Search results for "binding site"

showing 10 items of 856 documents

Selective MicroRNA-Offset RNA Expression in Human Embryonic Stem Cells

2015

Small RNA molecules, including microRNAs (miRNAs), play critical roles in regulating pluri-potency, proliferation and differentiation of embryonic stem cells. miRNA-offset RNAs (moRNAs) are similar in length to miRNAs, align to miRNA precursor (pre-miRNA) loci and are therefore believed to derive from processing of the pre-miRNA hairpin sequence. Recent next generation sequencing (NGS) studies have reported the presence of moRNAs in human neurons and cancer cells and in several tissues in mouse, including pluripotent stem cells. In order to gain additional knowledge about human moRNAs and their putative development-related expression, we applied NGS of small RNAs in human embryonic stem cel…

HUMAN DICERSmall RNAHuman Embryonic Stem CellsMolecular Sequence Datalcsh:MedicineGene ExpressionBiologyPLURIPOTENCYCell LinemicroRNAGene expressionmiRNA-offset RNAsELEMENTSHumansSmall nucleolar RNAlcsh:ScienceInduced pluripotent stem cellGene LibraryGENE-EXPRESSIONGeneticsBinding SitesMultidisciplinaryBase Sequenceta1184Gene Expression ProfilingMATURE MICRORNASMORNASlcsh:RComputational BiologyHigh-Throughput Nucleotide SequencingRNAMolecular Sequence AnnotationRNA sequencingembryonic stem cellsEmbryonic stem cellmicroRNAsCell biologyMicroRNAsMIRNASDISCOVERYMOUSE ES CELLSRNA Small Untranslatedlcsh:Q3111 BiomedicineRNA extractionFEEDER CELLSSequence AlignmentResearch ArticlePLOS ONE
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Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

2012

Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoprotein…

Halobacterium salinarumModels MolecularProtein FoldingProtein Denaturation01 natural sciencesBiotecnologiaBiochemistryBiophysics Simulationschemistry.chemical_compoundSensory RhodopsinsHalobacterium salinarum0303 health sciencesMultidisciplinarybiologyProtein StabilityQRTemperatureUltraviolet-visible spectroscopyThermal stabilityBacterial BiochemistryChemistryBiochemistryBacteriorhodopsinsRetinaldehydeMedicineProtonsResearch ArticleSteric effectsHydrogen bondingBioquímicaProtein StructureScienceRetinal bindingBiophysics010402 general chemistryMicrobiologyPhosphates03 medical and health sciencesBiology030304 developmental biologyAspartic AcidBinding SitesAdaptation OcularOrganic ChemistryOrganic SynthesisProteinsChromoproteinsRetinalBacteriorhodopsinBacteriologyBiological TransportChromophorebiology.organism_classification0104 chemical sciencesTransmembrane ProteinschemistryRetinaldehydeBiophysicsbiology.proteinMutant ProteinsPLoS ONE
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Fluorine Scan of Inhibitors of the Cysteine Protease Human Cathepsin L: Dipolar and Quadrupolar Effects in the π-Stacking of Fluorinated Phenyl Rings…

2016

The π-stacking of fluorinated benzene rings on protein backbone amide groups was investigated, using a dual approach comprising enzyme-ligand binding studies complemented by high-level quantum chemical calculations. In the experimental study, the phenyl substituent of triazine nitrile inhibitors of human cathepsin L (hCatL), which stacks onto the peptide amide bond Gly67-Gly68 at the entrance of the S3 pocket, was systematically fluorinated, and differences in inhibitory potency were measured in a fluorimetric assay. Binding affinity is influenced by lipophilicity (clog P), the dipole and quadrupole moments of the fluorinated rings, but also by additional interactions of the introduced fluo…

HalogenationNitrileStereochemistryCathepsin LStackingSubstituentchemistry.chemical_elementPeptideCysteine Proteinase InhibitorsMolecular Dynamics SimulationLigands010402 general chemistry01 natural sciencesBiochemistrychemistry.chemical_compoundAmideDrug DiscoveryHumansPeptide bondFluorometryGeneral Pharmacology Toxicology and PharmaceuticsTriazinePharmacologychemistry.chemical_classificationBinding SitesTriazines010405 organic chemistryOrganic ChemistryFluorineAmidesProtein Structure Tertiary0104 chemical sciencesKineticschemistryFluorineQuantum TheoryMolecular MedicineHydrophobic and Hydrophilic InteractionsChemMedChem
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Assessment of the Optimum Linker Tethering Site of Alternariol Haptens for Antibody Generation and Immunoassay Development

2021

Immunochemical methods for mycotoxin analysis require antigens with well-defined structures and antibodies with outstanding binding properties. Immunoreagents for the mycotoxins alternariol and/or alternariol monomethyl ether have typically been obtained with chemically uncharacterized haptens, and antigen conjugates have most likely been prepared with mixtures of functionalized molecules. For the first time, total synthesis was performed, in the present study, to obtain two haptens with opposite linker attachment locations. The functionalized synthetic haptens were purified and deeply characterized by different spectrometric methods, allowing the preparation of bioconjugates with unequivoc…

Hapten designImmunoassayLinker siteMolecular StructureHealth Toxicology and MutagenesisRImmunologic TestsMycotoxinsToxicologyArticlealternariolAlternariolLactonesalternariol; antibody; ELISA; hapten design; immunoassay; linker siteantibodyAntibody FormationMedicineELISABinding Sites Antibodyimmunoassaylinker siteHaptensAntibodyhapten design
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Spectrum of styrene-induced DNA adducts: the relationship to other biomarkers and prospects in human biomonitoring.

2002

Styrene is an important industrial chemical that has shown genotoxicity in many toxicology assays. This is believed to be related to the DNA-binding properties of styrene-7,8-oxide (SO), a major metabolite of styrene. In this review, we have summarized knowledge on various aspects of styrene genotoxicity, especially in order to understand the formation and removal of primary DNA lesions, and the usefulness of biomarkers for risk assessment. Biological significances of specific DNA adducts and their role in the cascade of genotoxic events are discussed. Links between markers of external and internal exposure are evaluated, as well as metabolic aspects leading to the formation of DNA adducts …

Health Toxicology and MutagenesisMetabolitePopulation10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiologyIn Vitro Techniquesmedicine.disease_causeRisk AssessmentStyrenechemistry.chemical_compoundDNA Adducts1311 GeneticsOccupational ExposureBiomonitoring2307 Health Toxicology and MutagenesisGeneticsmedicineAnimalsHumanseducationStyreneGeneticseducation.field_of_studyPrimary (chemistry)Binding SitesDNAchemistryBiochemistry570 Life sciences; biologyEpoxy CompoundsXenobioticGenotoxicityDNABiomarkersEnvironmental MonitoringMutagensMutation research
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A novel RNA-binding motif in influenza A virus non-structural protein 1.

1997

The solution NMR structure of the RNA-binding domain from influenza virus non-structural protein 1 exhibits a novel dimeric six-helical protein fold. Distributions of basic residues and conserved salt bridges of dimeric NS1(1-73) suggest that the face containing antiparallel helices 2 and 2′ forms a novel arginine-rich nucleic acid binding motif.

Helix bundleModels MolecularBinding SitesMagnetic Resonance SpectroscopyChemistryStructural proteinViral Nonstructural ProteinsAntiparallel (biochemistry)medicine.disease_causeVirusProtein Structure SecondaryBiochemistryStructural BiologyInfluenza A virusInfluenza A virusmedicineNucleic acidRNAStructural motifMolecular BiologySterile alpha motifDimerizationNature structural biology
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Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidiamalaca traust. Hemagglutinins

1982

The carbohydrate specificities of Ascidia malaca serum hemagglutinins were determined by hemagglutination inhibition tests. Analysis of agglutinins against rabbit and human A, B, O erythrocytes suggests that the size of the combining site corresponds to a disaccharide with a specificity for saccharides containing a D-galacto configuration (D-melibiose, D-raffinose, D-galactose, alpha-lactose, lactulose, L-arabinose). No anomeric specificity was observed with oligosaccharides. Hydroxyl groups probably involved in hydrogen-bond formation with agglutinin binding site, were identified as carbons C2, C4, C5 and C6 of D-galactose. Absorption experiments showed that two distinct agglutinins with s…

Hemagglutination Inhibition TestsErythrocytesImmunologyDisaccharideBiologyChromatography Affinitychemistry.chemical_compoundRaffinoseAgglutininSpecies SpecificityAffinity chromatographyAnimalsHumansUrochordataBinding sitePolyacrylamide gel electrophoresisBinding selectivityMelibioseBinding SitesGalactoseHemagglutination TestsHemagglutination Inhibition TestsAgglutination (biology)HemagglutininschemistryBiochemistryAntibody FormationCarbohydrate MetabolismRabbitsDevelopmental BiologyDevelopmental & Comparative Immunology
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Cyanide binding and heme cavity conformational transitions in **Drosophila melanogaster** hexacoordinate hemoglobin

2006

The reason for the presence of hemoglobin-like molecules in insects, such as Drosophila melanogaster, that live in fully aerobic environments has yet to be determined. Heme endogenous hexacoordination (where HisE7 and HisF8 axial ligands to the heme Fe atom are both provided by the protein) is a recently discovered mechanism proposed to modulate O-2 affinity in hemoglobins from different species. Previous results have shown that D. melanogaster hemoglobin 1 (product of the glob1 gene) displays heme endogenous hexacoordination in both the ferrous and ferric states. Here we present kinetic data characterizing the exogenous cyanide ligand binding process, and the three-dimensional structure (a…

HemeproteinStereochemistryProtein ConformationCyanideMolecular Sequence DataNeuroglobinNerve Tissue ProteinsHemeCrystallography X-RayLigandsBiochemistrychemistry.chemical_compoundHemoglobinsMiceSequence Analysis ProteinMelanogasterAnimalsDrosophila ProteinsHumansCRYSTAL-STRUCTUREHistidineHemeBinding SitesCyanidesbiologyCytoglobinCytoglobinHexacoordinatebiology.organism_classificationGlobinsFERRIC APLYSIAKineticsDrosophila melanogasterchemistryHUMAN NEUROGLOBINAPLYSIA-LIMACINA MYOGLOBINX-RAYHemoglobinDrosophila melanogaster
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Isolation of a hemin and hemoglobin binding outer membrane protein of Vibrio vulnificus biotype 2 (serogroup E)

2006

The eel pathogen Vibrio vulnificus biotype 2 (serogroup E) is able to use hemin (Hm) or hemoglobin (Hb) as the sole iron source for growth in vitro and in vivo. The mechanism of heme-iron acquisition in this bacterium requires a direct interaction through binding sites on the bacterial surface (constitutive outer membrane proteins). Using affinity chromatography techniques, a unique protein of around 36.5 kDa was isolated from cell envelopes of E86 strain regardless of the affinity ligand used, hemoglobin or hemin. This protein was purified from both iron-enriched and iron-restricted grown cells. These results support the hypothesis that in this pathogen Hm- and Hb-iron acquisition is media…

Hemoglobin bindingIronBlotting WesternReceptors Cell SurfaceVibrio vulnificusBiologyMicrobiologyMicrobiologyHemoglobinschemistry.chemical_compoundAffinity chromatographyGeneticsBinding siteMolecular BiologyHemeVibrioSepharosebiology.organism_classificationchemistryBiochemistryHeminHemoglobinBacterial outer membraneBacterial Outer Membrane ProteinsChromatography LiquidProtein BindingHeminFEMS Microbiology Letters
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Hepatitis B core particles as a universal display model: a structure-function basis for development

1999

AbstractBecause it exhibits a remarkable capability to accept mutational intervention and undergo correct folding and self-assembly in all viable prokaryotic and eukaryotic expression systems, hepatitis B core (HBc) protein has been favored over other proposed particulate carriers. Structurally, the unusual α-helical organization of HBc dimeric units allows introduction of foreign peptide sequences into several areas of HBc shells, including their most protruding spikes. Progress toward full resolution of the spatial structure as well as accumulation of chimeric HBc-based structures has brought closer the knowledge-based design of future vaccines, gene therapy tools and other artificial par…

Hepatitis B virusGenes ViralCryo-electron microscopyMacromolecular SubstancesProtein ConformationBiophysicsComputational biologyBiologyBiochemistryMolecular displayEpitopesProtein structureStructural BiologyGeneticsProkaryotic expressionAnimalsHumansMolecular BiologyDrug CarriersBinding SitesSpatial structureViral Core ProteinsStructure functionHepatitis B core proteinvirus diseasesCell BiologyBasis (universal algebra)Self-assemblyAntigenicityVirologyBiological EvolutionHepatitis B Core Antigensdigestive system diseasesFolding (chemistry)Protein structureElectron cryomicroscopyDimerizationHepatitis b coreFEBS Letters
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