Search results for "DOMAIN"

showing 10 items of 2485 documents

Endogenous β-neurexins on axons and within synapses show regulated dynamic behavior

2021

Summary: Neurexins are key organizer molecules that regulate synaptic function and are implicated in autism and schizophrenia. β-neurexins interact with numerous cell adhesion and receptor molecules, but their neuronal localization remains elusive. Using single-molecule tracking and high-resolution microscopy to detect neurexin1β and neurexin3β in primary hippocampal neurons from knockin mice, we demonstrate that endogenous β-neurexins are present in fewer than half of excitatory and inhibitory synapses. Moreover, we observe a large extrasynaptic pool of β-neurexins on axons and show that axonal β-neurexins diffuse with higher surface mobility than those transiently confined within synapses…

0301 basic medicineQH301-705.5Green Fluorescent ProteinsNerve Tissue ProteinsEndogenyHippocampal formationNeurotransmissionGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineProtein DomainsAnimalsPremovement neuronal activityneurotransmissionBiology (General)synaptic functionCell adhesionelectron microscopyintegumentary systemChemistryCell MembranefungiGlutamate receptorcell adhesionproteaseAxonsCell biologyMice Inbred C57BL030104 developmental biologyEctodomainProteolysisSynapsesExcitatory postsynaptic potentialsingle-particle tracking030217 neurology & neurosurgeryCell Reports
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Usherin defects lead to early-onset retinal dysfunction in zebrafish

2018

Mutations in USH2A are the most frequent cause of Usher syndrome and autosomal recessive nonsyndromic retinitis pigmentosa. To unravel the pathogenic mechanisms underlying USH2A-associated retinal degeneration and to evaluate future therapeutic strategies that could potentially halt the progression of this devastating disorder, an animal model is needed. The available Ush2a knock-out mouse model does not mimic the human phenotype, because it presents with only a mild and late-onset retinal degeneration. Using CRISPR/Cas9-technology, we introduced protein-truncating germline lesions into the zebrafish ush2a gene (ush2a(rmc1): c.2337_2342delinsAC; p.Cys780GlnfsTer32 and ush2a(b1245): c.15520_…

0301 basic medicineRetinal degenerationGenotyping TechniquesUsher syndrome2804 Cellular and Molecular NeuroscienceApoptosis030105 genetics & heredityBiologyArticleRetinaGermlineSensory disorders Donders Center for Medical Neuroscience [Radboudumc 12]Gene Knockout Techniques03 medical and health sciencesCellular and Molecular NeuroscienceUSH2 complex2809 Sensory SystemsAll institutes and research themes of the Radboud University Medical CenterRetinitis pigmentosaElectroretinographymedicineotorhinolaryngologic diseasesJournal ArticleAnimalsMicroscopy ImmunoelectronZebrafishZebrafishExtracellular Matrix ProteinsRetinal DegenerationMembrane ProteinsZebrafish ProteinsRetinal Photoreceptor Cell Outer Segmentmedicine.diseasebiology.organism_classification2731 OphthalmologySensory Systems10124 Institute of Molecular Life SciencesCell biologyDisease Models AnimalOphthalmology030104 developmental biologyGene Expression RegulationEctodomainMutation570 Life sciences; biologyXenotropic and Polytropic Retrovirus ReceptorUsher SyndromesErg
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Interaction between ROR1 and MuSK activation complex in myogenic cells

2017

The ROR family of receptor tyrosine kinases, ROR1 and ROR2, is known to play an important role during skeletal muscle regeneration. ROR1 has a critical role in regulating satellite cell (SC) proliferation during muscle regeneration, and proinflammatory cytokines such as TNF-α and IL-1β can induce expression of ROR1 in myogenic cells via NF-κB activation. While searching for ROR1-interacting proteins in myogenic cells, we identified MuSK as a ROR1-binding protein. MuSK interacts with and phosphorylates ROR1 at the cytoplasmic proline-rich domain. ROR1 also interacts with the MuSK activator Dok-7 independently of MuSK interaction. Collectively, our results identified ROR1 as a new interacting…

0301 basic medicineSatellite Cells Skeletal MuscleBiophysicsMuscle ProteinsReceptor Tyrosine Kinase-like Orphan ReceptorsBiochemistryReceptor tyrosine kinaseCell LineProinflammatory cytokineMice03 medical and health sciencesProtein DomainsStructural BiologyChlorocebus aethiopsGeneticsAnimalsHumansReceptors CholinergicProtein phosphorylationPhosphorylationMolecular BiologyCell ProliferationBinding SitesbiologyKinaseChemistryActivator (genetics)Receptor Protein-Tyrosine KinasesCell DifferentiationROR2Cell BiologyCell biologyHEK293 Cells030104 developmental biologyCOS CellsROR1biology.proteinPhosphorylationProtein BindingFEBS Letters
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On the origin of BAG(3) and its consequences for an expansion of BAG3's role in protein homeostasis

2021

The B-cell CLL 2-associated athanogene (BAG) protein family in general and BAG3, in particular, are pivotal elements of cellular protein homeostasis, with BAG3 playing a major role in macroautophagy. In particular, in the contexts of senescence and degeneration, BAG3 has exhibited an essential role often related to its capabilities to organize and remove aggregated proteins. Exciting studies in different species ranging from human, murine, zebrafish, and plant samples have delivered vital insights into BAG3s' (and other BAG proteins') functions and their regulations. However, so far no studies have addressed neither BAG3's evolution nor its phylogenetic position in the BAG family.

0301 basic medicineSenescenceProteasome Endopeptidase ComplexProtein family610 MedizinBiologyProtein HomeostasisBAG3BiochemistryEvolution MolecularWW domain03 medical and health sciences0302 clinical medicineProtein Domains610 Medical sciencesAutophagyAnimalsHumansMolecular BiologyZebrafishCellular SenescencePhylogenyAdaptor Proteins Signal TransducingAutophagyFungiCell BiologyPlantsbiology.organism_classificationCell biology030104 developmental biologyProteostasis030220 oncology & carcinogenesisProteolysisProteostasisbiology.proteinApoptosis Regulatory ProteinsSignal TransductionJournal of Cellular Biochemistry
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PCSK9-D374Y mediated LDL-R degradation can be functionally inhibited by EGF-A and truncated EGF-A peptides: An in vitro study.

2019

Abstract Background and aims Proprotein convertase subtilisin/kexin type 9 (PCSK9) binds to low density lipoprotein receptor (LDLR) through the LDLR epidermal growth factor-like repeat A (EGF-A) domain and induces receptor internalization and degradation. PCSK9 has emerged as a novel therapeutic target for hypercholesterolemia. Clinical studies with PCSK9 inhibiting antibodies have demonstrated strong LDL-c lowering effects, but other therapeutic approaches using small molecule inhibitors for targeting PCSK9 functions may offer supplementary therapeutic options. The aim of our study was to evaluate the effect of synthetic EGF-A analogs on mutated (D374Y) PCSK9-D374Y mediated LDLR degradatio…

0301 basic medicineSmall peptidesmedia_common.quotation_subject030204 cardiovascular system & hematologyDecoy strategyPCSK903 medical and health sciences0302 clinical medicineHumansInternalizationCells Culturedmedia_commonExpression vectorEpidermal Growth FactorChemistryPCSK9PCSK9 InhibitorsTransfectionProprotein convertasePCSK9 inhibitionIn vitroCell biologyEGF-A domain030104 developmental biologyLDLRReceptors LDLLDL receptorMutationKexinlipids (amino acids peptides and proteins)Proprotein Convertase 9Cardiology and Cardiovascular MedicineAtherosclerosis
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Dissecting the role of ADAM10 as a mediator of Staphylococcus aureus α-toxin action

2016

Staphylococcus aureus is a leading cause of bacterial infections in humans, including life-threatening diseases such as pneumonia and sepsis. Its small membrane-pore-forming α-toxin is considered an important virulence factor. By destroying cell–cell contacts through cleavage of cadherins, the metalloproteinase ADAM10 (a disintegrin and metalloproteinase 10) critically contributes to α-toxin-dependent pathology of experimental S. aureus infections in mice. Moreover, ADAM10 was proposed to be a receptor for α-toxin. However, it is unclear whether the catalytic activity or specific domains of ADAM10 are involved in mediating binding and/or subsequent cytotoxicity of α-toxin. Also, it is not k…

0301 basic medicineStaphylococcus aureusADAM10Bacterial Toxinsmedicine.disease_causeBiochemistryVirulence factorADAM10 ProteinHemolysin ProteinsMice03 medical and health sciencesCatalytic DomainmedicineDisintegrinAnimalsMolecular BiologyFurinCells CulturedMice KnockoutMetalloproteinasebiologyCadherinCell MembraneCell BiologyStaphylococcal InfectionsCadherinsCell biology030104 developmental biologyBiochemistryStaphylococcus aureusbiology.proteinCalciumIntracellularProtein BindingBiochemical Journal
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Targeting Bacterial Sortase A with Covalent Inhibitors: 27 New Starting Points for Structure-Based Hit-to-Lead Optimization.

2019

Because of its essential role as a bacterial virulence factor, enzyme sortase A (SrtA) has become an attractive target for the development of new antivirulence drugs against Gram-positive infections. Here we describe 27 compounds identified as covalent inhibitors of

0301 basic medicineStaphylococcus aureusMagnetic Resonance SpectroscopyAntivirulenceVirulence Factors030106 microbiologySmall Molecule Libraries03 medical and health sciencesMiceBacterial ProteinsCatalytic DomainDrug DiscoveryAnimalschemistry.chemical_classificationBinding SitesChemistryHit to leadFibroblastsAminoacyltransferasesAnti-Bacterial AgentsMolecular Docking SimulationCysteine Endopeptidases030104 developmental biologyInfectious DiseasesEnzymeBiochemistryCovalent bondSortase ABacterial virulenceNIH 3T3 CellsStructure basedACS infectious diseases
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Formyl-peptide receptor 2 governs leukocyte influx in local Staphylococcus aureus infections

2017

Leukocytes express formyl-peptide receptors (FPRs), which sense microbe-associated molecular pattern (MAMP) molecules, leading to leukocyte chemotaxis and activation. We recently demonstrated that phenol-soluble modulin (PSM) peptides from highly pathogenic Staphylococcus aureus are efficient ligands for the human FPR2. How PSM detection by FPR2 impacts on the course of S. aureus infections has remained unknown. We characterized the specificity of mouse FPR2 (mFpr2) using a receptor-transfected cell line, homeobox b8 (Hoxb8), and primary neutrophils isolated from wild-type (WT) or mFpr2−/− mice. The influx of leukocytes into the peritoneum of WT and mFpr2−/− mice was analyzed. We demonstrat…

0301 basic medicineStaphylococcus aureusNeutrophilsBacterial Toxinsmedicine.disease_causeLigandsBiochemistryCell DegranulationFormyl peptide receptor 2MicrobiologyCell Line03 medical and health sciencesMice0302 clinical medicinePeritoneumCell MovementGeneticsmedicineLeukocytesAnimalsHumansCalcium SignalingReceptors LipoxinReceptorMolecular BiologyHomeodomain ProteinsMice KnockoutInnate immune systemChemistryResearchHOXB8Staphylococcal InfectionsReceptors Formyl PeptideMice Inbred C57BLDisease Models Animal030104 developmental biologymedicine.anatomical_structureCell cultureStaphylococcus aureusGenes BacterialMutationFemaleLeukocyte chemotaxis030215 immunologyBiotechnology
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Interactions of human P-glycoprotein transport substrates and inhibitors at the drug binding domain: Functional and molecular docking analyses

2015

Rhodamine 123 (R123) transport substrate sensitizes P-glycoprotein (P-gp) to inhibition by compound 2c (cis-cis) N,N-bis(cyclohexanolamine)aryl ester isomer in a concentration-dependent manner in human MDR1-gene transfected mouse T-lymphoma L5178 cells as shown previously. By contrast, epirubicin (EPI) concentration changes left unaltered 2c IC50 values of EPI efflux. To clarify this discrepancy, defined molecular docking (DMD) analyses of 12 N,N-bis(cyclohexanolamine)aryl esters, the highly flexible aryl ester analog 4, and several P-gp substrate/non-substrate inhibitors were performed on human P-gp drug- or nucleotide-binding domains (DBD or NBD). DMD measurements yielded lowest binding e…

0301 basic medicineStereochemistryCell Culture TechniquesCancer drug resistance; Molecular docking; NN-Bis(cyclohexanolamine)aryl ester; P-glycoproteinPlasma protein bindingP-glycoproteinTransfectionBiochemistryRhodamine 123Substrate Specificity03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineCell Line TumorAnimalsRhodamine 123ATP Binding Cassette Transporter Subfamily B Member 1Binding siteP-glycoproteinEpirubicinPharmacologyBinding SitesbiologyMolecular StructureArylEstersCancer drug resistanceNCyclohexanolsMolecular Docking SimulationProtein Transport030104 developmental biologychemistryDocking (molecular)030220 oncology & carcinogenesisMolecular dockingbiology.proteinN-Bis(cyclohexanolamine)aryl esterEffluxBinding domainProtein Binding
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Towards Self-explanatory Ontology Visualization with Contextual Verbalization

2016

Ontologies are one of the core foundations of the Semantic Web. To participate in Semantic Web projects, domain experts need to be able to understand the ontologies involved. Visual notations can provide an overview of the ontology and help users to understand the connections among entities. However, the users first need to learn the visual notation before they can interpret it correctly. Controlled natural language representation would be readable right away and might be preferred in case of complex axioms, however, the structure of the ontology would remain less apparent. We propose to combine ontology visualizations with contextual ontology verbalizations of selected ontology (diagram) e…

0301 basic medicineStructure (mathematical logic)Computer sciencebusiness.industry05 social sciences050301 educationRepresentation (arts)Ontology (information science)computer.software_genreNotationlanguage.human_languageDomain (software engineering)03 medical and health sciences030104 developmental biologyControlled natural languagelanguageArtificial intelligencebusiness0503 educationcomputerSemantic WebNatural language processingAxiom
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