Search results for "DOMAINS"

showing 10 items of 269 documents

A novel rat CVB1-VP1 monoclonal antibody 3A6 detects a broad range of enteroviruses

2018

AbstractEnteroviruses (EVs) are common RNA viruses that cause diseases ranging from rash to paralytic poliomyelitis. For example, EV-A and EV-C viruses cause hand-foot and mouth disease and EV-B viruses cause encephalitis and myocarditis, which can result in severe morbidity and mortality. While new vaccines and treatments for EVs are under development, methods for studying and diagnosing EV infections are still limited and therefore new diagnostic tools are required. Our aim was to produce and characterize new antibodies that work in multiple applications and detect EVs in tissues and in vitro. Rats were immunized with Coxsackievirus B1 capsid protein VP1 and hybridomas were produced. Hybr…

Models Molecular0301 basic medicineBiolääketieteet - BiomedicineProtein Conformationmedicine.drug_classImmunoelectron microscopylcsh:MedicineEnzyme-Linked Immunosorbent AssayCoxsackievirusmedicine.disease_causeMonoclonal antibodyenterovirusesArticleEpitopeEpitopesMice03 medical and health sciencesProtein DomainsEnterovirus InfectionsmedicineantibodiesAnimalsHumanslcsh:ScienceMultidisciplinary030102 biochemistry & molecular biologybiologyPolioviruslcsh:Rvasta-aineetAntibodies Monoclonalbiology.organism_classificationAntibodies NeutralizingImmunohistochemistryVirologyEnterovirus B HumanRats3. Good healthenterovirukset030104 developmental biologyKasvibiologia mikrobiologia virologia - Plant biology microbiology virologybiology.proteinImmunohistochemistrylcsh:QCapsid ProteinsAntibodyClone (B-cell biology)Protein BindingScientific Reports
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Targeting Cavity-Creating p53 Cancer Mutations with Small-Molecule Stabilizers: the Y220X Paradigm

2020

We have previously shown that the thermolabile, cavity-creating p53 cancer mutant Y220C can be reactivated by small-molecule stabilizers. In our ongoing efforts to unearth druggable variants of the p53 mutome, we have now analyzed the effects of other cancer-associated mutations at codon 220 on the structure, stability, and dynamics of the p53 DNA-binding domain (DBD). We found that the oncogenic Y220H, Y220N, and Y220S mutations are also highly destabilizing, suggesting that they are largely unfolded under physiological conditions. A high-resolution crystal structure of the Y220S mutant DBD revealed a mutation-induced surface crevice similar to that of Y220C, whereas the corresponding pock…

Models Molecular0301 basic medicineMutantCarbazolesDruggabilityCancer therapyAntineoplastic Agents01 natural sciencesBiochemistryDNA-binding proteinStructure-Activity Relationship03 medical and health sciencesProtein DomainsHumansCancer mutationsThermolabileQD0415Protein Stability010405 organic chemistryChemistryArticlesGeneral MedicineSmall moleculeAffinities0104 chemical sciences030104 developmental biologyGene Expression RegulationMutationBiophysicsMolecular MedicineMutant ProteinsDrug Screening Assays AntitumorTumor Suppressor Protein p53CrystallizationProtein BindingQD0241ACS Chemical Biology
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Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis

2020

9 p.-5 fig.

Models Molecular0301 basic medicineProteasesBiologiaMolecular biologymedicine.medical_treatmentScienceAmino Acid MotifsBacillus thuringiensisGeneral Physics and Astronomy02 engineering and technologyGenetically modified cropsBiotecnologiaArticleProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesBacterial ProteinsProtein DomainsTetramerBacillus thuringiensisElectron microscopymedicineTrypsinlcsh:ScienceMultidisciplinaryProteasebiologyChemistryQfungifood and beveragesMidgutGeneral Chemistry021001 nanoscience & nanotechnologybiology.organism_classification030104 developmental biologyStructural biologyBiochemistrylcsh:QStructural biology0210 nano-technologyProteïnesFunction (biology)
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Metallothionein Gene Family in the Sea Urchin Paracentrotus lividus: Gene Structure, Differential Expression and Phylogenetic Analysis

2017

Metallothioneins (MT) are small and cysteine-rich proteins that bind metal ions such as zinc, copper, cadmium, and nickel. In order to shed some light on MT gene structure and evolution, we cloned seven Paracentrotus lividus MT genes, comparing them to Echinodermata and Chordata genes. Moreover, we performed a phylogenetic analysis of 32 MTs from different classes of echinoderms and 13 MTs from the most ancient chordates, highlighting the relationships between them. Since MTs have multiple roles in the cells, we performed RT-qPCR and in situ hybridization experiments to understand better MT functions in sea urchin embryos. Results showed that the expression of MTs is regulated throughout de…

Models Molecular0301 basic medicineProtein Conformationmetallothionein; multigene families; evolution; metal; echinoderms; embryonic development; gene expressionCatalysiGene OrderMetallothioneinSea urchinPhylogenySpectroscopyPhylogenetic treebiologyEchinodermMetalGene Expression Regulation DevelopmentalComputer Science Applications1707 Computer Vision and Pattern RecognitionExonsGeneral MedicineAnatomyMultigene familiemultigene familiesComputer Science ApplicationsCell biologymedicine.anatomical_structureMetalsMultigene FamilyParacentrotusEchinoderms; Embryonic development; Evolution; Gene expression; Metal; Metallothionein; Multigene families; Catalysis; Molecular Biology; Computer Science Applications1707 Computer Vision and Pattern Recognition; Spectroscopy; Physical and Theoretical Chemistry; Organic Chemistry; Inorganic ChemistryMesenchymeSettore BIO/11 - Biologia MolecolareIn situ hybridizationArticleCatalysisParacentrotus lividusInorganic Chemistry03 medical and health sciencesbiology.animalevolutionmedicineAnimalsGene familyProtein Interaction Domains and MotifsAmino Acid SequencePhysical and Theoretical ChemistryGeneMolecular BiologydevelopmentechinodermsOrganic Chemistrybiology.organism_classificationmetallothioneinAlternative Splicing030104 developmental biologyGene Expression RegulationEmbryonic developmentgene expression
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High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

2020

AbstractDuring storage in the silk gland, the N-terminal domain (NT) of spider silk proteins (spidroins) keeps the aggregation-prone repetitive region in solution at extreme concentrations. We observe that NTs from different spidroins have co-evolved with their respective repeat region, and now use an NT that is distantly related to previously used NTs, for efficient recombinant production of the amyloid-β peptide (Aβ) implicated in Alzheimer’s disease. A designed variant of NT from Nephila clavipes flagelliform spidroin, which in nature allows production and storage of β-hairpin repeat segments, gives exceptionally high yields of different human Aβ variants as a solubility tag. This tool e…

Models Molecular0301 basic medicineProtein domainBiophysicslcsh:MedicinePeptideBiosynthesis010402 general chemistryBiochemistry01 natural sciencesArticlelaw.invention03 medical and health sciencesProtein DomainslawAnimalsSpider silkAmino Acid SequenceNeurodegenerationlcsh:SciencePeptide sequencechemistry.chemical_classificationAmyloid beta-PeptidesMultidisciplinarybiologySpidroinlcsh:RNeurodegenerative diseasesNephila clavipesProteinsbiology.organism_classification0104 chemical sciences030104 developmental biologyBiochemistrychemistryYield (chemistry)Recombinant DNAlcsh:QPeptidesFibroinsScientific Reports
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Structure of the Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain.

2019

Summary TRPML2 is the least structurally characterized mammalian transient receptor potential mucolipin ion channel. The TRPML family hallmark is a large extracytosolic/lumenal domain (ELD) between transmembrane helices S1 and S2. We present crystal structures of the tetrameric human TRPML2 ELD at pH 6.5 (2.0 A) and 4.5 (2.95 A), corresponding to the pH values in recycling endosomes and lysosomes. Isothermal titration calorimetry shows Ca2+ binding to the highly acidic central pre-pore loop which is abrogated at low pH, in line with a pH-dependent channel regulation model. Small angle X-ray scattering confirms the ELD dimensions in solution. Changes in pH or Ca2+ concentration do not affect…

Models Molecular0303 health sciencesBinding SitesTRPMLEndosomeChemistrySmall-angle X-ray scatteringProtein Conformation030302 biochemistry & molecular biologyIsothermal titration calorimetryHydrogen-Ion ConcentrationCrystallography X-Ray03 medical and health sciencesTransient receptor potential channelTransmembrane domainTransient Receptor Potential ChannelsProtein DomainsStructural BiologyBiophysicsHumansCalciumMolecular BiologyProtein secondary structureIon channel030304 developmental biologyStructure (London, England : 1993)
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Determination of enrichment factors for modified RNA in MeRIP experiments

2019

In the growing field of RNA modification, precipitation techniques using antibodies play an important role. However, little is known about their specificities and protocols are missing to assess their effectiveness. Here we present a method to assess enrichment factors after MeRIP-type pulldown experiments, here exemplified with a commercial antibody against N6-methyladenosine (m6A). Testing different pulldown and elution conditions, we measure enrichment factors of 4-5 using m6A-containing mRNAs against an unmodified control of identical sequence. Both types of mRNA carry 32P labels at different nucleotides, allowing their relative quantification in a mixture after digestion to nucleotides…

Models MolecularAdenosineAbsolute quantificationMethylationProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular BiologyViral Proteins03 medical and health sciencesAdenosine TriphosphateRNA modificationEscherichia coliHumansImmunoprecipitationProtein Interaction Domains and MotifsNucleotideRNA MessengerMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMessenger RNACell-Free SystemChemistryElution030302 biochemistry & molecular biologyRNADNA-Directed RNA PolymerasesBiochemistryImmunoglobulin GIsotope LabelingChromatography Thin LayerPhosphorus RadioisotopesProtein BindingMethods
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Modulation of Structural Heterogeneity Controls Phytochrome Photoswitching

2019

Phytochromes sense red/far-red light and control many biological processes in plants, fungi, and bacteria. Although crystal structures of dark and light adapted states have been determined, the molecular mechanisms underlying photoactivation remains elusive. Here we demonstrate that the conserved tongue region of the PHY domain of a 57kDa photosensory module of Deinococcus radiodurans phytochrome, changes from a structurally heterogeneous dark state to an ordered light activated state. The results were obtained in solution by utilizing a laser-triggered activation approach detected on the atomic level with high-resolution protein NMR spectroscopy. The data suggest that photosignaling of phy…

Models MolecularLightTongue regionBiophysicsphototransduction03 medical and health sciences0302 clinical medicineProtein DomainsPHYmolekyylidynamiikkaprotein structureNMR-spektroskopiaNuclear Magnetic Resonance Biomolecular030304 developmental biologyphytochrome0303 health sciencesPhytochromebiologyChemistryProtein NMR SpectroscopyDeinococcus radioduransArticlesDarknessbiology.organism_classificationmolecular dynamicsNMRStructural heterogeneityDark stateModulationBiophysicsvalokemiaproteiinitDeinococcusPhytochrome030217 neurology & neurosurgeryBiophysical Journal
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Revisiting the cysteine-rich proteins encoded in the 3’-proximal open reading frame of the positive-sense single-stranded RNA of some monopartite fil…

2020

A reexamination of proteins with conserved cysteines and basic amino acids encoded by the 3 '-proximal gene of the positive-sense single-stranded RNA of some monopartite filamentous plant viruses has been carried out. The cysteines are involved in a putative Zn-finger domain, which, together with the basic amino acids, form part of the nuclear or nucleolar localization signals. An in-depth study of one of these proteins, p15 from grapevine B virus (GVB), has shown: (i) a three-dimensional structure with four alpha-helices predicted by two independent in silico approaches, (ii) the nucleolus as the main accumulation site by applying confocal laser microscopy to a fusion between p15 and the g…

Models MolecularProtein Conformation alpha-HelicalGrapevine virus BAgroinfiltrationEvolutionProtein ConformationProtein DomainProtein domainNicotiana benthamianaGene ExpressionBiologyEvolution MolecularOpen Reading Frames03 medical and health sciencesViral ProteinsProtein DomainsPlant CellsVirologyTobaccoGene expressionAmino Acid SequenceCloning MolecularGenePhylogeny030304 developmental biologyGenetics0303 health sciencesSequence Homology Amino Acid030306 microbiologyRNASettore AGR/12 - Patologia VegetaleGeneral Medicinebiology.organism_classificationVirologyRecombinant ProteinsPlant LeavesRNA silencingRNA ViralFlexiviridaeSequence AlignmentModel
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Synthesis and Inhibitory Studies of Phosphonic Acid Analogues of Homophenylalanine and Phenylalanine towards Alanyl Aminopeptidases.

2020

A library of novel phosphonic acid analogues of homophenylalanine and phenylalanine, containing fluorine and bromine atoms in the phenyl ring, have been synthesized. Their inhibitory properties against two important alanine aminopeptidases, of human (hAPN, CD13) and porcine (pAPN) origin, were evaluated. Enzymatic studies and comparison with literature data indicated the higher inhibitory potential of the homophenylalanine over phenylalanine derivatives towards both enzymes. Their inhibition constants were in the submicromolar range for hAPN and the micromolar range for pAPN, with 1-amino-3-(3-fluorophenyl) propylphosphonic acid (compound 15c) being one of the best low-molecular inhibitors …

Models MolecularProtein Conformation alpha-HelicalMolecular modelStereochemistryPhosphorous AcidsSwinePhenylalaninelcsh:QR1-502PhenylalanineCD13 Antigenscomputer-aided simulationsInhibitory postsynaptic potential01 natural sciencesBiochemistrylcsh:MicrobiologyArticlePhenylalanine derivativesSubstrate SpecificitySmall Molecule Libraries03 medical and health sciencesStructure-Activity RelationshipAnimalsHumansProtein Interaction Domains and MotifsEnzyme Inhibitorsphosphonic acid inhibitorsMolecular Biology030304 developmental biologyAlaninechemistry.chemical_classification0303 health sciencesInhibitory potentialBinding Sites010405 organic chemistryChemistryAminobutyratesFluorineBromine0104 chemical sciencesIsoenzymesKineticsEnzymehuman and porcine alanine aminopeptidasefluorine and bromine substitutionThermodynamicsProtein Conformation beta-StrandProtein BindingBiomolecules
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