Search results for "Protein Domain"

showing 10 items of 132 documents

The skeleton of the staghorn coral Acropora millepora: molecular and structural characterization.

2014

15 pages; International audience; The scleractinian coral Acropora millepora is one of the most studied species from the Great Barrier Reef. This species has been used to understand evolutionary, immune and developmental processes in cnidarians. It has also been subject of several ecological studies in order to elucidate reef responses to environmental changes such as temperature rise and ocean acidification (OA). In these contexts, several nucleic acid resources were made available. When combined to a recent proteomic analysis of the coral skeletal organic matrix (SOM), they enabled the identification of several skeletal matrix proteins, making A. millepora into an emerging model for biomi…

ProteomicsBiomineralizationPhysiologyCoralCell Membraneslcsh:MedicineSpectrum Analysis RamanBiochemistryAcropora milleporaMaterials PhysicsSpectroscopy Fourier Transform Infraredcristallcsh:ScienceMicrostructurecorailAcetic AcidAminationExtracellular Matrix ProteinsMineralsMultidisciplinarybiologyEcologyMonosaccharidesMineralogyAnthozoaBiochemistryprotéineCoralsPhysical SciencesCellular Structures and OrganellesCrystallizationcalciteResearch ArticleMaterials ScienceProtein domainmatrice extracellulaireMarine BiologyBone and BonesCalcium CarbonateAnthozoamonosaccharideAnimals14. Life underwater[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsIntegrin bindingStaghorn corallcsh:RBiology and Life SciencesProteinsMembrane ProteinsCell Biology[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialsbiology.organism_classificationTransmembrane ProteinsSolubilityEarth Scienceslcsh:QPhysiological ProcessesGelsFunction (biology)Biomineralization
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Zebrafish as a Model to Evaluate a CRISPR/Cas9-Based Exon Excision Approach as a Future Treatment Option for EYS-Associated Retinitis Pigmentosa

2021

Retinitis pigmentosa (RP) is an inherited retinal disease (IRD) with an overall prevalence of 1 in 4000 individuals. Mutations in EYS (Eyes shut homolog) are among the most frequent causes of non-syndromic autosomal recessively inherited RP and act via a loss-of-function mechanism. In light of the recent successes for other IRDs, we investigated the therapeutic potential of exon skipping for EYS-associated RP. CRISPR/Cas9 was employed to generate zebrafish from which the region encompassing the orthologous exons 37-41 of human EYS (eys exons 40-44) was excised from the genome. The excision of these exons was predicted to maintain the open reading frame and to result in the removal of exactl…

QH301-705.5CatalysisSensory disorders Donders Center for Medical Neuroscience [Radboudumc 12]ArticleInorganic ChemistryExonAll institutes and research themes of the Radboud University Medical CenterEYSProtein Domainsretinitis pigmentosaRetinitis pigmentosamedicineCRISPRCoding regionAnimals<i>EYS</i>Biology (General)Physical and Theoretical ChemistryOuter nuclear layerEye ProteinsQD1-999Molecular BiologyZebrafishCRISPR/Cas9SpectroscopyGeneticsexon skipping therapybiologyOrganic ChemistryphotoreceptorsGeneral MedicineExonsGenetic TherapyZebrafish Proteinsmedicine.diseasebiology.organism_classificationzebrafishExon skippingComputer Science ApplicationsChemistryOpen reading frameDisease Models Animalmedicine.anatomical_structurePhenotypeCRISPR-Cas Systemsantisense oligonucleotidesInternational Journal of Molecular Sciences
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A Comparative Study on Nickel Binding to Hpn-like Polypeptides from Two Helicobacter pylori Strains

2021

Combined potentiometric titration and isothermal titration calorimetry (ITC) methods were used to study the interactions of nickel(II) ions with the N-terminal fragments and histidine-rich fragments of Hpn-like protein from two Helicobacter pylori strains (11637 and 26695). The ITC measurements were performed at various temperatures and buffers in order to extract proton-independent reaction enthalpies of nickel binding to each of the studied protein fragments. We bring up the problem of ITC results of nickel binding to the Hpn-like protein being not always compatible with those from potentiometry and MS regarding the stoichiometry and affinity. The roles of the ATCUN motif and multiple His…

QH301-705.5Glutaminenickel bindingCalorimetry<i>H. pylori</i>glutamine-richArticleCatalysisInorganic ChemistryBacterial ProteinsProtein DomainsNickelHistidinenickel binding; <i>H. pylori</i>; Hpn-like; histidine-rich; glutamine-rich; ATCUN motifAmino Acid SequenceBiology (General)Physical and Theoretical ChemistryQD1-999Molecular BiologySpectroscopyHelicobacter pyloriHpn-likeOrganic ChemistryGeneral Medicinehistidine-richATCUN motifComputer Science ApplicationsChemistryPotentiometryPeptidesH. pyloriInternational Journal of Molecular Sciences
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Large-scale analysis of SARS-CoV-2 spike-glycoprotein mutants demonstrates the need for continuous screening of virus isolates

2021

Due to the widespread of the COVID-19 pandemic, the SARS-CoV-2 genome is evolving in diverse human populations. Several studies already reported different strains and an increase in the mutation rate. Particularly, mutations in SARS-CoV-2 spike-glycoprotein are of great interest as it mediates infection in human and recently approved mRNA vaccines are designed to induce immune responses against it. We analyzed 1,036,030 SARS-CoV-2 genome assemblies and 30,806 NGS datasets from GISAID and European Nucleotide Archive (ENA) focusing on non-synonymous mutations in the spike protein. Only around 2.5% of the samples contained the wild-type spike protein with no variation from the reference. Among…

RNA virusesMutation rateCoronavirusesEpidemiologyMolecular biologyT-LymphocytesMutantGene Identification and Analysismedicine.disease_causeGenomeWhite Blood CellsDatabase and Informatics MethodsSequencing techniquesMutation RateAnimal CellsDNA sequencingPathology and laboratory medicineGeneticsMutationMultidisciplinaryT CellsMicrobial MutationQRHigh-Throughput Nucleotide SequencingGenomicsMedical microbiologyVirusesSpike Glycoprotein CoronavirusMedicineSARS CoV 2PathogensCellular TypesTranscriptome AnalysisSequence AnalysisResearch ArticleNext-Generation SequencingSARS coronavirusBioinformaticsImmune CellsScienceImmunologyProtein domainSequence alignmentGenomicsGenome ViralBiologyMicrobiologyAntibodiesDNA sequencingProtein DomainsGeneticsmedicineHumansMutation DetectionPandemicsMedicine and health sciencesBlood CellsBiology and life sciencesSARS-CoV-2OrganismsViral pathogensComputational BiologyCOVID-19Cell BiologyGenome AnalysisMicrobial pathogensResearch and analysis methodsMolecular biology techniquesMutationSequence AlignmentPLOS ONE
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The Proteoglycan NG2 Is Complexed with α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors by the PDZ Glutamate Receptor Interactio…

2003

The proteoglycan NG2 is expressed by immature glial cells in the developing and adult central nervous system. Using the COOH-terminal region of NG2 as bait in a yeast two-hybrid screen, we identified the glutamate receptor interaction protein GRIP1, a multi-PDZ domain protein, as an interacting partner. NG2 exhibits a PDZ binding motif at the extreme COOH terminus which binds to the seventh PDZ domain of GRIP1. In addition to the published expression in neurons, GRIP1 is expressed by immature glial cells. GRIP1 is known to bind to the GluRB subunit of the AMPA glutamate receptor expressed by subpopulations of neurons and immature glial cells. In cultures of primary oligodendrocytes, cells c…

Receptor complexbiologyProtein subunitPDZ domainProtein domainGlutamate receptorCell BiologyAMPA receptorTransfectionBiochemistryMolecular biologynervous systemProteoglycanbiology.proteinMolecular BiologyJournal of Biological Chemistry
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PlaToLoCo: the first web meta-server for visualization and annotation of low complexity regions in proteins

2020

Abstract Low complexity regions (LCRs) in protein sequences are characterized by a less diverse amino acid composition compared to typically observed sequence diversity. Recent studies have shown that LCRs may co-occur with intrinsically disordered regions, are highly conserved in many organisms, and often play important roles in protein functions and in diseases. In previous decades, several methods have been developed to identify regions with LCRs or amino acid bias, but most of them as stand-alone applications and currently there is no web-based tool which allows users to explore LCRs in protein sequences with additional functional annotations. We aim to fill this gap by providing PlaToL…

Sequence analysisAcademicSubjects/SCI00010Protein domainComputational biologyBiologyDomain (software engineering)Computer graphics03 medical and health sciencesAnnotationProtein DomainsSequence Analysis ProteinGeneticsComputer GraphicsHumansAmino Acids030304 developmental biology0303 health sciencesIntersection (set theory)030302 biochemistry & molecular biologyMembrane ProteinsProteinsMolecular Sequence AnnotationVisualizationMolecular Sequence AnnotationWeb Server IssueSoftwareNucleic Acids Research
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Intrinsically disordered protein PID-2 modulates Z granules and is required for heritable piRNA-induced silencing in the Caenorhabditis elegans embryo

2020

Abstract In Caenorhabditis elegans, the piRNA (21U RNA) pathway is required to establish proper gene regulation and an immortal germline. To achieve this, PRG‐1‐bound 21U RNAs trigger silencing mechanisms mediated by RNA‐dependent RNA polymerase (RdRP)‐synthetized 22G RNAs. This silencing can become PRG‐1‐independent and heritable over many generations, a state termed RNA‐induced epigenetic gene silencing (RNAe). How and when RNAe is established, and how it is maintained, is not known. We show that maternally provided 21U RNAs can be sufficient for triggering RNAe in embryos. Additionally, we identify PID‐2, a protein containing intrinsically disordered regions (IDRs), as a factor required …

Small RNAPiwi-interacting RNApiRNABiologyGeneral Biochemistry Genetics and Molecular BiologyArticleEpigenesis Genetic570 Life sciences03 medical and health scienceschemistry.chemical_compound0302 clinical medicineProtein DomainsRNA polymeraseGene silencingAnimalsEpigeneticsGene SilencingRNA Small InterferingPID‐5Caenorhabditis elegansCaenorhabditis elegans ProteinsMolecular BiologyPID‐4Caenorhabditis elegans030304 developmental biologyPID‐2Regulation of gene expression0303 health sciencesGeneral Immunology and MicrobiologyGeneral NeuroscienceRNAGene Expression Regulation DevelopmentalArticlesbiology.organism_classificationRNA BiologyCell biologyIntrinsically Disordered ProteinschemistryArgonaute ProteinsZ granuleDevelopment & Differentiation030217 neurology & neurosurgeryProtein Binding570 Biowissenschaften
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Assessment of the probabilities for evolutionary structural changes in protein folds.

2007

Abstract Motivation: The evolution of protein sequences can be described by a stepwise process, where each step involves changes of a few amino acids. In a similar manner, the evolution of protein folds can be at least partially described by an analogous process, where each step involves comparatively simple changes affecting few secondary structure elements. A number of such evolution steps, justified by biologically confirmed examples, have previously been proposed by other researchers. However, unlike the situation with sequences, as far as we know there have been no attempts to estimate the comparative probabilities for different kinds of such structural changes. Results: We have tried …

Statistics and ProbabilityModels MolecularProtein FoldingProtein domainStructural alignmentBiologyBiochemistrySet (abstract data type)Evolution MolecularProtein structureSimilarity (network science)Sequence Analysis ProteinComputer SimulationMolecular BiologyProtein secondary structureConserved SequenceSequenceModels GeneticSequence Homology Amino AcidProteinsStructural Classification of Proteins databaseComputer Science ApplicationsComputational MathematicsComputational Theory and MathematicsModels ChemicalData Interpretation Statisticalsense organsAlgorithmSequence AlignmentBioinformatics (Oxford, England)
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Specific recognition and formation of two- dimensional streptavidin domains in monolayers: applications to molecular devices

1989

Abstract By virtue of the high-affinity specific interaction between the vitamin, biotin, and the protein, streptavidin, monolayers of synthetic lipids with biotin headgroups can tightly bind streptavidin at the lipid-water interface. Through this specific recognition fluorescently-labelled streptavidin spontaneously organizes in the plane of the interface to form large protein domains, directly visible in situ by fluorescence microscopy and exhibiting optical anisotropy. Further structural characterization has shown that these domains are two-dimensional protein crystals. Correlation with the known three-dimensional crystal structure of streptavidin indicates that two of streptavidin's fou…

StreptavidinBiotin bindingProtein domaintechnology industry and agricultureMetals and AlloysSurfaces and InterfacesSurfaces Coatings and FilmsElectronic Optical and Magnetic Materialschemistry.chemical_compoundCrystallographyBiotinchemistryBiotinylationMonolayerMaterials ChemistryFluorescence microscopeProtein crystallizationThin Solid Films
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Interaction between biotin lipids and streptavidin in monolayers: formation of oriented two-dimensional protein domains induced by surface recognitio…

1989

Highly specific ligand-receptor interactions generally characterize surface recognition reactions. Such processes can be simulated by streptavidin-biotin-specific binding. Biotin lipids have thus been synthesized, and their interaction with streptavidin (or avidin) at the air-water interface was directly shown by measurement of surface pressure isotherms and fluorescence microscopy. These proteins interact with the biotin lipid monolayer via specific binding or nonspecific adsorption. Both phenomena were clearly distinguished by use of the inactivated form of streptavidin. The binding of fluorescein-labeled streptavidin to monolayers was also directly observed by fluorescence microscopy. Th…

StreptavidinChemical PhenomenaSurface PropertiesProtein domainBiotinBiochemistrychemistry.chemical_compoundBiotinBacterial ProteinsMonolayerFluorescence microscopebiologyChemistryChemistry PhysicalPhosphatidylethanolaminestechnology industry and agricultureMembranes ArtificialHydrogen-Ion ConcentrationAvidinFluorescenceLipidsSpectrometry FluorescenceSolubilityBiotinylationbiology.proteinBiophysicsSpectrophotometry UltravioletStreptavidinAvidinBiochemistry
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