Search results for "ligands"

showing 10 items of 721 documents

High oxidation state aqueous organometallics: synthesis and structure of a dinuclear oxo(pentamethylcyclopentadienyl)acetato complex of molybdenum(IV…

2003

International audience; The zinc reduction of Cp*2Mo2O5 in a MeOH–H2O mixture in the presence of acetic acid affords the diamagnetic dinuclear compound [Cp*MoO(O2CCH3)]2. An X-ray structural investigation reveals a novel dioxo- and diacetato-bridged structure, with a relatively strong metal–metal bond [2.5524(3) Å]. The compound exhibits a reversible one-electron oxidation process in the cyclic voltammogram. A comparison with other related structures reveals the effect of the electric charge on the mononuclear or dinuclear structural choice.Zinc reduction of Cp*2Mo2O5 in water–methanol in the presence of acetic acid affords compound Cp*2Mo2O2(O2CCH3)2, whose dinuclar tetrabridged structure …

Inorganic chemistrychemistry.chemical_elementHalf-sandwich complexesZinc010402 general chemistry01 natural sciencesInorganic ChemistryAcetic acidchemistry.chemical_compoundOxidation stateAqueous organometallic chemistryMaterials Chemistry[CHIM.CRIS]Chemical Sciences/Cristallography[CHIM.COOR]Chemical Sciences/Coordination chemistryPhysical and Theoretical ChemistryMolybdenumAqueous solution010405 organic chemistryChemistryOxo ligands0104 chemical sciencesCrystallographyMolybdenumDiamagnetismMetal–metal bondingOxidation process
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Binding analyses of Cry1Ab and Cry1Ac with membrane vesicles from Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis.

2004

The binding properties of Bacillus thuringiensis toxins to brush border membrane vesicles of Dipel-resistant and -susceptible Ostrinia nubilalis larvae were compared using ligand-toxin immunoblot analysis, surface plasmon resonance (SPR), and radiolabeled toxin binding assays. In ligand-toxin immunoblot analysis, the number of Cry1Ab or Cry1Ac toxin binding proteins and the relative toxin binding intensity were similar in vesicles from resistant and susceptible larvae. Surface plasmon resonance with immobilized activated Cry1Ab toxin indicated that there were no significant differences in binding with fluid-phase vesicles from resistant and susceptible larvae. Homologous competition assays …

InsectaTime FactorsBrush borderBacterial ToxinsImmunoblottingBiophysicsBacillus thuringiensisReceptors Cell SurfacePlasma protein bindingBiologyMothsmedicine.disease_causeLigandsBiochemistryBinding CompetitiveCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsBinding sitePest Control BiologicalMolecular BiologyBinding SitesBacillus thuringiensis ToxinsDose-Response Relationship DrugMicrovilliToxinVesiclefungiCell Membranefood and beveragesCell BiologySurface Plasmon Resonancebiology.organism_classificationMolecular biologyEndotoxinsKineticsmedicine.anatomical_structureCry1AcBiochemistryInsect ProteinsProtein BindingBiochemical and biophysical research communications
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Ligands and receptors: common theme in insect storage protein transport.

1999

The passage of macromolecules through biological membranes is an essential process for all multicellular organisms. Insects have developed a mechanism different from that known for all other eukaryotes investigated so far. This review discusses the function and evolution of this mechanism. Insect pupae do not feed during metamorphosis. Therefore they depend on material that has been accumulated during the larval life. At the end of this period, shortly before pupariation, a rise in titer of ecdysteroid hormones induces the incorporation of a large fraction of storage proteins (hexamerins) from the body fluid into the fat body cells. The transport of hexamerins across the cell-membrane is me…

Insectamedia_common.quotation_subjectMolecular Sequence DataReceptors Cell SurfaceInsectBiologyLigandschemistry.chemical_compoundStorage proteinAnimalsAmino Acid SequenceMetamorphosisReceptorEcology Evolution Behavior and Systematicsmedia_commonchemistry.chemical_classificationEcdysteroidfungiGeneral MedicineTransport proteinCell biologychemistryBiochemistryInsect HormonesFunction (biology)PupariationSignal TransductionDie Naturwissenschaften
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The Fibril-associated Collagen IX Provides a Novel Mechanism for Cell Adhesion to Cartilaginous Matrix

2004

Collagen IX is the prototype fibril-associated collagen with interruptions in triple helix. In human cartilage it covers collagen fibrils, but its putative cellular receptors have been unknown. The reverse transcription-PCR analysis of human fetal tissues suggested that based on their distribution all four collagen receptor integrins, namely alpha1beta1, alpha2beta1, alpha10beta1, and alpha11beta1, are possible receptors for collagen IX. Furthermore primary chondrocytes and chondrosarcoma cells express the four integrins simultaneously. Chondrosarcoma cells, as well as Chinese hamster ovary cells transfected to express alpha1beta1, alpha2beta1, or alpha10beta1 integrin as their only collage…

Integrin alpha1Integrin alpha2LigandsPolymerase Chain ReactionBiochemistryCollagen receptorMiceCricetinaeReceptorbiologyReverse Transcriptase Polymerase Chain ReactionChemistryChinese hamster ovary cellRecombinant ProteinsCell biologyBiochemistryCollagenIntegrin alpha ChainsProtein BindingMolecular Sequence DataIntegrinChondrosarcomaCHO CellsFibrilCollagen Type IXCell LineChondrocytesMicroscopy Electron TransmissionCell Line TumorCell AdhesionEscherichia coliAnimalsHumansImmunoprecipitationAmino Acid SequenceRNA MessengerBinding siteCell adhesionMolecular BiologyBinding SitesSequence Homology Amino AcidCell BiologyProtein Structure TertiaryRatsMicroscopy ElectronCollagen type I alpha 1CartilageMutationMutagenesis Site-Directedbiology.proteinRNAPeptidesJournal of Biological Chemistry
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MMGBSA As a Tool To Understand the Binding Affinities of Filamin–Peptide Interactions

2013

Filamins (FLN) are large dimeric proteins that cross-link actin and work as important scaffolds in human cells. FLNs consist of an N-terminal actin-binding domain followed by 24 immunoglobulin-like domains (FLN1-24). FLN domains are divided into four subgroups based on their amino acid sequences. One of these subgroups, including domains 4, 9, 12, 17, 19, 21, and 23, shares a similar ligand-binding site between the β strands C and D. Several proteins, such as integrins β2 and β7, glycoprotein Ibα (GPIbα), and migfilin, have been shown to bind to this site. Here, we computationally estimated the binding free energies of filamin A (FLNa) subunits with bound peptides using the molecular mechan…

Integrin beta ChainsFilaminsGeneral Chemical EngineeringIntegrinPeptidePlasma protein bindingMolecular Dynamics SimulationLibrary and Information SciencesBiologyLigandsFilaminta3111Protein Structure SecondaryProtein structureProtein Interaction MappingHumansFLNAProtein Interaction Domains and MotifsBinding siteta116chemistry.chemical_classificationBinding Sitesta1182General ChemistryComputer Science ApplicationsAmino acidCytoskeletal ProteinsCrystallographyPlatelet Glycoprotein GPIb-IX ComplexchemistryCD18 AntigensBiophysicsbiology.proteinThermodynamicsPeptidesCell Adhesion MoleculesAlgorithmsProtein BindingJournal of Chemical Information and Modeling
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The collagen receptor integrins have distinct ligand recognition and signaling functions

2000

Distinct collagen subtypes are recognized by specific cell surface receptors. Two of the best known collagen receptors are members of the integrin family and are named alpha1beta1 and alpha2beta1. Integrin alpha1beta1 is abundant on smooth muscle cells, whereas the alpha2beta1 integrin is the major collagen receptor on epithelial cells and platelets. Many cell types, such as fibroblasts, osteoblasts, chondrocytes, endothelial cells, and lymphocytes may concomitantly express both of the receptors. We have studied the cell biology of these integrins at two levels. First, we have analyzed their ligand binding mechanism and specificity. Second, we have studied their signaling function inside th…

IntegrinsCell typeReceptors CollagenbiologyCell adhesion moleculeIntegrinLigandsLigand (biochemistry)p38 Mitogen-Activated Protein KinasesMolecular biologyIntegrin alpha1beta1Collagen receptorCell biologybiology.proteinAnimalsHumansPlateletMitogen-Activated Protein KinasesSignal transductionReceptorMolecular BiologySignal TransductionMatrix Biology
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The collagen receptor subfamily of the integrins

2003

The four collagen receptor integrins, alpha1beta1, alpha2beta1, alpha10beta1 and alpha11beta1, form a structurally and functionally distinct subgroup when compared to other members of the integrin family. In this review, we discuss the structures of these receptors and their differences in collagen binding and signalling function.

IntegrinsReceptors CollagenSubfamilybiologyChemistryIntegrinCell BiologyPlasma protein bindingLigandsBiochemistryProtein Structure TertiaryCollagen receptorCell biologyIntegrin alpha Mbiology.proteinAnimalsHumansSignal transductionReceptorFunction (biology)Protein BindingSignal TransductionThe International Journal of Biochemistry & Cell Biology
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Fluorescent organometallic rhodium(I) and ruthenium(II) metallodrugs with 4-ethylthio-1,8-naphthalimide ligands: Antiproliferative effects, cellular …

2018

Fluorescent 4-ethylthio-1,8-naphthalimides containing rhodium(I) N-heterocyclic carbene (NHC) and ruthenium (II) NHC fragments were synthesised and evaluated for their antiproliferative effects, cellular uptake and DNA-binding activity. Both types of organometallics triggered ligand dependent efficient cytotoxic effects against tumor cells with the rhodium(I) NHC derivatives causing stronger effects than the ruthenium (II) NHC analogues. Antiproliferative effects could also be observed against several pathogenic Gram-positive bacterial strains, whereas the growth of Gram-negative bacteria was not substantially affected. Cellular uptake was confirmed by atomic absorption spectroscopy as well…

Intercalation (chemistry)Fluorescent DyeLigands01 natural sciencesAntineoplastic Agentchemistry.chemical_compoundNeoplasmsDrug DiscoveryMoietyCell DeathBacterial InfectionsGeneral MedicineIntercalating AgentsNaphthalimideAnti-Bacterial AgentsRutheniumNaphthalimidesSettore CHIM/03 - Chimica Generale E InorganicaHumanStereochemistrychemistry.chemical_elementAntineoplastic AgentsLigandCarbene010402 general chemistryG-quadruplexBacterial InfectionRutheniumRhodiumCell Line TumorAnti-Bacterial AgentOrganometallic CompoundsG-QuadruplexeHumansRhodiumBioorganometallicFluorescent DyesGroup 2 organometallic chemistryCell ProliferationPharmacologyOrganometallic CompoundBacteria010405 organic chemistryLigandOrganic ChemistryIntercalating Agent0104 chemical sciencesG-QuadruplexeschemistryNeoplasmDrug Screening Assays AntitumorCarbene
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mGluR2/3 agonist LY379268, by enhancing the production of GDNF, induces a time-related phosphorylation of RET receptor and intracellular signaling Er…

2011

In the present study we aimed to verify if the enhancement of glial cell line-derived neurotrophic factor (GDNF) production in mouse striatum following treatment with LY379268 may also induce in the nigrostriatal system a time-related activation of RET receptor and its specific intracellular signaling. For this purpose, we have investigated the effects of LY379268 treatment on RET phosphorylation at the Tyr1062 and on downstream signaling Erk1/2, Akt and PLCγ1 pathway activation. The results showed that treatment with LY379268 (3 mg/kg) induces a significant increase of GDNF levels and time-related RET and Erk1/2 phosphorylation in the striatum. These increases were detected at 24 h and 48 …

Intracellular FluidMalemedicine.medical_specialtyTime FactorsMAP Kinase Signaling SystemSubstantia nigraStriatumReceptors Metabotropic GlutamateSettore BIO/09 - FisiologiaCellular and Molecular NeuroscienceMiceErk1/2Neurotrophic factorsInternal medicinemedicineGlial cell line-derived neurotrophic factorAnimalsGlial Cell Line-Derived Neurotrophic FactorAmino AcidsPhosphorylationReceptormGluR2/3Protein kinase BPharmacologyMitogen-Activated Protein Kinase 3biologyChemistryProto-Oncogene Proteins c-retLY379268Bridged Bicyclo Compounds HeterocyclicGDNFCorpus StriatumUp-RegulationMice Inbred C57BLEndocrinologynervous systembiology.proteinPhosphorylationTrK phosphorylationRETGDNF family of ligandsNeuropharmacology
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Bright Blue Phosphorescence from Cationic Bis-Cyclometalated Iridium(III) Isocyanide Complexes

2012

We report new bis-cyclometalated cationic indium(III) complexes [((CN)-N-boolean AND)(2)Ir(CN-tert-Bu)(2)](CF3SO3) that have tert-butyl isocyanides as neutral auxiliary ligands and 2-phenylpyridine or 2-(4'-fluoropheny1)-R-pyridines (where R is 4-methoxy, 4-tert-butyl, or 5-trifluoromethyl) as (CN)-N-boolean AND ligands. The complexes are white or pale yellow solids that show irreversible reduction and oxidation processes and have a large electrochemical gap of 3.58-3.83 V. They emit blue or bluegreen phosphorescence in liquid/solid solutions from a cyclometalating-ligand-centered excited state. Their emission spectra show vibronic structure with the highest-energy luminescence peak at 440-…

Ir(Iii) ComplexesIsocyanideCationic polymerizationchemistry.chemical_elementEmitting Electrochemical-CellsExcited-State PropertiesElectroluminescent DevicesPhotochemistryAncillary LigandsInorganic Chemistrychemistry.chemical_compoundchemistryExcited stateEfficient BlueIii ComplexesMetal-ComplexesEmission spectrumIridiumPhysical and Theoretical ChemistryPhosphorescenceLuminescenceTurn-On TimesPhotophysical PropertiesSolid solutionInorganic Chemistry
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