration. The l(2)not protein coding region, 1530 nt, is divided into two exons by an intron, 2645 nt, harboring the genes l(2)rot, co-transcribed from the same DNA strand, and l(2)tid, co-transcribed from the opposite DNA strand, located vis a vis. To determine proteins encoded by the genes described in this study polyclonal rabbit antibodies (Ab), anti-Not and anti-Rot, were generated. Immunostaining of developmental Western blots with t…

Embryo NonmammalianTranscription GeneticMolecular Sequence DataRestriction MappingGenes Insectmacromolecular substancesBiologyMannosyltransferasesAntibodiesExonTranscription (biology)GeneticsAnimalsDrosophila ProteinsNorthern blotAmino Acid SequenceMicroscopy ImmunoelectronGeneBody PatterningRegulation of gene expressionBase SequenceSequence Homology Amino Acidtechnology industry and agricultureIntronRNAGene Expression Regulation DevelopmentalMembrane ProteinsGeneral MedicineExonsMolecular biologyIntronsPeptide FragmentsAntisense RNADrosophila melanogasterGene Expression RegulationInsect ProteinsRabbitsSequence AlignmentGene
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An organizing region in metamorphosing hydrozoan planula larvae--stimulation of axis formation in both larval and in adult tissue.

2010

A novel wingless gene was isolated from the marine colonial hydroid Hydractinia echinata. Alignments and Bayesian inference analysis clearly assign the gene to the Wnt5A group. In line with data found for the brachyury ortholog of Hydractinia, He-wnt5A is expressed during metamorphosis in the posterior tip of the spindle-shaped planula larva, suggesting that the tip functions as a putative organizer during metamorphosis. Additionally, the outermost cells of the posterior tip are omitted from apoptosis during metamorphosis. In order to investigate this putative organizer function, we transplanted the posterior tip of metamorphosing animals into non-induced larvae and into primary polyps 24 h…

EmbryologyBrachyuryanimal structuresTime Factorsmedia_common.quotation_subjectMolecular Sequence DataApoptosisModels BiologicalHydractinia echinataHydractiniaIn Situ Nick-End LabelingAnimalsAmino Acid SequenceMetamorphosisPlanulaIn Situ HybridizationPhylogenymedia_commonBody PatterningRegulation of gene expressionLarvabiologySequence Homology Amino AcidfungiMetamorphosis BiologicalGene Expression Regulation DevelopmentalAnatomybiology.organism_classificationCell biologyWnt ProteinsHydrozoaLarvaHydroid (zoology)Tissue TransplantationDevelopmental BiologyThe International journal of developmental biology
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saliva, a new Drosophila gene expressed in the embryonic salivary glands with homologues in plants and vertebrates.

1998

saliva (slv) transcription begins at the salivary gland placodes and continues on throughout development as salivary glands invaginate and reach their final location and morphology. saliva is located cytogenetically in 76A/B, and encodes a 226-amino-acid protein with four hydrophobic domains. A Northern blot detects a 1.6-kb transcript throughout development. Database similarity searches reveal homology to proteins from Caenorhabditis, Lilium, Medicago and mouse.

EmbryologySalivaDNA ComplementaryEmbryo NonmammalianDNA PlantMolecular Sequence DataGenes InsectGenes PlantHomology (biology)Salivary Glandsstomatognathic systemmedicineAnimalsDrosophila ProteinsNorthern blotAmino Acid SequenceSalivary Proteins and PeptidesGeneIn Situ HybridizationbiologySalivary glandSequence Homology Amino AcidGene Expression Regulation DevelopmentalSequence Analysis DNAPlantsbiology.organism_classificationMolecular biologyCaenorhabditismedicine.anatomical_structureDrosophila melanogasterVertebratesDrosophila melanogasterSequence AlignmentDrosophila ProteinDevelopmental BiologyMechanisms of development
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Sequence similarity of mammalian epoxide hydrolases to the bacterial haloalkane dehalogenase and other related proteins Implication for the potential…

1994

Direct comparison of the amino acid sequences of microsomal and soluble epoxide hydrolase superficially indicates that these enzymes are unrelated. Both proteins, however, share significant sequence similarity to a bacterial haloalkane dehalogenase that has earlier been shown to belong to the alpha/beta hydrolase fold family of enzymes. The catalytic mechanism for the dehalogenase has been elucidated in detail [Verschueren et al. (1993) Nature 363, 693-698] and proceeds via an ester intermediate where the substrate is covalently bound to the enzyme. From these observations we conclude (i) that microsomal and soluble epoxide hydrolase are distantly related enzymes that have evolved from a co…

Epoxide hydrolase 2StereochemistryHydrolasesMolecular Sequence DataBiophysicsHydrolaseEsteraseBiochemistryEsteraseCatalysisChelataseα/β Hydrolase foldBacterial ProteinsStructural BiologyMicrosomesHydrolaseGeneticsAnimalsAmino Acid SequenceEpoxide hydrolaseMolecular BiologyDehalogenasePeroxidasechemistry.chemical_classificationEpoxide HydrolasesMammalsBacteriaSequence Homology Amino AcidCell BiologyLipaseBiological EvolutionEnzymechemistryBiochemistrySolubilityEpoxide HydrolasesLuciferaseHaloalkane dehalogenaseFEBS Letters
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