Search results for "Activation"

showing 10 items of 2079 documents

Identification of a novel activating mutation (Y842C) within the activation loop of FLT3 in patients with acute myeloid leukemia (AML).

2004

Fms-like tyrosine kinase 3 (FLT3) receptor mutations as internal tandem duplication (ITD) or within the kinase domain are detected in up to 35% of patients with acute myeloid leukemia (AML). N-benzoyl staurosporine (PKC412), a highly effective inhibitor of mutated FLT3 receptors, has significant antileukemic efficacy in patients with FLT3-mutated AML. Mutation screening of FLT3 exon 20 in AML patients (n = 110) revealed 2 patients with a novel mutation (Y842C) within the highly conserved activation loop of FLT3. FLT3-Y842C-transfected 32D cells showed constitutive FLT3 tyrosine phosphorylation and interleukin 3 (IL-3)-independent growth. Treatment with PKC412 led to inhibition of proliferat…

Models MolecularImmunologyBiologymedicine.disease_causeBiochemistryCell Linechemistry.chemical_compoundMicefluids and secretionshemic and lymphatic diseasesProto-Oncogene ProteinsmedicineSTAT5 Transcription FactorAnimalsHumansTyrosinePhosphotyrosineMutationCell CycleMyeloid leukemiaReceptor Protein-Tyrosine Kinaseshemic and immune systemsTyrosine phosphorylationCell BiologyHematologymedicine.diseaseMilk ProteinsProtein Structure TertiaryDNA-Binding ProteinsEnzyme ActivationLeukemiaLeukemia Myeloid AcutechemistryGene Expression Regulationfms-Like Tyrosine Kinase 3embryonic structuresFms-Like Tyrosine Kinase 3MutationCancer researchTrans-ActivatorsTyrosineSignal transductionTyrosine kinaseSignal TransductionBlood
researchProduct

A Short Caspase-3 Isoform Inhibits Chemotherapy-Induced Apoptosis by Blocking Apoptosome Assembly

2011

Alternative splicing of caspase-3 produces a short isoform caspase-3s that antagonizes caspase-3 apoptotic activity. However, the mechanism of apoptosis inhibition by caspase-3s remains unknown. Here we show that exogenous caspase-3 sensitizes MCF-7 and HBL100 breast cancers cells to chemotherapeutic treatments such as etoposide and methotrexate whereas co-transfection with caspase-3s strongly inhibits etoposide and methotrexate-induced apoptosis underlying thus the anti-apoptotic role of caspase-3s. In caspase-3 transfected cells, lamin-A and α-fodrin were cleaved when caspase-3 was activated by etoposide or methotrexate. When caspase-3s was co-transfected, this cleavage was strongly reduc…

Models MolecularImmunoprecipitationScienceBlotting WesternMolecular Sequence DataGene ExpressionApoptosisBreast NeoplasmsCaspase 3BiologyReal-Time Polymerase Chain ReactionBiochemistryRNA interferenceApoptosomesCell Line TumorMolecular Cell BiologyBreast CancermedicineHumansAmino Acid SequenceBiologyEtoposideDNA PrimersMultidisciplinaryCell DeathBase SequenceSequence Homology Amino AcidCaspase 3QRObstetrics and GynecologyTransfectionApoptosome assemblyMolecular biologyEnzymesEnzyme ActivationIsoenzymesApoptosisCancer researchMedicineApoptosomeResearch Articlemedicine.drugPLoS ONE
researchProduct

Density Functional Theory Study of the Trans-Trans-Cis (TTC)→Trans-Trans-Trans (TTT) Isomerization of a Photochromic Spiropyran Merocyanine

2008

Density Functional Theory (DFT) calculations have been performed on the TTC→TTT isomerization reaction of the open forms of the 1',3'-dihydro-8-bromo-6-nitro- 1',3',3'-trimethylspiro[2H-1-benzopyran-2,2'-(2H)indole (8-Br-6-nitro-BIPS) system. The calculations were carried out in vacuo and in methylene chloride solution at different temperatures. Results are compared with the available experimental values of free energy difference and activation energy in solution.

Models MolecularIndolesVacuumSpiropyran; photochromism; DFT calculation; solvent influence on activation energy; merocyanine.merocyaninesolvent influence on activation energyPharmaceutical ScienceDFT calculationPyrimidinonesPhotochemistryArticleAnalytical Chemistrylcsh:QD241-441Photochromismchemistry.chemical_compoundlcsh:Organic chemistryDrug DiscoveryBenzopyransMerocyaninePhysical and Theoretical ChemistryMethyleneFluorescent DyesIndole testSpiropyranMethylene ChlorideOrganic ChemistryStereoisomerismModels TheoreticalNitro CompoundsphotochromismSolutionschemistrymerocyanine.Chemistry (miscellaneous)ThermodynamicsMolecular MedicineDensity functional theorySpiropyranIsomerizationCis–trans isomerismMolecules
researchProduct

Signaling pathways of the TREM-1- and TLR4-mediated neutrophil oxidative burst.

2008

The triggering receptor expressed on myeloid cells 1 (TREM-1) is involved in the innate inflammatory response to microbial infections. Activation and expression of TREM-1 by polymorphonuclear neutrophils (PMN) occurs in concert with Toll-like receptors (TLR) such as TLR4 for bacterial lipopolysaccharide. However, it is currently unclear how this is mediated on a molecular level. Using pharmacological inhibitors and Western blot analysis we demonstrate that phosphatidyl inositide 3-kinase, phospholipase C and the mitogen-activated kinase p38MAPK are essential for the TREM-1- and TLR4-induced oxidative burst of human PMN. The activation of protein kinase B and extracellular signal-related kin…

Models MolecularLipopolysaccharideNeutrophilsBlotting WesternCell Separationp38 Mitogen-Activated Protein Kinaseschemistry.chemical_compoundPhosphatidylinositol 3-KinasesImmunology and AllergyHumansReceptors ImmunologicReceptorProtein kinase BRespiratory BurstMembrane GlycoproteinsPhospholipase CKinaseFlow CytometryTriggering Receptor Expressed on Myeloid Cells-1Respiratory burstCell biologyEnzyme ActivationToll-Like Receptor 4chemistryTLR4Signal transductionProto-Oncogene Proteins c-aktSignal TransductionJournal of innate immunity
researchProduct

Imidazolate bridged Cu(II)-Cu(II) and Cu(II)-Zn(II) complexes of a terpyridinophane azamacrocycle: a solution and solid state study.

2007

The dinuclear Cu2+ and Zn2+ as well as the mixed Cu2+-Zn2+ complexes of a 5,5''-pentaazaterpyridinophane ligand (L) are able to incorporate imidazolate (Im-) as a bridging ligand. The crystal structure of [Cu(2)L(Im)(Br)(H2O)](CF(3)SO(3))(2).3H2O (1) shows one copper coordinated by the three pyridine nitrogens of the terpyridine unit, one nitrogen of the imidazolate bridge (Im-) and one bromide anion occupying the axial position of a distorted square pyramid. The second copper atom is coordinated by the remaining imidazolate nitrogen, the three secondary nitrogens at the centre of the polyamine bridge and one water molecule that occupies the axial position. Magnetic measurements have been p…

Models MolecularMacrocyclic CompoundsMagnetic Resonance SpectroscopyPyridinesInorganic chemistrychemistry.chemical_elementCrystal structureCrystallography X-RayLigandsInorganic Chemistrychemistry.chemical_compoundMagneticsImidazolateElectrochemistryOrganometallic CompoundsImidazoleAza CompoundsMolecular StructureChemistryLigandSuperoxide DismutaseImidazolesTemperatureBridging ligandHydrogen-Ion ConcentrationCopperEnzyme ActivationSolutionsCrystallographyZincStability constants of complexesTerpyridineCopperDalton transactions (Cambridge, England : 2003)
researchProduct

The Nature of the Stimulus and of the Fumarate Binding Site of the Fumarate Sensor DcuS of Escherichia coli

2005

DcuS is a membrane-associated sensory histidine kinase of Escherichia coli specific for C(4) -dicarboxylates. The nature of the stimulus and its structural prerequisites were determined by measuring the induction of DcuS-dependent dcuB'-'lacZ gene expression. C(4)-dicarboxylates without or with substitutions at C2/C3 by hydrophilic (hydroxy, amino, or thiolate) groups stimulated gene expression in a similar way. When one carboxylate was replaced by sulfonate, methoxy, or nitro groups, only the latter (3-nitropropionate) was active. Thus, the ligand of DcuS has to carry two carboxylate or carboxylate/nitro groups 3.1-3.8 A apart from each other. The effector concentrations for half-maximal i…

Models MolecularMagnetic Resonance SpectroscopyHistidine KinaseRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeBiochemistryCitric AcidStructure-Activity Relationshipchemistry.chemical_compoundFumaratesEscherichia colimedicineDicarboxylic AcidsAmino Acid SequenceCarboxylatePhosphorylationBinding siteKinase activityTartratesMolecular BiologyEscherichia coliPeptide sequenceDicarboxylic Acid TransportersBinding SitesChemistryEscherichia coli ProteinsAutophosphorylationHistidine kinaseGene Expression Regulation BacterialCell BiologyNitro CompoundsPeptide FragmentsEnzyme ActivationLac OperonBiochemistryMutagenesis Site-DirectedPropionatesProtein KinasesSequence AlignmentBinding domainJournal of Biological Chemistry
researchProduct

Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

2004

Several mutants of the Bacillus thuringiensis Cry1Ca toxin affected with regard to specific activity towards Spodoptera exigua were studied. Alanine was used to replace single residues in loops 2 and 3 of domain II (mutant pPB19) and to replace residues 541– 544 in domain III (mutant pPB20). Additionally, a Cry1Ca mutant combining all mutations was constructed (mutant pPB21). Toxicity assays showed a marked decrease in toxicity against S. exigua for all mutants, while they retained their activity against Manduca sexta, confirming the importance of these residues in determining insect specificity. Parameters for binding to the specific receptors in BBMV (brush border membrane vesicles) of S.…

Models MolecularMutantLaboratory of Virologyaminopeptidase nmedicine.disease_causeBiochemistrybrush-border membraneToxin oligomerizationSubstrate SpecificityBacterial toxin; Manduca sexta; Mode of action; Protoxin activation; Toxin oligomerization; Toxin receptor bindingHemolysin Proteinsmanduca-sextaBacillus thuringiensisheliothis-virescensAlanine:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MicrovillibiologyPRI BioscienceBiochemistryMode of actionLarvaThermodynamicsResearch ArticleProtein BindingBacterial Toxinspink-bollwormBacillus thuringiensisSpodopteraSpodopteraBinding CompetitiveManduca sextaLaboratorium voor VirologieBacterial ProteinsExiguamedicineirreversible bindingAnimalscrystal proteinsProtoxin activationProtein Structure QuaternaryMode of actionMolecular BiologyBacillus thuringiensis ToxinsToxin receptor bindingToxininsecticidal toxinpore formationCytoplasmic VesiclesfungiUNESCO::CIENCIAS DE LA VIDA::BioquímicaBacterial toxinCell Biologybiology.organism_classificationProtein Structure TertiaryEndotoxinsManduca sextaMutationcryia delta-endotoxins
researchProduct

Single-molecule magnetic behavior in a neutral terbium(III) complex of a picolinate-based nitronyl nitroxide free radical

2011

The terdentate anionic picolinate-based nitronyl nitroxide (picNN) free radical forms neutral and robust homoleptic complexes with rare earth-metal ions. The nonacoordinated Tb3+ complex Tb(picNN)3• 6H2O is a single-molecule magnet with an activation energy barrier Δ = 22.8 ± 0.5 K and preexponential factor τ0 = (5.5 ± 1.1) × 10-9 s. It shows magnetic hysteresis below 1 K. © 2011 American Chemical Society.

Models MolecularNitroxide mediated radical polymerizationFree RadicalsMolecular Structurechemistry.chemical_elementTerbiumActivation energyPicolinic acidIron Chelating AgentsMagnetic hysteresisPhotochemistryIonInorganic ChemistryMagneticsCrystallographychemistry.chemical_compoundchemistryOrganometallic CompoundsMoleculeNitric Oxide DonorsPhysical and Theoretical ChemistryHomolepticPicolinic AcidsTerbium
researchProduct

Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron Cryomicroscopy

2009

Summary Phenoloxidases (POs) occur in all organisms and are involved in skin and hair coloring in mammals, and initiating melanization in wound healing. Mutation or overexpression of PO can cause albinism or melanoma, respectively. SDS can convert inactive PO and the oxygen carrier hemocyanin (Hc) into enzymatically active PO. Here we present single-particle cryo-EM maps at subnanometer resolution and pseudoatomic models of the 24-oligomeric Hc from scorpion Pandinus imperator in resting and SDS-activated states. Our structural analyses led to a plausible mechanism of Hc enzyme PO activation: upon SDS activation, the intrinsically flexible Hc domain I twists away from domains II and III in …

Models MolecularPROTEINSCopper proteinProtein Conformationmedicine.medical_treatmentProtein subunitArticleScorpions03 medical and health sciencesEnzyme activatorSurface-Active AgentsProtein structureStructural BiologyCatalytic DomainmedicineAnimalsBinding siteMolecular Biology030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMonophenol Monooxygenase030302 biochemistry & molecular biologyCryoelectron MicroscopyActive siteSodium Dodecyl SulfateHemocyaninEnzyme ActivationProtein SubunitsBiochemistryHemocyaninsbiology.proteinOxygen bindingStructure
researchProduct

Tips and turns of bacteriophytochrome photoactivation

2020

Phytochromes are ubiquitous photosensor proteins, which control the growth, reproduction and movement in plants, fungi and bacteria. Phytochromes switch between two photophysical states depending on the light conditions. In analogy to molecular machines, light absorption induces a series of structural changes that are transduced from the bilin chromophore, through the protein, and to the output domains. Recent progress towards understanding this structural mechanism of signal transduction has been manifold. We describe this progress with a focus on bacteriophytochromes. We describe the mechanism along three structural tiers, which are the chromophore-binding pocket, the photosensory module,…

Models MolecularProtein Conformation116 Chemical sciencesHISTIDINE KINASESSIGNAL-TRANSDUCTIONfotobiologiabacteriophytochrome photoactivation010402 general chemistry01 natural sciencesbakteeritPhytochrome B03 medical and health sciencesProtein structureBacterial ProteinsINDUCED PROTON RELEASEPHYTOCHROME-BCRYSTAL-STRUCTUREPhysical and Theoretical Chemistry030304 developmental biologyINDUCED CONFORMATIONAL-CHANGESPhysics0303 health sciencesRESONANCE RAMANMechanism (biology)AGROBACTERIUM-TUMEFACIENSPhotochemical ProcessesMolecular machine0104 chemical sciencesINFRARED FLUORESCENT PROTEINSCHROMOPHORE-BINDING DOMAINBiophysics1182 Biochemistry cell and molecular biologyvalokemiaproteiinitPhytochromeSignal TransductionPhotochemical & Photobiological Sciences
researchProduct