Search results for " binding"

showing 10 items of 1758 documents

CNS Macrophages Control Neurovascular Development via CD95L.

2017

The development of neurons and vessels shares striking anatomical and molecular features, and it is presumably orchestrated by an overlapping repertoire of extracellular signals. CNS macrophages have been implicated in various developmental functions, including the morphogenesis of neurons and vessels. However, whether CNS macrophages can coordinately influence neurovascular development and the identity of the signals involved therein is unclear. Here, we demonstrate that activity of the cell surface receptor CD95 regulates neuronal and vascular morphogenesis in the post-natal brain and retina. Furthermore, we identify CNS macrophages as the main source of CD95L, and macrophage-specific del…

0301 basic medicineFas Ligand ProteinAngiogenesisMorphogenesisvesselmicrogliaBiologyGeneral Biochemistry Genetics and Molecular BiologyRetina03 medical and health sciencesangiogenesisMiceCell surface receptorExtracellularmedicineHuman Umbilical Vein Endothelial CellsNeuritesAnimalsHumansfas Receptorlcsh:QH301-705.5Cell ProliferationRetinaMicrogliaKinaseMacrophagesneurovascular developmentBrainNeurovascular bundle030104 developmental biologymedicine.anatomical_structurecortexsrc-Family Kinasesnervous systemlcsh:Biology (General)ImmunologySynapsesCD95CD95LNeuroscienceCNS macrophagesProtein BindingSignal TransductionCell reports
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Skeletal Dysplasia Mutations Effect on Human Filamins’ Structure and Mechanosensing

2016

AbstractCells’ ability to sense mechanical cues in their environment is crucial for fundamental cellular processes, leading defects in mechanosensing to be linked to many diseases. The actin cross-linking protein Filamin has an important role in the conversion of mechanical forces into biochemical signals. Here, we reveal how mutations in Filamin genes known to cause Larsen syndrome and Frontometaphyseal dysplasia can affect the structure and therefore function of Filamin domains 16 and 17. Employing X-ray crystallography, the structure of these domains was first solved for the human Filamin B. The interaction seen between domains 16 and 17 is broken by shear force as revealed by steered mo…

0301 basic medicineFilaminsScienceProtein domainPeptide bindingPlasma protein bindingmacromolecular substancesBiologyMolecular Dynamics SimulationFilaminmedicine.disease_causeBioinformaticsCrystallography X-RayOsteochondrodysplasiasMechanotransduction CellularArticlecomputational biophysics03 medical and health sciences0302 clinical medicineProtein DomainsmedicineHumansLarsen syndromeForeheadMechanotransductionNMR-spektroskopiaActinMutationMultidisciplinaryBinding SitesQRSAXSmedicine.diseasecytoskeletal proteinsActinsCell biologybody regions030104 developmental biologyMutationMedicine030217 neurology & neurosurgeryröntgenkristallografiaProtein Binding
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Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases

2017

AbstractParvulins or rotamases form a distinct group within peptidyl prolyl cis-trans isomerases. Their exact mode of action as well as the role of conserved residues in the family are still not unambiguously resolved. Using backbone S2 order parameters and NOEs as restraints, we have generated dynamic structural ensembles of three distinct parvulins, SaPrsA, TbPin1 and CsPinA. The resulting ensembles are in good agreement with the experimental data but reveal important differences between the three enzymes. The largest difference can be attributed to the extent of the opening of the substrate binding cleft, along which motional mode the three molecules occupy distinct regions. Comparison w…

0301 basic medicineFine-tuningentsyymitStaphylococcus aureusparvulinsProtein ConformationParvulinenzymesTrypanosoma brucei bruceibinding cleftIsomeraseisomerasesArticleWW domain03 medical and health sciencesHumansAmino Acid SequenceMode of actionta116Multidisciplinary030102 biochemistry & molecular biologybiologyChemistryDynamics (mechanics)ta1182Peptidylprolyl IsomeraseArchaeaNIMA-Interacting Peptidylprolyl Isomerase030104 developmental biologyOrder (biology)PIN1Biophysicsbiology.proteinProtein BindingScientific Reports
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The Amino-Terminal Domain of GRK5 Inhibits Cardiac Hypertrophy through the Regulation of Calcium-Calmodulin Dependent Transcription Factors.

2018

We have recently demonstrated that the amino-terminal domain of G protein coupled receptor kinase (GRK) type 5, (GRK5-NT) inhibits NFκB activity in cardiac cells leading to a significant amelioration of LVH. Since GRK5-NT is known to bind calmodulin, this study aimed to evaluate the functional role of GRK5-NT in the regulation of calcium-calmodulin-dependent transcription factors. We found that the overexpression of GRK5-NT in cardiomyoblasts significantly reduced the activation and the nuclear translocation of NFAT and its cofactor GATA-4 in response to phenylephrine (PE). These results were confirmed in vivo in spontaneously hypertensive rats (SHR), in which intramyocardial adenovirus-med…

0301 basic medicineG-Protein-Coupled Receptor Kinase 5MalecalmodulinMutantWistarPlasma protein binding030204 cardiovascular system & hematologyCatalysilcsh:ChemistryPhenylephrine0302 clinical medicineRats Inbred SHRMyocytes Cardiaclcsh:QH301-705.5SpectroscopybiologyChemistrycardiac hypertrophyNFATComputer Science Applications1707 Computer Vision and Pattern RecognitionGeneral MedicineLeft VentricularComputer Science ApplicationsCell biologycardiac hypertrophy; transcription factors; calmodulin; GRKGRKHypertrophy Left VentricularCardiacProtein BindingInbred SHRCalmodulinCalmodulin; Cardiac hypertrophy; GRK; Transcription factors; Animals; Binding Sites; Calmodulin; Cell Line; G-Protein-Coupled Receptor Kinase 5; GATA4 Transcription Factor; Hypertrophy Left Ventricular; Male; Myocytes Cardiac; NFATC Transcription Factors; Phenylephrine; Protein Binding; Rats; Rats Inbred SHR; Rats Wistar; Catalysis; Molecular Biology; Spectroscopy; Computer Science Applications1707 Computer Vision and Pattern Recognition; Physical and Theoretical Chemistry; Organic Chemistry; Inorganic ChemistryCatalysisArticleCell LineInorganic Chemistry03 medical and health sciencesG-Protein-Coupled Receptor Kinase 5transcription factorsAnimalsPhysical and Theoretical ChemistryRats WistarTranscription factorMolecular BiologyG protein-coupled receptor kinaseMyocytesBinding SitesNFATC Transcription FactorsOrganic ChemistryHypertrophyNFATC Transcription FactorsGATA4 Transcription FactorRats030104 developmental biologylcsh:Biology (General)lcsh:QD1-999biology.proteinTranscription factorInternational journal of molecular sciences
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Sensory neuropathy in progressive motor neuronopathy(pmn)mice is associated with defects in microtubule polymerization and axonal transport

2016

Motor neuron diseases such as amyotrophic lateral sclerosis (ALS) are now recognized as multi-system disorders also involving various non-motor neuronal cell types. The precise extent and mechanistic basis of non-motor neuron damage in human ALS and ALS animal models remain however unclear. To address this, we here studied progressive motor neuronopathy (pmn) mice carrying a missense loss-of-function mutation in tubulin binding cofactor E (TBCE). These mice manifest a particularly aggressive form of motor axon dying back and display a microtubule loss, similar to that induced by human ALS-linked TUBA4A mutations. Using whole nerve confocal imaging of pmn × thy1.2-YFP16 fluorescent reporter …

0301 basic medicineGeneral NeuroscienceMotor neuronBiologymedicine.disease3. Good healthPathology and Forensic MedicineMicrotubule polymerizationTubulin binding03 medical and health sciences030104 developmental biology0302 clinical medicinemedicine.anatomical_structurenervous systemDorsal root ganglionmedicineAxoplasmic transportNeurology (clinical)NeuronAxonAmyotrophic lateral sclerosisNeuroscience030217 neurology & neurosurgeryBrain Pathology
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miR-22 suppresses DNA ligase III addiction in multiple myeloma

2019

Multiple myeloma (MM) is a hematologic malignancy characterized by high genomic instability. Here we provide evidence that hyper-activation of DNA ligase III (LIG3) is crucial for genomic instability and survival of MM cells. LIG3 mRNA expression in MM patients correlates with shorter survival and even increases with more advanced stage of disease. Knockdown of LIG3 impairs MM cells viability in vitro and in vivo, suggesting that neoplastic plasmacells are dependent on LIG3-driven repair. To investigate the mechanisms involved in LIG3 expression, we investigated the post-transcriptional regulation. We identified miR-22-3p as effective negative regulator of LIG3 in MM. Enforced expression of…

0301 basic medicineGenome instabilityCancer ResearchmiR-22 LIG3DNA repairDNA damageDNA repairApoptosisLIG3ArticleDNA Ligase ATP03 medical and health sciences0302 clinical medicinemicroRNABiomarkers TumorTumor Cells CulturedHumansPoly-ADP-Ribose Binding ProteinsCell ProliferationmiRNAchemistry.chemical_classificationRegulation of gene expressionGene knockdownDNA ligaseLeukemiamicroRNAChemistryHematologyPrognosisXenograft Model Antitumor AssaysGene Expression Regulation Neoplasticmultiple myelomaMicroRNAs030104 developmental biologyOncology030220 oncology & carcinogenesisCancer researchpharmacologyDNA DamageLeukemia
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Obstacles and opportunities in the functional analysis of extracellular vesicle RNA - an ISEV position paper

2017

The release of RNA-containing extracellular vesicles (EV) into the extracellular milieu has been demonstrated in a multitude of different in vitro cell systems and in a variety of body fluids. RNA-containing EV are in the limelight for their capacity to communicate genetically encoded messages to other cells, their suitability as candidate biomarkers for diseases, and their use as therapeutic agents. Although EV-RNA has attracted enormous interest from basic researchers, clinicians, and industry, we currently have limited knowledge on which mechanisms drive and regulate RNA incorporation into EV and on how RNA-encoded messages affect signalling processes in EV-targeted cells. Moreover, EV-R…

0301 basic medicineHistologymedia_common.quotation_subjectmRNAnon-coding RNAexosomesBiologyExosomesArticle03 medical and health sciencesQuantificationSettore BIO/10 - BiochimicaJournal ArticleMRNAexosomeOriginal Research Articleddc:610Functionlcsh:QH573-671Function (engineering)Non-coding RNAmedia_commonfunctionlcsh:CytologySortingRNAExtracellular vesicleCell BiologyExtracellular vesiclesNon-coding RNAData scienceRNA binding proteinquantificationExtracellular vesicles; RNA binding proteins; exosomes; function; mRNA; non-coding RNA; quantification; sortingCell biologyVariety (cybernetics)030104 developmental biologySignallingPosition paperRNA binding proteinsExtracellular vesicleExtracellular vesicles; Exosomes; Non-coding RNA; mRNA; Function; Sorting; RNA binding proteins; QuantificationFunctional analysis (psychology)sortingJournal of Extracellular Vesicles
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Regulatory Interaction between the Cellular Restriction Factor IFI16 and Viral pp65 (pUL83) Modulates Viral Gene Expression and IFI16 Protein Stabili…

2016

ABSTRACT A key player in the intrinsic resistance against human cytomegalovirus (HCMV) is the interferon-γ-inducible protein 16 (IFI16), which behaves as a viral DNA sensor in the first hours postinfection and as a repressor of viral gene transcription in the later stages. Previous studies on HCMV replication demonstrated that IFI16 binds to the viral protein kinase pUL97, undergoes phosphorylation, and relocalizes to the cytoplasm of infected cells. In this study, we demonstrate that the tegument protein pp65 (pUL83) recruits IFI16 to the promoter of the UL54 gene and downregulates viral replication, as shown by use of the HCMV mutant v65Stop, which lacks pp65 expression. Interestingly, at…

0301 basic medicineHuman cytomegalovirusViral proteinviruses030106 microbiologyImmunologyCytomegalovirusDNA-Directed DNA PolymeraseBiologymedicine.disease_causeVirus ReplicationMicrobiologyViral Matrix Proteins03 medical and health sciencesViral ProteinsVirologymedicineHumansNuclear proteinPromoter Regions GeneticGeneCells CulturedViral matrix proteinIFI16Protein Stabilityvirus diseasesNuclear ProteinsViral tegumentmedicine.diseasePhosphoproteinsMolecular biologyVirus-Cell Interactions030104 developmental biologyViral replicationInsect ScienceDNA ViralHost-Pathogen InteractionsProtein BindingJournal of virology
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Analysis of substrate binding in individual active sites of bifunctional human ATIC

2018

Aminoimidazolecarboxamide ribonucleotide formyl transferase (AICARFT): Inosine monophosphate cyclohydrolase (IMPCH, collectively called ATIC) is a bifunctional enzyme that catalyses the penultimate and final steps in the purine de novo biosynthesis pathway. The bifunctional protein is dimeric and each monomer contains two different active sites both of which are capable of binding nucleotide substrates, this means to a potential total of four distinct binding events might be observed. Within this work we used a combination of site-directed and truncation mutants of ATIC to independently investigate the binding at these two sites using calorimetry. A single S10W mutation is sufficient to blo…

0301 basic medicineHydroxymethyl and Formyl TransferasesModels MolecularRibonucleotideStereochemistryBiophysicsBiochemistryAnalytical ChemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMultienzyme ComplexesCatalytic DomainTransferaseHumansNucleotidePhosphofructokinase 2Bifunctional enzymesMolecular Biologychemistry.chemical_classification030102 biochemistry & molecular biologybiologyNucleotidesActive siteCooperative bindingIsothermal titration calorimetryXanthosine monophosphate030104 developmental biologyBiochemistrychemistryNucleotide DeaminasesMultiple binding sitesbiology.proteinIsothermal titration calorimetryProtein Binding
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ICTV Virus Taxonomy Profile: Pseudoviridae

2021

Pseudoviridae is a family of reverse-transcribing viruses with long terminal repeats (LTRs) belonging to the order Ortervirales. Pseudoviruses are commonly found integrated in the genomes of diverse plants, fungi and animals and are broadly known as Ty1/Copia LTR retrotransposons. Inside the cell, they form icosahedral virus particles, but unlike most other viruses, do not have an extracellular phase. This is a summary of the ICTV Report on the family Pseudoviridae, which is available at ictv.global/report/pseudoviridae.

0301 basic medicineINTRetroelementstaxonomy. Abbreviations: CPvirusesLTR030106 microbiologynucleocapsidRetrotransposonGenome ViralVirus Replicationvirus-like particlesGenomeVirusPRRTPPT03 medical and health sciencestaxonomyVirologyVLPRetrovirusesreverse transcriptaseICTV ReportcapsidRNA VirusesPBSVirus classificationbiologyAnimalfungiTerminal Repeat SequencesPseudoviridaeproteasepolypurine tractbiology.organism_classificationVirologyLong terminal repeatlong terminal repeat030104 developmental biology[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyRNA ViralintegraseRHNCIctv Virus Taxonomy Profileribonuclease HPseudoviridaeprimer binding site
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