Search results for "Multiprotein Complexe"

showing 10 items of 37 documents

Dense Bodies of a gH/gL/UL128/UL130/UL131 Pentamer-Repaired Towne Strain of Human Cytomegalovirus Induce an Enhanced Neutralizing Antibody Response

2019

The development of a vaccine against human cytomegalovirus infection (HCMV) is a high-priority medical goal. The viral pentameric protein complex consisting of glycoprotein H (gH)/gL/UL128-131A (PC) is considered to be an important vaccine component. Its relevance to the induction of a protective antibody response is, however, still a matter of debate. We addressed this issue by using subviral dense bodies (DBs) of HCMV. DBs are exceptionally immunogenic. Laboratory HCMV strain DBs harbor important neutralizing antibody targets, like the glycoproteins B, H, L, M, and N, but they are devoid of the PC. To be able to directly compare the impact of the PC on the levels of neutralizing antibody …

MaleHuman cytomegalovirusForeskinImmunologyCongenital cytomegalovirus infectionCytomegalovirusMutagenesis (molecular biology technique)MicrobiologyVirusCytomegalovirus VaccinesMiceViral Envelope ProteinsAntigenVirologyVaccines and Antiviral AgentsHuman Umbilical Vein Endothelial CellsmedicineAnimalsHumansNeutralizing antibodyCells Culturedchemistry.chemical_classificationMembrane GlycoproteinsbiologyImmunogenicitymedicine.diseaseAntibodies NeutralizingVirologychemistryMultiprotein ComplexesInsect ScienceCytomegalovirus Infectionsbiology.proteinRabbitsGlycoproteinJournal of Virology
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Muscle protein synthesis, mTORC1/MAPK/Hippo signaling, and capillary density are altered by blocking of myostatin and activins

2012

Loss of muscle mass and function occurs in various diseases. Myostatin blocking can attenuate muscle loss, but downstream signaling is not well known. Therefore, to elucidate associated signaling pathways, we used the soluble activin receptor IIb (sActRIIB-Fc) to block myostatin and activins in mice. Within 2 wk, the treatment rapidly increased muscle size as expected but decreased capillary density per area. sActRIIB-Fc increased muscle protein synthesis 1–2 days after the treatment correlating with enhanced mTORC1 signaling (phosphorylated rpS6 and S6K1, r = 0.8). Concurrently, increased REDD1 and eIF2Bε protein contents and phosphorylation of 4E-BP1 and AMPK was observed. In contrast, pr…

Malemedicine.medical_specialtyPhysiologyEndocrinology Diabetes and MetabolismMuscle ProteinsCell CountP70-S6 Kinase 1MyostatinMechanistic Target of Rapamycin Complex 1Protein Serine-Threonine KinasesBiologyMice03 medical and health sciences0302 clinical medicinePhysiology (medical)Internal medicinemedicineAnimalsHippo Signaling PathwayExtracellular Signal-Regulated MAP KinasesMuscle Skeletalta315030304 developmental biology0303 health sciencesHippo signaling pathwayMyogenesisTOR Serine-Threonine KinasesSkeletal muscleActivin receptorMyostatinActivinsCapillariesMice Inbred C57BLmedicine.anatomical_structureEndocrinologyHippo signalingMultiprotein ComplexesProtein Biosynthesisbiology.proteinIntercellular Signaling Peptides and ProteinsPhosphorylation030217 neurology & neurosurgerySignal TransductionAmerican Journal of Physiology-Endocrinology and Metabolism
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DNA origami as a nanoscale template for protein assembly

2009

We describe two general approaches to the utilization of DNA origami structures for the assembly of materials. In one approach, DNA origami is used as a prefabricated template for subsequent assembly of materials. In the other, materials are assembled simultaneously with the DNA origami, i.e. the DNA origami technique is used to drive the assembly of materials. Fabrication of complex protein structures is demonstrated by these two approaches. The latter approach has the potential to be extended to the assembly of multiple materials with single attachment chemistry.

Materials scienceMechanical EngineeringBioengineeringNanotechnologyDNAGeneral ChemistryNanostructuresComplex proteinMechanics of MaterialsMultiprotein ComplexesDNA nanotechnologyNanotechnologyDNA origamiGeneral Materials ScienceStreptavidinSelf-assemblyProtein MultimerizationElectrical and Electronic EngineeringNanoscopic scaleNanotechnology
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Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins

2005

Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they fo…

Models MolecularMolecular Sequence DataBiophysicsApoptosisPeptideIn Vitro TechniquesBiophysical PhenomenaIon ChannelsPermeabilityProtein Structure Secondarychemistry.chemical_compoundBcl-2-associated X proteinSpectroscopy Fourier Transform InfraredHumansChannels Receptors and Electrical SignalingAmino Acid SequencePeptide sequenceIon channelbcl-2-Associated X Proteinchemistry.chemical_classificationbiologyChemistryCircular DichroismPeptide FragmentsCell biologyCalceinMembraneProto-Oncogene Proteins c-bcl-2CytoplasmMultiprotein ComplexesLiposomesbiology.proteinPèptidsCarrier ProteinsBacterial outer membraneProteïnesBH3 Interacting Domain Death Agonist ProteinBiophysical Journal
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A Quantum Mechanic/Molecular Mechanic Study of the Wild-Type and N155S Mutant HIV-1 Integrase Complexed with Diketo Acid

2008

Integrase (IN) is one of the three human immunodeficiency virus type 1 (HIV-1) enzymes essential for effective viral replication. Recently, mutation studies have been reported that have shown that a certain degree of viral resistance to diketo acids (DKAs) appears when some amino acid residues of the IN active site are mutated. Mutations represent a fascinating experimental challenge, and we invite theoretical simulations for the disclosure of still unexplored features of enzyme reactions. The aim of this work is to understand the molecular mechanisms of HIV-1 IN drug resistance, which will be useful for designing anti-HIV inhibitors with unique resistance profiles. In this study, we use mo…

Models MolecularProtein ConformationStereochemistryBiophysicsIntegrase inhibitorIntegrase InhibitorsHIV IntegraseBiophysical Theory and ModelingMechanicsMolecular mechanicsProtein structureComputer SimulationMagnesiumTernary complexBinding SitesbiologyChemistryAminobutyratesWild typeActive siteLigand (biochemistry)PhenylbutyratesIntegraseModels ChemicalMultiprotein ComplexesMutagenesis Site-Directedbiology.proteinQuantum TheoryProtein BindingBiophysical Journal
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ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space.

2015

Molecular machines or macromolecular complexes are supramolecular assemblies of biomolecules that ensure cellular homeostasis. Structure determination of those complexes in a purified state is often a tedious undertaking due to the compositional complexity and the related relative structural instability. To improve the stability of macromolecular complexes in vitro, we present here a generic method that optimizes the stability, homogeneity and solubility of macromolecular complexes by sparse-matrix screening of their thermal unfolding behaviour in the presence of various buffers and small molecules. The method includes the automated analysis of thermal unfolding curves based on a newly deve…

Models MolecularProtein FoldingProtein ConformationSupramolecular chemistryBiochemistryArticleProtein structureComputer SimulationMolecular Biologychemistry.chemical_classificationBinding SitesBiomoleculeMolecular biophysicsCell BiologyMolecular machineChemical spacechemistryModels ChemicalChemical physicsMultiprotein ComplexesBiophysicsProtein foldingCrystallizationAlgorithmsSoftwareBiotechnologyMacromoleculeProtein BindingNature methods
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β2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding

2008

AbstractLeukocyte integrins of the β2 family are essential for immune cell-cell adhesion. In activated cells, β2 integrins are phosphorylated on the cytoplasmic Thr758, leading to 14-3-3 protein recruitment to the β2 integrin. The mutation of this phosphorylation site impairs cell adhesion, actin reorganization, and cell spreading. Thr758 is contained in a Thr triplet of β2 that also mediates binding to filamin. Here, we investigated the binding of filamin, talin, and 14-3-3 proteins to phosphorylated and unphosphorylated β2 integrins by biochemical methods and x-ray crystallography. 14-3-3 proteins bound only to the phosphorylated integrin cytoplasmic peptide, with a high affinity (Kd, 261…

Models MolecularTalinThreonineanimal structuresFilaminsT-LymphocytesStatic ElectricityImmunologyIntegrinCD18macromolecular substancesPlasma protein bindingIn Vitro TechniquesFilaminBiochemistryJurkat Cells03 medical and health sciencesFilamin bindingContractile Proteins0302 clinical medicineCell AdhesionHumansProtein Interaction Domains and MotifsPhosphorylationCell adhesion030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMicrofilament ProteinsCell BiologyHematologyIntercellular Adhesion Molecule-1Talin bindingRecombinant ProteinsCell biology14-3-3 ProteinsAmino Acid SubstitutionCD18 AntigensMultiprotein Complexes030220 oncology & carcinogenesisbiology.proteinPhosphorylationProtein BindingBlood
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Deregulation of the EGFR/PI3K/PTEN/Akt/mTORC1 pathway in breast cancer: possibilities for therapeutic intervention

2014

// Nicole M. Davis 1 , Melissa Sokolosky 1 , Kristin Stadelman 1 , Stephen L. Abrams 1 , Massimo Libra 2 , Saverio Candido 2 , Ferdinando Nicoletti 2 , Jerry Polesel 3 , Roberta Maestro 4 , Antonino D’Assoro 5 , Lyudmyla Drobot 6 , Dariusz Rakus 7 , Agnieszka Gizak 7 , Piotr Laidler 8 , Joanna Dulinska-Litewka 8 , Joerg Basecke 9 , Sanja Mijatovic 10 , Danijela Maksimovic-Ivanic 10 , Giuseppe Montalto 11,12 , Melchiorre Cervello 12 , Timothy L. Fitzgerald 13 , Zoya N. Demidenko 14 , Alberto M. Martelli 15 , Lucio Cocco 15 , Linda S. Steelman 1 and James A. McCubrey 1 1 Department of Microbiology and Immunology, Brody School of Medicine at East Carolina University Greenville, NC 27858 USA 2 …

Oncologymedicine.medical_specialtytherapy resistanceClass I Phosphatidylinositol 3-Kinasesmedicine.medical_treatmentBreast NeoplasmsReviewBiologyMechanistic Target of Rapamycin Complex 1PI3KMetastasisTargeted therapyPhosphatidylinositol 3-KinasesBreast cancerTARGETED THERAPYInternal medicinemedicinePTENHumansTargeted Therapy Therapy Resistance Mutations PI3K mTOR rapamycinskin and connective tissue diseasesProtein kinase BneoplasmsPI3K/AKT/mTOR pathwayRoswell Park Cancer InstituterapamycinTOR Serine-Threonine KinasesMTORPTEN PhosphohydrolaseCancerTargeted TherapyTherapy Resistancemedicine.diseaseTargeted Therapy; Therapy Resistance; Mutations; PI3K; mTOR; rapamycin3. Good healthErbB ReceptorsGene Expression Regulation NeoplasticOncologyMultiprotein ComplexesCancer researchbiology.proteinFemaleReceptor Epidermal Growth FactormutationRAPAMYCINProto-Oncogene Proteins c-aktMutationsSignal Transduction
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Htid-1, the human homolog of the Drosophila melanogaster l(2)tid tumor suppressor, defines a novel physiological role of APC.

2007

Htid-1, the human counterpart of the Drosophila tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) encodes three splice forms translated into three cytosolic - Tid50, Tid48 and Tid46 - and three mitochondrial - Tid43, Tid40 and Tid38 - proteins. Here we provide evidence for the association of the endogenous Tid50/Tid48 proteins with the adenomatous polyposis coli (APC) tumor suppressor in normal colon epithelium, colorectal cancer cells and mouse NIH3T3 fibroblasts. Using the Glutathione S-transferase binding assay we show that the N-terminal region including the Armadillo domain (ARM) of APC is sufficient to bind the Tid molecules. Using immunoprecipitation and confocal micro…

Patched ReceptorsBeta-cateninTumor suppressor geneAdenomatous polyposis coliAdenomatous Polyposis Coli ProteinReceptors Cell SurfacePlasma protein bindingLigandsMitochondrial ProteinsMiceCytosolCell Line TumorAnimalsDrosophila ProteinsGuanine Nucleotide Exchange FactorsHumansIntestinal MucosaActinHeat-Shock Proteinsbeta CateninPatched ReceptorsbiologySequence Homology Amino AcidGene Expression ProfilingTumor Suppressor ProteinsWnt signaling pathwayGene Expression Regulation DevelopmentalCell BiologyHSP40 Heat-Shock ProteinsActin cytoskeletonMolecular biologyCell biologyMitochondriaDrosophila melanogasterras GTPase-Activating ProteinsMultiprotein Complexesbiology.proteinNIH 3T3 CellsRho Guanine Nucleotide Exchange FactorsProtein BindingCellular signalling
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Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.

2014

Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification…

ProteomicsSaccharomyces cerevisiae Proteinslcsh:QH426-470Saccharomyces cerevisiaeBiochemistryMolecular GeneticsRNA TransferGene Expression Regulation FungalMolecular Cell BiologyGeneticsFungal GeneticsPhosphorylationPost-Translational ModificationUridineMolecular BiologyAdaptor Proteins Signal TransducingHistone AcetyltransferasesAlanineSpectrometric Identification of ProteinsBiology and life sciencesCasein Kinase INucleotidesMicrobial GeneticsProteinsCell BiologyPeptide Elongation Factorslcsh:GeneticsPhenotypeMultiprotein ComplexesRNAMolecular ComplexesTransfer RNAAnticodonsResearch ArticlePLoS genetics
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