Search results for "binding"

showing 10 items of 3896 documents

Hsp60, a Novel Target for Antitumor Therapy: Structure-Function Features and Prospective Drugs Design

2013

Heat shock protein 60 kDa (Hsp60) is a chaperone classically believed to be involved in assisting the correct folding of other mitochondrial proteins. Hsp60 also plays a role in cytoprotection against cell stressors, displaying for example, antiapoptotic potential. Despite the plethora of studies devoted to the mechanism of Hsp60's function, especially in prokaryotes, fundamental issues still remain unexplored, including the definition of its role in cancer. Key questions still unanswered pertain to the differences in structure-function features that might exist between the well-studied prokaryotic GroEL and the largely unexplored eukaryotic Hsp60 proteins. In this article we discuss these …

animal structuresBinding pocketCellAntineoplastic Agentschemical and pharmacologic phenomenaComputational biologyBiologyBioinformaticsFunctional domaincomplex mixturesChaperoninStructure-Activity RelationshipNeoplasmsHeat shock proteinDrug DiscoverymedicineHumansPharmacologyCompound dockingSettore BIO/16 - Anatomia UmanaCell growthfungiSettore CHIM/06 - Chimica OrganicaChaperonin 60Hsp60Settore CHIM/08 - Chimica FarmaceuticaCytoprotectionGroELmedicine.anatomical_structureSettore CHIM/03 - Chimica Generale E InorganicaCancer treatmentDrug DesignChaperone (protein)biology.proteinHSP60Protein foldingEpolactaeneCurrent Pharmaceutical Design
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Tracing the origin of the compensasome: evolutionary history of DEAH helicase and MYST acetyltransferase gene families.

2001

Dosage compensation in Drosophila is mediated by a complex of proteins and RNAs called the "compensasome." Two of the genes that encode proteins of the complex, maleless (mle) and males-absent-on-the-first (mof), respectively, belong to the DEAH helicase and MYST acetyltransferase gene families. We performed comprehensive phylogenetic and structural analyses to determine the evolutionary histories of these two gene families and thus to better understand the origin of the compensasome. All of the members of the DEAH and MYST families of the completely sequenced Saccharomyces cerevisiae and Caenorhabditis elegans genomes, as well as those so far (June 2000) found in Drosophila melanogaster (f…

animal structuresChromosomal Proteins Non-HistoneMolecular Sequence DataBiologyEvolution MolecularAcetyltransferasesGeneticsGene familyAnimalsDrosophila ProteinsAmino Acid SequenceMolecular BiologyGeneEcology Evolution Behavior and SystematicsCaenorhabditis elegansPhylogenyHistone AcetyltransferasesGeneticsDosage compensationSequence Homology Amino AcidfungiDNA HelicasesHelicaseNuclear Proteinsbiology.organism_classificationRNA Helicase ACaenorhabditisDNA-Binding ProteinsMultigene Familybiology.proteinDrosophila melanogasterRNA HelicasesTranscription FactorsMolecular biology and evolution
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A galectin links the aggregation factor to cells in the sponge (Geodia cydonium) system.

1996

The cDNA for the full-length lectin from the marine sponge Geodia cydonium was cloned. Analysis of the deduced aa sequence revealed that this lectin belongs to the group of galectins. The full-length galectin, which was obtained also in a recombinant form, has an M(r) of 20,877; in the processed form it is a 15 kDa polypeptide. The enriched aggregation factor from G.cydonium also was determined to contain, besides minimal amounts of the galectin, a 140 kDa polypeptide which is involved in cell-cell adhesion. Monoclonal antibodies have been raised against this protein; Fab' fragments prepared from them abolished cell-cell reaggregation. Cell reaggregation experiments revealed that the aggreg…

animal structuresDNA Complementarymedicine.drug_classGalectinsCellMolecular Sequence DataMonoclonal antibodyBiochemistrylaw.inventionlawComplementary DNALectinsotorhinolaryngologic diseasesmedicineAnimalsAmino Acid SequenceCloning MolecularCell adhesionGalectinCell AggregationbiologyBase SequenceChemistryLectinAntibodies MonoclonalPoriferastomatognathic diseasesmedicine.anatomical_structureBiochemistrybiology.proteinRecombinant DNAAntibodyCell Adhesion MoleculesProtein BindingGlycobiology
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Rapid changes in heat-shock cognate 70 levels, heat-shock cognate phosphorylation state, heat-shock transcription factor, and metal transcription fac…

2010

The aim of the present study was to analyze and compare the effects of several metals on the embryos of the sea urchin Paracentrotus lividus, a key species within the Mediterranean Sea ecosystem. Embryos were continuously exposed from fertilization to the following metals: 0.6 mg/l copper, 3 mg/l lead, and 6 mg/l nickel. The embryos were then monitored for metal responses at the gastrula stage, which occurred 24 h after exposure. A biochemical multi-experimental approach was taken and involved the investigation of the levels of HSC70 expression and the involvement of heat shock factor (HSF) and/or metal transcription factor (MTF) in the response. Immunoblotting assays and electrophoretic mo…

animal structuresEmbryo NonmammalianHealth Toxicology and MutagenesisEmbryonic DevelopmentManagement Monitoring Policy and LawBiologyToxicologyParacentrotus lividuschemistry.chemical_compoundHeat Shock Transcription Factorsbiology.animalMetals HeavyToxicity TestsMediterranean SeaAnimalsP.lividus embryos heahy metals HSC70 biomarkersSettore BIO/06 - Anatomia Comparata E CitologiaPhosphorylationSea urchinTranscription factorEmbryogenesisHSC70 Heat-Shock ProteinsEmbryoGeneral Medicinebiology.organism_classificationMolecular biologyCell biologyHeat shock factorDNA-Binding ProteinschemistrySea Urchinsembryonic structuresPhosphorylationDNAWater Pollutants ChemicalEnvironmental MonitoringTranscription Factors
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Evidence for differential and redundant function of the Sox genes Dichaete and SoxN during CNS development in Drosophila.

2002

Group B Sox-domain proteins encompass a class of conserved DNA-binding proteins expressed from the earliest stages of metazoan CNS development. In all higher organisms studied to date, related Group B Sox proteins are co-expressed in the developing CNS; in vertebrates there are three (Sox1, Sox2 and Sox3) and in Drosophila there are two (SoxNeuro and Dichaete). It has been suggested there may be a degree of functional redundancy in Sox function during CNS development. We describe the CNS phenotype of a null mutation in the Drosophila SoxNeuro gene and provide the first direct evidence for both redundant and differential Sox function during CNS development in Drosophila. In the lateral neuro…

animal structuresEmbryo NonmammalianMutantBiologyNervous SystemSOX Transcription FactorsSOX1NeuroblastSOX2Species SpecificityEctodermAnimalsDrosophila ProteinsMolecular BiologySOX Transcription FactorsGeneticsNeuroectodermHigh Mobility Group ProteinsGene Expression Regulation DevelopmentalPhenotypeNull alleleDNA-Binding ProteinsDrosophila melanogasterMutagenesisembryonic structuresVertebratesDevelopmental BiologyTranscription FactorsDevelopment (Cambridge, England)
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Distinct 5' SCL enhancers direct transcription to developing brain, spinal cord, and endothelium: neural expression is mediated by GATA factor bindin…

1999

The SCL gene encodes a basic helix-loop-helix transcription factor with a pivotal role in the development of endothelium and of all hematopoietic lineages. SCL is also expressed in the central nervous system, although its expression pattern has not been examined in detail and its function in neural development is unknown. In this article we present the first analysis of SCL transcriptional regulation in vivo. We have identified three spatially distinct regulatory modules, each of which was both necessary and sufficient to direct reporter gene expression in vivo to three different regions within the normal SCL expression domain, namely, developing endothelium, midbrain, and hindbrain/spinal …

animal structuresEmbryo NonmammalianTranscription GeneticHindbrainMice TransgenicChick EmbryoBiologybehavioral disciplines and activities03 medical and health sciencesMice0302 clinical medicineTranscription (biology)Genes Reporterhemic and lymphatic diseasesProto-Oncogene ProteinsBasic Helix-Loop-Helix Transcription FactorsAnimalsTissue DistributionEndotheliumEnhancerMolecular BiologyTranscription factorGeneIn Situ HybridizationT-Cell Acute Lymphocytic Leukemia Protein 1Zebrafish030304 developmental biologyRegulation of gene expressionGenetics0303 health sciencesReporter geneModels GeneticfungiBrainCell BiologyZebrafish ProteinsEmbryo MammalianCell biologyDNA-Binding ProteinsLac OperonSpinal CordNeural development030217 neurology & neurosurgeryDevelopmental BiologyTranscription FactorsDevelopmental biology
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Molecular markers for identified neuroblasts in the developing brain of Drosophila.

2003

The Drosophila brain develops from the procephalic neurogenic region of the ectoderm. About 100 neural precursor cells (neuroblasts) delaminate from this region on either side in a reproducible spatiotemporal pattern. We provide neuroblast maps from different stages of the early embryo (stages 9, 10 and 11, when the entire population of neuroblasts has formed), in which about 40 molecular markers representing the expression patterns of 34 different genes are linked to individual neuroblasts. In particular, we present a detailed description of the spatiotemporal patterns of expression in the procephalic neuroectoderm and in the neuroblast layer of the gap genes empty spiracles, hunchback, hu…

animal structuresFasciclin 2EctodermBiologyNeuroblastmedicineMorphogenesisAnimalsDrosophila ProteinsMolecular BiologyGap geneIn Situ HybridizationGeneticsHomeodomain ProteinsNeuronsNeuroectodermfungiGenes HomeoboxBrainGene Expression Regulation DevelopmentalNuclear ProteinsNeuromereCell biologyDNA-Binding Proteinsmedicine.anatomical_structureDrosophila melanogasternervous systemembryonic structuresTrans-ActivatorsHomeotic geneGanglion mother cellBiomarkersDevelopmental BiologyDevelopment (Cambridge, England)
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Study of the aminopeptidase N gene family in the lepidopterans Ostrinia nubilalis (Hübner) and Bombyx mori (L.): Sequences, mapping and expression

2010

Aminopeptidases N (APNs) are a class of ectoenzymes present in lepidopteran larvae midguts, involved in the Bacillus thuringiensis (Bt) toxins mode of action. In the present work, seven aminopeptidases have been cloned from the midgut of Ostrinia nubilalis, the major Lepidopteran corn pest in the temperate climates. Six sequences were identified as APNs because of the presence of the HEXXH(X)18E and GAMEN motifs, as well as the signal peptide and the GPI-anchor sequences. The remaining sequence did not contain the two cellular targeting signals, indicating it belonged to the puromycin-sensitive aminopeptidase (PSA) family. An in silico analysis allowed us to find orthologous sequences in Bo…

animal structuresGenetic LinkageSequence analysisMolecular Sequence DataSettore BIO/05 - ZoologiaSequence alignmentBt toxin-binding proteinCD13 AntigensMothsBiochemistryAminopeptidaseOstriniaPuromycin-Sensitive AminopeptidaseQuantitative PCRMidgut APNSequence Analysis ProteinBombyx moriSequence Homology Nucleic AcidBacillus thuringiensisAnimalsAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyGenePhylogenyGeneticsbiologyLarval development expressionGene Expression ProfilingfungiComputational BiologyBombyxbiology.organism_classificationMolecular biologyIsoenzymesSettore BIO/18 - GeneticaSettore AGR/11 - Entomologia Generale E ApplicataLarvaMultigene FamilyInsect ScienceInsect ProteinsPuromycin-sensitive aminopeptidaseSequence Alignment
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Functional characterization of the sea urchin sns chromatin insulator in erythroid cells.

2005

Abstract Chromatin insulators are regulatory elements that determine domains of genetic functions. We have previously described the characterization of a 265 bp insulator element, termed sns, localized at the 3′ end of the early histone H2A gene of the sea urchin Paracentrotus lividus. This sequence contains three cis-acting elements (Box A, Box B, and Box C + T) all needed for the enhancer-blocking activity in both sea urchin and human cells. The goal of this study was to further characterize the sea urchin sns insulator in the erythroid environment. We employed colony assays in human (K562) and mouse (MEL) erythroid cell lines. We tested the capability of sns to interfere with the communi…

animal structuresGlobin enhancerChromatin insulator; Enhancer blocking; Erythroid transcription factor; Globin enhancerSp1 Transcription FactorSettore BIO/11 - Biologia MolecolareElectrophoretic Mobility Shift AssayDNA-binding proteinParacentrotus lividusCell LineMiceErythroid Cellshemic and lymphatic diseasesbiology.animalHistone H2AAnimalsHumansGATA1 Transcription FactorChromatin insulatorEnhancerMolecular BiologySea urchinTranscription factorbiologyGene Transfer TechniquesGATA1Cell BiologyHematologybiology.organism_classificationLocus Control RegionMolecular biologyChromatinChromatinCell biologyGlobinsEnhancer Elements GeneticSea UrchinsParacentrotusMolecular MedicineEnhancer blockingInsulator ElementsErythroid transcription factorOctamer Transcription Factor-1Blood cells, moleculesdiseases
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Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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