Search results for "binding site"

showing 10 items of 856 documents

MPP1 links the Usher protein network and the Crumbs protein complex in the retina.

2007

Contains fulltext : 53571.pdf (Publisher’s version ) (Closed access) The highly ordered distribution of neurons is an essential feature of a functional mammalian retina. Disruptions in the apico-basal polarity complexes at the outer limiting membrane (OLM) of the retina are associated with retinal patterning defects in vertebrates. We have analyzed the binding repertoire of MPP5/Pals1, a key member of the apico-basal Crumbs polarity complex, that has functionally conserved counterparts in zebrafish (nagie oko) and Drosophila (Stardust). We show that MPP5 interacts with its MAGUK family member MPP1/p55 at the OLM. Mechanistically, this interaction involves heterodimerization of both MAGUK mo…

Scaffold proteinanimal structuresGenetics and epigenetic pathways of disease [NCMLS 6]BioinformaticsPDZ domainMolecular Sequence DataMice TransgenicNerve Tissue ProteinsNeuroinformatics [DCN 3]Models BiologicalRetinaMiceTwo-Hybrid System TechniquesCell polarityPerception and Action [DCN 1]GeneticsNeurosensory disorders [UMCN 3.3]Basal bodyAnimalsHumansAmino Acid SequenceRats WistarEye ProteinsMolecular BiologyZebrafishGenetics (clinical)ActinRenal disorder [IGMD 9]GeneticsExtracellular Matrix ProteinsBinding SitesbiologyModels GeneticCell MembraneMembrane ProteinsGeneral MedicineBlood Proteinsbiology.organism_classificationEmbryo MammalianCell biologyProtein Structure TertiaryRatsGenetic defects of metabolism [UMCN 5.1]Eye disordersense organsCellular energy metabolism [UMCN 5.3]Nucleoside-Phosphate KinaseFunctional Neurogenomics [DCN 2]Neural developmentHuman Molecular Genetics
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Carbohydrate-Mediated Biomolecular Recognition and Gating of Synthetic Ion Channels

2013

Nanochannel-based biosensing devices have been proposed for selective detection of protein analyte molecules. However, the design and miniaturization of reusable channel-based biosensors is still a challenge in nanoscience and biotechnology. We present here a reusable nanofluidic biosensor based on reversible lectin-carbohydrate interactions. The nanochannels are fabricated in heavy ion tracked polymer membranes. The channel walls are functionalized with p-aminophenyl alpha-D-mannopyranoside (APMP) monolayers through carbodiimide coupling chemistry. The chemical (mannopyranoside) groups on the inner channel walls serve as binding sites and interact with specific protein molecules. The bindi…

Self assembled monolayersAnalyteCell recognitionSolid state nanoporesChemistrySelf-assembled monolayerNanotechnologyGatingSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsGeneral EnergyNanofluidic diodeSaccharide binding siteFISICA APLICADASynthetic ion channelsMiniaturizationDna analysisConcanavalin AMannose labeled enzymesAsymmetric nanoporesPhysical and Theoretical ChemistryBiosensor
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Nucleotide variation in the VP7 gene affects PCR genotyping of G9 rotaviruses identified in Italy

2003

A modified (aFT9m) and a degenerate (aFT9d) version of the rotavirus G9-specific primer (aFT9) allowed strains that were previously untypable, because of point mutations accumulating at the primer binding site, to be G typed by reverse transcription-polymerase chain reaction. The strains were collected during 2001-2002 in Italy in hospitals of the Apulia region, from children affected by severe rotavirus-associated enteritis. Using a wide selection of G9 rotaviruses detected worldwide, sequencing of the G9 untypable strains, sequence comparison, and phylogenetic analysis showed that the Italian strains have strong genetic similarity (< or =99.4%) to G9 rotaviruses identified recently in man…

SerotypeRotavirusGenotypeReassortmentMolecular Sequence DataBiologymedicine.disease_causePolymerase Chain ReactionRotavirus InfectionsVirologyRotavirusGenetic variationGenotypemedicineHumansTypingChildGenotypingAntigens ViralPhylogenyDNA PrimersGeneticsBase SequenceGenetic VariationVirologyEnteritisInfectious DiseasesItalyCapsid ProteinsPrimer binding site
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EMBER—Embedding Multiple Molecular Fingerprints for Virtual Screening

2022

In recent years, the debate in the field of applications of Deep Learning to Virtual Screening has focused on the use of neural embeddings with respect to classical descriptors in order to encode both structural and physical properties of ligands and/or targets. The attention on embeddings with the increasing use of Graph Neural Networks aimed at overcoming molecular fingerprints that are short range embeddings for atomic neighborhoods. Here, we present EMBER, a novel molecular embedding made by seven molecular fingerprints arranged as different &ldquo;spectra&rdquo; to describe the same molecule, and we prove its effectiveness by using deep convolutional architecture that assesses ligands&…

Settore ING-INF/05 - Sistemi Di Elaborazione Delle InformazioniBinding SitesMolecular StructureDeep learning Drug design Embedding Virtual screeningResearchOrganic ChemistryGeneral MedicineLigandsCatalysisComputer Science ApplicationsInorganic ChemistryCDC2 Protein KinaseDrug DiscoveryMass Screeningdeep learning; drug design; virtual screening; embeddingNeural Networks ComputerPhysical and Theoretical ChemistryProtein KinasesMolecular BiologySpectroscopy
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Specific binding of VegT mRNA localization signal to membranes in Xenopus oocytes

2021

Abstract We have studied the interaction of a VegT mRNA localization signal sequence with the membranes of the mitochondrial cloud in Xenopus oocytes, and the binding of the VegT mRNA signal sequence to the lipid raft regions of the vesicles bounded by ordered and disordered phospholipid bilayers. RNA preference for the membranes of the mitochondrial cloud was confirmed using microscopy of a fluorescence resonance energy transfer from RNA molecules to membranes. Our studies show that VegT mRNA has a higher affinity for ordered regions of lipid bilayers. This conclusion is supported by the dissociation constant measurements for RNA-liposome complex and the visualization of the FRET signal be…

Signal peptideXenopusLipid vesiclesMitochondrial cloudProtein Sorting SignalsXenopus ProteinsXenopus laevis03 medical and health sciencesMembrane MicrodomainsRafts0302 clinical medicineFluorescence Resonance Energy TransferAnimalsLipid bilayerMolecular BiologyLipid raftXenopus oocytes030304 developmental biology0303 health sciencesMessenger RNABinding SitesbiologyChemistryVegT mRNARNACell BiologyMembrane RNAbiology.organism_classificationFörster resonance energy transferLiposomesOocytesFRETBiophysicsFemaleT-Box Domain Proteins030217 neurology & neurosurgeryBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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The crystal structure of bacteriophage Qβ at 3.5 å resolution

1996

Abstract Background: The capsid protein subunits of small RNA bacteriophages form a T=3 particle upon assembly and RNA encapsidation. Dimers of the capsid protein repress translation of the replicase gene product by binding to the ribosome binding site and this interaction is believed to initiate RNA encapsidation. We have determined the crystal structure of phage Qβ with the aim of clarifying which factors are the most important for particle assembly and RNA interaction in the small phages. Results The crystal structure of bacteriophage Qβ determined at 3.5 a resolution shows that the capsid is stabilized by disulfide bonds on each side of the flexible loops that are situated around the fi…

Small RNAcrystal structureProtein ConformationvirusesMolecular Sequence DataBeta sheetMS2RNA-dependent RNA polymeraseCapsidProtein structureStructural BiologyAmino Acid SequenceBinding siteMolecular BiologyAllolevivirusBinding SitesCrystallographySequence Homology Amino AcidbiologyRNA-Binding ProteinsRNAbiology.organism_classificationProtein Structure TertiaryCrystallographyCapsidBiophysicsSequence AlignmentBacteriophage QβStructure
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Advances in the investigation of dioxouranium(VI) complexes of interest for natural fluids

2012

Abstract The interactions of dioxouranium(VI) cation with different organic and inorganic ligands of environmental and biological interest were carefully examined with the aim to draw a chemical speciation picture of this ion in natural aquatic ecosystems and in biological fluids. Since UO22+ ion shows a significant tendency to hydrolyze, particular attention was paid in considering the hydrolysis species formation both in the presence and in absence of ligands. The results reported in the literature show that formation of the hydrolytic species assumes a great importance in the complexation models for all the UO22+-ligand systems considered. In particular, the following ligands have been t…

SpeciationDioxouranium(VI) complexes; Aqueous solutions; Inorganic ligands; Organic ligands; Speciation; SequestrationOrganic ligandsInorganic Chemistrychemistry.chemical_compoundComputational chemistryMaterials ChemistryAqueous solutionDioxouranium(VI) complexesOrganic chemistryMoleculeSettore CHIM/01 - Chimica AnaliticaCarboxylatePhysical and Theoretical ChemistryBinding siteAqueous solutionsDioxouranium(VI) complexechemistry.chemical_classificationInorganic ligandsAqueous solutionLigandSequestrationInorganic ligandUranylAmino acidchemistryOrganic ligandChemical stabilityCoordination Chemistry Reviews
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Structural reorganisation in polytopic receptors revealed by kinetic studies.

2010

One of the first kinetic studies of metal ion reorganisation between the different sites of a tritopic polyaza ligand reveals well defined pathways for the movement of the metal ion.

Spectrometry Mass Electrospray IonizationBinding SitesMacrocyclic CompoundsMagnetic Resonance SpectroscopyMolecular StructureStereochemistryChemistryLigandMetals and AlloysGeneral ChemistryKinetic energyLigandsCatalysisSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsMetalCrystallographyKineticsvisual_artMaterials ChemistryCeramics and Compositesvisual_art.visual_art_mediumReceptorCopperChemical communications (Cambridge, England)
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Oxacyclododecindione, a Novel Inhibitor of IL-4 Signaling from Exserohilum rostratum

2008

In a screening program for new metabolites from fungi inhibiting the IL-4 mediated signal transduction, a novel chlorinated macrocyclic lactone, designated as oxacyclododecindione, was isolated from fermentations of the imperfect fungus Exserohilum rostratum. The structure was determined by a combination of spectroscopic techniques. Oxacyclododecindione inhibits the IL-4 induced expression of the reporter gene secreted alkaline phosphatase (SEAP) in transiently transfected HepG2 cells with IC50 values of 20-25 ng/ml (54-67.5 nM). Studies on the mode of action of the compound revealed that the inhibition of the IL-4 dependent signaling pathway is caused by blocking the binding of the activat…

Spectrometry Mass Electrospray IonizationMacrocyclic CompoundsMagnetic Resonance Spectroscopyfood.ingredientBlotting WesternGene ExpressionBiologyTransfectionStructure-Activity Relationshipchemistry.chemical_compoundfoodCell Line TumorDrug DiscoveryHumansTranscription factorSTAT6PharmacologyReporter geneTyrosine phosphorylationTransfectionMolecular biologyExserohilumDNA binding sitechemistryBiochemistryFermentationInterleukin-4Mitosporic FungiSignal transductionSTAT6 Transcription FactorSignal TransductionThe Journal of Antibiotics
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Molecular mechanism of T-cell protein tyrosine phosphatase (TCPTP) activation by mitoxantrone.

2013

T-cell protein tyrosine phosphatase (TCPTP) is a ubiquitously expressed non-receptor protein tyrosine phosphatase. It is involved in the negative regulation of many cellular signaling pathways. Thus, activation of TCPTP could have important therapeutic applications in diseases such as cancer and inflammation. We have previously shown that the α-cytoplasmic tail of integrin α1β1 directly binds and activates TCPTP. In addition, we have identified in a large-scale high-throughput screen six small molecules that activate TCPTP. These small molecule activators include mitoxantrone and spermidine. In this study, we have investigated the molecular mechanism behind agonist-induced TCPTP activation.…

SpermidineProtein tyrosine phosphataseBiochemistryAnalytical Chemistry0302 clinical medicinePhosphorylationDatabases Protein0303 health sciencesProtein Tyrosine Phosphatase Non-Receptor Type 2biologyChemistrySmall molecule3. Good healthCell biologyisothermal titration calorimetryMolecular Docking Simulationmolecular dynamics simulation030220 oncology & carcinogenesis/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingThermodynamicsHydrophobic and Hydrophilic InteractionsProtein BindingSignal TransductionCell signalingintegrinIntegrinPhosphataseStatic ElectricityBiophysicsAntineoplastic AgentsMolecular Dynamics Simulationta3111mitoxantroneIntegrin alpha1beta1Small Molecule Libraries03 medical and health sciencesSDG 3 - Good Health and Well-beingdifferential scanning fluorimetryHumansBinding siteMolecular Biology030304 developmental biologyT-cell protein tyrosine phosphataseta1182ta3122In vitroProtein Structure TertiaryKineticsCytoplasmbiology.proteinMitoxantronePeptidesBiochimica et Biophysica Acta: Proteins and Proteomics
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