Search results for "Timer"

showing 10 items of 119 documents

Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE

2017

17 p.-8 fig.

0301 basic medicineProtein ConformationDimerlcsh:MedicineMolecular DynamicsCrystallography X-RayPhysical ChemistryBiochemistryDEAD-box RNA HelicasesMolecular dynamicschemistry.chemical_compoundComputational ChemistryNucleophileBiochemical Simulationslcsh:ScienceMultidisciplinaryCrystallographyChemistryOrganic CompoundsPhysicsEscherichia coli ProteinsCondensed Matter Physics3. Good healthPhysical sciencesChemistryCarbon-Sulfur LyasesBiochemistryCrystal StructureResearch ArticleChemical ElementsProtein subunitChemical physicschemistry.chemical_elementOxidative phosphorylationMolecular Dynamics Simulation03 medical and health sciencesThiolsEscherichia coliSolid State PhysicsProtein Interaction Domains and MotifsChemical BondingOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesComputational BiologyDimers (Chemical physics)Hydrogen BondingCell BiologySulfurAcceptorRedox sensitiveOxidative Stress030104 developmental biologyBiophysicslcsh:QProtein MultimerizationSulfur
researchProduct

Invited commentary to: ADAMTS13 deficiency is associated with abnormal distribution of von Willebrand factor multimers in patients with COVID-19 by T…

2021

2019-20 coronavirus outbreakCoronavirus disease 2019 (COVID-19)business.industrySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Letter to the Editors-in-ChiefHematologyAbnormal distributionVirologyVon Willebrand factor multimersADAMTS13Thrombosis ResearchMedicineIn patientbusinessThrombosis Research
researchProduct

Exploration of the Activation Mechanism of the Epigenetic Regulator MLL3: A QM/MM Study

2021

The mixed lineage leukemia 3 or MLL3 is the enzyme in charge of the writing of an epigenetic mark through the methylation of lysine 4 from the N-terminal domain of histone 3 and its deregulation has been related to several cancer lines. An interesting feature of this enzyme comes from its regulation mechanism, which involves its binding to an activating dimer before it can be catalytically functional. Once the trimer is formed, the reaction mechanism proceeds through the deprotonation of the lysine followed by the methyl-transfer reaction. Here we present a detailed exploration of the activation mechanism through a QM/MM approach focusing on both steps of the reaction, aiming to provide new…

570StereochemistryLysineTrimerMolecular Dynamics Simulation01 natural sciencesBiochemistryMicrobiologyenzyme catalysisDFTArticleEpigenesis GeneticEnzyme catalysisQM/MM03 medical and health sciencesResidue (chemistry)Deprotonation0103 physical sciencesprotein regulationHumanscancerCàncerMolecular Biology030304 developmental biology0303 health sciencesBinding Sites010304 chemical physicsbiologyChemistryLysineNuclear ProteinsMethylation540QR1-502DNA-Binding ProteinsHistonebiology.proteinTyrosinemethyltransferaseProtein MultimerizationProtonsProteïnesTranscription Factors
researchProduct

A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

2014

Abstract The discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organization were also suggestive of role(s) in innate immunity. Here we describe the purification, and biochemical and functional characterization of a novel RBL (DlRBL) from sea bass (Dicentrarchus labrax) serum. The purified DlRBL had electrophoretic mobilities corresponding to 24 kDa and 100 kDa under reducing and non-reducing conditions, respectively, suggesting that in plasma the DlRBL is p…

AgglutinationGram-negative bacteriaErythrocytesRhamnoselectin; D. labraxImmunologyAmino Acid MotifsMolecular Sequence DataRhamnoseArticlechemistry.chemical_compoundPlasmaPhagocytosisLectinsEscherichia coliAnimalsAmino Acid SequenceSea bassPeptide sequencePhylogenybiologyD. labraxLectinRhamnose bindingBacterial Infectionsbiology.organism_classificationImmunity InnateProtein Structure TertiaryBiochemistrychemistrybiology.proteinMacrophages PeritoneallectinBassRabbitsProtein MultimerizationSequence motifDevelopmental BiologyHomotetramerProtein Binding
researchProduct

Agonist-induced formation of FGFR1 homodimers and signaling differ among members of the FGF family

2011

Fibroblast growth factor receptor 1 (FGFR1) is known to be activated by homodimerization in the presence of both the FGF agonist ligand and heparan sulfate glycosaminoglycan. FGFR1 homodimers in turn trigger a variety of downstream signaling cascades via autophosphorylation of tyrosine residues in the cytoplasmic domain of FGFR1. By means of Bioluminescence Energy Resonance Transfer (BRET) as a sign of FGFR1 homodimerization, we evaluated in HEK293T cells the effects of all known FGF agonist ligands on homodimer formation. A significant correlation between BRET(2) signaling and ERK1/2 phosphorylation was observed, leading to a further characterization of the binding and signaling properties…

AgonistMAPK/ERK pathwaymedicine.drug_classBiophysicsSettore BIO/11 - Biologia MolecolareBiologyLigandsFibroblast growth factorSettore BIO/09 - FisiologiaBiochemistrychemistry.chemical_compoundFluorescence Resonance Energy TransfermedicineHumansReceptor Fibroblast Growth Factor Type 1Molecular BiologyMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Fibroblast growth factor receptor 1HEK 293 cellsAutophosphorylationCell BiologyHeparan sulfateFibroblast growth factors FGFR1 Homodimerization BRET MAPKCell biologyFibroblast Growth Factorsstomatognathic diseasesHEK293 CellschemistrySettore BIO/14 - FarmacologiaPhosphorylationHeparitin SulfateProtein MultimerizationBiochemical and Biophysical Research Communications
researchProduct

Amyloid Fibrils Formation of Concanavalin A at Basic pH

2011

Mechanisms of partial unfolding and aggregation of proteins are of extreme interest in view of the fact that several human pathologies are characterized by the formation and deposition of protein-insoluble material, mainly composed of amyloid fibrils. Here we report on an experimental study on the heat-induced aggregation mechanisms, at basic pH, of concanavalin A (ConA), used as a model system. Thioflavin T (ThT) fluorescence and multiangle light scattering allowed us to detect different intertwined steps in the formation of ConA aggregates. In particular, the ThT fluorescence increase, observed in the first phase of aggregation, reveals the formation of intermolecular β-sheet structure wh…

Amyloid Fibrils Concanavalin A Light scatteringAmyloidLightMultiangle light scatteringFibrilProtein Structure SecondaryLight scatteringchemistry.chemical_compoundPhase (matter)Scattering Small AngleConcanavalin AMaterials ChemistryBenzothiazolesPhysical and Theoretical ChemistrybiologyIntermolecular forceTemperatureHydrogen-Ion ConcentrationFluorescenceSurfaces Coatings and FilmsThiazolesCrystallographySpectrometry FluorescencechemistryConcanavalin ABiophysicsbiology.proteinThioflavinProtein MultimerizationThe Journal of Physical Chemistry B
researchProduct

Cholesterol facilitates interactions between α‐synuclein oligomers and charge‐neutral membranes

2015

AbstractOligomeric species formed during α-synuclein fibrillation are suggested to be membrane-disrupting agents, and have been associated with cytotoxicity in Parkinson’s disease. The majority of studies, however, have revealed that the effect of α-synuclein oligomers is only noticeable on systems composed of anionic lipids, while the more physiologically relevant zwitterionic lipids remain intact. We present experimental evidence for significant morphological changes in zwitterionic membranes containing cholesterol, induced by α-synuclein oligomers. Depending on the lipid composition, model membranes are either unperturbed, disrupt, or undergo dramatic morphological changes and segregate …

AmyloidParkinson's diseaseFluorescent DyeBiophysicsPlasma protein bindingBiochemistryOligomerProtein Structure SecondaryMultiphoton microscopyMembrane phase separationCell membranechemistry.chemical_compoundGeneticStructural Biology2-NaphthylamineLaurdan fluorescenceGeneticsFluorescence microscopemedicineMolecular BiologyFluorescent DyesLaurateα-SynucleinMembranesChemistryMedicine (all)2-NaphthylamineCell MembraneMembraneCell BiologySettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CholesterolMembranemedicine.anatomical_structureBiophysicBiochemistryStructural biologyOligomeralpha-SynucleinParkinson’s diseaseProtein MultimerizationLaurdanLauratesProtein BindingFEBS Letters
researchProduct

Generation of TCR-Engineered T Cells and Their Use To Control the Performance of T Cell Assays

2015

Abstract The systematic assessment of the human immune system bears huge potential to guide rational development of novel immunotherapies and clinical decision making. Multiple assays to monitor the quantity, phenotype, and function of Ag-specific T cells are commonly used to unravel patients’ immune signatures in various disease settings and during therapeutic interventions. When compared with tests measuring soluble analytes, cellular immune assays have a higher variation, which is a major technical factor limiting their broad adoption in clinical immunology. The key solution may arise from continuous control of assay performance using TCR-engineered reference samples. We developed a simp…

AnalyteT-LymphocytesT cellImmunologyReceptors Antigen T-CellGene ExpressionT-Cell Antigen Receptor SpecificityComputational biologyImmunologic TestsBiologyImmune systemClinical decision makingHLA AntigensmedicineHumansImmunology and AllergyT-cell receptorLimitingmedicine.anatomical_structureImmunologyImmunotherapyProtein MultimerizationSources of errorGenetic EngineeringPeptidesFunction (biology)The Journal of Immunology
researchProduct

Allorestricted T lymphocytes with a high avidity T-cell receptor towards NY-ESO-1 have potent anti-tumor activity.

2009

The cancer-testis antigen NY-ESO-1 has been targeted as a tumor-associated antigen by immunotherapeutical strategies, such as cancer vaccines. The prerequisite for a T-cell-based therapy is the induction of T cells capable of recognizing the NY-ESO-1-expressing tumor cells. In this study, we generated human T lymphocytes directed against the immunodominant NY-ESO-1(157-165) epitope known to be naturally presented with HLA-A*0201. We succeeded to isolate autorestricted and allorestricted T lymphocytes with low, intermediate or high avidity TCRs against the NY-ESO-1 peptide. The avidity of the established CTL populations correlated with their capacity of lysing HLA-A2-positive, NY-ESO-1-expre…

Cancer ResearchAdoptive cell transferReceptors Antigen T-Cellchemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayStreptamerBiologyEpitopeAntigenAntigens NeoplasmHLA-A2 AntigenCytotoxic T cellHumansAvidityAntigen PresentationHLA-A AntigensT-cell receptorAntibody-Dependent Cell CytotoxicityMembrane ProteinsT lymphocyteCytotoxicity Tests ImmunologicFlow CytometryPeptide FragmentsNeoplasm ProteinsGenes T-Cell ReceptorOncologyImmunologyProtein MultimerizationT-Lymphocytes CytotoxicInternational journal of cancer
researchProduct

Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane

2021

The spatial distribution of proteins in cell membranes is crucial for signal transduction, cell communication and membrane trafficking. Members of the Tetraspanin family organize functional protein clusters within the plasma membrane into so-called Tetraspanin-enriched microdomains (TEMs). Direct interactions between Tetraspanins are believed to be important for this organization. However, studies thus far have utilized mainly co-immunoprecipitation methods that cannot distinguish between direct and indirect, through common partners, interactions. Here we study Tetraspanin 8 homointeractions in living cells via quantitative fluorescence microscopy. We demonstrate that Tetraspanin 8 exists i…

Cell signalingTetraspaninsLipoylationDimerTransfectionBiochemistryArticleProtein–protein interactionchemistry.chemical_compoundMembrane MicrodomainsTetraspaninFluorescence Resonance Energy TransferHumansMolecular BiologyChemistryCell BiologyDissociation constantHEK293 CellsMembraneMicroscopy FluorescenceMembrane proteinembryonic structuresBiophysicsThermodynamicsProtein MultimerizationSignal transductionSignal TransductionBiochemical Journal
researchProduct