Search results for "structural biology"

showing 10 items of 827 documents

Induction of the peroxisome proliferator activated receptor by fenofibrate in rat liver

1992

AbstractThe process of peroxisome proliferation in rodent liver by hypolipidemic compounds and related substances has recently been shown to be receptor-madiated. In the present study, we have examined the effect of oral administration of the strong peroxisome proliferator fenofibrate on the hepatic expression level of the peroxisome proliferator activated receptor (PPAR) in rats. Immunoblots of rat liver cytosols and nuclear extracs using antibodies raised against recombinant PPAR/β-galactosidase fusion proteins revealed a pronounced increase in the amount of PPAR protein in response to fenofibrate treatment. This induction could also be confirmed at the level or RNA by Northern blotting. …

Male1303 BiochemistryReceptors Cytoplasmic and Nuclear10050 Institute of Pharmacology and ToxicologyPeroxisome proliferator-activated receptorPPARMicrobodiesPolymerase Chain ReactionBiochemistryPPAR agonist1307 Cell BiologyMiceCytosol1315 Structural BiologyFenofibrateStructural Biologychemistry.chemical_classificationMice Inbred BALB CFenofibrateOligodeoxyribonucleotidesPeroxisome proliferator-activated receptor alphaFusion proteinmedicine.drugmedicine.medical_specialtyPeroxisome proliferator-activated receptor gammamRNAMolecular Sequence DataBiophysicsPeroxisome ProliferationReceptors Cell Surface610 Medicine & healthBiology1311 GeneticsInternal medicine1312 Molecular BiologyGeneticsmedicineAnimalsNorthern blotMolecular BiologyAntibodyHypolipidemic compoundCell NucleusMessenger RNABase SequenceImmune SeraCell BiologyBlotting NorthernRatsMice Inbred C57BLEndocrinologychemistry570 Life sciences; biologyTranscription Factors1304 BiophysicsFEBS Letters
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Organic matrices in metazoan calcium carbonate skeletons: composition, functions, evolution.

2016

9 pages; International audience; Calcium carbonate skeletal tissues in metazoans comprise a small quantity of occluded organic macromolecules, mostly proteins and polysaccharides that constitute the skeletal matrix. Because its functions in modulating the biomineralization process are well known, the skeletal matrix has been extensively studied, successively via classical biochemical approaches, via molecular biology and, in recent years, via transcriptomics and proteomics. The optimistic view that the deposition of calcium carbonate minerals requires a limited number of macromolecules has been challenged, in the last decade, by high-throughput approaches. Such approaches have made possible…

0301 basic medicineBiomineralizationProteomicsComputational biologyBiologyProteomicsSkeletal tissueCalcium Carbonatebiomineralization ; metazoan ; calcification ; skeleton ; skeletal matrix ; proteomicsCalcificationEvolution Molecular03 medical and health scienceschemistry.chemical_compoundMatrix (mathematics)Calcification PhysiologicMetazoanStructural Biology[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsSkeleton[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsRapid identificationSkeletal matrix030104 developmental biologyCalcium carbonatechemistryBiochemistryBiomineralization
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Recombinant NeutraLite Avidin: a non-glycosylated, acidic mutant of chicken avidin that exhibits high affinity for biotin and low non-specific bindin…

2000

AbstractA recombinant non-glycosylated and acidic form of avidin was designed and expressed in soluble form in baculovirus-infected insect cells. The mutations were based on the same principles that guided the design of the chemically and enzymatically modified avidin derivative, known as NeutraLite Avidin. In this novel recombinant avidin derivative, five out of the eight arginine residues were replaced with neutral amino acids, and two of the lysine residues were replaced by glutamic acid. In addition, the carbohydrate-bearing asparagine-17 residue was altered to an isoleucine, according to the known sequences of avidin-related genes. The resultant mutant protein, termed recombinant Neutr…

StreptavidinGlycosylationMolecular Sequence DataBiophysicsBiotinChick EmbryoNon-specific bindingBiochemistrylaw.inventionchemistry.chemical_compoundBiotinstomatognathic systemStructural BiologylawMutant proteinNon-glycosylated mutantGeneticsAnimalsHumansAmino Acid SequenceIsoelectric PointProtein Structure QuaternaryMolecular BiologyCells CulturedbiologyAvidin-biotin technologyDNACell BiologyProtein engineeringrespiratory systemAvidinRecombinant ProteinsKineticsAmino Acid SubstitutionchemistryBiochemistryBiotinylationMutationbiology.proteinRecombinant DNAThermodynamicsProtein engineeringEndopeptidase KIsoleucineBaculoviridaeProtein BindingAvidinFEBS Letters
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Evolutionary stability of topologically associating domains is associated with conserved gene regulation

2018

AbstractBackgroundThe human genome is highly organized in the three-dimensional nucleus. Chromosomes fold locally into topologically associating domains (TADs) defined by increased intra-domain chromatin contacts. TADs contribute to gene regulation by restricting chromatin interactions of regulatory sequences, such as enhancers, with their target genes. Disruption of TADs can result in altered gene expression and is associated to genetic diseases and cancers. However, it is not clear to which extent TAD regions are conserved in evolution and whether disruption of TADs by evolutionary rearrangements can alter gene expression.ResultsHere, we hypothesize that TADs represent essential functiona…

0301 basic medicinePhysiologyEvolutionGenome rearrangementsGene ExpressionGenomicsPlant ScienceComputational biologyBiologyGenomeGeneral Biochemistry Genetics and Molecular BiologyEvolution Molecular03 medical and health sciencesMiceStructural BiologyHi-CGene expressionAnimalsHumansEnhancerlcsh:QH301-705.5GeneSelectionEcology Evolution Behavior and SystematicsRegulation of gene expressionGenomeTopologically associating domainsGenome HumanCell BiologyTADChromatin Assembly and DisassemblyChromatinGene regulation030104 developmental biologylcsh:Biology (General)Gene Expression RegulationRegulatory sequenceHuman genomeGeneral Agricultural and Biological SciencesStructural variantsChromatin interactions3D genome architectureDevelopmental BiologyBiotechnologyResearch ArticleBMC Biology
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Cellular stress induces cap-independent alpha-enolase/MBP-1 translation.

2015

AbstractMyc promoter-binding protein-1 (MBP-1) is a shorter protein variant of the glycolytic enzyme alpha-enolase. Although several lines of evidence indicate that MBP-1 acts as a tumor suppressor, the cellular mechanisms and signaling pathways underlying MBP-1 expression still remain largely elusive. To dissect these pathways, we used the SkBr3 breast cancer cell line and non-tumorigenic HEK293T cells ectopically overexpressing alpha-enolase/MBP-1. Here, we demonstrate that induced cell stresses promote MBP-1 expression through the AKT/PERK/eIF2α signaling axis. Our results contribute to shedding light on the molecular mechanisms underlying MBP-1 expression in non-tumorigenic and cancer c…

Alpha-enolaseCellEukaryotic Initiation Factor-2Alternative translationBiochemistryeIF-2 KinaseBreast cancerHEK293 CellStructural BiologyProtein IsoformsbiologyMedicine (all)Translation (biology)Recombinant ProteinEndoplasmic Reticulum StressRecombinant ProteinsNeoplasm ProteinsDNA-Binding ProteinsGene Expression Regulation Neoplasticmedicine.anatomical_structureFemaleSignal transductionMyc promoter-binding protein-1Breast NeoplasmHumanSignal TransductionCell SurvivalDNA-Binding ProteinRecombinant Fusion ProteinsBiophysicsBreast NeoplasmsNeoplasm ProteinGeneticCell Line TumorEndoplasmic reticulum streGeneticsmedicineBiomarkers TumorHumansGene SilencingMolecular BiologyProtein kinase BTumor Suppressor ProteinTumor Suppressor ProteinsHEK 293 cellsProtein IsoformCell BiologySettore BIO/18 - GeneticaHEK293 CellsBiophysicGene Expression RegulationPhosphopyruvate HydrataseCancer cellbiology.proteinUnfolded protein responseCancer researchProto-Oncogene Proteins c-aktRecombinant Fusion ProteinFEBS letters
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Principal component analysis on molecular descriptors as an alternative point of view in the search of new Hsp90 inhibitors

2009

Inhibiting a protein that regulates multiple signal transduction pathways in cancer cells is an attractive goal for cancer therapy. Heat shock protein 90 (Hsp90) is one of the most promising molecular targets for such an approach. In fact, Hsp90 is a ubiquitous molecular chaperone protein that is involved in folding, activating and assembling of many key mediators of signal transduction, cellular growth, differentiation, stress-response and apoptothic pathways. With the aim to analyze which molecular descriptors have the higher importance in the binding interactions of these classes, we first performed molecular docking experiments on the 187 Hsp90 inhibitors included in the BindingDB, a pu…

Databases FactualProtein ConformationDrug Evaluation PreclinicalCancer therapyPrincipal component analysiNaphtholsBiochemistryBinding databaseMolecular descriptorsStructure-Activity RelationshipStructural BiologyMolecular descriptorHeat shock proteinComputer SimulationHSP90 Heat-Shock ProteinsPrincipal Component AnalysisBinding SitesbiologyHeat shock proteinOrganic ChemistryComputational BiologyIsoxazolesHsp90Settore CHIM/08 - Chimica FarmaceuticaComputational MathematicsBiochemistryPurinesDocking (molecular)Principal component analysisMolecular dockingbiology.proteinPyrazolesBindingDBSignal transduction
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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

2001

AbstractLipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

Models Molecular0106 biological sciencesTime FactorsProtein ConformationPlasma protein bindingLigands01 natural sciencesBiochemistryProtein structureStructural BiologyReceptorAllosteryTriticumComputingMilieux_MISCELLANEOUSPlant Proteins0303 health sciencesFungal proteinfood and beveragesCell biologyBiochemistryPlant lipid transfer proteinsAllosteric SiteProtein BindingReceptorPhytophthoraLipid transfer proteinAllosteric regulationBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding CompetitiveFungal Proteins03 medical and health sciencesTobaccoGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesDose-Response Relationship DrugAlgal ProteinsCell MembraneElicitinCell BiologyAntigens PlantModels TheoreticalLipid MetabolismElicitinCarrier Proteins010606 plant biology & botanyFEBS Letters
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Structure and function of the vacuolar Ccc1/VIT1 family of iron transporters and its regulation in fungi

2020

Iron is an essential micronutrient for most living beings since it participates as a redox active cofactor in many biological processes including cellular respiration, lipid biosynthesis, DNA replication and repair, and ribosome biogenesis and recycling. However, when present in excess, iron can participate in Fenton reactions and generate reactive oxygen species that damage cells at the level of proteins, lipids and nucleic acids. Organisms have developed different molecular strategies to protect themselves against the harmful effects of high concentrations of iron. In the case of fungi and plants, detoxification mainly occurs by importing cytosolic iron into the vacuole through the Ccc1/V…

ISC Iron-sulfur lusterCS Consistency scoreCcc1Ribosome biogenesisVacuoleReview ArticleYRE Yap response elementsBiochemistryBiotecnologia0302 clinical medicineStructural BiologyCg Candida glabrata0303 health sciencesMAFFT Multiple Alignment using Fast Fourier TransformNRAMP Natural Resistance-Associated Macrophage ProteinbiologyVIT1ChemistryMBD Metal-binding domainPlantsComputer Science ApplicationsBiochemistry030220 oncology & carcinogenesisCRD Cysteine-rich domainEg Eucalyptus grandisIron detoxificationBiotechnologyCBC CCAAT-binding core complexlcsh:BiotechnologySaccharomyces cerevisiaeVTL Vacuolar iron transporter-likeBiophysicsVIT Vacuolar iron transporterbZIP basic leucine-zipper03 medical and health sciencesFongsLipid biosynthesislcsh:TP248.13-248.65GeneticsFe IronIron transportTranscription factor030304 developmental biologyComputingMethodologies_COMPUTERGRAPHICSBLOSUM BLOcks SUbstitution MatrixTMD Transmembrane domainML Maximum-likelihoodIron regulationDNA replicationFungibiology.organism_classificationYeastYeastMetabolic pathwayH HelixHap Heme activator proteinVacuoleROS Reactive oxygen speciesFerroComputational and Structural Biotechnology Journal
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Scanning Electron Microscopy and X-Ray Microanalysis

2003

Structural Biologymedia_common.quotation_subjectGeneral Physics and AstronomyGeneral Materials ScienceCell BiologyArtHumanitiesmedia_commonX ray microanalysisMicron
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Structural insights into the GTPase domain of Escherichia coli MnmE protein

2007

The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well…

Models MolecularTRNA modificationMagnetic Resonance SpectroscopyGTP'aluminium fluoridehomology modelingMolecular Sequence DataGTPaseGuanosine triphosphateGuanosine DiphosphateBiochemistryeraGTP Phosphohydrolaseschemistry.chemical_compoundStructural BiologyEscherichia coliAmino Acid SequenceHomology modelingBinding siteGTPaseMolecular BiologyBinding SitesSequence Homology Amino AcidChemistryEscherichia coli ProteinsTrmENMRRecombinant ProteinsKineticsBiochemistryMnmEGuanosine diphosphateRap2AGTP PhosphohydrolasesGuanosine TriphosphateSequence AlignmentRasProteins: Structure, Function, and Bioinformatics
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