Search results for "Protein multimerization"

showing 9 items of 99 documents

Aβ Oligomers and Fibrillar Aggregates Induce Different Apoptotic Pathways in LAN5 Neuroblastoma Cell Cultures

2009

Fibril deposit formation of amyloid beta-protein (Abeta) in the brain is a hallmark of Alzheimer's disease (AD). Increasing evidence suggests that toxicity is linked to diffusible Abeta oligomers, which have been found in soluble brain extracts of AD patients, rather than to insoluble fibers. Here we report a study of the toxicity of two distinct forms of recombinant Abeta small oligomers and fibrillar aggregates to simulate the action of diffusible Abeta oligomers and amyloid plaques on neuronal cells. Different techniques, including dynamic light scattering, fluorescence, and scanning electron microscopy, have been used to characterize the two forms of Abeta. Under similar conditions and …

Time FactorsAmyloidCell SurvivalBiophysicsApoptosisBiologyFibrilCaspase 8Substrate SpecificityNeuroblastomaCytosolCell Line TumormedicineHumansEnzyme InhibitorsProtein Structure QuaternaryCaspase-9Amyloid beta-PeptidesDose-Response Relationship DrugProteinCytochrome cNeurodegenerationCytochromes cHydrogen-Ion Concentrationmedicine.diseaseCaspase InhibitorsPeptide FragmentsCell biologyProtein TransportCytosolApoptosisMicroscopy Electron Scanningbiology.proteinProtein MultimerizationProtein BindingSignal TransductionBiophysical Journal
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Inhibitor-Induced Dimerization of an Essential Oxidoreductase from African Trypanosomes

2018

Trypanosomal and leishmanial infections claim tens of thousands of lives each year. The metabolism of these unicellular eukaryotic parasites differs from the human host and their enzymes thus constitute promising drug targets. Tryparedoxin (Tpx) from Trypanosoma brucei is the essential oxidoreductase in the parasite's hydroperoxide-clearance cascade. In vitro and in vivo functional assays show that a small, selective inhibitor efficiently inhibits Tpx. With X-ray crystallography, SAXS, analytical SEC, SEC-MALS, MD simulations, ITC, and NMR spectroscopy, we show how covalent binding of this monofunctional inhibitor leads to Tpx dimerization. Intra- and intermolecular inhibitor-inhibitor, pro…

TrypanosomaProtein ConformationSpermidineDimerTrypanosoma brucei bruceiAntiprotozoal AgentsMolecular Dynamics SimulationTrypanosoma brucei010402 general chemistry01 natural sciencesCatalysischemistry.chemical_compoundThioredoxinsBacterial ProteinsIn vivoOxidoreductaseAnimalsHumansEnzyme Inhibitorschemistry.chemical_classificationbiology010405 organic chemistryHydrogen PeroxideGeneral ChemistryNuclear magnetic resonance spectroscopyLigand (biochemistry)biology.organism_classificationGlutathione0104 chemical sciencesEnzymechemistryBiochemistryDrug DesignChemically induced dimerizationProtein MultimerizationOxidoreductasesOxidation-ReductionProtein BindingAngewandte Chemie International Edition
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Probing protein interactions in the membrane-containing virus PRD1.

2015

PRD1 is a Gram-negative bacteria infecting complex tailless icosahedral virus with an inner membrane. This type virus of the family Tectiviridae contains at least 18 structural protein species, of which several are membrane associated. Vertices of the PRD1 virion consist of complexes recognizing the host cell, except for one special vertex through which the genome is packaged. Despite extensive knowledge of the overall structure of the PRD1 virion and several individual proteins at the atomic level, the locations and interactions of various integral membrane proteins and membrane-associated proteins still remain a mystery. Here, we demonstrated that blue native PAGE can be used to probe pro…

Viral Structural Proteins0303 health sciencesVesicle-associated membrane protein 8Macromolecular Substances030302 biochemistry & molecular biologyMutantMembrane ProteinsBiologyVirologyTransmembrane proteinProtein–protein interaction03 medical and health sciencesLytic cycleVirologyProtein Interaction MappingInner membraneTectiviridaeBacteriophage PRD1Electrophoresis Polyacrylamide GelProtein MultimerizationIntegral membrane protein030304 developmental biologyThe Journal of general virology
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Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk

2019

Web spiders connect silk proteins, so-called spidroins, into fibers of extraordinary toughness. The spidroin N-terminal domain (NTD) plays a pivotal role in this process: it polymerizes spidroins through a complex mechanism of dimerization. Here we analyze sequences of spidroin NTDs and find an unusually high content of the amino acid methionine. We simultaneously mutate all methionines present in the hydrophobic core of a spidroin NTD from a nursery web spider’s dragline silk to leucine. The mutated NTD is strongly stabilized and folds at the theoretical speed limit. The structure of the mutant is preserved, yet its ability to dimerize is substantially impaired. We find that side chains of…

congenital hereditary and neonatal diseases and abnormalitiesProtein Foldinggenetic structuresProtein ConformationScienceSilkmacromolecular substancesCircular dichroismcomplex mixturesArticleMethionineddc:590ddc:570AnimalsAmino Acid Sequencelcsh:ScienceFluorescence spectroscopySequence Homology Amino AcidfungiQtechnology industry and agricultureSpidersSpectrometry FluorescenceMutationThermodynamicslcsh:QProtein MultimerizationFibroinsSolution-state NMRHydrophobic and Hydrophilic InteractionsAlgorithmsNature Communications
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Mini-Review: Two Brothers in Crime – The Interplay of TRESK and TREK in Human Diseases

2021

Abstract TWIK-related spinal cord potassium (TRESK) and TWIK-related potassium (TREK) channels are both subfamilies of the two-pore domain potassium (K2P) channel group. Despite major structural, pharmacological, as well as biophysical differences, emerging data suggest that channels of these two subfamilies are functionally more closely related than previously assumed. Recent studies, for instance, indicate an assembling of TRESK and TREK subunits, leading to the formation of heterodimeric channels with different functional properties compared to homodimeric ones. Formation of tandems consisting of TRESK and TREK subunits might thus multiply the functional diversity of both TRESK and TREK …

endocrine systemPain syndromePotassium ChannelsGeneral NeuroscienceContext (language use)BiologyMini reviewFunctional diversityPotassium Channels Tandem Pore DomainNeuroinflammatory DiseasesHumansProtein Multimerizationhuman activitiesNeuroscienceNeuroscience Letters
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Differential regulation of hexameric and dodecameric hemocyanin from A. leptodactylus

2013

The oxygen binding properties of hemocyanins are regulated on a short time scale by effectors such as l-lactate, urate and protons, and on longer time scales by expression of the different types of subunits. For Astacus leptodactylus it was shown previously that acclimation to higher temperatures leads to increased levels of a 6-meric hemocyanin species, whereas at lower temperatures the 12-meric form prevails. Here we show that the temperature dependence of the two forms supports the idea, that the maintenance of high affinity towards oxygen is the driving force for the differential expression of these hemocyanins. Furthermore, the two different types of hemocyanin differ not only in the a…

medicine.medical_treatmentProtein subunitAllosteric regulationBiophysicschemistry.chemical_elementAstacus leptodactylusBiochemistryOxygenAnalytical ChemistryAllosteric RegulationmedicineAnimalsBinding siteMolecular BiologyBinding SitesbiologyChemistryTemperatureIsothermal titration calorimetryHemocyaninbiology.organism_classificationUric AcidOxygenBiochemistryHemocyaninsLactatesBiophysicsAnuraProtein MultimerizationProtonsOxygen bindingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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A novel microtubule de-stabilizing complementarity-determining region C36L1 peptide displays antitumor activity against melanoma in vitro and in vivo

2015

AbstractShort peptide sequences from complementarity-determining regions (CDRs) of different immunoglobulins may exert anti-infective, immunomodulatory and antitumor activities regardless of the specificity of the original monoclonal antibody (mAb). In this sense, they resemble early molecules of innate immunity. C36L1 was identified as a bioactive light-chain CDR1 peptide by screening 19 conserved CDR sequences targeting murine B16F10-Nex2 melanoma. The 17-amino acid peptide is readily taken up by melanoma cells and acts on microtubules causing depolymerization, stress of the endoplasmic reticulum and intrinsic apoptosis. At low concentrations, C36L1 inhibited migration, invasion and proli…

rho GTP-Binding ProteinsMelanoma ExperimentalAntineoplastic AgentsApoptosisPeptideComplementarity determining regionBiologyEndoplasmic ReticulumMicrotubulesArticleMicePhosphatidylinositol 3-KinasesCell MovementTubulinCell Line TumormedicineAnimalsNeoplasm MetastasisMelanomaPI3K/AKT/mTOR pathwayCell Proliferationchemistry.chemical_classificationMultidisciplinaryInnate immune systemCell growthMelanomaIntrinsic apoptosisPTEN Phosphohydrolasemedicine.diseaseComplementarity Determining RegionsMolecular biologyMitochondriaDisease Models AnimalchemistryCell cultureCancer researchProtein MultimerizationPeptidesProto-Oncogene Proteins c-aktSignal TransductionScientific Reports
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Design, synthesis and structure-activity relationship of 2-(3',4',5'-trimethoxybenzoyl)-benzo[b]furan derivatives as a novel class of inhibitors of t…

2009

The biological importance of microtubules in mitosis and cell division makes them an interesting target for the development of anticancer agents. Small molecules such as benzo[b]furans are attractive as inhibitors of tubulin polymerization. Thus, a new class of inhibitors of tubulin polymerization based on the 2-(3′,4′,5′-trimethoxybenzoyl)-benzo[b]furan molecular skeleton, with electron-donating (Me, OMe or OH) or electron-withdrawing (F, Cl and Br) substituents on the benzene ring, was synthesized and evaluated for antiproliferative activity, inhibition of tubulin polymerization and cell cycle effects. Adding a methyl group at the C-3 position resulted in increased activity. The most prom…

structure-activityStereochemistryClinical BiochemistryPharmaceutical ScienceAntineoplastic Agentsmacromolecular substancesBiochemistryChemical synthesisArticleStructure-Activity Relationshipchemistry.chemical_compoundbenzo[b]furansMicrotubuleCell Line TumorFuranDrug DiscoveryHumansStructure–activity relationshipMolecular BiologyBenzofuransCell ProliferationBinding SitesDose-Response Relationship DrugbiologyChemistryTubulin ModulatorsCell growthCell CycleOrganic ChemistrySmall moleculeTubulin Modulatorstubulin polymerizationTubulinDrug Designbiology.proteinMolecular MedicineProtein MultimerizationColchicine
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The Extracellular δ-Domain is Essential for the Formation of CD81 Tetraspanin Webs

2014

AbstractCD81 is a ubiquitously expressed member of the tetraspanin family. It forms large molecular platforms, so-called tetraspanin webs that play physiological roles in a variety of cellular functions and are involved in viral and parasite infections. We have investigated which part of the CD81 molecule is required for the formation of domains in the cell membranes of T-cells and hepatocytes. Surprisingly, we find that large CD81 platforms assemble via the short extracellular δ-domain, independent from a strong primary partner binding and from weak interactions mediated by palmitoylation. The δ-domain is also essential for the platforms to function during viral entry. We propose that, ins…

virusesLipoylationBiophysicschemical and pharmacologic phenomenaPlasma protein bindingBiologyTetraspanin 28Jurkat CellsProtein structurePalmitoylationTetraspaninViral entryExtracellularHumansComputingMilieux_MISCELLANEOUS[PHYS]Physics [physics]MembranesHep G2 Cellsbiochemical phenomena metabolism and nutritionCell biologyProtein Structure TertiaryProtein MultimerizationProtein Processing Post-TranslationalFunction (biology)CD81Protein Binding
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